Full text data of PSMA7
PSMA7
(HSPC)
[Confidence: high (present in two of the MS resources)]
Proteasome subunit alpha type-7; 3.4.25.1 (Proteasome subunit RC6-1; Proteasome subunit XAPC7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasome subunit alpha type-7; 3.4.25.1 (Proteasome subunit RC6-1; Proteasome subunit XAPC7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00024175
IPI00024175 Splice isoform 1 of O14818 Proteasome subunit alpha type 7 Splice isoform 1 of O14818 Proteasome subunit alpha type 7 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 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
IPI00024175 Splice isoform 1 of O14818 Proteasome subunit alpha type 7 Splice isoform 1 of O14818 Proteasome subunit alpha type 7 membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 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
O14818
ID PSA7_HUMAN Reviewed; 248 AA.
AC O14818; B2R515; Q5JXJ2; Q9BR53; Q9H4K5; Q9UEU8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Proteasome subunit alpha type-7;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit RC6-1;
DE AltName: Full=Proteasome subunit XAPC7;
GN Name=PSMA7; Synonyms=HSPC;
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), AND INTERACTION WITH HBX.
RX PubMed=8764072;
RA Huang J., Kwong J., Sun E.C.-Y., Liang T.J.;
RT "Proteasome complex as a potential cellular target of hepatitis B
RT virus X protein.";
RL J. Virol. 70:5582-5591(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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] (ISOFORMS 1 AND 3).
RC TISSUE=Leukocyte, and Lung;
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 96-109, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH HBX.
RX PubMed=10748218; DOI=10.1074/jbc.M910378199;
RA Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., Liang T.J.;
RT "Structural and functional characterization of interaction between
RT hepatitis B virus X protein and the proteasome complex.";
RL J. Biol. Chem. 275:15157-15165(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=11389899; DOI=10.1016/S0014-5793(01)02499-1;
RA Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E.;
RT "Binding and regulation of HIF-1alpha by a subunit of the proteasome
RT complex, PSMA7.";
RL FEBS Lett. 498:62-66(2001).
RN [11]
RP FUNCTION.
RX PubMed=11713272; DOI=10.1128/MCB.21.24.8357-8364.2001;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Manns M.P.,
RA Wong-Staal F.;
RT "Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus
RT internal ribosome entry site-mediated translation.";
RL Mol. Cell. Biol. 21:8357-8364(2001).
RN [12]
RP INDUCTION.
RX PubMed=11574696;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Wong-Staal F.;
RT "C-SPACE (cleavage-specific amplification of cDNA ends): a novel
RT method of ribozyme-mediated gene identification.";
RL Nucleic Acids Res. 29:E94-E94(2001).
RN [13]
RP FUNCTION.
RX PubMed=12119296; DOI=10.1074/jbc.M204751200;
RA Lin H.K., Altuwaijri S., Lin W.J., Kan P.Y., Collins L.L., Chang C.;
RT "Proteasome activity is required for androgen receptor transcriptional
RT activity via regulation of androgen receptor nuclear translocation and
RT interaction with coregulators in prostate cancer cells.";
RL J. Biol. Chem. 277:36570-36576(2002).
RN [14]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [15]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [16]
RP INTERACTION WITH RAB7A.
RX PubMed=14998988; DOI=10.1074/jbc.M401022200;
RA Dong J., Chen W., Welford A., Wandinger-Ness A.;
RT "The proteasome alpha-subunit XAPC7 interacts specifically with Rab7
RT and late endosomes.";
RL J. Biol. Chem. 279:21334-21342(2004).
RN [17]
RP INTERACTION WITH PARK2.
RX PubMed=15987638; DOI=10.1016/j.febslet.2005.06.003;
RA Dachsel J.C., Lucking C.B., Deeg S., Schultz E., Lalowski M.,
RA Casademunt E., Corti O., Hampe C., Patenge N., Vaupel K., Yamamoto A.,
RA Dichgans M., Brice A., Wanker E.E., Kahle P.J., Gasser T.;
RT "Parkin interacts with the proteasome subunit alpha4.";
RL FEBS Lett. 579:3913-3919(2005).
RN [18]
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 [19]
RP INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 AND
RP ABL2, AND MUTAGENESIS OF TYR-153.
RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,
RA Cao C.;
RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome
RT subunit PSMA7 regulates proteasome degradation.";
RL Mol. Cell 22:317-327(2006).
RN [20]
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 [21]
RP INDUCTION.
RX PubMed=18202793;
RA Hu X.T., Chen W., Wang D., Shi Q.L., Zhang F.B., Liao Y.Q., Jin M.,
RA He C.;
RT "The proteasome subunit PSMA7 located on the 20q13 amplicon is
RT overexpressed and associated with liver metastasis in colorectal
RT cancer.";
RL Oncol. Rep. 19:441-446(2008).
RN [22]
RP INTERACTION WITH EMAP2.
RX PubMed=19362550; DOI=10.1016/j.yexcr.2009.03.021;
RA Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G.,
RA Libutti S.K.;
RT "Endothelial monocyte activating polypeptide-II modulates endothelial
RT cell responses by degrading hypoxia-inducible factor-1alpha through
RT interaction with PSMA7, a component of the proteasome.";
RL Exp. Cell Res. 315:1850-1859(2009).
RN [23]
RP FUNCTION, AND INTERACTION WITH MAVS.
RX PubMed=19734229; DOI=10.4049/jimmunol.0901646;
RA Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L.,
RA Zhang Y., He X., Xu Y., Shi W., Zhong H.;
RT "Negative regulation of MAVS-mediated innate immune response by
RT PSMA7.";
RL J. Immunol. 183:4241-4248(2009).
RN [24]
RP FUNCTION.
RX PubMed=19442227; DOI=10.2174/092986609788167824;
RA Du H., Huang X., Wang S., Wu Y., Xu W., Li M.;
RT "PSMA7, a potential biomarker of diseases.";
RL Protein Pept. Lett. 16:486-489(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, AND MASS 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 [26]
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. Plays an important role in the regulation of cell
CC proliferation or cell cycle control, transcriptional regulation,
CC immune and stress response, cell differentiation, and apoptosis.
CC Interacts with some important proteins involved in transcription
CC factor regulation, cell cycle transition, viral replication and
CC even tumor initiation and progression. Inhibits the
CC transactivation function of HIF-1A under both normoxic and
CC hypoxia-mimicking conditions. The interaction with EMAP2 increases
CC the proteasome-mediated HIF-1A degradation under the hypoxic
CC conditions. Plays a role in hepatitis C virus internal ribosome
CC entry site-mediated translation. Mediates nuclear translocation of
CC the androgen receptor (AR) and thereby enhances androgen-mediated
CC transactivation. Promotes MAVS degradation and thereby negatively
CC regulates MAVS-mediated innate immune response.
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. PSMA7 interacts directly with the
CC PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.
CC Interacts with HIV-1 TAT protein. Interacts with hepatitis B virus
CC X protein (HBX). Interacts with HIF1A. Interacts with RAB7A.
CC Interacts with PARK2. Interacts with ABL1 and ABL2. Interacts with
CC EMAP2. Interacts with MAVS.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-603272, EBI-603272;
CC P25786:PSMA1; NbExp=9; IntAct=EBI-603272, EBI-359352;
CC P25787:PSMA2; NbExp=5; IntAct=EBI-603272, EBI-603262;
CC P25788:PSMA3; NbExp=6; IntAct=EBI-603272, EBI-348380;
CC P25789:PSMA4; NbExp=8; IntAct=EBI-603272, EBI-359310;
CC P28066:PSMA5; NbExp=2; IntAct=EBI-603272, EBI-355475;
CC P60900:PSMA6; NbExp=11; IntAct=EBI-603272, EBI-357793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some
CC isoforms;
CC Name=1;
CC IsoId=O14818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14818-2; Sequence=VSP_005281;
CC Name=3;
CC IsoId=O14818-4; Sequence=VSP_046556, VSP_046557;
CC -!- INDUCTION: Down-regulated by the ribozyme Rz3'X. Up-regulated in
CC colorectal cancer tissues.
CC -!- PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of
CC proteasomal activity and cell cycle transition blocks.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; AF022815; AAB81515.1; -; mRNA.
DR EMBL; AF054185; AAC99402.1; -; mRNA.
DR EMBL; BT007165; AAP35829.1; -; mRNA.
DR EMBL; AK312025; BAG34962.1; -; mRNA.
DR EMBL; AL078633; CAC04017.1; -; Genomic_DNA.
DR EMBL; AL078633; CAC04018.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75398.1; -; Genomic_DNA.
DR EMBL; BC004427; AAH04427.1; -; mRNA.
DR EMBL; BI906714; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; PC2326; PC2326.
DR RefSeq; NP_002783.1; NM_002792.3.
DR UniGene; Hs.233952; -.
DR ProteinModelPortal; O14818; -.
DR SMR; O14818; 2-232.
DR IntAct; O14818; 29.
DR MINT; MINT-5000782; -.
DR STRING; 9606.ENSP00000359910; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.979; -.
DR PhosphoSite; O14818; -.
DR REPRODUCTION-2DPAGE; IPI00024175; -.
DR UCD-2DPAGE; O14818; -.
DR PaxDb; O14818; -.
DR PRIDE; O14818; -.
DR DNASU; 5688; -.
DR Ensembl; ENST00000370858; ENSP00000359895; ENSG00000101182.
DR Ensembl; ENST00000370861; ENSP00000359898; ENSG00000101182.
DR Ensembl; ENST00000370873; ENSP00000359910; ENSG00000101182.
DR GeneID; 5688; -.
DR KEGG; hsa:5688; -.
DR UCSC; uc002ybx.2; human.
DR CTD; 5688; -.
DR GeneCards; GC20M060711; -.
DR HGNC; HGNC:9536; PSMA7.
DR HPA; HPA047266; -.
DR MIM; 606607; gene.
DR neXtProt; NX_O14818; -.
DR PharmGKB; PA33881; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; O14818; -.
DR KO; K02731; -.
DR OMA; ITRHIAG; -.
DR PhylomeDB; O14818; -.
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; PSMA7; human.
DR GeneWiki; PSMA7; -.
DR GenomeRNAi; 5688; -.
DR NextBio; 22094; -.
DR PRO; PR:O14818; -.
DR ArrayExpress; O14818; -.
DR Bgee; O14818; -.
DR CleanEx; HS_PSMA7; -.
DR Genevestigator; O14818; -.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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; Host-virus interaction;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT CHAIN 1 248 Proteasome subunit alpha type-7.
FT /FTId=PRO_0000124142.
FT MOD_RES 153 153 Phosphotyrosine; by ABL1 and ABL2.
FT MOD_RES 227 227 N6-acetyllysine.
FT CARBOHYD 130 130 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 70 Missing (in isoform 2).
FT /FTId=VSP_005281.
FT VAR_SEQ 117 149 RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP -> VGAC
FT PLACSPLAAGQSRLRHGGSCHVTSGESEN (in isoform
FT 3).
FT /FTId=VSP_046556.
FT VAR_SEQ 150 248 Missing (in isoform 3).
FT /FTId=VSP_046557.
FT MUTAGEN 153 153 Y->F: Displays impaired G1/S transition
FT and S/G2 progression.
FT CONFLICT 160 160 A -> S (in Ref. 2; AAC99402).
SQ SEQUENCE 248 AA; 27887 MW; 5DD0276A1C2DEF91 CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE
KKKQKKAS
//
ID PSA7_HUMAN Reviewed; 248 AA.
AC O14818; B2R515; Q5JXJ2; Q9BR53; Q9H4K5; Q9UEU8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Proteasome subunit alpha type-7;
DE EC=3.4.25.1;
DE AltName: Full=Proteasome subunit RC6-1;
DE AltName: Full=Proteasome subunit XAPC7;
GN Name=PSMA7; Synonyms=HSPC;
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), AND INTERACTION WITH HBX.
RX PubMed=8764072;
RA Huang J., Kwong J., Sun E.C.-Y., Liang T.J.;
RT "Proteasome complex as a potential cellular target of hepatitis B
RT virus X protein.";
RL J. Virol. 70:5582-5591(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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] (ISOFORMS 1 AND 3).
RC TISSUE=Leukocyte, and Lung;
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 96-109, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH HBX.
RX PubMed=10748218; DOI=10.1074/jbc.M910378199;
RA Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., Liang T.J.;
RT "Structural and functional characterization of interaction between
RT hepatitis B virus X protein and the proteasome complex.";
RL J. Biol. Chem. 275:15157-15165(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=11389899; DOI=10.1016/S0014-5793(01)02499-1;
RA Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E.;
RT "Binding and regulation of HIF-1alpha by a subunit of the proteasome
RT complex, PSMA7.";
RL FEBS Lett. 498:62-66(2001).
RN [11]
RP FUNCTION.
RX PubMed=11713272; DOI=10.1128/MCB.21.24.8357-8364.2001;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Manns M.P.,
RA Wong-Staal F.;
RT "Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus
RT internal ribosome entry site-mediated translation.";
RL Mol. Cell. Biol. 21:8357-8364(2001).
RN [12]
RP INDUCTION.
RX PubMed=11574696;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Wong-Staal F.;
RT "C-SPACE (cleavage-specific amplification of cDNA ends): a novel
RT method of ribozyme-mediated gene identification.";
RL Nucleic Acids Res. 29:E94-E94(2001).
RN [13]
RP FUNCTION.
RX PubMed=12119296; DOI=10.1074/jbc.M204751200;
RA Lin H.K., Altuwaijri S., Lin W.J., Kan P.Y., Collins L.L., Chang C.;
RT "Proteasome activity is required for androgen receptor transcriptional
RT activity via regulation of androgen receptor nuclear translocation and
RT interaction with coregulators in prostate cancer cells.";
RL J. Biol. Chem. 277:36570-36576(2002).
RN [14]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [15]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [16]
RP INTERACTION WITH RAB7A.
RX PubMed=14998988; DOI=10.1074/jbc.M401022200;
RA Dong J., Chen W., Welford A., Wandinger-Ness A.;
RT "The proteasome alpha-subunit XAPC7 interacts specifically with Rab7
RT and late endosomes.";
RL J. Biol. Chem. 279:21334-21342(2004).
RN [17]
RP INTERACTION WITH PARK2.
RX PubMed=15987638; DOI=10.1016/j.febslet.2005.06.003;
RA Dachsel J.C., Lucking C.B., Deeg S., Schultz E., Lalowski M.,
RA Casademunt E., Corti O., Hampe C., Patenge N., Vaupel K., Yamamoto A.,
RA Dichgans M., Brice A., Wanker E.E., Kahle P.J., Gasser T.;
RT "Parkin interacts with the proteasome subunit alpha4.";
RL FEBS Lett. 579:3913-3919(2005).
RN [18]
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 [19]
RP INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 AND
RP ABL2, AND MUTAGENESIS OF TYR-153.
RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,
RA Cao C.;
RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome
RT subunit PSMA7 regulates proteasome degradation.";
RL Mol. Cell 22:317-327(2006).
RN [20]
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 [21]
RP INDUCTION.
RX PubMed=18202793;
RA Hu X.T., Chen W., Wang D., Shi Q.L., Zhang F.B., Liao Y.Q., Jin M.,
RA He C.;
RT "The proteasome subunit PSMA7 located on the 20q13 amplicon is
RT overexpressed and associated with liver metastasis in colorectal
RT cancer.";
RL Oncol. Rep. 19:441-446(2008).
RN [22]
RP INTERACTION WITH EMAP2.
RX PubMed=19362550; DOI=10.1016/j.yexcr.2009.03.021;
RA Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G.,
RA Libutti S.K.;
RT "Endothelial monocyte activating polypeptide-II modulates endothelial
RT cell responses by degrading hypoxia-inducible factor-1alpha through
RT interaction with PSMA7, a component of the proteasome.";
RL Exp. Cell Res. 315:1850-1859(2009).
RN [23]
RP FUNCTION, AND INTERACTION WITH MAVS.
RX PubMed=19734229; DOI=10.4049/jimmunol.0901646;
RA Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L.,
RA Zhang Y., He X., Xu Y., Shi W., Zhong H.;
RT "Negative regulation of MAVS-mediated innate immune response by
RT PSMA7.";
RL J. Immunol. 183:4241-4248(2009).
RN [24]
RP FUNCTION.
RX PubMed=19442227; DOI=10.2174/092986609788167824;
RA Du H., Huang X., Wang S., Wu Y., Xu W., Li M.;
RT "PSMA7, a potential biomarker of diseases.";
RL Protein Pept. Lett. 16:486-489(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, AND MASS 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 [26]
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. Plays an important role in the regulation of cell
CC proliferation or cell cycle control, transcriptional regulation,
CC immune and stress response, cell differentiation, and apoptosis.
CC Interacts with some important proteins involved in transcription
CC factor regulation, cell cycle transition, viral replication and
CC even tumor initiation and progression. Inhibits the
CC transactivation function of HIF-1A under both normoxic and
CC hypoxia-mimicking conditions. The interaction with EMAP2 increases
CC the proteasome-mediated HIF-1A degradation under the hypoxic
CC conditions. Plays a role in hepatitis C virus internal ribosome
CC entry site-mediated translation. Mediates nuclear translocation of
CC the androgen receptor (AR) and thereby enhances androgen-mediated
CC transactivation. Promotes MAVS degradation and thereby negatively
CC regulates MAVS-mediated innate immune response.
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. PSMA7 interacts directly with the
CC PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.
CC Interacts with HIV-1 TAT protein. Interacts with hepatitis B virus
CC X protein (HBX). Interacts with HIF1A. Interacts with RAB7A.
CC Interacts with PARK2. Interacts with ABL1 and ABL2. Interacts with
CC EMAP2. Interacts with MAVS.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-603272, EBI-603272;
CC P25786:PSMA1; NbExp=9; IntAct=EBI-603272, EBI-359352;
CC P25787:PSMA2; NbExp=5; IntAct=EBI-603272, EBI-603262;
CC P25788:PSMA3; NbExp=6; IntAct=EBI-603272, EBI-348380;
CC P25789:PSMA4; NbExp=8; IntAct=EBI-603272, EBI-359310;
CC P28066:PSMA5; NbExp=2; IntAct=EBI-603272, EBI-355475;
CC P60900:PSMA6; NbExp=11; IntAct=EBI-603272, EBI-357793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some
CC isoforms;
CC Name=1;
CC IsoId=O14818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14818-2; Sequence=VSP_005281;
CC Name=3;
CC IsoId=O14818-4; Sequence=VSP_046556, VSP_046557;
CC -!- INDUCTION: Down-regulated by the ribozyme Rz3'X. Up-regulated in
CC colorectal cancer tissues.
CC -!- PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of
CC proteasomal activity and cell cycle transition blocks.
CC -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR EMBL; AF022815; AAB81515.1; -; mRNA.
DR EMBL; AF054185; AAC99402.1; -; mRNA.
DR EMBL; BT007165; AAP35829.1; -; mRNA.
DR EMBL; AK312025; BAG34962.1; -; mRNA.
DR EMBL; AL078633; CAC04017.1; -; Genomic_DNA.
DR EMBL; AL078633; CAC04018.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75398.1; -; Genomic_DNA.
DR EMBL; BC004427; AAH04427.1; -; mRNA.
DR EMBL; BI906714; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; PC2326; PC2326.
DR RefSeq; NP_002783.1; NM_002792.3.
DR UniGene; Hs.233952; -.
DR ProteinModelPortal; O14818; -.
DR SMR; O14818; 2-232.
DR IntAct; O14818; 29.
DR MINT; MINT-5000782; -.
DR STRING; 9606.ENSP00000359910; -.
DR ChEMBL; CHEMBL2364701; -.
DR MEROPS; T01.979; -.
DR PhosphoSite; O14818; -.
DR REPRODUCTION-2DPAGE; IPI00024175; -.
DR UCD-2DPAGE; O14818; -.
DR PaxDb; O14818; -.
DR PRIDE; O14818; -.
DR DNASU; 5688; -.
DR Ensembl; ENST00000370858; ENSP00000359895; ENSG00000101182.
DR Ensembl; ENST00000370861; ENSP00000359898; ENSG00000101182.
DR Ensembl; ENST00000370873; ENSP00000359910; ENSG00000101182.
DR GeneID; 5688; -.
DR KEGG; hsa:5688; -.
DR UCSC; uc002ybx.2; human.
DR CTD; 5688; -.
DR GeneCards; GC20M060711; -.
DR HGNC; HGNC:9536; PSMA7.
DR HPA; HPA047266; -.
DR MIM; 606607; gene.
DR neXtProt; NX_O14818; -.
DR PharmGKB; PA33881; -.
DR eggNOG; COG0638; -.
DR HOGENOM; HOG000091085; -.
DR HOVERGEN; HBG003005; -.
DR InParanoid; O14818; -.
DR KO; K02731; -.
DR OMA; ITRHIAG; -.
DR PhylomeDB; O14818; -.
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; PSMA7; human.
DR GeneWiki; PSMA7; -.
DR GenomeRNAi; 5688; -.
DR NextBio; 22094; -.
DR PRO; PR:O14818; -.
DR ArrayExpress; O14818; -.
DR Bgee; O14818; -.
DR CleanEx; HS_PSMA7; -.
DR Genevestigator; O14818; -.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
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; Host-virus interaction;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Threonine protease.
FT CHAIN 1 248 Proteasome subunit alpha type-7.
FT /FTId=PRO_0000124142.
FT MOD_RES 153 153 Phosphotyrosine; by ABL1 and ABL2.
FT MOD_RES 227 227 N6-acetyllysine.
FT CARBOHYD 130 130 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 70 Missing (in isoform 2).
FT /FTId=VSP_005281.
FT VAR_SEQ 117 149 RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP -> VGAC
FT PLACSPLAAGQSRLRHGGSCHVTSGESEN (in isoform
FT 3).
FT /FTId=VSP_046556.
FT VAR_SEQ 150 248 Missing (in isoform 3).
FT /FTId=VSP_046557.
FT MUTAGEN 153 153 Y->F: Displays impaired G1/S transition
FT and S/G2 progression.
FT CONFLICT 160 160 A -> S (in Ref. 2; AAC99402).
SQ SEQUENCE 248 AA; 27887 MW; 5DD0276A1C2DEF91 CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE
KKKQKKAS
//
MIM
606607
*RECORD*
*FIELD* NO
606607
*FIELD* TI
*606607 PROTEASOME SUBUNIT, ALPHA-TYPE, 7; PSMA7
;;XAPC7;;
PROTEASOME SUBUNIT ALPHA-4
read more*FIELD* TX
CLONING
The hepatitis B virus X (HBX) protein is a well-conserved 16-kD
phosphoprotein expressed in both nucleus and cytoplasm. It is critical
for the life cycle of the virus. HBX message is detectable in infected
liver, as are antibodies to the less-detectable protein. Using a yeast
2-hybrid screen of a HeLa cell cDNA library with HBX as the probe,
followed by further probing of the HeLa cell library, Huang et al.
(1996) obtained a cDNA encoding PSMA7, which they termed XAPC7. The
deduced 248-amino acid PSMA7 protein is 33% identical to HC8 (PSMA3;
176843) and has higher homology with Drosophila and Arabidopsis
proteasome subunits. Northern blot analysis revealed expression of a
1.0-kb PSMA7 transcript in several human cell lines. Western blot
analysis showed that PSMA7 is expressed as a 28-kD proteasome subunit
protein.
MAPPING
Gross (2013) mapped the PSMA7 gene to chromosome 20q13.33 based on an
alignment of the PSMA7 sequence (GenBank GENBANK AF022815) with the
genomic sequence (GRCh37).
GENE FUNCTION
Huang et al. (1996) found that residues 188 to 198 in the C terminus of
PSMA7, but not these residues in other proteasome subunits, specifically
interacted with HBX and that the N terminus of HBX, which is required
for its transactivation function, was not necessary for its interaction
with PSMA7. Luciferase reporter assays demonstrated that antisense PSMA7
blocked the transactivation function of HBX. Huang et al. (1996)
proposed that HBX, by interacting with PSMA7, may interfere with the
activities of the proteasome complex.
Using a yeast 2-hybrid screen of a fetal brain cDNA library with parkin
(PARK2; 602544) and 2 parkin mutants as baits, Dachsel et al. (2005)
isolated PSMA7, which they termed alpha-4. Coimmunoprecipitation
experiments showed that the interaction occurred between residues 179 to
248 of PSMA7 and the C terminus of PARKIN, including the IBR-RING2
motif.
Liu et al. (2006) found that ABL (ABL1; 189980) and ARG (ABL2; 164690)
tyrosine kinases associated with and phosphorylated PSMA7 on tyr153,
leading to reduced proteasome-dependent proteolysis. Cells expressing a
phosphorylation mutant of PSMA7 displayed impaired G1/S transition and
S/G2 progression. Oxidative stress and ionizing irradiation resulted in
increased formation of ABL-PSMA7 complexes and PSMA7 phosphorylation.
Liu et al. (2006) concluded that phosphorylation of PSMA7 regulates
proteasome activity.
MOLECULAR GENETICS
For discussion of mutation in the PSMA7 gene as a possible cause of an
intellectual disability phenotype, see 606607.0001.
*FIELD* AV
.0001
VARIANT OF UNKNOWN SIGNIFICANCE
PSMA7, ALA112PHE
This variant is classified as a variant of unknown significance because
its contribution to intellectual disability has not been confirmed.
In a male patient with severe intellectual disability, borderline
microcephaly (head circumference, 54.5 cm, 1.9 SD), mild dysmorphic
features including thick eyebrows and retrognathia, mild kyphosis,
hirsutism, and short toes, de Ligt et al. (2012) identified a de novo
heterozygous 335C-A transversion, resulting in an ala112-to-asp (A112D)
substitution.
*FIELD* RF
1. Dachsel, J. C.; Lucking, C. B.; Deeg, S.; Schultz, E.; Lalowski,
M.; Casademunt, E.; Corti, O.; Hampe, C.; Patenge, N.; Vaupel, K.;
Yamamoto, A.; Dichgans, M.; Brice, A.; Wanker, E. E.; Kahle, P. J.;
Gasser, T.: Parkin interacts with the proteasome subunit alpha-4. FEBS
Lett. 579: 3913-3919, 2005.
2. de Ligt, J.; Willemsen, M. H.; van Bon, B. W. M.; Kleefstra, T.;
Yntema, H. G.; Kroes, T.; Vulto-van Silfhout, A. T.; Koolen, D. A.;
de Vries, P.; Gilissen, C.; del Rosario, M.; Hoischen, A.; Scheffer,
H.; de Vries, B. B. A.; Brunner, H. G.; Veltman, J. A.; Vissers, L.
E. L. M.: Diagnostic exome sequencing in persons with severe intellectual
disability. New Eng. J. Med. 367: 1921-1929, 2012.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/13/2013.
4. Huang, J.; Kwong, J.; Sun, E. C.-Y.; Liang, T. J.: Proteasome
complex as a potential cellular target of hepatitis B virus X protein. J.
Virol. 70: 5582-5591, 1996.
5. Liu, X.; Huang, W.; Li, C.; Li, P.; Yuan, J.; Li, X.; Qiu, X.-B.;
Ma, Q.; Cao, C.: Interaction between c-Abl and Arg tyrosine kinases
and proteasome subunit PSMA7 regulates proteasome degradation. Molec.
Cell 22: 317-327, 2006.
*FIELD* CN
Matthew B. Gross - updated: 02/13/2013
Ada Hamosh - updated: 2/13/2013
Paul J. Converse - updated: 7/6/2007
Patricia A. Hartz - updated: 6/13/2006
*FIELD* CD
Paul J. Converse: 1/11/2002
*FIELD* ED
mgross: 02/13/2013
carol: 2/13/2013
mgross: 7/27/2007
terry: 7/6/2007
mgross: 6/14/2006
terry: 6/13/2006
mgross: 1/14/2002
mgross: 1/11/2002
*RECORD*
*FIELD* NO
606607
*FIELD* TI
*606607 PROTEASOME SUBUNIT, ALPHA-TYPE, 7; PSMA7
;;XAPC7;;
PROTEASOME SUBUNIT ALPHA-4
read more*FIELD* TX
CLONING
The hepatitis B virus X (HBX) protein is a well-conserved 16-kD
phosphoprotein expressed in both nucleus and cytoplasm. It is critical
for the life cycle of the virus. HBX message is detectable in infected
liver, as are antibodies to the less-detectable protein. Using a yeast
2-hybrid screen of a HeLa cell cDNA library with HBX as the probe,
followed by further probing of the HeLa cell library, Huang et al.
(1996) obtained a cDNA encoding PSMA7, which they termed XAPC7. The
deduced 248-amino acid PSMA7 protein is 33% identical to HC8 (PSMA3;
176843) and has higher homology with Drosophila and Arabidopsis
proteasome subunits. Northern blot analysis revealed expression of a
1.0-kb PSMA7 transcript in several human cell lines. Western blot
analysis showed that PSMA7 is expressed as a 28-kD proteasome subunit
protein.
MAPPING
Gross (2013) mapped the PSMA7 gene to chromosome 20q13.33 based on an
alignment of the PSMA7 sequence (GenBank GENBANK AF022815) with the
genomic sequence (GRCh37).
GENE FUNCTION
Huang et al. (1996) found that residues 188 to 198 in the C terminus of
PSMA7, but not these residues in other proteasome subunits, specifically
interacted with HBX and that the N terminus of HBX, which is required
for its transactivation function, was not necessary for its interaction
with PSMA7. Luciferase reporter assays demonstrated that antisense PSMA7
blocked the transactivation function of HBX. Huang et al. (1996)
proposed that HBX, by interacting with PSMA7, may interfere with the
activities of the proteasome complex.
Using a yeast 2-hybrid screen of a fetal brain cDNA library with parkin
(PARK2; 602544) and 2 parkin mutants as baits, Dachsel et al. (2005)
isolated PSMA7, which they termed alpha-4. Coimmunoprecipitation
experiments showed that the interaction occurred between residues 179 to
248 of PSMA7 and the C terminus of PARKIN, including the IBR-RING2
motif.
Liu et al. (2006) found that ABL (ABL1; 189980) and ARG (ABL2; 164690)
tyrosine kinases associated with and phosphorylated PSMA7 on tyr153,
leading to reduced proteasome-dependent proteolysis. Cells expressing a
phosphorylation mutant of PSMA7 displayed impaired G1/S transition and
S/G2 progression. Oxidative stress and ionizing irradiation resulted in
increased formation of ABL-PSMA7 complexes and PSMA7 phosphorylation.
Liu et al. (2006) concluded that phosphorylation of PSMA7 regulates
proteasome activity.
MOLECULAR GENETICS
For discussion of mutation in the PSMA7 gene as a possible cause of an
intellectual disability phenotype, see 606607.0001.
*FIELD* AV
.0001
VARIANT OF UNKNOWN SIGNIFICANCE
PSMA7, ALA112PHE
This variant is classified as a variant of unknown significance because
its contribution to intellectual disability has not been confirmed.
In a male patient with severe intellectual disability, borderline
microcephaly (head circumference, 54.5 cm, 1.9 SD), mild dysmorphic
features including thick eyebrows and retrognathia, mild kyphosis,
hirsutism, and short toes, de Ligt et al. (2012) identified a de novo
heterozygous 335C-A transversion, resulting in an ala112-to-asp (A112D)
substitution.
*FIELD* RF
1. Dachsel, J. C.; Lucking, C. B.; Deeg, S.; Schultz, E.; Lalowski,
M.; Casademunt, E.; Corti, O.; Hampe, C.; Patenge, N.; Vaupel, K.;
Yamamoto, A.; Dichgans, M.; Brice, A.; Wanker, E. E.; Kahle, P. J.;
Gasser, T.: Parkin interacts with the proteasome subunit alpha-4. FEBS
Lett. 579: 3913-3919, 2005.
2. de Ligt, J.; Willemsen, M. H.; van Bon, B. W. M.; Kleefstra, T.;
Yntema, H. G.; Kroes, T.; Vulto-van Silfhout, A. T.; Koolen, D. A.;
de Vries, P.; Gilissen, C.; del Rosario, M.; Hoischen, A.; Scheffer,
H.; de Vries, B. B. A.; Brunner, H. G.; Veltman, J. A.; Vissers, L.
E. L. M.: Diagnostic exome sequencing in persons with severe intellectual
disability. New Eng. J. Med. 367: 1921-1929, 2012.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/13/2013.
4. Huang, J.; Kwong, J.; Sun, E. C.-Y.; Liang, T. J.: Proteasome
complex as a potential cellular target of hepatitis B virus X protein. J.
Virol. 70: 5582-5591, 1996.
5. Liu, X.; Huang, W.; Li, C.; Li, P.; Yuan, J.; Li, X.; Qiu, X.-B.;
Ma, Q.; Cao, C.: Interaction between c-Abl and Arg tyrosine kinases
and proteasome subunit PSMA7 regulates proteasome degradation. Molec.
Cell 22: 317-327, 2006.
*FIELD* CN
Matthew B. Gross - updated: 02/13/2013
Ada Hamosh - updated: 2/13/2013
Paul J. Converse - updated: 7/6/2007
Patricia A. Hartz - updated: 6/13/2006
*FIELD* CD
Paul J. Converse: 1/11/2002
*FIELD* ED
mgross: 02/13/2013
carol: 2/13/2013
mgross: 7/27/2007
terry: 7/6/2007
mgross: 6/14/2006
terry: 6/13/2006
mgross: 1/14/2002
mgross: 1/11/2002