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Q14134

- TRI29_HUMAN

UniProt

Q14134 - TRI29_HUMAN

Protein

Tripartite motif-containing protein 29

Gene

TRIM29

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    It is able to complement the radiosensitivity defect of an ataxia telangiectasia (AT) fibroblast cell line.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri220 – 26041B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. sequence-specific DNA binding transcription factor activity Source: ProtInc
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of protein localization to nucleus Source: Ensembl
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tripartite motif-containing protein 29
    Alternative name(s):
    Ataxia telangiectasia group D-associated protein
    Gene namesi
    Name:TRIM29
    Synonyms:ATDC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:17274. TRIM29.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Colocalizes with intermediate filaments.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38218.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 588588Tripartite motif-containing protein 29PRO_0000056242Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine3 Publications
    Modified residuei104 – 1041Phosphoserine4 Publications
    Modified residuei476 – 4761Phosphothreonine2 Publications
    Modified residuei489 – 4891Phosphoserine2 Publications

    Post-translational modificationi

    Constitutively phosphorylated by PKC on serine/threonine in A431 cells.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14134.
    PaxDbiQ14134.
    PRIDEiQ14134.

    PTM databases

    PhosphoSiteiQ14134.

    Expressioni

    Tissue specificityi

    Expressed in placenta, prostate and thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ14134.
    BgeeiQ14134.
    CleanExiHS_TRIM29.
    GenevestigatoriQ14134.

    Organism-specific databases

    HPAiHPA020053.

    Interactioni

    Subunit structurei

    Interacts with VIM and HINT1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151692EBI-702370,EBI-710484
    DVL2O146415EBI-702370,EBI-740850
    GCC1Q96CN92EBI-702370,EBI-746252
    GSK3BP498412EBI-702370,EBI-373586

    Protein-protein interaction databases

    BioGridi117177. 39 interactions.
    IntActiQ14134. 20 interactions.
    MINTiMINT-1183268.
    STRINGi9606.ENSP00000343129.

    Structurei

    Secondary structure

    1
    588
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi217 – 2215
    Turni226 – 2283
    Beta strandi234 – 2396
    Helixi245 – 2495
    Turni250 – 2523
    Beta strandi253 – 2553
    Beta strandi257 – 2593
    Helixi260 – 2678

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CSVNMR-A212-270[»]
    ProteinModelPortaliQ14134.
    SMRiQ14134. Positions 168-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14134.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili259 – 35294Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri220 – 26041B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG149777.
    HOGENOMiHOG000154677.
    HOVERGENiHBG061597.
    InParanoidiQ14134.
    KOiK12010.
    OMAiLEQNFRD.
    OrthoDBiEOG7J446B.
    PhylomeDBiQ14134.
    TreeFamiTF351086.

    Family and domain databases

    Gene3Di4.10.45.10. 1 hit.
    InterProiIPR000315. Znf_B-box.
    [Graphical view]
    PfamiPF00643. zf-B_box. 1 hit.
    [Graphical view]
    SMARTiSM00336. BBOX. 1 hit.
    [Graphical view]
    PROSITEiPS50119. ZF_BBOX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q14134-1) [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

    MEAADASRSN GSSPEARDAR SPSGPSGSLE NGTKADGKDA KTTNGHGGEA    50
    AEGKSLGSAL KPGEGRSALF AGNEWRRPII QFVESGDDKN SNYFSMDSME 100
    GKRSPYAGLQ LGAAKKPPVT FAEKGELRKS IFSESRKPTV SIMEPGETRR 150
    NSYPRADTGL FSRSKSGSEE VLCDSCIGNK QKAVKSCLVC QASFCELHLK 200
    PHLEGAAFRD HQLLEPIRDF EARKCPVHGK TMELFCQTDQ TCICYLCMFQ 250
    EHKNHSTVTV EEAKAEKETE LSLQKEQLQL KIIEIEDEAE KWQKEKDRIK 300
    SFTTNEKAIL EQNFRDLVRD LEKQKEEVRA ALEQREQDAV DQVKVIMDAL 350
    DERAKVLHED KQTREQLHSI SDSVLFLQEF GALMSNYSLP PPLPTYHVLL 400
    EGEGLGQSLG NFKDDLLNVC MRHVEKMCKA DLSRNFIERN HMENGGDHRY 450
    VNNYTNSFGG EWSAPDTMKR YSMYLTPKGG VRTSYQPSSP GRFTKETTQK 500
    NFNNLYGTKG NYTSRVWEYS SSIQNSDNDL PVVQGSSSFS LKGYPSLMRS 550
    QSPKAQPQTW KSGKQTMLSH YRPFYVNKGN GIGSNEAP 588
    Length:588
    Mass (Da):65,835
    Last modified:October 17, 2006 - v2
    Checksum:i7CBAD7A4C43A311C
    GO
    Isoform Beta (identifier: Q14134-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-588: SHYRPFYVNKGNGIGSNEAP → VV

    Note: No experimental confirmation available.

    Show »
    Length:570
    Mass (Da):63,844
    Checksum:iD5A14625B49E5FAC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti126 – 1272EL → DV(PubMed:8188213)Curated
    Sequence conflicti126 – 1272EL → DV(PubMed:11331580)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti514 – 5141S → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035962

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei569 – 58820SHYRP…SNEAP → VV in isoform Beta. 1 PublicationVSP_011999Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24203 mRNA. Translation: AAA35762.1.
    AF230388 mRNA. Translation: AAG50167.1.
    AF230389 mRNA. Translation: AAG50168.1.
    BC017352 mRNA. Translation: AAH17352.1.
    CCDSiCCDS8428.1. [Q14134-1]
    PIRiA49618.
    RefSeqiNP_036233.2. NM_012101.3. [Q14134-1]
    XP_005271544.1. XM_005271487.1. [Q14134-1]
    UniGeneiHs.504115.

    Genome annotation databases

    EnsembliENST00000341846; ENSP00000343129; ENSG00000137699. [Q14134-1]
    GeneIDi23650.
    KEGGihsa:23650.
    UCSCiuc001pwz.3. human. [Q14134-1]

    Polymorphism databases

    DMDMi116242825.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L24203 mRNA. Translation: AAA35762.1 .
    AF230388 mRNA. Translation: AAG50167.1 .
    AF230389 mRNA. Translation: AAG50168.1 .
    BC017352 mRNA. Translation: AAH17352.1 .
    CCDSi CCDS8428.1. [Q14134-1 ]
    PIRi A49618.
    RefSeqi NP_036233.2. NM_012101.3. [Q14134-1 ]
    XP_005271544.1. XM_005271487.1. [Q14134-1 ]
    UniGenei Hs.504115.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CSV NMR - A 212-270 [» ]
    ProteinModelPortali Q14134.
    SMRi Q14134. Positions 168-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117177. 39 interactions.
    IntActi Q14134. 20 interactions.
    MINTi MINT-1183268.
    STRINGi 9606.ENSP00000343129.

    PTM databases

    PhosphoSitei Q14134.

    Polymorphism databases

    DMDMi 116242825.

    Proteomic databases

    MaxQBi Q14134.
    PaxDbi Q14134.
    PRIDEi Q14134.

    Protocols and materials databases

    DNASUi 23650.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341846 ; ENSP00000343129 ; ENSG00000137699 . [Q14134-1 ]
    GeneIDi 23650.
    KEGGi hsa:23650.
    UCSCi uc001pwz.3. human. [Q14134-1 ]

    Organism-specific databases

    CTDi 23650.
    GeneCardsi GC11M120015.
    HGNCi HGNC:17274. TRIM29.
    HPAi HPA020053.
    MIMi 610658. gene.
    neXtProti NX_Q14134.
    PharmGKBi PA38218.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149777.
    HOGENOMi HOG000154677.
    HOVERGENi HBG061597.
    InParanoidi Q14134.
    KOi K12010.
    OMAi LEQNFRD.
    OrthoDBi EOG7J446B.
    PhylomeDBi Q14134.
    TreeFami TF351086.

    Miscellaneous databases

    ChiTaRSi TRIM29. human.
    EvolutionaryTracei Q14134.
    GeneWikii TRIM29.
    GenomeRNAii 23650.
    NextBioi 46485.
    PROi Q14134.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14134.
    Bgeei Q14134.
    CleanExi HS_TRIM29.
    Genevestigatori Q14134.

    Family and domain databases

    Gene3Di 4.10.45.10. 1 hit.
    InterProi IPR000315. Znf_B-box.
    [Graphical view ]
    Pfami PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    SMARTi SM00336. BBOX. 1 hit.
    [Graphical view ]
    PROSITEi PS50119. ZF_BBOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of a candidate gene for ataxia-telangiectasia group D (ATDC)."
      Leonhardt E.A., Kapp L.N., Young B.R., Murnane J.P.
      Genomics 19:130-136(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), TISSUE SPECIFICITY.
    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] (ISOFORM ALPHA).
      Tissue: Astrocytoma.
    4. "The product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitor."
      Brzoska P.M., Chen H., Zhu Y., Levin N.A., Disatnik M.H., Mochly-Rosen D., Murnane J.P., Christman M.F.
      Proc. Natl. Acad. Sci. U.S.A. 92:7824-7828(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VIM AND HINT1, SUBCELLULAR LOCATION.
    5. "Expression of the ATDC (ataxia telangiectasia group D-complementing) gene in A431 human squamous carcinoma cells."
      Laderoute K.R., Knapp A.M., Green C.J., Sutherland R.M., Kapp L.N.
      Int. J. Cancer 66:772-778(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    6. "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 SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-104; THR-476 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-21 AND SER-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Solution structure of the ZF-B_box type2 domain of human tripartite motif protein TRIM29 isoform alpha."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 212-270.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-514.

    Entry informationi

    Entry nameiTRI29_HUMAN
    AccessioniPrimary (citable) accession number: Q14134
    Secondary accession number(s): Q96AA9, Q9BZY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 130 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3