PSMF1_HUMAN
ID PSMF1_HUMAN Reviewed; 271 AA.
AC Q92530; A0AVQ9; D3DVW3; Q9H4I1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Proteasome inhibitor PI31 subunit;
DE Short=hPI31;
GN Name=PSMF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-36, FUNCTION, AND SUBUNIT.
RX PubMed=10764772; DOI=10.1074/jbc.m001697200;
RA McCutchen-Maloney S.L., Matsuda K., Shimbara N., Binns D.D., Tanaka K.,
RA Slaughter C.A., DeMartino G.N.;
RT "cDNA cloning, expression, and functional characterization of PI31, a
RT proline-rich inhibitor of the proteasome.";
RL J. Biol. Chem. 275:18557-18565(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-36.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-36.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-231, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-151, INTERACTION WITH FBXO7,
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF VAL-6; ILE-83 AND ILE-90.
RX PubMed=18495667; DOI=10.1074/jbc.m709900200;
RA Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M.,
RA Meziane E.K., McDonald N.Q.;
RT "Structure of a conserved dimerization domain within the F-box protein
RT Fbxo7 and the PI31 proteasome inhibitor.";
RL J. Biol. Chem. 283:22325-22335(2008).
CC -!- FUNCTION: Plays an important role in control of proteasome function.
CC Inhibits the hydrolysis of protein and peptide substrates by the 20S
CC proteasome. Also inhibits the activation of the proteasome by the
CC proteasome regulatory proteins PA700 and PA28.
CC {ECO:0000269|PubMed:10764772}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with FBXO7. Interacts with
CC the 20S proteasome. {ECO:0000269|PubMed:10764772,
CC ECO:0000269|PubMed:18495667}.
CC -!- INTERACTION:
CC Q92530; O95400: CD2BP2; NbExp=2; IntAct=EBI-945916, EBI-768015;
CC Q92530; Q9Y3I1: FBXO7; NbExp=9; IntAct=EBI-945916, EBI-1161222;
CC Q92530; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-945916, EBI-10226858;
CC Q92530; P54652: HSPA2; NbExp=3; IntAct=EBI-945916, EBI-356991;
CC Q92530; O95751: LDOC1; NbExp=3; IntAct=EBI-945916, EBI-740738;
CC Q92530; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-945916, EBI-739832;
CC Q92530; Q9P286: PAK5; NbExp=3; IntAct=EBI-945916, EBI-741896;
CC Q92530; Q14088: RAB33A; NbExp=3; IntAct=EBI-945916, EBI-744685;
CC Q92530; Q9NWB1: RBFOX1; NbExp=2; IntAct=EBI-945916, EBI-945906;
CC Q92530; Q96A09: TENT5B; NbExp=3; IntAct=EBI-945916, EBI-752030;
CC Q92530; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-945916, EBI-10259086;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18495667}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:18495667}.
CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC {ECO:0000305}.
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DR EMBL; D88378; BAA13603.1; -; mRNA.
DR EMBL; AL031665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10650.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10651.1; -; Genomic_DNA.
DR EMBL; BC126462; AAI26463.1; -; mRNA.
DR CCDS; CCDS13010.1; -.
DR RefSeq; NP_001310336.1; NM_001323407.1.
DR RefSeq; NP_006805.2; NM_006814.4.
DR RefSeq; NP_848693.2; NM_178578.3.
DR PDB; 2VT8; X-ray; 2.60 A; A/B=1-151.
DR PDB; 4OUH; X-ray; 2.00 A; A/B/C/D=1-158.
DR PDBsum; 2VT8; -.
DR PDBsum; 4OUH; -.
DR AlphaFoldDB; Q92530; -.
DR SMR; Q92530; -.
DR BioGRID; 114872; 88.
DR IntAct; Q92530; 51.
DR MINT; Q92530; -.
DR STRING; 9606.ENSP00000338039; -.
DR GlyGen; Q92530; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92530; -.
DR PhosphoSitePlus; Q92530; -.
DR SwissPalm; Q92530; -.
DR BioMuta; PSMF1; -.
DR DMDM; 134047876; -.
DR EPD; Q92530; -.
DR jPOST; Q92530; -.
DR MassIVE; Q92530; -.
DR MaxQB; Q92530; -.
DR PaxDb; Q92530; -.
DR PeptideAtlas; Q92530; -.
DR PRIDE; Q92530; -.
DR ProteomicsDB; 75291; -.
DR Antibodypedia; 23029; 288 antibodies from 36 providers.
DR DNASU; 9491; -.
DR Ensembl; ENST00000333082.7; ENSP00000327704.3; ENSG00000125818.18.
DR Ensembl; ENST00000335877.11; ENSP00000338039.6; ENSG00000125818.18.
DR GeneID; 9491; -.
DR KEGG; hsa:9491; -.
DR MANE-Select; ENST00000335877.11; ENSP00000338039.6; NM_006814.5; NP_006805.2.
DR UCSC; uc002wel.4; human.
DR CTD; 9491; -.
DR DisGeNET; 9491; -.
DR GeneCards; PSMF1; -.
DR HGNC; HGNC:9571; PSMF1.
DR HPA; ENSG00000125818; Low tissue specificity.
DR MIM; 617858; gene.
DR neXtProt; NX_Q92530; -.
DR OpenTargets; ENSG00000125818; -.
DR PharmGKB; PA33917; -.
DR VEuPathDB; HostDB:ENSG00000125818; -.
DR eggNOG; KOG4761; Eukaryota.
DR GeneTree; ENSGT00390000012257; -.
DR HOGENOM; CLU_090116_0_0_1; -.
DR InParanoid; Q92530; -.
DR OMA; NICVEPE; -.
DR OrthoDB; 1614691at2759; -.
DR PhylomeDB; Q92530; -.
DR TreeFam; TF106238; -.
DR PathwayCommons; Q92530; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q92530; -.
DR SIGNOR; Q92530; -.
DR BioGRID-ORCS; 9491; 95 hits in 1093 CRISPR screens.
DR ChiTaRS; PSMF1; human.
DR EvolutionaryTrace; Q92530; -.
DR GeneWiki; PSMF1; -.
DR GenomeRNAi; 9491; -.
DR Pharos; Q92530; Tbio.
DR PRO; PR:Q92530; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q92530; protein.
DR Bgee; ENSG00000125818; Expressed in sperm and 211 other tissues.
DR ExpressionAtlas; Q92530; baseline and differential.
DR Genevisible; Q92530; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005839; C:proteasome core complex; NAS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR InterPro; IPR045128; PI31-like.
DR InterPro; IPR013886; PI31_Prot_C.
DR InterPro; IPR021625; PI31_Prot_N.
DR PANTHER; PTHR13266; PTHR13266; 1.
DR Pfam; PF08577; PI31_Prot_C; 1.
DR Pfam; PF11566; PI31_Prot_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum; Methylation;
KW Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..271
FT /note="Proteasome inhibitor PI31 subunit"
FT /id="PRO_0000220920"
FT REGION 2..150
FT /note="Important for homodimerization and interaction with
FT FBXO7"
FT /evidence="ECO:0000269|PubMed:18495667"
FT REGION 222..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT MOD_RES 219
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL8"
FT MOD_RES 231
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VARIANT 36
FT /note="F -> C (in dbSNP:rs1803415)"
FT /evidence="ECO:0000269|PubMed:10764772,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_024564"
FT VARIANT 174
FT /note="H -> R (in dbSNP:rs2235587)"
FT /id="VAR_022153"
FT MUTAGEN 6
FT /note="V->R: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:18495667"
FT MUTAGEN 83
FT /note="I->E: Abolishes interaction with FBXO7, but has no
FT effect on homodimerization; when associated with E-90."
FT /evidence="ECO:0000269|PubMed:18495667"
FT MUTAGEN 90
FT /note="I->E: Abolishes interaction with FBXO7, but has no
FT effect on homodimerization; when associated with E-83."
FT /evidence="ECO:0000269|PubMed:18495667"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:4OUH"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4OUH"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 62..73
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:4OUH"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2VT8"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:4OUH"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4OUH"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:4OUH"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:4OUH"
SQ SEQUENCE 271 AA; 29817 MW; C669F8210AFAD727 CRC64;
MAGLEVLFAS AAPAITCRQD ALVCFLHWEV VTHGYFGLGV GDQPGPNDKK SELLPAGWNN
NKDLYVLRYE YKDGSRKLLV KAITVESSMI LNVLEYGSQQ VADLTLNLDD YIDAEHLGDF
HRTYKNSEEL RSRIVSGIIT PIHEQWEKAN VSSPHREFPP ATAREVDPLR IPPHHPHTSR
QPPWCDPLGP FVVGGEDLDP FGPRRGGMIV DPLRSGFPRA LIDPSSGLPN RLPPGAVPPG
ARFDPFGPIG TSPPGPNPDH LPPPGYDDMY L
