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P25786

- PSA1_HUMAN

UniProt

P25786 - PSA1_HUMAN

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Protein

Proteasome subunit alpha type-1

Gene

PSMA1

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. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  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

Immunity

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
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_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
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

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
30 kDa prosomal protein
Short name:
PROS-30
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu chain
Gene namesi
Name:PSMA1
Synonyms:HC2, NU, PROS30, PSC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:9530. PSMA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Proteasome subunit alpha type-1PRO_0000124060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei14 – 141Phosphoserine2 Publications
Glycosylationi110 – 1101O-linked (GlcNAc)By similarity
Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25786.
PaxDbiP25786.
PRIDEiP25786.

2D gel databases

OGPiP25786.
REPRODUCTION-2DPAGEIPI00016832.

PTM databases

PhosphoSiteiP25786.

Expressioni

Inductioni

Induced in breast cancer tissue (at protein level). Up-regulated in liver tumor tissues.3 Publications

Gene expression databases

BgeeiP25786.
CleanExiHS_PSMA1.
ExpressionAtlasiP25786. baseline.
GenevestigatoriP25786.

Organism-specific databases

HPAiHPA037646.
HPA043891.

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. Interacts with bacterial lipopolysaccharide (LPS) (By similarity). Interacts with NOTCH3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MTUS2Q5JR593EBI-359352,EBI-742948
PSMA2P257875EBI-359352,EBI-603262
PSMA3P257883EBI-359352,EBI-348380
PSMA4P257893EBI-359352,EBI-359310
PSMA7O148189EBI-359352,EBI-603272

Protein-protein interaction databases

BioGridi111655. 117 interactions.
DIPiDIP-29369N.
IntActiP25786. 55 interactions.
MINTiMINT-1155600.
STRINGi9606.ENSP00000315309.

Structurei

3D structure databases

ProteinModelPortaliP25786.
SMRiP25786. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiP25786.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiP25786.
TreeFamiTF106206.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Short (identifier: P25786-1) [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
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK
60 70 80 90 100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD
110 120 130 140 150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS
160 170 180 190 200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP
210 220 230 240 250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPAQPA
260
DEPAEKADEP MEH
Length:263
Mass (Da):29,556
Last modified:May 1, 1992 - v1
Checksum:i3F159C5BCEFE8DED
GO
Isoform Long (identifier: P25786-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQLSKVK

Show »
Length:269
Mass (Da):30,239
Checksum:iDB7435F82890F923
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152SP → TA in AAA92734. (PubMed:1398136)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371G → V.2 Publications
Corresponds to variant rs17850016 [ dbSNP | Ensembl ].
VAR_067454

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MQLSKVK in isoform Long. 1 PublicationVSP_005279

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61969 mRNA. Translation: CAA43961.1.
D00759 mRNA. Translation: BAA00656.1.
M64992 mRNA. Translation: AAA92734.1.
BT006647 mRNA. Translation: AAP35293.1.
AK290765 mRNA. Translation: BAF83454.1.
CH471064 Genomic DNA. Translation: EAW68479.1.
BC002577 mRNA. Translation: AAH02577.1.
BC005932 mRNA. Translation: AAH05932.1.
BC008472 mRNA. Translation: AAH08472.1.
BC009576 mRNA. Translation: AAH09576.1.
BC015105 mRNA. Translation: AAH15105.1.
BC015356 mRNA. Translation: AAH15356.1.
BC022372 mRNA. Translation: AAH22372.1.
CCDSiCCDS31431.1. [P25786-2]
CCDS7816.1. [P25786-1]
PIRiJC1445.
RefSeqiNP_002777.1. NM_002786.3. [P25786-1]
NP_683877.1. NM_148976.2. [P25786-2]
UniGeneiHs.102798.

Genome annotation databases

EnsembliENST00000396394; ENSP00000379676; ENSG00000129084. [P25786-1]
ENST00000418988; ENSP00000414359; ENSG00000129084. [P25786-2]
GeneIDi5682.
KEGGihsa:5682.
UCSCiuc001mlk.3. human. [P25786-1]
uc001mll.3. human. [P25786-2]

Polymorphism databases

DMDMi130848.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61969 mRNA. Translation: CAA43961.1 .
D00759 mRNA. Translation: BAA00656.1 .
M64992 mRNA. Translation: AAA92734.1 .
BT006647 mRNA. Translation: AAP35293.1 .
AK290765 mRNA. Translation: BAF83454.1 .
CH471064 Genomic DNA. Translation: EAW68479.1 .
BC002577 mRNA. Translation: AAH02577.1 .
BC005932 mRNA. Translation: AAH05932.1 .
BC008472 mRNA. Translation: AAH08472.1 .
BC009576 mRNA. Translation: AAH09576.1 .
BC015105 mRNA. Translation: AAH15105.1 .
BC015356 mRNA. Translation: AAH15356.1 .
BC022372 mRNA. Translation: AAH22372.1 .
CCDSi CCDS31431.1. [P25786-2 ]
CCDS7816.1. [P25786-1 ]
PIRi JC1445.
RefSeqi NP_002777.1. NM_002786.3. [P25786-1 ]
NP_683877.1. NM_148976.2. [P25786-2 ]
UniGenei Hs.102798.

3D structure databases

ProteinModelPortali P25786.
SMRi P25786. Positions 4-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111655. 117 interactions.
DIPi DIP-29369N.
IntActi P25786. 55 interactions.
MINTi MINT-1155600.
STRINGi 9606.ENSP00000315309.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.976.

PTM databases

PhosphoSitei P25786.

Polymorphism databases

DMDMi 130848.

2D gel databases

OGPi P25786.
REPRODUCTION-2DPAGE IPI00016832.

Proteomic databases

MaxQBi P25786.
PaxDbi P25786.
PRIDEi P25786.

Protocols and materials databases

DNASUi 5682.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000396394 ; ENSP00000379676 ; ENSG00000129084 . [P25786-1 ]
ENST00000418988 ; ENSP00000414359 ; ENSG00000129084 . [P25786-2 ]
GeneIDi 5682.
KEGGi hsa:5682.
UCSCi uc001mlk.3. human. [P25786-1 ]
uc001mll.3. human. [P25786-2 ]

Organism-specific databases

CTDi 5682.
GeneCardsi GC11M014526.
HGNCi HGNC:9530. PSMA1.
HPAi HPA037646.
HPA043891.
MIMi 602854. gene.
neXtProti NX_P25786.
PharmGKBi PA33875.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074855.
HOGENOMi HOG000091080.
HOVERGENi HBG105373.
InParanoidi P25786.
KOi K02725.
OMAi FMKQQCL.
OrthoDBi EOG7WQ7T1.
PhylomeDBi P25786.
TreeFami TF106206.

Enzyme and pathway databases

Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
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_206597. Degradation of GLI2 by the proteasome.
REACT_228111. Hedgehog ligand biogenesis.
REACT_228209. Hh ligand biogenesis disease.
REACT_231645. GLI3 is processed to GLI3R by the proteasome.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_267605. Degradation of GLI1 by the proteasome.
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 PSMA1. human.
GeneWikii Proteasome_(prosome,_macropain)_subunit,_alpha_1.
GenomeRNAii 5682.
NextBioi 22062.
PROi P25786.
SOURCEi Search...

Gene expression databases

Bgeei P25786.
CleanExi HS_PSMA1.
ExpressionAtlasi P25786. baseline.
Genevestigatori P25786.

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. "The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous."
    DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., Dawson P.A., Slaughter C.A.
    Biochim. Biophys. Acta 1079:29-38(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  2. "Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)."
    Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A.
    Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  3. "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human prosomes."
    Silva-Pereira I., Bey F., Coux O., Scherrer K.
    Gene 120:235-242(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "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], VARIANT VAL-37.
  5. "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 SHORT).
  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] (ISOFORM SHORT), VARIANT VAL-37.
    Tissue: Bone marrow, Brain, Ovary, Placenta and Prostate.
  8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
    Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
    Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 63-82.
  10. "Comparative proteome analysis of breast cancer and adjacent normal breast tissues in human."
    Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.
    Genomics Proteomics Bioinformatics 4:165-172(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
    Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
    Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Conserved signal peptide of Notch3 inhibits interaction with proteasome."
    Zhang Y., Jia L., Lee S.J., Wang M.M.
    Biochem. Biophys. Res. Commun. 355:245-251(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOTCH3.
  13. "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.
  14. "Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics."
    Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E., Yang H.
    Breast Cancer Res. Treat. 104:21-30(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSA1_HUMAN
AccessioniPrimary (citable) accession number: P25786
Secondary accession number(s): A8K400, Q53YE8, Q9BRV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 172 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3