matrixdb Institut de Biologie et de Chimie des Prot\u00c3\u00a9ines, 7, passage du Vercors 69 367 Lyon cedex 07 FRANCE matrixdb@ibcp.fr http://matrixdb.ibcp.fr Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. Biochem. J. (0264-6021) 2006 imex curation Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Accepted 2016-JUN-23 AT 08:58 BST AT 08:58 BST by ORCHARD Biochem. J. (0264-6021) 2006 Only protein-protein interactions imex curation The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. Biochem. J. (0264-6021) 2006 imex curation Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Only protein-protein interactions crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Accepted 2016-JUN-23 AT 08:58 BST AT 08:58 BST by ORCHARD Biochem. J. (0264-6021) 2006 Only protein-protein interactions imex curation The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro. Biochem. J. (0264-6021) 2006 imex curation Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Only protein-protein interactions in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy antibody detection identification by antibody antibody detection Väisänen M.R., Väisänen T., Tu H., Pirilä P., Sormunen R., Pihlajaniemi T. taina.pihlajaniemi@oulu.fi Accepted 2016-JUN-23 AT 08:58 BST AT 08:58 BST by ORCHARD Biochem. J. (0264-6021) 2006 Only protein-protein interactions imex curation coda1_human Collagen alpha-1(XIII) chain COL13A1 COLXIIIA1 protein protein human Homo sapiens Human MVAERTHKAAATGARGPGELGAPGTVALVAARAERGARLPSPGSCGLLTLALCSLALSLLAHFRTAELQARVLRLEAERGEQQMETAILGRVNQLLDEKWKLHSRRRREAPKTSPGCNCPPGPPGPTGRPGLPGDKGAIGMPGRVGSPGDAGLSIIGPRGPPGQPGTRGFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEYPHRECLSSMPAALRSSQIIALKLLPLLNSVRLAPPPVIKRRTFQGEQSQASIQGPPGPPGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAGNSIGGGRGEPGPPGLPGPPGPKGEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEIRTLALMGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGHPGSPGEKGEKGETGQAGSPGEKGEAGEKGNPGAEVPGLPGPEGPPGPPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGASGLDGRPGPPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDGLPVQGCWNK FD12CA80CC93540F finc_human Fibronectin FN1 FN Cold-insoluble globulin protein protein human Homo sapiens Human MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE DIP protein P02751 original sequence version: 119 DIP protein P02751 original sequence version: 131 DIP protein P02751 original sequence version: 154 DIP protein P02751 original sequence version: 156 DIP protein P02751 original sequence version: 157 DIP protein P02751 original sequence version: 155 DIP protein P02751 original sequence version: 194 6C436A7A5FEE6DEB collagen-fn1-1 3 6 unspecified role unspecified role neutral component neutral component human-plasma homo sapiens blood plasma plasma blood plasma 10 unspecified role unspecified role neutral component neutral component nucl transfection nucleic acid transfection nucl transfection tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag exp feature detect experimental feature detection exp feature detect c-term range C-terminal range c-term range c-term range C-terminal range c-term range binding site sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain colocalization colocalization Figure 3 delNC4 variant of collagen XIII showed a markedly reduced associationwith the fibronectin matrix collagen-fn1-5 4 6 unspecified role unspecified role neutral component neutral component human-plasma homo sapiens blood plasma plasma blood plasma 10 unspecified role unspecified role neutral component neutral component binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain colocalization colocalization Figure 1 collagen-fn1-3 2 10 unspecified role unspecified role bait bait binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag predetermined featur predetermined feature predetermined featur c-term range C-terminal range c-term range c-term range C-terminal range c-term range 6 unspecified role unspecified role prey prey binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain human-plasma homo sapiens blood plasma plasma blood plasma direct interaction direct interaction Figure 5 collagen_xiii_human Type XIII collagen Collagen type XIII trimer Type XIII collagen COL13A1 trimer 5 unspecified role unspecified role direct interaction direct interaction human Homo sapiens Human stable complex stable complex biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion biological system reconstruction evidence based on inference from background scientific knowledge used in manual assertion Nonfibrillar collagen that has been detected at low levels in all connective tissue-producing cells so may serve a general function in connective tissues. Collagen XIII contains a transmembrane domain and the protein has been localized to the plasma membrane. Binds heparin. Homotrimer. Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the centre of the superhelix. created with intact-jami-dbscripts