Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25786

- PSA1_HUMAN

UniProt

P25786 - PSA1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: UniProtKB
    2. RNA binding Source: ProtInc
    3. 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

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Keywords - Biological processi

    Immunity

    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

    MEROPSiT01.976.

    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: UniProt
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. polysome Source: ProtInc
    7. proteasome complex Source: ProtInc
    8. proteasome core complex Source: UniProtKB
    9. proteasome core complex, alpha-subunit complex Source: InterPro

    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.
    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. 106 interactions.
    DIPiDIP-29369N.
    IntActiP25786. 54 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.
    HOGENOMiHOG000091080.
    HOVERGENiHBG105373.
    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

    MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK    50
    RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD 100
    RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS 150
    ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP 200
    AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPAQPA 250
    DEPAEKADEP MEH 263
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 106 interactions.
    DIPi DIP-29369N.
    IntActi P25786. 54 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.
    HOGENOMi HOG000091080.
    HOVERGENi HBG105373.
    KOi K02725.
    OMAi FMKQQCL.
    OrthoDBi EOG7WQ7T1.
    PhylomeDBi P25786.
    TreeFami TF106206.

    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 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.
    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

    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: October 1, 2014
    This is version 170 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