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O14818

- PSA7_HUMAN

UniProt

O14818 - PSA7_HUMAN

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Protein

Proteasome subunit alpha type-7

Gene

PSMA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. gene expression Source: Reactome
  10. mitotic cell cycle Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. protein polyubiquitination Source: Reactome
  16. regulation of apoptotic process Source: Reactome
  17. regulation of cellular amino acid metabolic process Source: Reactome
  18. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  19. RNA metabolic process Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7 (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit RC6-1
Proteasome subunit XAPC7
Gene namesi
Name:PSMA7
Synonyms:HSPC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9536. PSMA7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProt
  5. proteasome complex Source: UniProtKB
  6. proteasome core complex Source: UniProtKB
  7. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531Y → F: Displays impaired G1/S transition and S/G2 progression. 1 Publication

Organism-specific databases

PharmGKBiPA33881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Proteasome subunit alpha type-7PRO_0000124142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi130 – 1301O-linked (GlcNAc)By similarity
Modified residuei153 – 1531Phosphotyrosine; by ABL1 and ABL21 Publication
Modified residuei227 – 2271N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO14818.
PaxDbiO14818.
PRIDEiO14818.

2D gel databases

REPRODUCTION-2DPAGEIPI00024175.
UCD-2DPAGEO14818.

PTM databases

PhosphoSiteiO14818.

Expressioni

Inductioni

Down-regulated by the ribozyme Rz3'X. Up-regulated in colorectal cancer tissues.2 Publications

Gene expression databases

BgeeiO14818.
CleanExiHS_PSMA7.
GenevestigatoriO14818.

Organism-specific databases

HPAiHPA047266.

Interactioni

Subunit structurei

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.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-603272,EBI-603272
PSMA1P257869EBI-603272,EBI-359352
PSMA2P257875EBI-603272,EBI-603262
PSMA3P257886EBI-603272,EBI-348380
PSMA4P257898EBI-603272,EBI-359310
PSMA5P280662EBI-603272,EBI-355475
PSMA6P6090011EBI-603272,EBI-357793

Protein-protein interaction databases

BioGridi111661. 102 interactions.
DIPiDIP-29363N.
IntActiO14818. 29 interactions.
MINTiMINT-5000782.
STRINGi9606.ENSP00000359910.

Structurei

3D structure databases

ProteinModelPortaliO14818.
SMRiO14818. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiO14818.
KOiK02731.
OMAiITRHIAG.
PhylomeDBiO14818.
TreeFamiTF106212.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: O14818-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV
60 70 80 90 100
AKLQDERTVR KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED
110 120 130 140 150
PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS
160 170 180 190 200
GTYHAWKANA IGRGAKSVRE FLEKNYTDEA IETDDLTIKL VIKALLEVVQ
210 220 230 240
SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE KKKQKKAS
Length:248
Mass (Da):27,887
Last modified:January 1, 1998 - v1
Checksum:i5DD0276A1C2DEF91
GO
Isoform 2 (identifier: O14818-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:178
Mass (Da):20,193
Checksum:iA4A7D8924670D890
GO
Isoform 3 (identifier: O14818-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-149: RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP → VGACPLACSPLAAGQSRLRHGGSCHVTSGESEN
     150-248: Missing.

Show »
Length:149
Mass (Da):16,135
Checksum:i90D6129907EDE5C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601A → S in AAC99402. (PubMed:11042152)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7070Missing in isoform 2. CuratedVSP_005281Add
BLAST
Alternative sequencei117 – 14933RYTQS…YQTDP → VGACPLACSPLAAGQSRLRH GGSCHVTSGESEN in isoform 3. 1 PublicationVSP_046556Add
BLAST
Alternative sequencei150 – 24899Missing in isoform 3. 1 PublicationVSP_046557Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BI906714 mRNA. No translation available.
CCDSiCCDS13489.1. [O14818-1]
PIRiPC2326.
RefSeqiNP_002783.1. NM_002792.3. [O14818-1]
UniGeneiHs.233952.

Genome annotation databases

EnsembliENST00000370858; ENSP00000359895; ENSG00000101182. [O14818-4]
ENST00000370861; ENSP00000359898; ENSG00000101182. [O14818-2]
ENST00000370873; ENSP00000359910; ENSG00000101182. [O14818-1]
GeneIDi5688.
KEGGihsa:5688.
UCSCiuc002ybx.2. human. [O14818-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
BI906714 mRNA. No translation available.
CCDSi CCDS13489.1. [O14818-1 ]
PIRi PC2326.
RefSeqi NP_002783.1. NM_002792.3. [O14818-1 ]
UniGenei Hs.233952.

3D structure databases

ProteinModelPortali O14818.
SMRi O14818. Positions 2-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111661. 102 interactions.
DIPi DIP-29363N.
IntActi O14818. 29 interactions.
MINTi MINT-5000782.
STRINGi 9606.ENSP00000359910.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.979.

PTM databases

PhosphoSitei O14818.

2D gel databases

REPRODUCTION-2DPAGE IPI00024175.
UCD-2DPAGE O14818.

Proteomic databases

MaxQBi O14818.
PaxDbi O14818.
PRIDEi O14818.

Protocols and materials databases

DNASUi 5688.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370858 ; ENSP00000359895 ; ENSG00000101182 . [O14818-4 ]
ENST00000370861 ; ENSP00000359898 ; ENSG00000101182 . [O14818-2 ]
ENST00000370873 ; ENSP00000359910 ; ENSG00000101182 . [O14818-1 ]
GeneIDi 5688.
KEGGi hsa:5688.
UCSCi uc002ybx.2. human. [O14818-1 ]

Organism-specific databases

CTDi 5688.
GeneCardsi GC20M060711.
HGNCi HGNC:9536. PSMA7.
HPAi HPA047266.
MIMi 606607. gene.
neXtProti NX_O14818.
PharmGKBi PA33881.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074753.
HOGENOMi HOG000091085.
HOVERGENi HBG003005.
InParanoidi O14818.
KOi K02731.
OMAi ITRHIAG.
PhylomeDBi O14818.
TreeFami TF106212.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMA7. human.
GeneWikii PSMA7.
GenomeRNAii 5688.
NextBioi 22094.
PROi O14818.
SOURCEi Search...

Gene expression databases

Bgeei O14818.
CleanExi HS_PSMA7.
Genevestigatori O14818.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] (ISOFORMS 1 AND 3).
    Tissue: Leukocyte and Lung.
  8. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 96-109, IDENTIFICATION BY 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. 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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSA7_HUMAN
AccessioniPrimary (citable) accession number: O14818
Secondary accession number(s): B2R515
, Q5JXJ2, Q9BR53, Q9H4K5, Q9UEU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3