Full text data of PSMA5
PSMA5
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-5; 3.4.25.1 (Macropain zeta chain; Multicatalytic endopeptidase complex zeta chain; Proteasome zeta chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-5; 3.4.25.1 (Macropain zeta chain; Multicatalytic endopeptidase complex zeta chain; Proteasome zeta chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00291922
IPI00291922 Proteasome subunit alpha type 5 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 n/a found at its expected molecular weight found at molecular weight
IPI00291922 Proteasome subunit alpha type 5 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 n/a found at its expected molecular weight found at molecular weight
UniProt
P28066
ID PSA5_HUMAN Reviewed; 241 AA.
AC P28066; B2R8F6; B4E2V4; Q3T1C1; Q6IBF7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-OCT-2003, sequence version 3.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Proteasome subunit alpha type-5;
DE EC=3.4.25.1;
DE AltName: Full=Macropain zeta chain;
DE AltName: Full=Multicatalytic endopeptidase complex zeta chain;
DE AltName: Full=Proteasome zeta chain;
GN Name=PSMA5;
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=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 [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 54-58; 67-73; 94-99 AND 120-128.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [8]
RP PROTEIN SEQUENCE OF 169-187.
RA Bienvenut W.V., Vuadens F., Crettaz D., Tissot J.-D., Quadroni M.;
RL Submitted (OCT-2003) to UniProtKB.
RN [9]
RP INDUCTION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=11771738;
RA Engidawork E., Juranville J.F., Fountoulakis M., Dierssen M.,
RA Lubec G.;
RT "Selective upregulation of the ubiquitin-proteasome proteolytic
RT pathway proteins, proteasome zeta chain and isopeptidase T in fetal
RT Down syndrome.";
RL J. Neural Transm. 61:117-130(2001).
RN [10]
RP INTERACTION WITH PSMG1 AND PSMG2.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-55, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [17]
RP INDUCTION.
RX PubMed=19734940; DOI=10.1038/onc.2009.264;
RA Arlt A., Bauer I., Schafmayer C., Tepel J., Mueerkoester S.S.,
RA Brosch M., Roeder C., Kalthoff H., Hampe J., Moyer M.P., Foelsch U.R.,
RA Schaefer H.;
RT "Increased proteasome subunit protein expression and proteasome
RT activity in colon cancer relate to an enhanced activation of nuclear
RT factor E2-related factor 2 (Nrf2).";
RL Oncogene 28:3983-3996(2009).
RN [18]
RP IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, 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 [20]
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 [21]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(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.
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. PSMA5 interacts directly with the
CC PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.
CC -!- INTERACTION:
CC O14818:PSMA7; NbExp=2; IntAct=EBI-355475, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28066-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28066-2; Sequence=VSP_046241;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
CC -!- INDUCTION: Up-regulated in colon cancer cell lines. Up-regulated
CC in fetal Down syndrome (DS) brain (at protein level). May be the
CC target of the transcriptional activator NFE2L2.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X61970; CAA43962.1; -; mRNA.
DR EMBL; CR456847; CAG33128.1; -; mRNA.
DR EMBL; AK304448; BAG65266.1; -; mRNA.
DR EMBL; AK313351; BAG36153.1; -; mRNA.
DR EMBL; AL356735; CAH70887.1; -; Genomic_DNA.
DR EMBL; AL390252; CAH70887.1; JOINED; Genomic_DNA.
DR EMBL; AL390252; CAI13171.1; -; Genomic_DNA.
DR EMBL; AL356735; CAI13171.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56381.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56383.1; -; Genomic_DNA.
DR EMBL; BC102018; AAI02019.1; -; mRNA.
DR EMBL; BC102019; AAI02020.1; -; mRNA.
DR EMBL; BC102020; AAI02021.1; -; mRNA.
DR EMBL; BC103751; AAI03752.1; -; mRNA.
DR PIR; S17521; S17521.
DR RefSeq; NP_001186701.1; NM_001199772.1.
DR RefSeq; NP_001186702.1; NM_001199773.1.
DR RefSeq; NP_001186703.1; NM_001199774.1.
DR RefSeq; NP_002781.2; NM_002790.3.
DR UniGene; Hs.485246; -.
DR ProteinModelPortal; P28066; -.
DR SMR; P28066; 9-241.
DR IntAct; P28066; 16.
DR MINT; MINT-1178571; -.
DR STRING; 9606.ENSP00000271308; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.975; -.
DR PhosphoSite; P28066; -.
DR DMDM; 38258905; -.
DR DOSAC-COBS-2DPAGE; P28066; -.
DR REPRODUCTION-2DPAGE; IPI00291922; -.
DR SWISS-2DPAGE; P28066; -.
DR PaxDb; P28066; -.
DR PeptideAtlas; P28066; -.
DR PRIDE; P28066; -.
DR DNASU; 5686; -.
DR Ensembl; ENST00000271308; ENSP00000271308; ENSG00000143106.
DR Ensembl; ENST00000538610; ENSP00000440618; ENSG00000143106.
DR GeneID; 5686; -.
DR KEGG; hsa:5686; -.
DR UCSC; uc001dxn.3; human.
DR CTD; 5686; -.
DR GeneCards; GC01M109944; -.
DR HGNC; HGNC:9534; PSMA5.
DR HPA; HPA028392; -.
DR HPA; HPA028398; -.
DR HPA; HPA028441; -.
DR MIM; 176844; gene.
DR neXtProt; NX_P28066; -.
DR PharmGKB; PA33879; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P28066; -.
DR KO; K02729; -.
DR OMA; HAFTYDE; -.
DR OrthoDB; EOG769ZKB; -.
DR PhylomeDB; P28066; -.
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; PSMA5; -.
DR GenomeRNAi; 5686; -.
DR NextBio; 22086; -.
DR PRO; PR:P28066; -.
DR Bgee; P28066; -.
DR CleanEx; HS_PSMA5; -.
DR Genevestigator; P28066; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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: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: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; Nucleus;
KW Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease.
FT CHAIN 1 241 Proteasome subunit alpha type-5.
FT /FTId=PRO_0000124117.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 55 55 Phosphothreonine.
FT MOD_RES 56 56 Phosphoserine.
FT CARBOHYD 198 198 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 58 Missing (in isoform 2).
FT /FTId=VSP_046241.
FT CONFLICT 27 27 A -> D (in Ref. 1; CAA43962).
FT CONFLICT 184 184 V -> L (in Ref. 1; CAA43962).
SQ SEQUENCE 241 AA; 26411 MW; 5610CDA00469120A CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I
//
ID PSA5_HUMAN Reviewed; 241 AA.
AC P28066; B2R8F6; B4E2V4; Q3T1C1; Q6IBF7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-OCT-2003, sequence version 3.
DT 22-JAN-2014, entry version 154.
DE RecName: Full=Proteasome subunit alpha type-5;
DE EC=3.4.25.1;
DE AltName: Full=Macropain zeta chain;
DE AltName: Full=Multicatalytic endopeptidase complex zeta chain;
DE AltName: Full=Proteasome zeta chain;
GN Name=PSMA5;
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=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 [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 54-58; 67-73; 94-99 AND 120-128.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [8]
RP PROTEIN SEQUENCE OF 169-187.
RA Bienvenut W.V., Vuadens F., Crettaz D., Tissot J.-D., Quadroni M.;
RL Submitted (OCT-2003) to UniProtKB.
RN [9]
RP INDUCTION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=11771738;
RA Engidawork E., Juranville J.F., Fountoulakis M., Dierssen M.,
RA Lubec G.;
RT "Selective upregulation of the ubiquitin-proteasome proteolytic
RT pathway proteins, proteasome zeta chain and isopeptidase T in fetal
RT Down syndrome.";
RL J. Neural Transm. 61:117-130(2001).
RN [10]
RP INTERACTION WITH PSMG1 AND PSMG2.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-55, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [17]
RP INDUCTION.
RX PubMed=19734940; DOI=10.1038/onc.2009.264;
RA Arlt A., Bauer I., Schafmayer C., Tepel J., Mueerkoester S.S.,
RA Brosch M., Roeder C., Kalthoff H., Hampe J., Moyer M.P., Foelsch U.R.,
RA Schaefer H.;
RT "Increased proteasome subunit protein expression and proteasome
RT activity in colon cancer relate to an enhanced activation of nuclear
RT factor E2-related factor 2 (Nrf2).";
RL Oncogene 28:3983-3996(2009).
RN [18]
RP IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, 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 [20]
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 [21]
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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(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.
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. PSMA5 interacts directly with the
CC PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.
CC -!- INTERACTION:
CC O14818:PSMA7; NbExp=2; IntAct=EBI-355475, EBI-603272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28066-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28066-2; Sequence=VSP_046241;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
CC -!- INDUCTION: Up-regulated in colon cancer cell lines. Up-regulated
CC in fetal Down syndrome (DS) brain (at protein level). May be the
CC target of the transcriptional activator NFE2L2.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; X61970; CAA43962.1; -; mRNA.
DR EMBL; CR456847; CAG33128.1; -; mRNA.
DR EMBL; AK304448; BAG65266.1; -; mRNA.
DR EMBL; AK313351; BAG36153.1; -; mRNA.
DR EMBL; AL356735; CAH70887.1; -; Genomic_DNA.
DR EMBL; AL390252; CAH70887.1; JOINED; Genomic_DNA.
DR EMBL; AL390252; CAI13171.1; -; Genomic_DNA.
DR EMBL; AL356735; CAI13171.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56381.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56383.1; -; Genomic_DNA.
DR EMBL; BC102018; AAI02019.1; -; mRNA.
DR EMBL; BC102019; AAI02020.1; -; mRNA.
DR EMBL; BC102020; AAI02021.1; -; mRNA.
DR EMBL; BC103751; AAI03752.1; -; mRNA.
DR PIR; S17521; S17521.
DR RefSeq; NP_001186701.1; NM_001199772.1.
DR RefSeq; NP_001186702.1; NM_001199773.1.
DR RefSeq; NP_001186703.1; NM_001199774.1.
DR RefSeq; NP_002781.2; NM_002790.3.
DR UniGene; Hs.485246; -.
DR ProteinModelPortal; P28066; -.
DR SMR; P28066; 9-241.
DR IntAct; P28066; 16.
DR MINT; MINT-1178571; -.
DR STRING; 9606.ENSP00000271308; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.975; -.
DR PhosphoSite; P28066; -.
DR DMDM; 38258905; -.
DR DOSAC-COBS-2DPAGE; P28066; -.
DR REPRODUCTION-2DPAGE; IPI00291922; -.
DR SWISS-2DPAGE; P28066; -.
DR PaxDb; P28066; -.
DR PeptideAtlas; P28066; -.
DR PRIDE; P28066; -.
DR DNASU; 5686; -.
DR Ensembl; ENST00000271308; ENSP00000271308; ENSG00000143106.
DR Ensembl; ENST00000538610; ENSP00000440618; ENSG00000143106.
DR GeneID; 5686; -.
DR KEGG; hsa:5686; -.
DR UCSC; uc001dxn.3; human.
DR CTD; 5686; -.
DR GeneCards; GC01M109944; -.
DR HGNC; HGNC:9534; PSMA5.
DR HPA; HPA028392; -.
DR HPA; HPA028398; -.
DR HPA; HPA028441; -.
DR MIM; 176844; gene.
DR neXtProt; NX_P28066; -.
DR PharmGKB; PA33879; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; P28066; -.
DR KO; K02729; -.
DR OMA; HAFTYDE; -.
DR OrthoDB; EOG769ZKB; -.
DR PhylomeDB; P28066; -.
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; PSMA5; -.
DR GenomeRNAi; 5686; -.
DR NextBio; 22086; -.
DR PRO; PR:P28066; -.
DR Bgee; P28066; -.
DR CleanEx; HS_PSMA5; -.
DR Genevestigator; P28066; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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: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: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; Nucleus;
KW Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease.
FT CHAIN 1 241 Proteasome subunit alpha type-5.
FT /FTId=PRO_0000124117.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 16 16 Phosphoserine.
FT MOD_RES 55 55 Phosphothreonine.
FT MOD_RES 56 56 Phosphoserine.
FT CARBOHYD 198 198 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 58 Missing (in isoform 2).
FT /FTId=VSP_046241.
FT CONFLICT 27 27 A -> D (in Ref. 1; CAA43962).
FT CONFLICT 184 184 V -> L (in Ref. 1; CAA43962).
SQ SEQUENCE 241 AA; 26411 MW; 5610CDA00469120A CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I
//
MIM
176844
*RECORD*
*FIELD* NO
176844
*FIELD* TI
*176844 PROTEASOME SUBUNIT, ALPHA-TYPE, 5; PSMA5
;;PROTEASOME COMPONENT 5; PSC5;;
PROTEASOME SUBUNIT ZETA
read more*FIELD* TX
See 176842.
DeMartino et al. (1991) cloned the PSMA5 gene, termed 'subunit zeta' by
them. The cDNA encoded a 241-amino acid polypeptide. The calculated and
observed molecular masses were 26 kD and 29 kD, respectively. Northern
blot analysis revealed an mRNA of 1.2 kb in both human placenta and HeLa
cells.
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.
To determine whether the order in a cluster of genes that had been
mapped to chromosome 1q in the Chinese hamster by a coamplification
mapping technique is conserved in the human genome, Mayau et al. (1998)
screened the YAC library from the CEPH laboratory by PCR. They found
that, as in the hamster, the PSMA5 gene was close to GNAI3 (139370),
which is located at 1p13.
*FIELD* RF
1. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
2. 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.
3. Mayau, V.; Baron, B.; Buttin, G.; Debatisse, M.: Twelve genes,
including the unassigned proteasome zeta subunit gene, ordered within
the human 1p13 region. Mammalian Genome 9: 331-333, 1998.
*FIELD* CN
Victor A. McKusick - updated: 9/4/1998
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
kayiaros: 07/13/1999
alopez: 10/12/1998
alopez: 10/8/1998
alopez: 9/9/1998
carol: 9/4/1998
alopez: 7/16/1998
dkim: 7/7/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/22/1991
carol: 7/10/1991
*RECORD*
*FIELD* NO
176844
*FIELD* TI
*176844 PROTEASOME SUBUNIT, ALPHA-TYPE, 5; PSMA5
;;PROTEASOME COMPONENT 5; PSC5;;
PROTEASOME SUBUNIT ZETA
read more*FIELD* TX
See 176842.
DeMartino et al. (1991) cloned the PSMA5 gene, termed 'subunit zeta' by
them. The cDNA encoded a 241-amino acid polypeptide. The calculated and
observed molecular masses were 26 kD and 29 kD, respectively. Northern
blot analysis revealed an mRNA of 1.2 kb in both human placenta and HeLa
cells.
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.
To determine whether the order in a cluster of genes that had been
mapped to chromosome 1q in the Chinese hamster by a coamplification
mapping technique is conserved in the human genome, Mayau et al. (1998)
screened the YAC library from the CEPH laboratory by PCR. They found
that, as in the hamster, the PSMA5 gene was close to GNAI3 (139370),
which is located at 1p13.
*FIELD* RF
1. Coux, O.; Tanaka, K.; Goldberg, A. L.: Structure and functions
of the 20S and 26S proteasomes. Ann. Rev. Biochem. 65: 801-847,
1996.
2. 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.
3. Mayau, V.; Baron, B.; Buttin, G.; Debatisse, M.: Twelve genes,
including the unassigned proteasome zeta subunit gene, ordered within
the human 1p13 region. Mammalian Genome 9: 331-333, 1998.
*FIELD* CN
Victor A. McKusick - updated: 9/4/1998
*FIELD* CD
Victor A. McKusick: 7/10/1991
*FIELD* ED
kayiaros: 07/13/1999
alopez: 10/12/1998
alopez: 10/8/1998
alopez: 9/9/1998
carol: 9/4/1998
alopez: 7/16/1998
dkim: 7/7/1998
mark: 8/11/1995
supermim: 3/16/1992
carol: 7/22/1991
carol: 7/10/1991