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P26350

- PTMA_MOUSE

UniProt

P26350 - PTMA_MOUSE

Protein

Prothymosin alpha

Gene

Ptma

Organism
Mus musculus (Mouse)
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 - Molecular functioni

    1. histone binding Source: MGI

    GO - Biological processi

    1. histone exchange Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prothymosin alpha
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Ptma
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:97803. Ptma.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 111111Prothymosin alphaPRO_0000423256Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate2 Publications
    Chaini2 – 111110Prothymosin alpha, N-terminally processedPRO_0000299251Add
    BLAST
    Peptidei2 – 2928Thymosin alphaPRO_0000029866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylserine; in Prothymosin alpha, N-terminally processed1 Publication
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei8 – 81PhosphothreonineBy similarity
    Modified residuei9 – 91PhosphoserineBy similarity
    Modified residuei10 – 101PhosphoserineBy similarity
    Modified residuei13 – 131PhosphothreonineBy similarity
    Modified residuei14 – 141PhosphothreonineBy similarity
    Modified residuei15 – 151N6-acetyllysine; alternate1 Publication
    Modified residuei15 – 151N6-succinyllysine; alternate1 Publication
    Modified residuei102 – 1021PhosphothreonineBy similarity
    Modified residuei103 – 1031N6-acetyllysine1 Publication
    Modified residuei107 – 1071PhosphothreonineBy similarity

    Post-translational modificationi

    Covalently linked to a small RNA of about 20 nucleotides.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26350.
    PaxDbiP26350.
    PRIDEiP26350.

    PTM databases

    PhosphoSiteiP26350.

    Miscellaneous databases

    PMAP-CutDBP26350.

    Expressioni

    Gene expression databases

    BgeeiP26350.
    CleanExiMM_PTMA.
    GenevestigatoriP26350.

    Interactioni

    Protein-protein interaction databases

    BioGridi202469. 4 interactions.

    Structurei

    Secondary structure

    1
    111
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni42 – 443

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z32X-ray2.00B39-54[»]
    ProteinModelPortaliP26350.
    SMRiP26350. Positions 2-29.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26350.

    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

    eggNOGiNOG44821.
    HOVERGENiHBG078507.
    InParanoidiP26350.
    KOiK13784.
    OMAiSERCHIS.
    OrthoDBiEOG70PC27.
    TreeFamiTF350357.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P26350-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAQ NEENGEQEAD    50
    NEVDEEEEEG GEEEEEEEEG DGEEEDGDED EEAEAPTGKR VAEDDEDDDV 100
    DTKKQKTEED D 111
    Length:111
    Mass (Da):12,254
    Last modified:January 23, 2007 - v2
    Checksum:i345FACE953A3E8FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061K → KK AA sequence (PubMed:2226839)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56135 mRNA. Translation: CAA39601.1.
    AK037980 mRNA. Translation: BAC29913.1.
    AK084218 mRNA. Translation: BAC39141.1.
    AK132003 mRNA. Translation: BAE20932.1.
    AK142076 mRNA. Translation: BAE24932.1.
    AK145650 mRNA. Translation: BAE26566.1.
    AK153953 mRNA. Translation: BAE32276.1.
    BC081453 mRNA. Translation: AAH81453.1.
    BC083135 mRNA. Translation: AAH83135.1.
    CCDSiCCDS35649.1.
    PIRiS15073.
    RefSeqiNP_032998.1. NM_008972.2.
    UniGeneiMm.19187.

    Genome annotation databases

    EnsembliENSMUST00000045897; ENSMUSP00000044188; ENSMUSG00000026238.
    GeneIDi19231.
    KEGGimmu:19231.
    UCSCiuc007bvp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56135 mRNA. Translation: CAA39601.1 .
    AK037980 mRNA. Translation: BAC29913.1 .
    AK084218 mRNA. Translation: BAC39141.1 .
    AK132003 mRNA. Translation: BAE20932.1 .
    AK142076 mRNA. Translation: BAE24932.1 .
    AK145650 mRNA. Translation: BAE26566.1 .
    AK153953 mRNA. Translation: BAE32276.1 .
    BC081453 mRNA. Translation: AAH81453.1 .
    BC083135 mRNA. Translation: AAH83135.1 .
    CCDSi CCDS35649.1.
    PIRi S15073.
    RefSeqi NP_032998.1. NM_008972.2.
    UniGenei Mm.19187.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z32 X-ray 2.00 B 39-54 [» ]
    ProteinModelPortali P26350.
    SMRi P26350. Positions 2-29.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202469. 4 interactions.

    PTM databases

    PhosphoSitei P26350.

    Proteomic databases

    MaxQBi P26350.
    PaxDbi P26350.
    PRIDEi P26350.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045897 ; ENSMUSP00000044188 ; ENSMUSG00000026238 .
    GeneIDi 19231.
    KEGGi mmu:19231.
    UCSCi uc007bvp.1. mouse.

    Organism-specific databases

    CTDi 5757.
    MGIi MGI:97803. Ptma.

    Phylogenomic databases

    eggNOGi NOG44821.
    HOVERGENi HBG078507.
    InParanoidi P26350.
    KOi K13784.
    OMAi SERCHIS.
    OrthoDBi EOG70PC27.
    TreeFami TF350357.

    Miscellaneous databases

    ChiTaRSi PTMA. mouse.
    EvolutionaryTracei P26350.
    NextBioi 296040.
    PMAP-CutDB P26350.
    PROi P26350.
    SOURCEi Search...

    Gene expression databases

    Bgeei P26350.
    CleanExi MM_PTMA.
    Genevestigatori P26350.

    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. "Nucleotide sequence of the murine prothymosin alpha cDNA and its deduced primary and secondary protein structure."
      Schmidt G., Werner D.
      Biochim. Biophys. Acta 1088:442-444(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Eye and Thymus.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain and Limb.
    4. "Depression of prothymosin alpha production in murine thymus correlates with staphylococcal enterotoxin-B-induced immunosuppression."
      Low T.L.K., Pan T.L., Lin Y.S.
      FEBS Lett. 273:1-5(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-111.
    5. "Prothymosin alpha is an evolutionary conserved protein covalently linked to a small RNA."
      Makarova T., Grebenshikov N., Egorov C., Vartapetian A., Bogdanov A.
      FEBS Lett. 257:247-250(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-18; 22-68 AND 91-103.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-15 AND LYS-103, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPTMA_MOUSE
    AccessioniPrimary (citable) accession number: P26350
    Secondary accession number(s): Q3UQV6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3