Full text data of PSMA1
PSMA1
(HC2, NU, PROS30, PSC2)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-1; 3.4.25.1 (30 kDa prosomal protein; PROS-30; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome component C2; Proteasome nu chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-1; 3.4.25.1 (30 kDa prosomal protein; PROS-30; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome component C2; Proteasome nu chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00016832
IPI00016832 Splice Isoform 1 Of Proteasome subunit Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation 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 Isoform 1 or 2 found at its expected molecular weight found at molecular weight
IPI00016832 Splice Isoform 1 Of Proteasome subunit Cleavage of peptide bonds with very broad specificity, proteasome: 15 subunits, C3 regulatory effect through tyrosine phosphorilation 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 Isoform 1 or 2 found at its expected molecular weight found at molecular weight
UniProt
P25786
ID PSA1_HUMAN Reviewed; 263 AA.
AC P25786; A8K400; Q53YE8; Q9BRV9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 1.
DT 22-JAN-2014, entry version 162.
DE RecName: Full=Proteasome subunit alpha type-1;
DE EC=3.4.25.1;
DE AltName: Full=30 kDa prosomal protein;
DE Short=PROS-30;
DE AltName: Full=Macropain subunit C2;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE AltName: Full=Proteasome component C2;
DE AltName: Full=Proteasome nu chain;
GN Name=PSMA1; Synonyms=HC2, NU, PROS30, PSC2;
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 SHORT).
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=1398136; DOI=10.1016/0378-1119(92)90098-A;
RA Silva-Pereira I., Bey F., Coux O., Scherrer K.;
RT "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human
RT prosomes.";
RL Gene 120:235-242(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-37.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT
RP VAL-37.
RC TISSUE=Bone marrow, Brain, Ovary, Placenta, and Prostate;
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 [8]
RP PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 63-82.
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [10]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=17127214; DOI=10.1016/S1672-0229(06)60029-6;
RA Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.;
RT "Comparative proteome analysis of breast cancer and adjacent normal
RT breast tissues in human.";
RL Genomics Proteomics Bioinformatics 4:165-172(2006).
RN [11]
RP INDUCTION.
RX PubMed=16317774; DOI=10.1002/pmic.200500218;
RA Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA Zhang X., Yang X.;
RT "The up-regulation of proteasome subunits and lysosomal proteases in
RT hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL Proteomics 6:498-504(2006).
RN [12]
RP INTERACTION WITH NOTCH3.
RX PubMed=17292860; DOI=10.1016/j.bbrc.2007.01.151;
RA Zhang Y., Jia L., Lee S.J., Wang M.M.;
RT "Conserved signal peptide of Notch3 inhibits interaction with
RT proteasome.";
RL Biochem. Biophys. Res. Commun. 355:245-251(2007).
RN [13]
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 [14]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
RA Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
RA Yang H.;
RT "Over-expression of genes and proteins of ubiquitin specific
RT peptidases (USPs) and proteasome subunits (PSs) in breast cancer
RT tissue observed by the methods of RFDD-PCR and proteomics.";
RL Breast Cancer Res. Treat. 104:21-30(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. Mediates the lipopolysaccharide-induced signal
CC transduction in the macrophage proteasome (By similarity). Might
CC be involved in the anti-inflammatory response of macrophages
CC during the interaction with C.albicans heat-inactivated cells (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with bacterial
CC lipopolysaccharide (LPS) (By similarity). Interacts with NOTCH3.
CC -!- INTERACTION:
CC Q5JR59:MTUS2; NbExp=3; IntAct=EBI-359352, EBI-742948;
CC P25787:PSMA2; NbExp=5; IntAct=EBI-359352, EBI-603262;
CC P25788:PSMA3; NbExp=3; IntAct=EBI-359352, EBI-348380;
CC P25789:PSMA4; NbExp=3; IntAct=EBI-359352, EBI-359310;
CC O14818:PSMA7; NbExp=9; IntAct=EBI-359352, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Short;
CC IsoId=P25786-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=P25786-2; Sequence=VSP_005279;
CC -!- INDUCTION: Induced in breast cancer tissue (at protein level). Up-
CC regulated in liver tumor tissues.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X61969; CAA43961.1; -; mRNA.
DR EMBL; D00759; BAA00656.1; -; mRNA.
DR EMBL; M64992; AAA92734.1; -; mRNA.
DR EMBL; BT006647; AAP35293.1; -; mRNA.
DR EMBL; AK290765; BAF83454.1; -; mRNA.
DR EMBL; CH471064; EAW68479.1; -; Genomic_DNA.
DR EMBL; BC002577; AAH02577.1; -; mRNA.
DR EMBL; BC005932; AAH05932.1; -; mRNA.
DR EMBL; BC008472; AAH08472.1; -; mRNA.
DR EMBL; BC009576; AAH09576.1; -; mRNA.
DR EMBL; BC015105; AAH15105.1; -; mRNA.
DR EMBL; BC015356; AAH15356.1; -; mRNA.
DR EMBL; BC022372; AAH22372.1; -; mRNA.
DR PIR; JC1445; JC1445.
DR RefSeq; NP_002777.1; NM_002786.3.
DR RefSeq; NP_683877.1; NM_148976.2.
DR UniGene; Hs.102798; -.
DR ProteinModelPortal; P25786; -.
DR SMR; P25786; 4-241.
DR DIP; DIP-29369N; -.
DR IntAct; P25786; 54.
DR MINT; MINT-1155600; -.
DR STRING; 9606.ENSP00000315309; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.976; -.
DR PhosphoSite; P25786; -.
DR DMDM; 130848; -.
DR OGP; P25786; -.
DR REPRODUCTION-2DPAGE; IPI00016832; -.
DR PaxDb; P25786; -.
DR PRIDE; P25786; -.
DR DNASU; 5682; -.
DR Ensembl; ENST00000396393; ENSP00000379675; ENSG00000129084.
DR Ensembl; ENST00000396394; ENSP00000379676; ENSG00000129084.
DR Ensembl; ENST00000418988; ENSP00000414359; ENSG00000129084.
DR GeneID; 5682; -.
DR KEGG; hsa:5682; -.
DR UCSC; uc001mlk.3; human.
DR CTD; 5682; -.
DR GeneCards; GC11M014526; -.
DR HGNC; HGNC:9530; PSMA1.
DR HPA; HPA037646; -.
DR MIM; 602854; gene.
DR neXtProt; NX_P25786; -.
DR PharmGKB; PA33875; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091080; -.
DR HOVERGEN; HBG105373; -.
DR KO; K02725; -.
DR OMA; FMKQQCL; -.
DR OrthoDB; EOG7WQ7T1; -.
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 ChiTaRS; PSMA1; human.
DR GeneWiki; Proteasome_(prosome,_macropain)_subunit,_alpha_1; -.
DR GenomeRNAi; 5682; -.
DR NextBio; 22062; -.
DR PRO; PR:P25786; -.
DR ArrayExpress; P25786; -.
DR Bgee; P25786; -.
DR CleanEx; HS_PSMA1; -.
DR Genevestigator; P25786; -.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005844; C:polysome; TAS:ProtInc.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
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 InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR023332; Proteasome_suA-type.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Ubl conjugation.
FT CHAIN 1 263 Proteasome subunit alpha type-1.
FT /FTId=PRO_0000124060.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT CARBOHYD 110 110 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 1 M -> MQLSKVK (in isoform Long).
FT /FTId=VSP_005279.
FT VARIANT 37 37 G -> V (in dbSNP:rs17850016).
FT /FTId=VAR_067454.
FT CONFLICT 14 15 SP -> TA (in Ref. 3; AAA92734).
SQ SEQUENCE 263 AA; 29556 MW; 3F159C5BCEFE8DED CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP
QRKAQPAQPA DEPAEKADEP MEH
//
ID PSA1_HUMAN Reviewed; 263 AA.
AC P25786; A8K400; Q53YE8; Q9BRV9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1992, sequence version 1.
DT 22-JAN-2014, entry version 162.
DE RecName: Full=Proteasome subunit alpha type-1;
DE EC=3.4.25.1;
DE AltName: Full=30 kDa prosomal protein;
DE Short=PROS-30;
DE AltName: Full=Macropain subunit C2;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE AltName: Full=Proteasome component C2;
DE AltName: Full=Proteasome nu chain;
GN Name=PSMA1; Synonyms=HC2, NU, PROS30, PSC2;
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 SHORT).
RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
RA Moomaw C.R., Dawson P.A., Slaughter C.A.;
RT "The primary structures of four subunits of the human, high-molecular-
RT weight proteinase, macropain (proteasome), are distinct but
RT homologous.";
RL Biochim. Biophys. Acta 1079:29-38(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
RA Tanaka K., Ichihara A.;
RT "Molecular cloning and sequence analysis of cDNAs for five major
RT subunits of human proteasomes (multi-catalytic proteinase
RT complexes).";
RL Biochim. Biophys. Acta 1089:95-102(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=1398136; DOI=10.1016/0378-1119(92)90098-A;
RA Silva-Pereira I., Bey F., Coux O., Scherrer K.;
RT "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human
RT prosomes.";
RL Gene 120:235-242(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-37.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT
RP VAL-37.
RC TISSUE=Bone marrow, Brain, Ovary, Placenta, and Prostate;
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 [8]
RP PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 63-82.
RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT "Human proteasome subunits from 2-dimensional gels identified by
RT partial sequencing.";
RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN [10]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=17127214; DOI=10.1016/S1672-0229(06)60029-6;
RA Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.;
RT "Comparative proteome analysis of breast cancer and adjacent normal
RT breast tissues in human.";
RL Genomics Proteomics Bioinformatics 4:165-172(2006).
RN [11]
RP INDUCTION.
RX PubMed=16317774; DOI=10.1002/pmic.200500218;
RA Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA Zhang X., Yang X.;
RT "The up-regulation of proteasome subunits and lysosomal proteases in
RT hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL Proteomics 6:498-504(2006).
RN [12]
RP INTERACTION WITH NOTCH3.
RX PubMed=17292860; DOI=10.1016/j.bbrc.2007.01.151;
RA Zhang Y., Jia L., Lee S.J., Wang M.M.;
RT "Conserved signal peptide of Notch3 inhibits interaction with
RT proteasome.";
RL Biochem. Biophys. Res. Commun. 355:245-251(2007).
RN [13]
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 [14]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
RA Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
RA Yang H.;
RT "Over-expression of genes and proteins of ubiquitin specific
RT peptidases (USPs) and proteasome subunits (PSs) in breast cancer
RT tissue observed by the methods of RFDD-PCR and proteomics.";
RL Breast Cancer Res. Treat. 104:21-30(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC which is characterized by its ability to cleave peptides with Arg,
CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. Mediates the lipopolysaccharide-induced signal
CC transduction in the macrophage proteasome (By similarity). Might
CC be involved in the anti-inflammatory response of macrophages
CC during the interaction with C.albicans heat-inactivated cells (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC specificity.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC two 19S regulatory subunits. The 20S proteasome core is composed
CC of 28 subunits that are arranged in four stacked rings, resulting
CC in a barrel-shaped structure. The two end rings are each formed by
CC seven alpha subunits, and the two central rings are each formed by
CC seven beta subunits. The catalytic chamber with the active sites
CC is on the inside of the barrel. Interacts with bacterial
CC lipopolysaccharide (LPS) (By similarity). Interacts with NOTCH3.
CC -!- INTERACTION:
CC Q5JR59:MTUS2; NbExp=3; IntAct=EBI-359352, EBI-742948;
CC P25787:PSMA2; NbExp=5; IntAct=EBI-359352, EBI-603262;
CC P25788:PSMA3; NbExp=3; IntAct=EBI-359352, EBI-348380;
CC P25789:PSMA4; NbExp=3; IntAct=EBI-359352, EBI-359310;
CC O14818:PSMA7; NbExp=9; IntAct=EBI-359352, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Short;
CC IsoId=P25786-1; Sequence=Displayed;
CC Name=Long;
CC IsoId=P25786-2; Sequence=VSP_005279;
CC -!- INDUCTION: Induced in breast cancer tissue (at protein level). Up-
CC regulated in liver tumor tissues.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X61969; CAA43961.1; -; mRNA.
DR EMBL; D00759; BAA00656.1; -; mRNA.
DR EMBL; M64992; AAA92734.1; -; mRNA.
DR EMBL; BT006647; AAP35293.1; -; mRNA.
DR EMBL; AK290765; BAF83454.1; -; mRNA.
DR EMBL; CH471064; EAW68479.1; -; Genomic_DNA.
DR EMBL; BC002577; AAH02577.1; -; mRNA.
DR EMBL; BC005932; AAH05932.1; -; mRNA.
DR EMBL; BC008472; AAH08472.1; -; mRNA.
DR EMBL; BC009576; AAH09576.1; -; mRNA.
DR EMBL; BC015105; AAH15105.1; -; mRNA.
DR EMBL; BC015356; AAH15356.1; -; mRNA.
DR EMBL; BC022372; AAH22372.1; -; mRNA.
DR PIR; JC1445; JC1445.
DR RefSeq; NP_002777.1; NM_002786.3.
DR RefSeq; NP_683877.1; NM_148976.2.
DR UniGene; Hs.102798; -.
DR ProteinModelPortal; P25786; -.
DR SMR; P25786; 4-241.
DR DIP; DIP-29369N; -.
DR IntAct; P25786; 54.
DR MINT; MINT-1155600; -.
DR STRING; 9606.ENSP00000315309; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.976; -.
DR PhosphoSite; P25786; -.
DR DMDM; 130848; -.
DR OGP; P25786; -.
DR REPRODUCTION-2DPAGE; IPI00016832; -.
DR PaxDb; P25786; -.
DR PRIDE; P25786; -.
DR DNASU; 5682; -.
DR Ensembl; ENST00000396393; ENSP00000379675; ENSG00000129084.
DR Ensembl; ENST00000396394; ENSP00000379676; ENSG00000129084.
DR Ensembl; ENST00000418988; ENSP00000414359; ENSG00000129084.
DR GeneID; 5682; -.
DR KEGG; hsa:5682; -.
DR UCSC; uc001mlk.3; human.
DR CTD; 5682; -.
DR GeneCards; GC11M014526; -.
DR HGNC; HGNC:9530; PSMA1.
DR HPA; HPA037646; -.
DR MIM; 602854; gene.
DR neXtProt; NX_P25786; -.
DR PharmGKB; PA33875; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091080; -.
DR HOVERGEN; HBG105373; -.
DR KO; K02725; -.
DR OMA; FMKQQCL; -.
DR OrthoDB; EOG7WQ7T1; -.
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 ChiTaRS; PSMA1; human.
DR GeneWiki; Proteasome_(prosome,_macropain)_subunit,_alpha_1; -.
DR GenomeRNAi; 5682; -.
DR NextBio; 22062; -.
DR PRO; PR:P25786; -.
DR ArrayExpress; P25786; -.
DR Bgee; P25786; -.
DR CleanEx; HS_PSMA1; -.
DR Genevestigator; P25786; -.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005844; C:polysome; TAS:ProtInc.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
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:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
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 InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR023332; Proteasome_suA-type.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Immunity;
KW Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Protease;
KW Proteasome; Reference proteome; Threonine protease; Ubl conjugation.
FT CHAIN 1 263 Proteasome subunit alpha type-1.
FT /FTId=PRO_0000124060.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT CARBOHYD 110 110 O-linked (GlcNAc) (By similarity).
FT CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 1 M -> MQLSKVK (in isoform Long).
FT /FTId=VSP_005279.
FT VARIANT 37 37 G -> V (in dbSNP:rs17850016).
FT /FTId=VAR_067454.
FT CONFLICT 14 15 SP -> TA (in Ref. 3; AAA92734).
SQ SEQUENCE 263 AA; 29556 MW; 3F159C5BCEFE8DED CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP
QRKAQPAQPA DEPAEKADEP MEH
//
MIM
602854
*RECORD*
*FIELD* NO
602854
*FIELD* TI
*602854 PROTEASOME SUBUNIT, ALPHA-TYPE, 1; PSMA1
;;PROTEASOME SUBUNIT NU;;
HC2;;
PROS30
read more*FIELD* TX
DeMartino et al. (1991) cloned the PSMA1 gene, termed 'subunit nu' by
them. The cDNA encoded a 263-amino acid polypeptide. The calculated and
observed molecular masses are 29.5 kD and 35 kD, respectively. Northern
blot analysis revealed an 1.4-kb mRNA in human placenta and HeLa cells.
Coux et al. (1996) noted that 2 proteins, HC2 (29.5 kD) and Pros30 (30.2
kD), are encoded by the PSMA1 gene.
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The alpha subunits comprise the outer rings of the
proteasome. Some alpha subunits contain a functional nuclear
localization signal; proteasomes are found in both the nuclear and
cytoplasmic compartments of the cell. Alpha subunits may constitute a
physical barrier that limits access of cytosolic proteins into the inner
proteolytic chamber.
Bey et al. (1993) mapped the PSMA1 gene to chromosome 11p15.1 by
fluorescence in situ hybridization.
*FIELD* RF
1. Bey, F.; Silva Pereira, I.; Coux, O.; Viegas-Pequignot, E.; Recillas
Targa, F.; Nothwang, H. G.; Dutrillaux, B.; Scherrer, K.: The prosomal
RNA-binding protein p27K is a member of the alpha-type human prosomal
gene family. Molec. Gen. Genet. 237: 193-205, 1993.
2. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
3. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
kayiaros: 07/13/1999
alopez: 7/16/1998
*RECORD*
*FIELD* NO
602854
*FIELD* TI
*602854 PROTEASOME SUBUNIT, ALPHA-TYPE, 1; PSMA1
;;PROTEASOME SUBUNIT NU;;
HC2;;
PROS30
read more*FIELD* TX
DeMartino et al. (1991) cloned the PSMA1 gene, termed 'subunit nu' by
them. The cDNA encoded a 263-amino acid polypeptide. The calculated and
observed molecular masses are 29.5 kD and 35 kD, respectively. Northern
blot analysis revealed an 1.4-kb mRNA in human placenta and HeLa cells.
Coux et al. (1996) noted that 2 proteins, HC2 (29.5 kD) and Pros30 (30.2
kD), are encoded by the PSMA1 gene.
Coux et al. (1996) reviewed the structures and functions of the 20S
proteasome subunits. The alpha subunits comprise the outer rings of the
proteasome. Some alpha subunits contain a functional nuclear
localization signal; proteasomes are found in both the nuclear and
cytoplasmic compartments of the cell. Alpha subunits may constitute a
physical barrier that limits access of cytosolic proteins into the inner
proteolytic chamber.
Bey et al. (1993) mapped the PSMA1 gene to chromosome 11p15.1 by
fluorescence in situ hybridization.
*FIELD* RF
1. Bey, F.; Silva Pereira, I.; Coux, O.; Viegas-Pequignot, E.; Recillas
Targa, F.; Nothwang, H. G.; Dutrillaux, B.; Scherrer, K.: The prosomal
RNA-binding protein p27K is a member of the alpha-type human prosomal
gene family. Molec. Gen. Genet. 237: 193-205, 1993.
2. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
3. DeMartino, G. N.; Orth, K.; McCullough, M. L.; Lee, L. W.; Munn,
T. Z.; Moomaw, C. R.; Dawson, P. A.; Slaughter, C. A.: The primary
structures of four subunits of the human, high molecular weight proteinase,
macropain (proteasome), are distinct but homologous. Biochim. Biophys.
Acta 1079: 29-38, 1991.
*FIELD* CD
Jennifer P. Macke: 7/15/1998
*FIELD* ED
kayiaros: 07/13/1999
alopez: 7/16/1998