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P25789

- PSA4_HUMAN

UniProt

P25789 - PSA4_HUMAN

Protein

Proteasome subunit alpha type-4

Gene

PSMA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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.

    Catalytic activityi

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

    GO - Molecular functioni

    1. 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

    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

    MEROPSiT01.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-4 (EC:3.4.25.1)
    Alternative name(s):
    Macropain subunit C9
    Multicatalytic endopeptidase complex subunit C9
    Proteasome component C9
    Proteasome subunit L
    Gene namesi
    Name:PSMA4
    Synonyms:HC9, PSC9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9533. PSMA4.

    Subcellular locationi

    Cytoplasm. Nucleus. CytoplasmP-body By similarity
    Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProt
    6. proteasome complex Source: ProtInc
    7. proteasome core complex Source: UniProtKB
    8. proteasome core complex, alpha-subunit complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33878.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Proteasome subunit alpha type-4PRO_0000124103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131Phosphoserine2 Publications
    Modified residuei75 – 751Phosphoserine1 Publication
    Modified residuei127 – 1271N6-acetyllysine1 Publication
    Modified residuei176 – 1761N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP25789.
    PaxDbiP25789.
    PRIDEiP25789.

    2D gel databases

    UCD-2DPAGEP25789.

    PTM databases

    PhosphoSiteiP25789.

    Expressioni

    Inductioni

    Down-regulated by antioxidants BO-653 and probucol.1 Publication

    Gene expression databases

    ArrayExpressiP25789.
    BgeeiP25789.
    CleanExiHS_PSMA4.
    GenevestigatoriP25789.

    Organism-specific databases

    HPAiCAB004973.

    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. Interaction with HTLV-1 TAX protein favors NFKB1 activation.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSMA1P257863EBI-359310,EBI-359352
    PSMA2P257877EBI-359310,EBI-603262
    PSMA3P257884EBI-359310,EBI-348380
    PSMA6P609004EBI-359310,EBI-357793
    PSMA7O148188EBI-359310,EBI-603272

    Protein-protein interaction databases

    BioGridi111658. 82 interactions.
    DIPiDIP-29365N.
    IntActiP25789. 19 interactions.
    MINTiMINT-5002513.
    STRINGi9606.ENSP00000044462.

    Structurei

    3D structure databases

    ProteinModelPortaliP25789.
    SMRiP25789. Positions 2-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiP25789.
    KOiK02728.
    OMAiKQEYKDD.
    PhylomeDBiP25789.
    TreeFamiTF106209.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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 1 (identifier: P25789-1) [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

    MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR    50
    NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ 100
    YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS 150
    DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAIKVLNKT 200
    MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE 250
    KKEKEQKEKD K 261
    Length:261
    Mass (Da):29,484
    Last modified:May 1, 1992 - v1
    Checksum:i7867422B1B31F3B9
    GO
    Isoform 2 (identifier: P25789-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:190
    Mass (Da):21,365
    Checksum:i0F5AC7AC01335F6A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7171Missing in isoform 2. 1 PublicationVSP_043102Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00763 mRNA. Translation: BAA00660.1.
    BT009784 mRNA. Translation: AAP88786.1.
    AC027228 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99163.1.
    CH471136 Genomic DNA. Translation: EAW99164.1.
    BC005361 mRNA. Translation: AAH05361.1.
    BC022445 mRNA. Translation: AAH22445.1.
    BC022817 mRNA. Translation: AAH22817.2.
    BC047667 mRNA. Translation: AAH47667.1.
    BC093069 mRNA. Translation: AAH93069.1.
    CCDSiCCDS10303.1. [P25789-1]
    CCDS45319.1. [P25789-2]
    PIRiS15972. SNHUC9.
    RefSeqiNP_001096137.1. NM_001102667.1. [P25789-1]
    NP_001096138.1. NM_001102668.1. [P25789-2]
    NP_002780.1. NM_002789.4. [P25789-1]
    UniGeneiHs.251531.

    Genome annotation databases

    EnsembliENST00000044462; ENSP00000044462; ENSG00000041357. [P25789-1]
    ENST00000413382; ENSP00000402118; ENSG00000041357. [P25789-2]
    ENST00000559082; ENSP00000453887; ENSG00000041357. [P25789-1]
    GeneIDi5685.
    KEGGihsa:5685.
    UCSCiuc002bdu.4. human. [P25789-1]

    Polymorphism databases

    DMDMi130861.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00763 mRNA. Translation: BAA00660.1 .
    BT009784 mRNA. Translation: AAP88786.1 .
    AC027228 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99163.1 .
    CH471136 Genomic DNA. Translation: EAW99164.1 .
    BC005361 mRNA. Translation: AAH05361.1 .
    BC022445 mRNA. Translation: AAH22445.1 .
    BC022817 mRNA. Translation: AAH22817.2 .
    BC047667 mRNA. Translation: AAH47667.1 .
    BC093069 mRNA. Translation: AAH93069.1 .
    CCDSi CCDS10303.1. [P25789-1 ]
    CCDS45319.1. [P25789-2 ]
    PIRi S15972. SNHUC9.
    RefSeqi NP_001096137.1. NM_001102667.1. [P25789-1 ]
    NP_001096138.1. NM_001102668.1. [P25789-2 ]
    NP_002780.1. NM_002789.4. [P25789-1 ]
    UniGenei Hs.251531.

    3D structure databases

    ProteinModelPortali P25789.
    SMRi P25789. Positions 2-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111658. 82 interactions.
    DIPi DIP-29365N.
    IntActi P25789. 19 interactions.
    MINTi MINT-5002513.
    STRINGi 9606.ENSP00000044462.

    Chemistry

    ChEMBLi CHEMBL2364701.

    Protein family/group databases

    MEROPSi T01.973.

    PTM databases

    PhosphoSitei P25789.

    Polymorphism databases

    DMDMi 130861.

    2D gel databases

    UCD-2DPAGE P25789.

    Proteomic databases

    MaxQBi P25789.
    PaxDbi P25789.
    PRIDEi P25789.

    Protocols and materials databases

    DNASUi 5685.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000044462 ; ENSP00000044462 ; ENSG00000041357 . [P25789-1 ]
    ENST00000413382 ; ENSP00000402118 ; ENSG00000041357 . [P25789-2 ]
    ENST00000559082 ; ENSP00000453887 ; ENSG00000041357 . [P25789-1 ]
    GeneIDi 5685.
    KEGGi hsa:5685.
    UCSCi uc002bdu.4. human. [P25789-1 ]

    Organism-specific databases

    CTDi 5685.
    GeneCardsi GC15P078832.
    HGNCi HGNC:9533. PSMA4.
    HPAi CAB004973.
    MIMi 176846. gene.
    neXtProti NX_P25789.
    PharmGKBi PA33878.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0638.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi P25789.
    KOi K02728.
    OMAi KQEYKDD.
    PhylomeDBi P25789.
    TreeFami TF106209.

    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 PSMA4. human.
    GeneWikii PSMA4.
    GenomeRNAii 5685.
    NextBioi 22078.
    PROi P25789.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25789.
    Bgeei P25789.
    CleanExi HS_PSMA4.
    Genevestigatori P25789.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR016050. Proteasome_bsu_CS.
    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. "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 1).
    2. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Blood, Brain, Lung, Pancreas and Urinary bladder.
    6. "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 18-39.
    7. "Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome."
      Rousset R., Desbois C., Bantignies F., Jalinot P.
      Nature 381:328-331(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX.
    8. "Gene expression induced by BO-653, probucol and BHQ in human endothelial cells."
      Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H., Hamakubo T., Niki E., Kodama T., Noguchi N.
      J. Atheroscler. Thromb. 7:223-230(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY BO-653 AND PROBUCOL.
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-127 AND LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPSA4_HUMAN
    AccessioniPrimary (citable) accession number: P25789
    Secondary accession number(s): D3DW86
    , Q53XP2, Q567Q5, Q8TBD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 156 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 15
      Human chromosome 15: 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