ID PSD12_HUMAN Reviewed; 456 AA. AC O00232; Q53HA2; Q6P053; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 07-JUL-2009, entry version 77. DE RecName: Full=26S proteasome non-ATPase regulatory subunit 12; DE AltName: Full=26S proteasome regulatory subunit p55; GN Name=PSMD12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98086225; PubMed=9426256; DOI=10.1016/S0378-1119(97)00524-6; RA Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., RA DeMartino G.N., Tanahashi N., Tanaka K.; RT "cDNA cloning and functional analysis of p44.5 and p55, two regulatory RT subunits of the 26S proteasome."; RL Gene 203:241-250(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [5] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human RT 26S proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [6] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which CC is involved in the ATP-dependent degradation of ubiquitinated CC proteins. CC -!- SUBUNIT: Component of the PA700 complex. CC -!- INTERACTION: CC Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-359733, EBI-1056358; CC O75832:PSMD10; NbExp=1; IntAct=EBI-359733, EBI-752185; CC Q15008:PSMD6; NbExp=1; IntAct=EBI-359733, EBI-359701; CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family. CC -!- SIMILARITY: Contains 1 PCI domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB003103; BAA19749.1; -; mRNA. DR EMBL; AK222679; BAD96399.1; -; mRNA. DR EMBL; BC019062; AAH19062.1; -; mRNA. DR EMBL; BC065826; AAH65826.1; ALT_INIT; mRNA. DR IPI; IPI00185374; -. DR PIR; PC6501; JC6523. DR RefSeq; NP_002807.1; -. DR UniGene; Hs.646575; -. DR DIP; DIP:27549N; -. DR IntAct; O00232; 9. DR PhosphoSite; O00232; -. DR PeptideAtlas; O00232; -. DR PRIDE; O00232; -. DR Ensembl; ENSG00000197170; Homo sapiens. DR GeneID; 5718; -. DR KEGG; hsa:5718; -. DR UCSC; uc002jfy.1; human. DR GeneCards; GC17M062764; -. DR H-InvDB; HIX0014093; -. DR HGNC; HGNC:9557; PSMD12. DR MIM; 604450; gene. DR PharmGKB; PA33903; -. DR HOGENOM; O00232; -. DR HOVERGEN; O00232; -. DR OMA; O00232; WDALNEN. DR Reactome; REACT_11045; Signaling by Wnt. DR Reactome; REACT_13; Metabolism of amino acids. DR Reactome; REACT_13635; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; REACT_152; Cell Cycle, Mitotic. DR Reactome; REACT_1538; Cell Cycle Checkpoints. DR Reactome; REACT_383; DNA Replication. DR Reactome; REACT_578; Apoptosis. DR Reactome; REACT_6185; HIV Infection. DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2. DR NextBio; 22216; -. DR ArrayExpress; O00232; -. DR Bgee; O00232; -. DR CleanEx; HS_PSMD12; -. DR GermOnline; ENSG00000197170; Homo sapiens. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW. DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome. DR GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome. DR GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome. DR InterPro; IPR000717; PCI. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; KW Polymorphism; Proteasome. FT INIT_MET 1 1 Removed. FT CHAIN 2 456 26S proteasome non-ATPase regulatory FT subunit 12. FT /FTId=PRO_0000173861. FT DOMAIN 237 417 PCI. FT MOD_RES 2 2 N-acetylalanine. FT VARIANT 358 358 V -> A (in dbSNP:rs2230680). FT /FTId=VAR_051558. FT CONFLICT 300 300 P -> S (in Ref. 2; BAD96399). FT CONFLICT 398 398 V -> D (in Ref. 2; BAD96399). SQ SEQUENCE 456 AA; 52904 MW; 97D0BDBDB0C96195 CRC64; MADGGSERAD GRIVKMEVDY SATVDQRLPE CAKLAKEGRL QEVIETLLSL EKQTRTASDM VSTSRILVAV VKMCYEAKEW DLLNENIMLL SKRRSQLKQA VAKMVQQCCT YVEEITDLPI KLRLIDTLRM VTEGKIYVEI ERARLTKTLA TIKEQNGDVK EAASILQELQ VETYGSMEKK ERVEFILEQM RLCLAVKDYI RTQIISKKIN TKFFQEENTE KLKLKYYNLM IQLDQHEGSY LSICKHYRAI YDTPCIQAES EKWQQALKSV VLYVILAPFD NEQSDLVHRI SGDKKLEEIP KYKDLLKLFT TMELMRWSTL VEDYGMELRK GSLESPATDV FGSTEEGEKR WKDLKNRVVE HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK TIFAKVDRLA GIINFQRPKD PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE MIHNLQ //