Full text data of PSMD12
PSMD12
[Confidence: high (present in two of the MS resources)]
26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5; 26S proteasome regulatory subunit p55)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5; 26S proteasome regulatory subunit p55)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00185374
IPI00185374 26S proteasome non-ATPase regulatory subunit 12 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00185374 26S proteasome non-ATPase regulatory subunit 12 The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
O00232
ID PSD12_HUMAN Reviewed; 456 AA.
AC O00232; A6NP15; Q53HA2; Q6P053;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 12;
DE AltName: Full=26S proteasome regulatory subunit RPN5;
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] (ISOFORM 1).
RX 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] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-368, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00232-2; Sequence=VSP_042718;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65826.1; Type=Erroneous initiation;
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DR EMBL; AB003103; BAA19749.1; -; mRNA.
DR EMBL; AK091198; BAG52303.1; -; mRNA.
DR EMBL; AK222679; BAD96399.1; -; mRNA.
DR EMBL; AC110921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89028.1; -; Genomic_DNA.
DR EMBL; BC019062; AAH19062.1; -; mRNA.
DR EMBL; BC065826; AAH65826.1; ALT_INIT; mRNA.
DR PIR; PC6501; JC6523.
DR RefSeq; NP_002807.1; NM_002816.3.
DR RefSeq; NP_777360.1; NM_174871.2.
DR UniGene; Hs.592689; -.
DR ProteinModelPortal; O00232; -.
DR SMR; O00232; 44-416.
DR DIP; DIP-27549N; -.
DR IntAct; O00232; 21.
DR MINT; MINT-5003729; -.
DR STRING; 9606.ENSP00000348442; -.
DR PhosphoSite; O00232; -.
DR PaxDb; O00232; -.
DR PeptideAtlas; O00232; -.
DR PRIDE; O00232; -.
DR DNASU; 5718; -.
DR Ensembl; ENST00000356126; ENSP00000348442; ENSG00000197170.
DR Ensembl; ENST00000357146; ENSP00000349667; ENSG00000197170.
DR GeneID; 5718; -.
DR KEGG; hsa:5718; -.
DR UCSC; uc002jfy.3; human.
DR CTD; 5718; -.
DR GeneCards; GC17M065334; -.
DR HGNC; HGNC:9557; PSMD12.
DR HPA; HPA023119; -.
DR MIM; 604450; gene.
DR neXtProt; NX_O00232; -.
DR PharmGKB; PA33903; -.
DR eggNOG; COG5071; -.
DR HOGENOM; HOG000194265; -.
DR HOVERGEN; HBG053739; -.
DR InParanoid; O00232; -.
DR KO; K03035; -.
DR OMA; WARIDRP; -.
DR OrthoDB; EOG7SJD4B; -.
DR PhylomeDB; O00232; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD12; -.
DR GenomeRNAi; 5718; -.
DR NextBio; 22216; -.
DR PRO; PR:O00232; -.
DR ArrayExpress; O00232; -.
DR Bgee; O00232; -.
DR CleanEx; HS_PSMD12; -.
DR Genevestigator; O00232; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Polymorphism; Proteasome;
KW Reference proteome.
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 MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 368 368 N6-acetyllysine.
FT VAR_SEQ 37 56 Missing (in isoform 2).
FT /FTId=VSP_042718.
FT VARIANT 358 358 V -> A (in dbSNP:rs2230680).
FT /FTId=VAR_051558.
FT CONFLICT 300 300 P -> S (in Ref. 3; BAD96399).
FT CONFLICT 398 398 V -> D (in Ref. 3; 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
//
ID PSD12_HUMAN Reviewed; 456 AA.
AC O00232; A6NP15; Q53HA2; Q6P053;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 12;
DE AltName: Full=26S proteasome regulatory subunit RPN5;
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] (ISOFORM 1).
RX 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] (ISOFORM 2).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-368, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00232-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00232-2; Sequence=VSP_042718;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC -!- SIMILARITY: Contains 1 PCI domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65826.1; Type=Erroneous initiation;
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DR EMBL; AB003103; BAA19749.1; -; mRNA.
DR EMBL; AK091198; BAG52303.1; -; mRNA.
DR EMBL; AK222679; BAD96399.1; -; mRNA.
DR EMBL; AC110921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89028.1; -; Genomic_DNA.
DR EMBL; BC019062; AAH19062.1; -; mRNA.
DR EMBL; BC065826; AAH65826.1; ALT_INIT; mRNA.
DR PIR; PC6501; JC6523.
DR RefSeq; NP_002807.1; NM_002816.3.
DR RefSeq; NP_777360.1; NM_174871.2.
DR UniGene; Hs.592689; -.
DR ProteinModelPortal; O00232; -.
DR SMR; O00232; 44-416.
DR DIP; DIP-27549N; -.
DR IntAct; O00232; 21.
DR MINT; MINT-5003729; -.
DR STRING; 9606.ENSP00000348442; -.
DR PhosphoSite; O00232; -.
DR PaxDb; O00232; -.
DR PeptideAtlas; O00232; -.
DR PRIDE; O00232; -.
DR DNASU; 5718; -.
DR Ensembl; ENST00000356126; ENSP00000348442; ENSG00000197170.
DR Ensembl; ENST00000357146; ENSP00000349667; ENSG00000197170.
DR GeneID; 5718; -.
DR KEGG; hsa:5718; -.
DR UCSC; uc002jfy.3; human.
DR CTD; 5718; -.
DR GeneCards; GC17M065334; -.
DR HGNC; HGNC:9557; PSMD12.
DR HPA; HPA023119; -.
DR MIM; 604450; gene.
DR neXtProt; NX_O00232; -.
DR PharmGKB; PA33903; -.
DR eggNOG; COG5071; -.
DR HOGENOM; HOG000194265; -.
DR HOVERGEN; HBG053739; -.
DR InParanoid; O00232; -.
DR KO; K03035; -.
DR OMA; WARIDRP; -.
DR OrthoDB; EOG7SJD4B; -.
DR PhylomeDB; O00232; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13505; Proteasome mediated degradation of PAK-2p34.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_383; DNA Replication.
DR Reactome; REACT_578; Apoptosis.
DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; PSMD12; -.
DR GenomeRNAi; 5718; -.
DR NextBio; 22216; -.
DR PRO; PR:O00232; -.
DR ArrayExpress; O00232; -.
DR Bgee; O00232; -.
DR CleanEx; HS_PSMD12; -.
DR Genevestigator; O00232; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Polymorphism; Proteasome;
KW Reference proteome.
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 MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 368 368 N6-acetyllysine.
FT VAR_SEQ 37 56 Missing (in isoform 2).
FT /FTId=VSP_042718.
FT VARIANT 358 358 V -> A (in dbSNP:rs2230680).
FT /FTId=VAR_051558.
FT CONFLICT 300 300 P -> S (in Ref. 3; BAD96399).
FT CONFLICT 398 398 V -> D (in Ref. 3; 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
//
MIM
604450
*RECORD*
*FIELD* NO
604450
*FIELD* TI
*604450 PROTEASOME 26S SUBUNIT, NON-ATPase, 12; PSMD12
;;p55
*FIELD* TX
The 26S proteasome is responsible for the ATP-dependent degradation of a
read morevariety of cellular proteins. Selective breakdown of these proteins is
mediated by the ubiquitin pathway. The 26S proteasome is a 2,000-kD
protein complex composed of the 20S proteasome, which is the catalytic
subcomplex, and PA700, which is the regulatory subcomplex. The
approximately 700-kD PA700 complex consists of approximately 20
heterogeneous proteins ranging from 25 to 112 kD. These subunits can be
divided into 2 classes, those that are members of the AAA (ATPases
associated with various cellular activities) family and those that are
not.
Saito et al. (1997) sequenced peptides from the p55 subunit of the
bovine PA700 complex. They identified a human EST encoding a homologous
protein and used this EST to isolate hepatoblastoma HepG2 cell cDNAs
encoding human p55, also called PSMD12. The deduced 456-amino acid
PSMD12 protein has a calculated molecular mass of 52,903 Da. The authors
identified a putative S. cerevisiae homolog, which they named NAS5, that
shares 41.1% amino acid sequence identity with PSMD12. Disruption of the
NAS5 gene resulted in lethality.
*FIELD* RF
1. Saito, A.; Watanabe, T. K.; Shimada, Y.; Fujiwara, T.; Slaughter,
C. A.; DeMartino, G. N.; Tanahashi, N.; Tanaka, K.: cDNA cloning
and functional analysis of p44.5 and p55, two regulatory subunits
of the 26S proteasome. Gene 203: 241-250, 1997.
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
mgross: 01/21/2000
psherman: 1/20/2000
*RECORD*
*FIELD* NO
604450
*FIELD* TI
*604450 PROTEASOME 26S SUBUNIT, NON-ATPase, 12; PSMD12
;;p55
*FIELD* TX
The 26S proteasome is responsible for the ATP-dependent degradation of a
read morevariety of cellular proteins. Selective breakdown of these proteins is
mediated by the ubiquitin pathway. The 26S proteasome is a 2,000-kD
protein complex composed of the 20S proteasome, which is the catalytic
subcomplex, and PA700, which is the regulatory subcomplex. The
approximately 700-kD PA700 complex consists of approximately 20
heterogeneous proteins ranging from 25 to 112 kD. These subunits can be
divided into 2 classes, those that are members of the AAA (ATPases
associated with various cellular activities) family and those that are
not.
Saito et al. (1997) sequenced peptides from the p55 subunit of the
bovine PA700 complex. They identified a human EST encoding a homologous
protein and used this EST to isolate hepatoblastoma HepG2 cell cDNAs
encoding human p55, also called PSMD12. The deduced 456-amino acid
PSMD12 protein has a calculated molecular mass of 52,903 Da. The authors
identified a putative S. cerevisiae homolog, which they named NAS5, that
shares 41.1% amino acid sequence identity with PSMD12. Disruption of the
NAS5 gene resulted in lethality.
*FIELD* RF
1. Saito, A.; Watanabe, T. K.; Shimada, Y.; Fujiwara, T.; Slaughter,
C. A.; DeMartino, G. N.; Tanahashi, N.; Tanaka, K.: cDNA cloning
and functional analysis of p44.5 and p55, two regulatory subunits
of the 26S proteasome. Gene 203: 241-250, 1997.
*FIELD* CD
Patti M. Sherman: 1/20/2000
*FIELD* ED
mgross: 01/21/2000
psherman: 1/20/2000