UniProt UniProt http://www.uniprot.org Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13. Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13. The Journal of biological chemistry 2019 imex curation Hemmis CW., Heard SC., Hill CP. chris@biochem.utah.edu 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hemmis CW., Heard SC., Hill CP. Ubiquitin was mapped to the UBC gene from the Addgene contruct. chris@biochem.utah.edu Accepted 2020-FEB-17 AT 11:46 GMT AT 11:46 GMT by MGT The Journal of biological chemistry 2019 Only protein-protein interactions imex curation imex curation Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13. Phosphorylation of Tyr-950 in the proteasome scaffolding protein RPN2 modulates its interaction with the ubiquitin receptor RPN13. The Journal of biological chemistry 2019 imex curation Hemmis CW., Heard SC., Hill CP. chris@biochem.utah.edu 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps tag fluorescence tag visualisation by fluorescence tag fluorescence Hemmis CW., Heard SC., Hill CP. Table 2 - in each case I've taken the top line (phosphorylated or not phosphorylated as the 'wild-type' and compared mutants with that. The way the authors did it I think was too complicated for our data model chris@biochem.utah.edu Accepted 2020-FEB-17 AT 11:46 GMT AT 11:46 GMT by MGT The Journal of biological chemistry 2019 Only protein-protein interactions imex curation imex curation ubc_human Polyubiquitin-C UBC protein protein human Homo sapiens Human MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGV B6E7BC06FEE77196 psmd1_human 26S proteasome non-ATPase regulatory subunit 1 PSMD1 26S proteasome regulatory subunit RPN2 26S proteasome regulatory subunit S1 26S proteasome subunit p112 protein protein human Homo sapiens Human MITSAAGIISLLDEDEPQLKEFALHKLNAVVNDFWAEISESVDKIEVLYEDEGFRSRQFAALVASKVFYHLGAFEESLNYALGAGDLFNVNDNSEYVETIIAKCIDHYTKQCVENADLPEGEKKPIDQRLEGIVNKMFQRCLDDHKYKQAIGIALETRRLDVFEKTILESNDVPGMLAYSLKLCMSLMQNKQFRNKVLRVLVKIYMNLEKPDFINVCQCLIFLDDPQAVSDILEKLVKEDNLLMAYQICFDLYESASQQFLSSVIQNLRTVGTPIASVPGSTNTGTVPGSEKDSDSMETEEKTSSAFVGKTPEASPEPKDQTLKMIKILSGEMAIELHLQFLIRNNNTDLMILKNTKDAVRNSVCHTATVIANSFMHCGTTSDQFLRDNLEWLARATNWAKFTATASLGVIHKGHEKEALQLMATYLPKDTSPGSAYQEGGGLYALGLIHANHGGDIIDYLLNQLKNASNDIVRHGGSLGLGLAAMGTARQDVYDLLKTNLYQDDAVTGEAAGLALGLVMLGSKNAQAIEDMVGYAQETQHEKILRGLAVGIALVMYGRMEEADALIESLCRDKDPILRRSGMYTVAMAYCGSGNNKAIRRLLHVAVSDVNDDVRRAAVESLGFILFRTPEQCPSVVSLLSESYNPHVRYGAAMALGICCAGTGNKEAINLLEPMTNDPVNYVRQGALIASALIMIQQTEITCPKVNQFRQLYSKVINDKHDDVMAKFGAILAQGILDAGGHNVTISLQSRTGHTHMPSVVGVLVFTQFWFWFPLSHFLSLAYTPTCVIGLNKDLKMPKVQYKSNCKPSTFAYPAPLEVPKEKEKEKVSTAVLSITAKAKKKEKEKEKKEEEKMEVDEAEKKEEKEKKKEPEPNFQLLDNPARVMPAQLKVLTMPETCRYQPFKPLSIGGIIILKDTSEDIEELVEPVAAHGPKIEEEEQEPEPPEPFEYIDD B8682146082D21FA adrm1_human Proteasomal ubiquitin receptor ADRM1 Adhesion-regulating molecule 1 110 kDa cell membrane glycoprotein Rpn13 homolog Proteasome regulatory particle non-ATPase 13 ADRM1 GP110 protein protein human Homo sapiens Human MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD DIP protein Q16186 original sequence version: 116 DIP protein Q16186 original sequence version: 93 2D38811DCA231864 adrm1-psmd1-2 2 5 unspecified role unspecified role neutral component neutral component purified purified pru domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component tyr-950 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain increasing-ptm ptm increasing an interaction increasing-ptm region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c-terminal fluorescein fluorescein label fluorescein c-term range C-terminal range c-term range c-term range C-terminal range c-term range chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Fig. 1 The RPN2940–952–RPN13PRU binding interaction was quantified using fluorescence polarization (FP) assays. adrm1-psmd1-3 1 5 unspecified role unspecified role neutral component neutral component purified purified pru domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component tyr-950 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association Table 1 adrm1-psmd1-4 2 4 unspecified role unspecified role neutral component neutral component tyr-950 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain observed-ptm observed-ptm observed ptm observed-ptm region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c-terminal fluorescein fluorescein label fluorescein c-term range C-terminal range c-term range c-term range C-terminal range c-term range chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component purified purified pru domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q16186:p.Arg104Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R E Tue Jun 30 17:14:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Glu' Q16186:p.Lys83Ala mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K A Tue Jun 30 19:03:07 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys83Ala' Q16186:p.Lys97Ala mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K A Tue Jun 30 20:06:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Ala' Q16186:p.Lys97Asp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K D Tue Jun 30 16:24:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Asp' Q16186:p.Lys97Glu mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain K E Tue Jun 30 19:44:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Glu' Q16186:p.Arg104Ala mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R A Tue Jun 30 18:29:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Ala' Q16186:p.Arg104Asp mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength certain certain sequence position certain certain certain sequence position certain R D Tue Jun 30 16:04:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Asp' ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 2 The RPN2940–952–RPN13PRU binding interaction was quantified using fluorescence polarization (FP) assays. adrm1-psmd1-5 2 4 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c-terminal fluorescein fluorescein label fluorescein c-term range C-terminal range c-term range c-term range C-terminal range c-term range chemical synthesis Chemical synthesis (Chemical synthesis) 5 unspecified role unspecified role neutral component neutral component purified purified pru domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q16186:p.Arg104Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R E Tue Jun 30 15:59:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Glu' Q16186:p.Lys83Ala mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain K A Tue Jun 30 16:50:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys83Ala' Q16186:p.Lys97Ala mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K A Tue Jun 30 19:41:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Ala' Q16186:p.Lys97Asp mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K D Tue Jun 30 18:37:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Asp' Q16186:p.Lys97Glu mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain K E Tue Jun 30 20:22:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys97Glu' Q16186:p.Arg104Ala mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R A Tue Jun 30 19:57:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Ala' Q16186:p.Arg104Asp mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain R D Tue Jun 30 20:15:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg104Asp' ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 2 The RPN2940–952–RPN13PRU binding interaction was quantified using fluorescence polarization (FP) assays.