Proteasome subunit alpha type-7 - Homo sapiens (Human)

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.
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. Ref.8
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1A family.

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-603272,EBI-603272
IKBKE	Q14164	1	EBI-603272,EBI-307369
NME2	P22392	1	EBI-603272,EBI-713693
PSMA1	P25786	3	EBI-603272,EBI-359352
PSMA2	P25787	1	EBI-603272,EBI-603262
PSMA3	P25788	1	EBI-603272,EBI-348380
PSMA4	P25789	4	EBI-603272,EBI-359310
PSMA5	P28066	1	EBI-603272,EBI-355475
PSMA6	P60900	3	EBI-603272,EBI-357793
TIMP2	P16035	1	EBI-603272,EBI-1033507

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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.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 248

247

Proteasome subunit alpha type-7

PRO_0000124142

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.9

Natural variations

Alternative sequence

1 – 70

70

Missing in isoform 2.

VSP_005281

Experimental info

Sequence conflict

160

1

A → S in AAC99402. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 5DD0276A1C2DEF91
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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

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Isoform 2.

Checksum: A4A7D8924670D890
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FASTA

178

20,193

Isoform 3 (Sequence not available).

FASTA

–

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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: 8764072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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: 11042152] [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]	"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. Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[6]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 96-109, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[7]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004) [PubMed: 14759258] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[8]	"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: 16251969] [Abstract] Cited for: INTERACTION WITH PSMG1 AND PSMG2.
[9]	"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: 17323924] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AF022815 mRNA. Translation: AAB81515.1. AF054185 mRNA. Translation: AAC99402.1. BT007165 mRNA. Translation: AAP35829.1. AL078633 Genomic DNA. Translation: CAC04017.1. AL078633 Genomic DNA. Translation: CAC04018.1. BC004427 mRNA. Translation: AAH04427.1.
IPI	IPI00024175. IPI00218372.
PIR	PC2326.
RefSeq	NP_002783.1.
UniGene	Hs.233952
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P40303.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14818. 21 interactions.
Protein family/group databases
MEROPS	T01.974.
PTM databases
PhosphoSite	O14818.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00024175.
Proteomic databases
PRIDE	O14818.
Genome annotation databases
Ensembl	ENSG00000101182. Homo sapiens. [Contig view]
GeneID	5688.
KEGG	hsa:5688.
NMPDR	fig\|9606.3.peg.20608.
Organism-specific databases
GeneCards	GC20M060145.
H-InvDB	HIX0015973. HIX0022328.
HGNC	HGNC:9536. PSMA7.
MIM	606607. gene.
PharmGKB	PA33881.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O14818.
HOVERGEN	O14818.
OMA	O14818. HVFQVEY.
Enzyme and pathway databases
BRENDA	3.4.25.1. 247.
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	O14818.
Bgee	O14818.
CleanEx	HS_PSMA7.
GermOnline	ENSG00000101182. Homo sapiens.
Family and domain databases
InterPro	IPR001353. Proteasome_alpha_beta_su. IPR000426. Proteasome_asu_CS. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22094.
SOURCE	Search...

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Entry information

Entry name

PSA7_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents