O14818 (PSA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-7
EC=3.4.25.1

Alternative name(s):
Proteasome subunit RC6-1
Proteasome subunit XAPC7

Gene names

Name:	PSMA7
Synonyms:	HSPC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. Ref.10 Ref.11 Ref.13 Ref.23 Ref.24
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly. Interacts with HIV-1 TAT protein. Interacts with hepatitis B virus X protein (HBX). Interacts with HIF1A. Interacts with RAB7A. Interacts with PARK2. Interacts with ABL1 and ABL2. Interacts with EMAP2. Interacts with MAVS. Ref.1 Ref.9 Ref.10 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23
Subcellular location	Cytoplasm. Nucleus.
Induction	Down-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues. Ref.12 Ref.21
Post-translational modification	Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from sequence or structural similarity. Source: UniProtKB proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-603272,EBI-603272
PSMA1	P25786	7	EBI-603272,EBI-359352
PSMA2	P25787	2	EBI-603272,EBI-603262
PSMA3	P25788	4	EBI-603272,EBI-348380
PSMA4	P25789	6	EBI-603272,EBI-359310
PSMA6	P60900	6	EBI-603272,EBI-357793

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: O14818-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O14818-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Isoform 3 (identifier: O14818-4)

The sequence of this isoform is not available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 248	248	Proteasome subunit alpha type-7		PRO_0000124142
Amino acid modifications
	Modified residue	153	1	Phosphotyrosine; by ABL1 and ABL2 Ref.19
	Modified residue	227	1	N6-acetyllysine Ref.25
	Glycosylation	130	1	O-linked (GlcNAc...) By similarity
Natural variations
	Alternative sequence	1 – 70	70	Missing in isoform 2.		VSP_005281
Experimental info
	Mutagenesis	153	1	Y → F: Displays impaired G1/S transition and S/G2 progression. Ref.19
	Sequence conflict	160	1	A → S in AAC99402. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 5DD0276A1C2DEF91	FASTA	248	27,887
	10 20 30 40 50 60 MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR 70 80 90 100 110 120 KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ 130 140 150 160 170 180 SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA 190 200 210 220 230 240 IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
	Isoform 2 [UniParc]. Checksum: A4A7D8924670D890	FASTA	178	20,193
	10 20 30 40 50 60 MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ SNGRRPFGIS 70 80 90 100 110 120 ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA IETDDLTIKL 130 140 150 160 170 VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
	Isoform 3 (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Proteasome complex as a potential cellular target of hepatitis B virus X protein." Huang J., Kwong J., Sun E.C.-Y., Liang T.J. J. Virol. 70:5582-5591(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HBX.
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Urinary bladder.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[8]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 96-109, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex." Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., Liang T.J. J. Biol. Chem. 275:15157-15165(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HBX.
[10]	"Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7." Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E. FEBS Lett. 498:62-66(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIF1A.
[11]	"Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation." Kruger M., Beger C., Welch P.J., Barber J.R., Manns M.P., Wong-Staal F. Mol. Cell. Biol. 21:8357-8364(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"C-SPACE (cleavage-specific amplification of cDNA ends): a novel method of ribozyme-mediated gene identification." Kruger M., Beger C., Welch P.J., Barber J.R., Wong-Staal F. Nucleic Acids Res. 29:E94-E94(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[13]	"Proteasome activity is required for androgen receptor transcriptional activity via regulation of androgen receptor nuclear translocation and interaction with coregulators in prostate cancer cells." Lin H.K., Altuwaijri S., Lin W.J., Kan P.Y., Collins L.L., Chang C. J. Biol. Chem. 277:36570-36576(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits." Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E. FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[15]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[16]	"The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes." Dong J., Chen W., Welford A., Wandinger-Ness A. J. Biol. Chem. 279:21334-21342(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB7A.
[17]	"Parkin interacts with the proteasome subunit alpha4." 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. FEBS Lett. 579:3913-3919(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARK2.
[18]	"A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes." Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y., Natsume T., Tanaka K., Murata S. Nature 437:1381-1385(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMG1 AND PSMG2.
[19]	"Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation." Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C. Mol. Cell 22:317-327(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 AND ABL2, MUTAGENESIS OF TYR-153.
[20]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[21]	"The proteasome subunit PSMA7 located on the 20q13 amplicon is overexpressed and associated with liver metastasis in colorectal cancer." Hu X.T., Chen W., Wang D., Shi Q.L., Zhang F.B., Liao Y.Q., Jin M., He C. Oncol. Rep. 19:441-446(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[22]	"Endothelial monocyte activating polypeptide-II modulates endothelial cell responses by degrading hypoxia-inducible factor-1alpha through interaction with PSMA7, a component of the proteasome." Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G., Libutti S.K. Exp. Cell Res. 315:1850-1859(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EMAP2.
[23]	"Negative regulation of MAVS-mediated innate immune response by PSMA7." Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L., Zhang Y., He X., Xu Y., Shi W., Zhong H. J. Immunol. 183:4241-4248(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAVS.
[24]	"PSMA7, a potential biomarker of diseases." Du H., Huang X., Wang S., Wu Y., Xu W., Li M. Protein Pept. Lett. 16:486-489(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, MASS SPECTROMETRY.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF022815 mRNA. Translation: AAB81515.1. AF054185 mRNA. Translation: AAC99402.1. BT007165 mRNA. Translation: AAP35829.1. AK312025 mRNA. Translation: BAG34962.1. AL078633 Genomic DNA. Translation: CAC04017.1. AL078633 Genomic DNA. Translation: CAC04018.1. CH471077 Genomic DNA. Translation: EAW75398.1. BC004427 mRNA. Translation: AAH04427.1.
IPI	IPI00024175. IPI00218372.
PIR	PC2326.
RefSeq	NP_002783.1. NM_002792.3.
UniGene	Hs.233952.
3D structure databases
ProteinModelPortal	O14818.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14818. 16 interactions.
MINT	MINT-5000782.
STRING	9606.ENSP00000359910.
Protein family/group databases
MEROPS	T01.979.
PTM databases
PhosphoSite	O14818.
2D gel databases
REPRODUCTION-2DPAGE	IPI00024175.
UCD-2DPAGE	O14818.
Proteomic databases
PaxDb	O14818.
PRIDE	O14818.
Protocols and materials databases
DNASU	5688.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370861; ENSP00000359898; ENSG00000101182. ENST00000370873; ENSP00000359910; ENSG00000101182.
GeneID	5688.
KEGG	hsa:5688.
UCSC	uc002ybx.1. human.
Organism-specific databases
CTD	5688.
GeneCards	GC20M060711.
HGNC	HGNC:9536. PSMA7.
MIM	606607. gene.
neXtProt	NX_O14818.
PharmGKB	PA33881.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091085.
HOVERGEN	HBG003005.
InParanoid	O14818.
KO	K02731.
OMA	PVSIEYI.
OrthoDB	EOG4TQM9T.
PhylomeDB	O14818.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_115566. Cell Cycle. REACT_116125. Disease. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_21257. Metabolism of RNA. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	O14818.
Bgee	O14818.
CleanEx	HS_PSMA7.
Genevestigator	O14818.
GermOnline	ENSG00000101182. Homo sapiens.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_N. IPR023332. Proteasome_suA-type. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
SMART	SM00948. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PSMA7. human.
GenomeRNAi	5688.
NextBio	22094.
SOURCE	Search...

Entry information

Entry name

PSA7_HUMAN

Accession

Primary (citable) accession number: O14818
Secondary accession number(s): B2R515 , Q9BR53, Q9H4K5, Q9UEU8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 141 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.