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)

Q9UQ80

- PA2G4_HUMAN

UniProt

Q9UQ80 - PA2G4_HUMAN

Protein

Proliferation-associated protein 2G4

Gene

PA2G4

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 146 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May play a role in a ERBB3-regulated signal transduction pathway. Seems be involved in growth regulation. Acts a corepressor of the androgen receptor (AR) and is regulated by the ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription of some E2F1-regulated promoters, probably by recruiting histone acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and 5.8S mature rRNAs, several rRNA precursors and probably U3 small nucleolar RNA. May be involved in regulation of intermediate and late steps of rRNA processing. May be involved in ribosome assembly. Mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site) By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. sequence-specific DNA binding transcription factor activity Source: MGI
    5. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. cell proliferation Source: ProtInc
    3. negative regulation of transcription, DNA-templated Source: MGI
    4. regulation of translation Source: UniProtKB-KW
    5. rRNA processing Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein

    Keywords - Biological processi

    rRNA processing, Transcription, Transcription regulation, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Protein family/group databases

    MEROPSiM24.973.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proliferation-associated protein 2G4
    Alternative name(s):
    Cell cycle protein p38-2G4 homolog
    Short name:
    hG4-1
    ErbB3-binding protein 1
    Gene namesi
    Name:PA2G4
    Synonyms:EBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8550. PA2G4.

    Subcellular locationi

    Cytoplasm. Nucleusnucleolus
    Note: Tranlocates to the nucleus upon treatment with HRG.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleolus Source: UniProtKB
    5. nucleus Source: MGI
    6. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 223KYK → AYA: Loss of nucleolar localization. 1 Publication
    Mutagenesisi363 – 3631S → A: No effect on in vitro phosphorylation by PKC. 2 Publications
    Mutagenesisi364 – 3652RK → AA: Only partial nucleolar localization. 1 Publication
    Mutagenesisi366 – 3661T → A: Decreases in vitro phosphorylation by PKC. 2 Publications

    Organism-specific databases

    PharmGKBiPA32877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 394393Proliferation-associated protein 2G4PRO_0000148989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine6 Publications
    Modified residuei2 – 21Phosphoserine4 Publications
    Modified residuei361 – 3611Phosphoserine3 Publications
    Modified residuei366 – 3661Phosphothreonine1 Publication
    Modified residuei386 – 3861Phosphothreonine7 Publications

    Post-translational modificationi

    Phosphorylated on serine and threonine residues. Phosphorylation is enhanced by HRG treatment. Basal phosphorylation is PKC-dependent and HRG-induced phosphorylation is predominantly PKC-independent.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UQ80.
    PaxDbiQ9UQ80.
    PRIDEiQ9UQ80.

    2D gel databases

    SWISS-2DPAGEQ9UQ80.

    PTM databases

    PhosphoSiteiQ9UQ80.

    Expressioni

    Tissue specificityi

    Expressed in several cell lines tested, including primary and transformed cell lines.1 Publication

    Gene expression databases

    ArrayExpressiQ9UQ80.
    BgeeiQ9UQ80.
    CleanExiHS_PA2G4.
    GenevestigatoriQ9UQ80.

    Organism-specific databases

    HPAiCAB011711.
    CAB012428.
    HPA016484.

    Interactioni

    Subunit structurei

    Interacts with the cytoplasmic domain of non-phosphorylated ERBB3; the interaction requires PKC activity. Interacts with AR. Treatment with HRG leads to dissociation from ERBB3 and increases association with AR. Interacts with NCL/nucleolin. Component of a ribonucleoprotein complex containing at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1 (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18, RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24. Interacts with HDAC2. Interacts with RB1; the interaction is enhanced upon PA2G4 dephosphorylation.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCLP193382EBI-924893,EBI-346967
    RB1P064004EBI-924893,EBI-491274
    SIN3AQ96ST34EBI-924893,EBI-347218

    Protein-protein interaction databases

    BioGridi111075. 77 interactions.
    IntActiQ9UQ80. 43 interactions.
    MINTiMINT-5000754.
    STRINGi9606.ENSP00000302886.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 3824
    Helixi45 – 6117
    Beta strandi72 – 8211
    Beta strandi85 – 873
    Beta strandi105 – 11410
    Beta strandi117 – 12610
    Helixi137 – 15620
    Helixi163 – 17513
    Turni176 – 1783
    Beta strandi186 – 1916
    Beta strandi194 – 1963
    Beta strandi200 – 2045
    Helixi207 – 2126
    Beta strandi223 – 23311
    Beta strandi246 – 2494
    Helixi260 – 27314
    Helixi280 – 2823
    Helixi287 – 29812
    Beta strandi301 – 3055
    Beta strandi316 – 32611
    Beta strandi329 – 3324
    Helixi340 – 3423
    Helixi352 – 3598

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q8KX-ray1.60A2-394[»]
    3J2Ielectron microscopy11.90A1-394[»]
    ProteinModelPortaliQ9UQ80.
    SMRiQ9UQ80. Positions 7-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UQ80.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 4847Necessary for nucleolar localizationAdd
    BLAST
    Regioni46 – 549RNA-binding
    Regioni301 – 39494Necessary for nucleolar localizationAdd
    BLAST
    Regioni361 – 37515Interaction with RNABy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M24 family.Curated

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000168207.
    HOVERGENiHBG053117.
    InParanoidiQ9UQ80.
    OMAiICHFSPI.
    OrthoDBiEOG7SFHXD.
    PhylomeDBiQ9UQ80.
    TreeFamiTF300010.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    InterProiIPR004545. Pap_1.
    IPR000994. Pept_M24_structural-domain.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00495. crvDNA_42K. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UQ80-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE    50
    KGDAMIMEET GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL 100
    KEGDLVKIDL GVHVDGFIAN VAHTFVVDVA QGTQVTGRKA DVIKAAHLCA 150
    EAALRLVKPG NQNTQVTEAW NKVAHSFNCT PIEGMLSHQL KQHVIDGEKT 200
    IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA GQRTTIYKRD 250
    PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE 300
    LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ 350
    DAELKALLQS SASRKTQKKK KKKASKTAEN ATSGETLEEN EAGD 394
    Length:394
    Mass (Da):43,787
    Last modified:January 23, 2007 - v3
    Checksum:iCD45466507AD6047
    GO

    Sequence cautioni

    The sequence AAD00646.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti381 – 3811A → P in AAB91536. (PubMed:9345902)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59435 mRNA. Translation: AAB91536.1.
    U87954 mRNA. Translation: AAD00646.1. Different initiation.
    AF104670, AF104668, AF104669 Genomic DNA. Translation: AAD05561.1.
    BC001951 mRNA. Translation: AAH01951.1.
    BC007561 mRNA. Translation: AAH07561.1.
    BC069786 mRNA. Translation: AAH69786.1.
    CCDSiCCDS8902.1.
    RefSeqiNP_006182.2. NM_006191.2.
    UniGeneiHs.524498.
    Hs.745109.

    Genome annotation databases

    EnsembliENST00000303305; ENSP00000302886; ENSG00000170515.
    GeneIDi5036.
    KEGGihsa:5036.
    UCSCiuc001sjm.3. human.

    Polymorphism databases

    DMDMi13632817.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59435 mRNA. Translation: AAB91536.1 .
    U87954 mRNA. Translation: AAD00646.1 . Different initiation.
    AF104670 , AF104668 , AF104669 Genomic DNA. Translation: AAD05561.1 .
    BC001951 mRNA. Translation: AAH01951.1 .
    BC007561 mRNA. Translation: AAH07561.1 .
    BC069786 mRNA. Translation: AAH69786.1 .
    CCDSi CCDS8902.1.
    RefSeqi NP_006182.2. NM_006191.2.
    UniGenei Hs.524498.
    Hs.745109.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q8K X-ray 1.60 A 2-394 [» ]
    3J2I electron microscopy 11.90 A 1-394 [» ]
    ProteinModelPortali Q9UQ80.
    SMRi Q9UQ80. Positions 7-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111075. 77 interactions.
    IntActi Q9UQ80. 43 interactions.
    MINTi MINT-5000754.
    STRINGi 9606.ENSP00000302886.

    Protein family/group databases

    MEROPSi M24.973.

    PTM databases

    PhosphoSitei Q9UQ80.

    Polymorphism databases

    DMDMi 13632817.

    2D gel databases

    SWISS-2DPAGE Q9UQ80.

    Proteomic databases

    MaxQBi Q9UQ80.
    PaxDbi Q9UQ80.
    PRIDEi Q9UQ80.

    Protocols and materials databases

    DNASUi 5036.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303305 ; ENSP00000302886 ; ENSG00000170515 .
    GeneIDi 5036.
    KEGGi hsa:5036.
    UCSCi uc001sjm.3. human.

    Organism-specific databases

    CTDi 5036.
    GeneCardsi GC12P056498.
    HGNCi HGNC:8550. PA2G4.
    HPAi CAB011711.
    CAB012428.
    HPA016484.
    MIMi 602145. gene.
    neXtProti NX_Q9UQ80.
    PharmGKBi PA32877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000168207.
    HOVERGENi HBG053117.
    InParanoidi Q9UQ80.
    OMAi ICHFSPI.
    OrthoDBi EOG7SFHXD.
    PhylomeDBi Q9UQ80.
    TreeFami TF300010.

    Miscellaneous databases

    EvolutionaryTracei Q9UQ80.
    GeneWikii PA2G4.
    GenomeRNAii 5036.
    NextBioi 19404.
    PROi Q9UQ80.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQ80.
    Bgeei Q9UQ80.
    CleanExi HS_PA2G4.
    Genevestigatori Q9UQ80.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    InterProi IPR004545. Pap_1.
    IPR000994. Pept_M24_structural-domain.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00495. crvDNA_42K. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a protein highly homologous to the mouse cell cycle protein p38-2G4."
      Lamartine J., Seri M., Cinti R., Heitzmann F., Creaven M., Radomski N., Jost E., Lenoir G.M., Romeo G., Sylla B.S.
      Cytogenet. Cell Genet. 78:31-35(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin."
      Yoo J.Y., Wang X.W., Rishi A.K., Lessor T., Xia X.M., Gustafson T.A., Hamburger A.W.
      Br. J. Cancer 82:683-690(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ERBB3, SUBCELLULAR LOCATION.
      Tissue: Brain.
    3. "Genomic structure of the human PA2G4 gene."
      Caroli F., Lamartine J., Sylla B.S., Romeo G., Seri M.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
      Tissue: Lung and Skin.
    5. Cited for: PROTEIN SEQUENCE OF 2-20; 23-30; 34-62; 73-101; 156-172; 200-211; 216-236; 264-281 AND 299-364, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma, Mammary carcinoma and Ovarian carcinoma.
    6. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 34-51; 216-236; 264-271; 299-311; 333-344 AND 377-394, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    7. "Regulation of the ErbB3 binding protein Ebp1 by protein kinase C."
      Lessor T.J., Hamburger A.W.
      Mol. Cell. Endocrinol. 175:185-191(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB3, PHOSPHORYLATION, PHOSPHORYLATION BY PKC, PHOSPHORYLATION AT THR-366, MUTAGENESIS OF SER-363 AND THR-366.
    8. "Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation."
      Xia X., Cheng A., Lessor T., Zhang Y., Hamburger A.W.
      J. Cell. Physiol. 187:209-217(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH RB1.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases."
      Zhang Y., Woodford N., Xia X., Hamburger A.W.
      Nucleic Acids Res. 31:2168-2177(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN E2F1-MEDIATED TRANSCRIPTION REPRESSION, INTERACTION WITH HDAC2.
    11. "EBP1 is a nucleolar growth-regulating protein that is part of pre-ribosomal ribonucleoprotein complexes."
      Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.
      Oncogene 23:4454-4465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RRNA PROCESSING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING, IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX, ASSOCIATION WITH RRNA, ASSOCIATION WITH U3 SNORNA, MUTAGENESIS OF 20-LYS--LYS-22 AND 364-ARG-LYS-365.
    12. "Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling."
      Zhang Y., Hamburger A.W.
      Br. J. Cancer 92:140-146(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH ERBB3 AND AR.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-361 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions."
      Kowalinski E., Bange G., Bradatsch B., Hurt E., Wild K., Sinning I.
      FEBS Lett. 581:4450-4454(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH 5S RIBOSOMAL RNA, LACK OF METAL COFACTOR, LACK OF AMINOPEPTIDASE ACTIVITY.

    Entry informationi

    Entry nameiPA2G4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQ80
    Secondary accession number(s): O43846, Q9UM59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 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

    Caution

    Although it belongs to the peptidase M24 family, it does not contain metal cofactors and lacks aminopeptidase activity.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3