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O94811

- TPPP_HUMAN

UniProt

O94811 - TPPP_HUMAN

Protein

Tubulin polymerization-promoting protein

Gene

TPPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    May play a role in the polymerization of tubulin into microtubules, microtubule bundling and the stabilization of existing microtubules, thus maintaining the integrity of the microtubule network. May play a role in mitotic spindle assembly and nuclear envelope breakdown.3 Publications

    GO - Molecular functioni

    1. microtubule binding Source: HGNC
    2. protein binding Source: UniProtKB
    3. tubulin binding Source: UniProtKB

    GO - Biological processi

    1. microtubule bundle formation Source: UniProtKB
    2. microtubule polymerization Source: UniProtKB
    3. positive regulation of protein complex assembly Source: HGNC
    4. positive regulation of protein polymerization Source: HGNC

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin polymerization-promoting protein
    Short name:
    TPPP
    Alternative name(s):
    25 kDa brain-specific protein
    TPPP/p25
    p24
    p25-alpha
    Gene namesi
    Name:TPPP
    Synonyms:TPPP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:24164. TPPP.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Nucleus
    Note: Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule Source: Ensembl
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162406809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 219219Tubulin polymerization-promoting proteinPRO_0000221135Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphothreonine; by CDK5; in vitro3 Publications
    Modified residuei18 – 181Phosphoserine; by CDK5 and MAPK1; in vitro3 Publications
    Modified residuei32 – 321Phosphoserine; by PKA; in vitro5 Publications
    Modified residuei35 – 351Phosphoserine2 Publications
    Modified residuei45 – 451Phosphoserine2 Publications
    Modified residuei92 – 921Phosphothreonine; by PKA; in vitro2 Publications
    Glycosylationi152 – 1521O-linked (GlcNAc)By similarity
    Modified residuei159 – 1591Phosphoserine; by PKA; in vitro2 Publications
    Modified residuei160 – 1601Phosphoserine; by CDK5 and MAPK1; in vitro2 Publications

    Post-translational modificationi

    Poor substrate for GSK3 By similarity. Phosphorylated by LIMK1 on serine residues. Phosphorylation may alter the tubulin polymerization activity.By similarity5 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO94811.
    PaxDbiO94811.
    PRIDEiO94811.

    2D gel databases

    UCD-2DPAGEO94811.

    PTM databases

    PhosphoSiteiO94811.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO94811.
    BgeeiO94811.
    CleanExiHS_TPPP.
    GenevestigatoriO94811.

    Organism-specific databases

    HPAiHPA036575.
    HPA036576.

    Interactioni

    Subunit structurei

    Homodimer. Binds tubulin; binding is inhibited by GTP By similarity. Interacts with GSK3 By similarity. Interacts with MAPK1 By similarity. Interacts with GAPDH; the interaction is direct By similarity. Interacts with LIMK1 (via the PDZ domain); the interaction is direct.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi116259. 4 interactions.
    IntActiO94811. 3 interactions.
    MINTiMINT-2798227.
    STRINGi9606.ENSP00000353785.

    Structurei

    3D structure databases

    ProteinModelPortaliO94811.
    SMRiO94811. Positions 43-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 116116Mediates interaction with LIMK1Add
    BLAST

    Sequence similaritiesi

    Belongs to the TPPP family.Curated

    Phylogenomic databases

    eggNOGiNOG271804.
    HOGENOMiHOG000260314.
    HOVERGENiHBG036683.
    InParanoidiO94811.
    OMAiHAGTYDH.
    OrthoDBiEOG7NGQDH.
    PhylomeDBiO94811.
    TreeFamiTF314440.

    Family and domain databases

    InterProiIPR008907. P25-alpha.
    [Graphical view]
    PANTHERiPTHR12932. PTHR12932. 1 hit.
    PfamiPF05517. p25-alpha. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O94811-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKAKPAKA ANRTPPKSPG DPSKDRAAKR LSLESEGAGE GAAASPELSA    50
    LEEAFRRFAV HGDARATGRE MHGKNWSKLC KDCQVIDGRN VTVTDVDIVF 100
    SKIKGKSCRT ITFEQFQEAL EELAKKRFKD KSSEEAVREV HRLIEGKAPI 150
    ISGVTKAISS PTVSRLTDTT KFTGSHKERF DPSGKGKGKA GRVDLVDESG 200
    YVSGYKHAGT YDQKVQGGK 219
    Length:219
    Mass (Da):23,694
    Last modified:May 1, 1999 - v1
    Checksum:iF8B2C814EA59129A
    GO

    Sequence cautioni

    The sequence AAH40496.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017016 mRNA. Translation: BAA36164.1.
    BT020035 mRNA. Translation: AAV38838.1.
    BC040496 mRNA. Translation: AAH40496.1. Different initiation.
    CCDSiCCDS3856.1.
    RefSeqiNP_008961.1. NM_007030.2.
    UniGeneiHs.481466.

    Genome annotation databases

    EnsembliENST00000360578; ENSP00000353785; ENSG00000171368.
    GeneIDi11076.
    KEGGihsa:11076.
    UCSCiuc003jbg.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017016 mRNA. Translation: BAA36164.1 .
    BT020035 mRNA. Translation: AAV38838.1 .
    BC040496 mRNA. Translation: AAH40496.1 . Different initiation.
    CCDSi CCDS3856.1.
    RefSeqi NP_008961.1. NM_007030.2.
    UniGenei Hs.481466.

    3D structure databases

    ProteinModelPortali O94811.
    SMRi O94811. Positions 43-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116259. 4 interactions.
    IntActi O94811. 3 interactions.
    MINTi MINT-2798227.
    STRINGi 9606.ENSP00000353785.

    Chemistry

    BindingDBi O94811.

    PTM databases

    PhosphoSitei O94811.

    2D gel databases

    UCD-2DPAGE O94811.

    Proteomic databases

    MaxQBi O94811.
    PaxDbi O94811.
    PRIDEi O94811.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360578 ; ENSP00000353785 ; ENSG00000171368 .
    GeneIDi 11076.
    KEGGi hsa:11076.
    UCSCi uc003jbg.4. human.

    Organism-specific databases

    CTDi 11076.
    GeneCardsi GC05M000659.
    HGNCi HGNC:24164. TPPP.
    HPAi HPA036575.
    HPA036576.
    MIMi 608773. gene.
    neXtProti NX_O94811.
    PharmGKBi PA162406809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271804.
    HOGENOMi HOG000260314.
    HOVERGENi HBG036683.
    InParanoidi O94811.
    OMAi HAGTYDH.
    OrthoDBi EOG7NGQDH.
    PhylomeDBi O94811.
    TreeFami TF314440.

    Miscellaneous databases

    GeneWikii TPPP.
    GenomeRNAii 11076.
    NextBioi 42106.
    PROi O94811.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94811.
    Bgeei O94811.
    CleanExi HS_TPPP.
    Genevestigatori O94811.

    Family and domain databases

    InterProi IPR008907. P25-alpha.
    [Graphical view ]
    PANTHERi PTHR12932. PTHR12932. 1 hit.
    Pfami PF05517. p25-alpha. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human gene whose product shares significant homology with the bovine brain-specific protein p25 on chromosome 5p15.3."
      Seki N., Hattori A., Sugano S., Suzuki Y., Nakagawara A., Muramatsu M.-A., Hori T.-A., Saito T.
      J. Hum. Genet. 44:121-122(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Neuroblastoma.
    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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Tissue: Brain.
    4. "p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies."
      Lindersson E., Lundvig D., Petersen C., Madsen P., Nyengaard J.R., Hoejrup P., Moos T., Otzen D., Gai W.-P., Blumbergs P.C., Jensen P.H.
      J. Biol. Chem. 280:5703-5715(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGGREGATED SNCA, SUBCELLULAR LOCATION.
    5. "Tubulin polymerization promoting proteins (TPPPs): members of a new family with distinct structures and functions."
      Vincze O., Toekesi N., Olah J., Hlavanda E., Zotter A., Horvath I., Lehotzky A., Tirian L., Medzihradszky K.F., Kovacs J., Orosz F., Ovadi J.
      Biochemistry 45:13818-13826(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies."
      Olah J., Toekesi N., Vincze O., Horvath I., Lehotzky A., Erdei A., Szajli E., Medzihradszky K.F., Orosz F., Kovacs G.G., Ovadi J.
      FEBS Lett. 580:5807-5814(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules."
      Acevedo K., Li R., Soo P., Suryadinata R., Sarcevic B., Valova V.A., Graham M.E., Robinson P.J., Bernard O.
      Exp. Cell Res. 313:4091-4106(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LIMK1, PHOSPHORYLATION.
    8. "Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP): identification of sites targeted by different kinases."
      Hlavanda E., Klement E., Kokai E., Kovacs J., Vincze O., Toekesi N., Orosz F., Medzihradszky K.F., Dombradi V., Ovadi J.
      J. Biol. Chem. 282:29531-29539(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-14; SER-18; SER-32; THR-92; SER-159 AND SER-160.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-18; SER-32; SER-35 AND SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiTPPP_HUMAN
    AccessioniPrimary (citable) accession number: O94811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 12, 2003
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 106 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

    Miscellaneous

    Unstructured protein. Interacts with aggregated SNCA and may have a pro-aggregatory role in synucleinopathies.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3