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P06454

- PTMA_HUMAN

UniProt

P06454 - PTMA_HUMAN

Protein

Prothymosin alpha

Gene

PTMA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.

    GO - Biological processi

    1. transcription, DNA-templated Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prothymosin alpha
    Cleaved into the following 2 chains:
    Gene namesi
    Name:PTMA
    Synonyms:TMSA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9623. PTMA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33966.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 111111Prothymosin alphaPRO_0000423255Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate8 Publications
    Chaini2 – 111110Prothymosin alpha, N-terminally processedPRO_0000299250Add
    BLAST
    Peptidei2 – 2928Thymosin alpha-1PRO_0000029865Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylserine; in Prothymosin alpha, N-terminally processed9 Publications
    Modified residuei2 – 21Phosphoserine6 Publications
    Modified residuei8 – 81PhosphothreonineBy similarity
    Modified residuei9 – 91Phosphoserine1 Publication
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei13 – 131PhosphothreonineBy similarity
    Modified residuei14 – 141PhosphothreonineBy similarity
    Modified residuei15 – 151N6-acetyllysine; alternate1 Publication
    Modified residuei15 – 151N6-succinyllysine; alternateBy similarity
    Modified residuei102 – 1021Phosphothreonine1 Publication
    Modified residuei103 – 1031N6-acetyllysineBy similarity
    Modified residuei107 – 1071Phosphothreonine1 Publication

    Post-translational modificationi

    Covalently linked to a small RNA of about 20 nucleotides.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06454.
    PaxDbiP06454.
    PRIDEiP06454.

    PTM databases

    PhosphoSiteiP06454.

    Miscellaneous databases

    PMAP-CutDBP06454.

    Expressioni

    Gene expression databases

    BgeeiP06454.
    CleanExiHS_PTMA.
    GenevestigatoriP06454.

    Organism-specific databases

    HPAiHPA047183.

    Interactioni

    Protein-protein interaction databases

    BioGridi111724. 63 interactions.
    IntActiP06454. 6 interactions.
    MINTiMINT-138772.
    STRINGi9606.ENSP00000344547.

    Structurei

    Secondary structure

    1
    111
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64
    Helixi9 – 2820

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L9INMR-A2-29[»]
    ProteinModelPortaliP06454.
    SMRiP06454. Positions 2-29.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi42 – 10160Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the pro/parathymosin family.Curated

    Phylogenomic databases

    eggNOGiNOG259527.
    HOGENOMiHOG000089972.
    KOiK13784.
    TreeFamiTF350357.

    Family and domain databases

    InterProiIPR004931. Pro/parathymosin.
    [Graphical view]
    PANTHERiPTHR22745. PTHR22745. 1 hit.
    PfamiPF03247. Prothymosin. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06454-1) [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

    MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAE NEENGEQEAD    50
    NEVDEEEEEG GEEEEEEEEG DGEEEDGDED EEAESATGKR AAEDDEDDDV 100
    DTKKQKTDED D 111
    Length:111
    Mass (Da):12,203
    Last modified:January 23, 2007 - v2
    Checksum:i910BBF9D8D14B8E7
    GO
    Isoform 2 (identifier: P06454-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         40-40: Missing.

    Show »
    Length:110
    Mass (Da):12,074
    Checksum:i3A76436E79930993
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei40 – 401Missing in isoform 2. 4 PublicationsVSP_011508

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14630 mRNA. Translation: AAA61182.1.
    M14483 mRNA. Translation: AAA61183.1.
    M67480, J04797 Genomic DNA. Translation: AAA63240.1.
    M67480, J04797 Genomic DNA. Translation: AAA63239.1.
    M26708 mRNA. Translation: AAA60213.1.
    AF348514 mRNA. Translation: AAK30146.1.
    BC051265 mRNA. Translation: AAH51265.1.
    BC066905 mRNA. Translation: AAH66905.1.
    BC070480 mRNA. Translation: AAH70480.1.
    BC071647 mRNA. Translation: AAH71647.1.
    BC071879 mRNA. Translation: AAH71879.1.
    S56449 Genomic DNA. Translation: AAD13882.1.
    CCDSiCCDS42833.1. [P06454-1]
    CCDS46541.1. [P06454-2]
    PIRiA42004. TNHUA.
    C33356.
    RefSeqiNP_001092755.1. NM_001099285.1. [P06454-1]
    NP_002814.3. NM_002823.4. [P06454-2]
    UniGeneiHs.459927.

    Genome annotation databases

    EnsembliENST00000341369; ENSP00000344547; ENSG00000187514. [P06454-1]
    ENST00000409115; ENSP00000386819; ENSG00000187514. [P06454-2]
    GeneIDi5757.
    KEGGihsa:5757.
    UCSCiuc002vsc.4. human. [P06454-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14630 mRNA. Translation: AAA61182.1 .
    M14483 mRNA. Translation: AAA61183.1 .
    M67480 , J04797 Genomic DNA. Translation: AAA63240.1 .
    M67480 , J04797 Genomic DNA. Translation: AAA63239.1 .
    M26708 mRNA. Translation: AAA60213.1 .
    AF348514 mRNA. Translation: AAK30146.1 .
    BC051265 mRNA. Translation: AAH51265.1 .
    BC066905 mRNA. Translation: AAH66905.1 .
    BC070480 mRNA. Translation: AAH70480.1 .
    BC071647 mRNA. Translation: AAH71647.1 .
    BC071879 mRNA. Translation: AAH71879.1 .
    S56449 Genomic DNA. Translation: AAD13882.1 .
    CCDSi CCDS42833.1. [P06454-1 ]
    CCDS46541.1. [P06454-2 ]
    PIRi A42004. TNHUA.
    C33356.
    RefSeqi NP_001092755.1. NM_001099285.1. [P06454-1 ]
    NP_002814.3. NM_002823.4. [P06454-2 ]
    UniGenei Hs.459927.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L9I NMR - A 2-29 [» ]
    ProteinModelPortali P06454.
    SMRi P06454. Positions 2-29.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111724. 63 interactions.
    IntActi P06454. 6 interactions.
    MINTi MINT-138772.
    STRINGi 9606.ENSP00000344547.

    PTM databases

    PhosphoSitei P06454.

    Proteomic databases

    MaxQBi P06454.
    PaxDbi P06454.
    PRIDEi P06454.

    Protocols and materials databases

    DNASUi 5757.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341369 ; ENSP00000344547 ; ENSG00000187514 . [P06454-1 ]
    ENST00000409115 ; ENSP00000386819 ; ENSG00000187514 . [P06454-2 ]
    GeneIDi 5757.
    KEGGi hsa:5757.
    UCSCi uc002vsc.4. human. [P06454-1 ]

    Organism-specific databases

    CTDi 5757.
    GeneCardsi GC02P232536.
    HGNCi HGNC:9623. PTMA.
    HPAi HPA047183.
    MIMi 188390. gene.
    neXtProti NX_P06454.
    PharmGKBi PA33966.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259527.
    HOGENOMi HOG000089972.
    KOi K13784.
    TreeFami TF350357.

    Miscellaneous databases

    ChiTaRSi PTMA. human.
    GeneWikii Thymosin_%CE%B11.
    GenomeRNAii 5757.
    NextBioi 22406.
    PMAP-CutDB P06454.
    PROi P06454.
    SOURCEi Search...

    Gene expression databases

    Bgeei P06454.
    CleanExi HS_PTMA.
    Genevestigatori P06454.

    Family and domain databases

    InterProi IPR004931. Pro/parathymosin.
    [Graphical view ]
    PANTHERi PTHR22745. PTHR22745. 1 hit.
    Pfami PF03247. Prothymosin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human prothymosin alpha gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA."
      Eschenfeldt W.H., Berger S.L.
      Proc. Natl. Acad. Sci. U.S.A. 83:9403-9407(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Isolation and partial sequencing of the human prothymosin alpha gene family. Evidence against export of the gene products."
      Eschenfeldt W.H., Manrow R.E., Krug M.S., Berger S.L.
      J. Biol. Chem. 264:7546-7555(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    4. "The expression of prothymosin alpha gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation."
      Gomez-Marquez J., Segade F., Dosil M., Pichel J.G., Bustelo X.R., Freire M.
      J. Biol. Chem. 264:8451-8454(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "A novel prothymosin alpha cDNA from thymus."
      Li Z., Fan Q., Huang W., An L.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal thymus.
    6. "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 2).
      Tissue: Cervix, Lung, PNS, Skin and Testis.
    7. "Prothymosin alpha gene in humans: organization of its promoter region and localization to chromosome 2."
      Szabo P., Panneerselvam C., Clinton M., Frangou-Lazaridis M., Weksler D., Whittington E., Macera M.J., Grzeschik K.H., Selvakumar A., Horecker B.L.
      Hum. Genet. 90:629-634(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
    8. Cited for: PARTIAL PROTEIN SEQUENCE.
    9. Cited for: PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2.
    10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 SER-2 AND THR-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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 SER-2 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: STRUCTURE BY NMR OF 2-29, ACETYLATION AT SER-2.

    Entry informationi

    Entry nameiPTMA_HUMAN
    AccessioniPrimary (citable) accession number: P06454
    Secondary accession number(s): Q15249, Q15592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 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

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

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3