IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Erythrocyte membranes("ghosts"), normal and stripped (depleted of cytoskeleton). rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC crosslink cross-linking study crosslink sequence tag sequence tag identification sequence tag Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. EGS-ethylene glycolbis(succinimidylsuccinate) DRMs (Detergent Resistant Membranes) were prepared from normal erythrocyte membranes by Density Gradient Centrifugation from an alkaline 50% sucrose fraction and subsequently cross-linked. Stomatin complexes were isolated by immunoaffinity chromatography. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC crosslink cross-linking study crosslink sequence tag sequence tag identification sequence tag Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Cross linker:DSS - disuccinimidyl suberate DRMs (Detergent Resistant Membranes) were prepared from cytoskeleton-depleted membranes by Density Gradient Centrifugation and subsequently cross-linked. Stomatin complexes were isolated by immunoaffinity chromatography. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC density sedimentation cosedimentation through density gradient density sedimentation western blot western blot Immuno blot Immuno blot Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Normal erythrocyte membranes OR DRMs (Detergent Resistant Membranes) were prepared by Density Gradient Centrifugation from an alkaline 50% sucrose fraction. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC crosslink cross-linking study crosslink sequence tag sequence tag identification sequence tag Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Cross linker:EGS - ethylene glycolbis(succinimidylsuccinate) Cytoskeleton stripped erythrocyte membranes ("ghosts") were prepared from erythrocytes by filtering/pelleting followed by hypotonic lysis and incubation with sodium hydroxide. Cross-linked membrane proteins were loaded onto a column of monoclonal anti-stomatin antibody bound to CNBr-activated Sepharose. Stomatin-complexes were isolated and analyzed via MS. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC crosslink cross-linking study crosslink sequence tag sequence tag identification sequence tag Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Cross linker:EGS - ethylene glycolbis(succinimidylsuccinate) DRMs (Detergent Resistant Membranes) were prepared from cytoskeleton-depleted membranes by Density Gradient Centrifugation and subsequently cross-linked. Stomatin complexes were isolated by immunoaffinity chromatography. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochimica et biophysica acta 2013 imex curation Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. rainer.prohaska@meduniwien.ac.at 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-erythrocyte Homo sapiens erythrocyte Erythrocyte, Red blood cell; Corpuscle; RBC crosslink cross-linking study crosslink sequence tag sequence tag identification sequence tag Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R., Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R. I have omitted dimerisation/oligomerisation of Stomatin as I dont know if it is intra or inter moleulcular binding. Cross linker:DSS - disuccinimidyl suberate Cytoskeleton stripped erythrocyte membranes ("ghosts") were prepared from erythrocytes by filtering/pelleting followed by hypotonic lysis and incubation with sodium hydroxide. Cross-linked membrane proteins were loaded onto a column of monoclonal anti-stomatin antibody bound to CNBr-activated Sepharose. rainer.prohaska@meduniwien.ac.at Accepted 2017-NOV-10 AT 10:42 GMT AT 10:42 GMT by PPORRAS Biochimica et biophysica acta 2013 Only protein-protein interactions imex curation imex curation added two extra interactions - hope these are OK as the colours are difficult to distinguish.; added cd47_human Leukocyte surface antigen CD47 CD47 MER6 Integrin-associated protein Antigenic surface determinant protein OA3 Protein MER6 protein protein human Homo sapiens Human MWPLVAALLLGSACCGSAQLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTFDGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTELTREGETIIELKYRVVSWFSPNENILIVIFPIFAILLFWGQFGIKTLKYRSGGMDEKTIALLVAGLVITVIVIVGAILFVPGEYSLKNATGLGLIVTSTGILILLHYYVFSTAIGLTSFVIAILVIQVIAYILAVVGLSLCIAACIPMHGPLLISGLSILALAQLLGLVYMKFVASNQKTIQPPRKAVEEPLNAFKESKGMMNDE 5D20730A2632D550 epb42_human Protein 4.2 EPB42 E42P Erythrocyte membrane protein band 4.2 protein protein human Homo sapiens Human MGQALGIKSCDFQAARNNEEHHTKALSSRRLFVRRGQPFTIILYFRAPVRAFLPALKKVALTAQTGEQPSKINRTQATFPISSLGDRKWWSAVVEERDAQSWTISVTTPADAVIGHYSLLLQVSGRKQLLLGQFTLLFNPWNREDAVFLKNEAQRMEYLLNQNGLIYLGTADCIQAESWDFGQFEGDVIDLSLRLLSKDKQVEKWSQPVHVARVLGALLHFLKEQRVLPTPQTQATQEGALLNKRRGSVPILRQWLTGRGRPVYDGQAWVLAAVACTVLRCLGIPARVVTTFASAQGTGGRLLIDEYYNEEGLQNGEGQRGRIWIFQTSTECWMTRPALPQGYDGWQILHPSAPNGGGVLGSCDLVPVRAVKEGTLGLTPAVSDLFAAINASCVVWKCCEDGTLELTDSNTKYVGNNISTKGVGSDRCEDITQNYKYPEGSLQEKEVLERVEKEKMEREKDNGIRPPSLETASPLYLLLKAPSSLPLRGDAQISVTLVNHSEQEKAVQLAIGVQAVHYNGVLAAKLWRKKLHLTLSANLEKIITIGLFFSNFERNPPENTFLRLTAMATHSESNLSCFAQEDIAICRPHLAIKMPEKAEQYQPLTASVSLQNSLDAPMEDCVISILGRGLIHRERSYRFRSVWPENTMCAKFQFTPTHVGLQRLTVEVDCNMFQNLTNYKSVTVVAPELSA 38225C311E478580 kell_human Kell blood group glycoprotein KEL protein protein human Homo sapiens Human MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARRVLTAILILGLLLCFSVLLFYNFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW 604A168AD300EDB4 stom_human Stomatin STOM BND7 EPB72 Protein 7.2b Erythrocyte band 7 integral membrane protein Erythrocyte membrane protein band 7.2 protein protein human Homo sapiens Human MAEKRHTRDSEAQRLPDSFKDSPSKGLGPCGWILVAFSFLFTVITFPISIWMCIKIIKEYERAIIFRLGRILQGGAKGPGLFFILPCTDSFIKVDMRTISFDIPPQEILTKDSVTISVDGVVYYRVQNATLAVANITNADSATRLLAQTTLRNVLGTKNLSQILSDREEIAHNMQSTLDDATDAWGIKVERVEIKDVKLPVQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASMVITESPAALQLRYLQTLTTIAAEKNSTIVFPLPIDMLQGIIGAKHSHLG 5FEDA92230D99A24 bcam_human Basal cell adhesion molecule BCAM Auberger B antigen B-CAM cell surface glycoprotein F8/G253 antigen LU Lutheran antigen Lutheran blood group glycoprotein MSK19 protein protein human Homo sapiens Human MEPPDAPAQARGAPRLLLLAVLLAAHPDAQAEVRLSVPPLVEVMRGKSVILDCTPTGTHDHYMLEWFLTDRSGARPRLASAEMQGSELQVTMHDTRGRSPPYQLDSQGRLVLAEAQVGDERDYVCVVRAGAAGTAEATARLNVFAKPEATEVSPNKGTLSVMEDSAQEIATCNSRNGNPAPKITWYRNGQRLEVPVEMNPEGYMTSRTVREASGLLSLTSTLYLRLRKDDRDASFHCAAHYSLPEGRHGRLDSPTFHLTLHYPTEHVQFWVGSPSTPAGWVREGDTVQLLCRGDGSPSPEYTLFRLQDEQEEVLNVNLEGNLTLEGVTRGQSGTYGCRVEDYDAADDVQLSKTLELRVAYLDPLELSEGKVLSLPLNSSAVVNCSVHGLPTPALRWTKDSTPLGDGPMLSLSSITFDSNGTYVCEASLPTVPVLSRTQNFTLLVQGSPELKTAEIEPKADGSWREGDEVTLICSARGHPDPKLSWSQLGGSPAEPIPGRQGWVSSSLTLKVTSALSRDGISCEASNPHGNKRHVFHFGTVSPQTSQAGVAVMAVAVSVGLLLLVVAVFYCVRRKGGPCCRQRREKGAPPPGEPGLSHSGSEQPEQTGLLMGGASGGARGGSGGFGDEC C88F4F5C640C3F5B icam4_human Intercellular adhesion molecule 4 ICAM4 LW Landsteiner-Wiener blood group glycoprotein protein protein human Homo sapiens Human MGSLFPLSLLFFLAAAYPGVGSALGRRTKRAQSPKGSPLAPSGTSVPFWVRMSPEFVAVQPGKSVQLNCSNSCPQPQNSSLRTPLRQGKTLRGPGWVSYQLLDVRAWSSLAHCLVTCAGKTRWATSRITAYKPPHSVILEPPVLKGRKYTLRCHVTQVFPVGYLVVTLRHGSRVIYSESLERFTGLDLANVTLTYEFAAGPRDFWQPVICHARLNLDGLVVRNSSAPITLMLAWSPAPTALASGSIAALVGILLTVGAAYLCKCLAMKSQA 2F6BC8BABD79E615 ut1_human Urea transporter 1 SLC14A1 HUT11 JK RACH1 Solute carrier family 14 member 1 UT1 UTE Urea transporter, erythrocyte protein protein human Homo sapiens Human MEDSPTMVRVDSPTMVRGENQVSPCQGRRCFPKALGYVTGDMKELANQLKDKPVVLQFIDWILRGISQVVFVNNPVSGILILVGLLVQNPWWALTGWLGTVVSTLMALLLSQDRSLIASGLYGYNATLVGVLMAVFSDKGDYFWWLLLPVCAMSMTCPIFSSALNSMLSKWDLPVFTLPFNMALSMYLSATGHYNPFFPAKLVIPITTAPNISWSDLSALELLKSIPVGVGQIYGCDNPWTGGIFLGAILLSSPLMCLHAAIGSLLGIAAGLSLSAPFEDIYFGLWGFNSSLACIAMGGMFMALTWQTHLLALGCALFTAYLGVGMANFMAEVGLPACTWPFCLATLLFLIMTTKNSNIYKMPLSKVTYPEENRIFYLQAKKRMVESPL 08625B8B66C310F2 s29a1_human Equilibrative nucleoside transporter 1 SLC29A1 ENT1 Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter Nucleoside transporter, es-type Solute carrier family 29 member 1 protein protein human Homo sapiens Human MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARLVFVPLLLLCNIKPRRYLTVVFEHDAWFIFFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGAIMAFFLCLGLALGAVFSFLFRAIV F18535A95DEBC95D flot2_human Flotillin-2 FLOT2 ESA1 M17S1 Epidermal surface antigen Membrane component chromosome 17 surface marker 1 protein protein human Homo sapiens Human MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAELPASVHALTGVDLSKIPLIKKATGVQV F690BFE0151D3BD7 aqp1_human Aquaporin-1 Aquaporin-CHIP Water channel protein for red blood cells and kidney proximal tubule Urine water channel AQP1 CHIP28 protein protein human Homo sapiens Human MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK DIP protein P29972 original sequence version: 162 DIP protein P29972 original sequence version: 93 BA204D82FB26352E sptb1_human Spectrin beta chain, erythrocytic Beta-I spectrin SPTB SPTB1 protein protein human Homo sapiens Human MTSATEFENVGNQPPYSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRITDLYKDLRDGRMLIKLLEVLSGEMLPKPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGRETRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFNVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQTITVLNSRKFANSLTGVQQQLQAFSTYRTVEKPPKFQEKGNLEVLLFTIQSRMRANNQKVYTPHDGKLVSDINRAWESLEEAEYRRELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVAQDNFGYDLAAVEAAKKKHEAIETDTAAYEERVRALEDLAQELEKENYHDQKRITARKDNILRLWSYLQELLQSRRQRLETTLALQKLFQDMLHSIDWMDEIKAHLLSAEFGKHLLEVEDLLQKHKLMEADIAIQGDKVKAITAATLKFTEGKGYQPCDPQVIQDRISHLEQCFEELSNMAAGRKAQLEQSKRLWKFFWEMDEAESWIKEKEQIYSSLDYGKDLTSVLILQRKHKAFEDELRGLDAHLEQIFQEAHGMVARKQFGHPQIEARIKEVSAQWDQLKDLAAFCKKNLQDAENFFQFQGDADDLKAWLQDAHRLLSGEDVGQDEGATRALGKKHKDFLEELEESRGVMEHLEQQAQGFPEEFRDSPDVTHRLQALRELYQQVVAQADLRQQRLQEALDLYTVFGETDACELWMGEKEKWLAEMEMPDTLEDLEVVQHRFDILDQEMKTLMTQIDGVNLAANSLVESGHPRSREVKQYQDHLNTRWQAFQTLVSERREAVDSALRVHNYCVDCEETSKWITDKTKVVESTKDLGRDLAGIIAIQRKLSGLERDVAAIQARVDALERESQQLMDSHPEQKEDIGQRQKHLEELWQGLQQSLQGQEDLLGEVSQLQAFLQDLDDFQAWLSITQKAVASEDMPESLPEAEQLLQQHAGIKDEIDGHQDSYQRVKESGEKVIQGQTDPEYLLLGQRLEGLDTGWNALGRMWESRSHTLAQCLGFQEFQKDAKQAEAILSNQEYTLAHLEPPDSLEAAEAGIRKFEDFLGSMENNRDKVLSPVDSGNKLVAEGNLYSDKIKEKVQLIEDRHRKNNEKAQEASVLLRDNLELQNFLQNCQELTLWINDKLLTSQDVSYDEARNLHNKWLKHQAFVAELASHEGWLENIDAEGKQLMDEKPQFTALVSQKLEALHRLWDELQATTKEKTQHLSAARSSDLRLQTHADLNKWISAMEDQLRSDDPGKDLTSVNRMLAKLKRVEDQVNVRKEELGELFAQVPSMGEEGGDADLSIEKRFLDLLEPLGRRKKQLESSRAKLQISRDLEDETLWVEERLPLAQSADYGTNLQTVQLFMKKNQTLQNEILGHTPRVEDVLQRGQQLVEAAEIDCQDLEERLGHLQSSWDRLREAAAGRLQRLRDANEAQQYYLDADEAEAWIGEQELYVISDEIPKDEEGAIVMLKRHLRQQRAVEDYGRNIKQLASRAQGLLSAGHPEGEQIIRLQGQVDKHYAGLKDVAEERKRKLENMYHLFQLKRETDDLEQWISEKELVASSPEMGQDFDHVTLLRDKFRDFARETGAIGQERVDNVNAFIERLIDAGHSEAATIAEWKDGLNEMWADLLELIDTRMQLLAASYDLHRYFYTGAEILGLIDEKHRELPEDVGLDASTAESFHRVHTAFERELHLLGVQVQQFQDVATRLQTAYAGEKAEAIQNKEQEVSAAWQALLDACAGRRTQLVDTADKFRFFSMARDLLSWMESIIRQIETQERPRDVSSVELLMKYHQGINAEIETRSKNFSACLELGESLLQRQHQASEEIREKLQQVMSRRKEMNEKWEARWERLRMLLEVCQFSRDASVAEAWLIAQEPYLASGDFGHTVDSVEKLIKRHEAFEKSTASWAERFAALEKPTTLELKERQIAERPAEETGPQEEEGETAGEAPVSHHAATERTSPVSLWSRLSSSWESLQPEPSHPY 311AE5CD53237610 b3at_human Band 3 anion transport protein SLC4A1 AE1 DI EPB3 Anion exchange protein 1 Solute carrier family 4 member 1 protein protein human Homo sapiens Human MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:109270]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape Defects in SLC4A1 are the cause of autosomal dominant distal renal tubular acidosis (dRTA) [MIM:179800]. This disease is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis Defects in SLC4A1 are the cause of autosomal recessive distal renal tubular acidosis (dRTA) [MIM:611590] Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin mint Defects in SLC4A1 are a cause of hereditary spherocytosis (HS) [MIM:109270]. HS is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal 35EC3EE7AFF27D2F at2b4_human Plasma membrane calcium-transporting ATPase 4 Plasma membrane calcium ATPase isoform 4 Plasma membrane calcium pump isoform 4 Matrix-remodeling-associated protein 1 ATP2B4 ATP2B2 MXRA1 protein protein human Homo sapiens Human MTNPSDRVLPANSMAESREGDFGCTVMELRKLMELRSRDALTQINVHYGGVQNLCSRLKTSPVEGLSGNPADLEKRRQVFGHNVIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPAGEENELCGQVATTPEDENEAQAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQCRIEQEQKFSIIRNGQLIQLPVAEIVVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIILTLLGVNEDDEGEKKKKGKKQGVPENRNKAKTQDGVALEIQPLNSQEGIDNEEKDKKAVKVPKKEKSVLQGKLTRLAVQIGKAGLLMSALTVFILILYFVIDNFVINRRPWLPECTPIYIQYFVKFFIIGITVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYIGGIHYRQIPSPDVFLPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALLGFVTDLKQDYQAVRNEVPEEKLYKVYTFNSVRKSMSTVIRNPNGGFRMYSKGASEIILRKCNRILDRKGEAVPFKNKDRDDMVRTVIEPMACDGLRTICIAYRDFDDTEPSWDNENEILTELTCIAVVGIEDPVRPEVPDAIAKCKQAGITVRMVTGDNINTARAIATKCGILTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGEHRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTESLLKRRPYGRNKPLISRTMMKNILGHAFYQLIVIFILVFAGEKFFDIDSGRKAPLHSPPSQHYTIVFNTFVLMQLFNEINSRKIHGEKNVFSGIYRNIIFCSVVLGTFICQIFIVEFGGKPFSCTSLSLSQWLWCLFIGIGELLWGQFISAIPTRSLKFLKEAGHGTTKEEITKDAEGLDEIDHAEMELRRGQILWFRGLNRIQTQIDVINTFQTGASFKGVLRRQNMGQHLDVKLVPSSSYIKVVKAFHSSLHESIQKPYNQKSIHSFMTHPEFAIEEELPRTPLLDEEEEENPDKASKFGTRVLLLDGEVTPYANTNNNAVDCNQVQLPQSDSSLQSLETSV 568544103CD5F494 spta1_human Spectrin alpha chain, erythrocytic 1 SPTA1 Erythroid alpha-spectrin SPTA protein protein human Homo sapiens Human MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSAEALLQKHEDFEEAFTAQEEKIITVDKTATKLIGDDHYDSENIKAIRDGLLARRDALREKAATRRRLLKESLLLQKLYEDSDDLKNWINKKKKLADDEDYKDIQNLKSRVQKQQVFEKELAVNKTQLENIQKTGQEMIEGGHYASDNVTTRLSEVASLWEELLEATKQKGTQLHEANQQLQFENNAEDLQRWLEDVEWQVTSEDYGKGLAEVQNRLRKHGLLESAVAARQDQVDILTDLAAYFEEIGHPDSKDIRARQESLVCRFEALKEPLATRKKKLLDLLHLQLICRDTEDEEAWIQETEPSATSTYLGKDLIASKKLLNRHRVILENIASHEPRIQEITERGNKMVEEGHFAAEDVASRVKSLNQNMESLRARAARRQNDLEANVQFQQYLADLHEAETWIREKEPIVDNTNYGADEEAAGALLKKHEAFLLDLNSFGDSMKALRNQANACQQQQAAPVEGVAGEQRVMALYDFQARSPREVTMKKGDVLTLLSSINKDWWKVEAADHQGIVPAVYVRRLAHDEFPMLPQRRREEPGNITQRQEQIENQYRSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKAENTGVELDDVWELQKKFDEFQKDLNTNEPRLRDINKVADDLLFEGLLTPEGAQIRQELNSRWGSLQRLADEQRQLLGSAHAVEVFHREADDTKEQIEKKCQALSAADPGSDLFSVQALQRRHEGFERDLVPLGDKVTILGETAERLSESHPDATEDLQRQKMELNEAWEDLQGRTKDRKESLNEAQKFYLFLSKARDLQNWISSIGGMVSSQELAEDLTGIEILLERHQEHRADMEAEAPTFQALEDFSAELIDSGHHASPEIEKKLQAVKLERDDLEKAWEKRKKILDQCLELQMFQGNCDQVESWMVARENSLRSDDKSSLDSLEALMKKRDDLDKAITAQEGKITDLEHFAESLIADEHYAKEEIATRLQRVLDRWKALKAQLIDERTKLGDYANLKQFYRDLEELEEWISEMLPTACDESYKDATNIQRKYLKHQTFAHEVDGRSEQVHGVINLGNSLIECSACDGNEEAMKEQLEQLKEHWDHLLERTNDKGKKLNEASRQQRFNTSIRDFEFWLSEAETLLAMKDQARDLASAGNLLKKHQLLEREMLAREDALKDLNTLAEDLLSSGTFNVDQIVKKKDNVNKRFLNVQELAAAHHEKLKEAYALFQFFQDLDDEESWIEEKLIRVSSQDYGRDLQGVQNLLKKHKRLEGELVAHEPAIQNVLDMAEKLKDKAAVGQEEIQLRLAQFVEHWEKLKELAKARGLKLEESLEYLQFMQNAEEEEAWINEKNALAVRGDCGDTLAATQSLLMKHEALENDFAVHETRVQNVCAQGEDILNKVLQEESQNKEISSKIEALNEKTPSLAKAIAAWKLQLEDDYAFQEFNWKADVVEAWIADKETSLKTNGNGADLGDFLTLLAKQDTLDASLQSFQQERLPEITDLKDKLISAQHNQSKAIEERYAALLKRWEQLLEASAVHRQKLLEKQLPLQKAEDLFVEFAHKASALNNWCEKMEENLSEPVHCVSLNEIRQLQKDHEDFLASLARAQADFKCLLELDQQIKALGVPSSPYTWLTVEVLERTWKHLSDIIEEREQELQKEEARQVKNFEMCQEFEQNASTFLQWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIVDLGDNLEDALILDIKYSTIGLAQQWDQLYQLGLRMQHNLEQQIQAKDIKGVSEETLKEFSTIYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEDEHEPKFEKFLDAVDPGRKGYVSLEDYTAFLIDKESENIKSSDEIENAFQALAEGKSYITKEDMKQALTPEQVSFCATHMQQYMDPRGRSHLSGYDYVGFTNSYFGN B60680145C58DF55 g3p_human Glyceraldehyde-3-phosphate dehydrogenase GAPDH OK/SW-cl.12 CDABP0047 GAPD Peptidyl-cysteine S-nitrosylase GAPDH protein protein human Homo sapiens Human MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE DIP protein P04406 original sequence version: null DIP protein P04406 original sequence version: 196 DIP protein P04406 original sequence version: 198 DIP protein P04406 original sequence version: 156 C9C135E8AE3E8744 aldoa_human Fructose-bisphosphate aldolase A Muscle-type aldolase Lung cancer antigen NY-LU-1 ALDOA ALDA protein protein human Homo sapiens Human MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFVSNHAY DIP protein P04075 original sequence version: null 0AAED80F755A7BE8 glpa_human Glycophorin-A PAS-2 Sialoglycoprotein alpha MN sialoglycoprotein GYPA GPA protein protein human Homo sapiens Human MYGKIIFVLLLSEIVSISASSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ 48A5450E22FA99C9 flot1_human Flotillin-1 FLOT1 protein protein human Homo sapiens Human MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILTRLPESVERLTGVSISQVNHKPLRTA C69E5421E565F53A gtr1_human Solute carrier family 2, facilitated glucose transporter member 1 Glucose transporter type 1, erythrocyte/brain HepG2 glucose transporter SLC2A1 GLUT1 protein protein human Homo sapiens Human MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV DIP protein P11166 original sequence version: null E71E1C6BD1B00B1E s40a1_human Solute carrier family 40 member 1 Ferroportin-1 Iron-regulated transporter 1 SLC40A1 FPN1 IREG1 SLC11A3 MSTP079 protein protein human Homo sapiens Human MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHELLTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLKEEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAFTWLRRKCGLVRTGLISGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFIQGESITPTKIPEITTEIYMSNGSNSANIVPETSPESVPIISVSLLFAGVIAARIGLWSFDLTVTQLLQENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHIMYFRFAQNTLGNKLFACGPDAKEVRKENQANTSVV E4D6B5594C904959 flot1-slc2a1-1 5 19 unspecified role unspecified role neutral component neutral component 9 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component 14 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 1, supp fig 1ii Proteins found in the 500 kDa band. 25345-2 1 19 unspecified role unspecified role prey prey 11 unspecified role unspecified role bait bait physical association physical association 1Ca stom-slc4a1-1 1 19 unspecified role unspecified role bait bait 11 unspecified role unspecified role prey prey physical association physical association 1Cb slc2a1-slc4a1-2 5 19 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 1, supp fig 1 Proteins found in the 130 kDa band. MS-analysis of these bands clearly revealed the presence of 3 major proteins: stomatin, glucose transporter-1 (GLUT1/SLC2A1), and the anion exchanger (band 3/AE1/SLC4A1) flot1-slc2a1-2 5 19 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 1, supp fig 1i Proteins found in the 300 kDa band. epb42-flot1-3 7 19 unspecified role unspecified role neutral component neutral component 18 unspecified role unspecified role neutral component neutral component 21 unspecified role unspecified role neutral component neutral component 12 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component 14 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure2, supp fig 2 proteins found in 500 kDa band slc2a1-slc4a1-3 7 19 unspecified role unspecified role neutral component neutral component 23 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 2, supp fig 2 proteins found in 300 kDa band bcam-flot1-1 7 19 unspecified role unspecified role neutral component neutral component 21 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure2, supp fig 2i proteins found in >500 kDa band aldoa-flot1-1 3 19 unspecified role unspecified role neutral component neutral component 22 unspecified role unspecified role neutral component neutral component 12 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component 17 unspecified role unspecified role neutral component neutral component 23 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 3D, supp fig 3 proteins found in both 300 and 500 kDa band aldoa-aqp1-1 6 19 unspecified role unspecified role neutral component neutral component 20 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 9 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 15 unspecified role unspecified role neutral component neutral component 27 unspecified role unspecified role neutral component neutral component 17 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4 proteins found in >500 kDa band (blue) aqp1-bcam-1 6 19 unspecified role unspecified role neutral component neutral component 20 unspecified role unspecified role neutral component neutral component 14 unspecified role unspecified role neutral component neutral component 8 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 15 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4i proteins found in 500 kDa band (brown) bcam-cd47-1 6 19 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4ii proteins found in 70 kDa band (green) flot1-flot2-7 6 19 unspecified role unspecified role neutral component neutral component 17 unspecified role unspecified role neutral component neutral component 8 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4iii proteins found in 65 kDa band (purple) aqp1-cd47-1 6 19 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component 17 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4iv proteins found in = 60 kDa band (medium blue) aqp1-cd47-2 2 19 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component association association Figure 5B-F slc2a1-slc4a1-4 4 19 unspecified role unspecified role neutral component neutral component 16 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component colocalization colocalization Figure 5A proteins from DRMs flot2-slc2a1-1 4 19 unspecified role unspecified role neutral component neutral component 24 unspecified role unspecified role neutral component neutral component 26 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component colocalization colocalization Figure 5A-2 proteins from non- DRMs aqp1-flot1-1 6 19 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component physical association physical association Figure 4, supp fig 4v proteins found in = 20 kDa band (pale blue) aqp1-flot1-2 6 19 unspecified role unspecified role neutral component neutral component 25 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component association association Figure 4, supp fig 4vi proteins found in = 30 kDa band (orange) slc2a1-slc4a1-1 2 19 unspecified role unspecified role neutral component neutral component 11 unspecified role unspecified role neutral component neutral component physical association physical association Figure 5B-Fi 800 kDa band