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Protein

Tripartite motif-containing protein 29

Gene

TRIM29

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

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. sequence-specific DNA binding transcription factor activity Source: ProtInc
  2. 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
Complete GO annotation...

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: HPA
  2. intermediate filament cytoskeleton Source: HPA
  3. nucleoplasm Source: HPA
Complete GO annotation...

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 – 211Phosphoserine2 Publications
Modified residuei104 – 1041Phosphoserine3 Publications
Modified residuei476 – 4761Phosphothreonine1 Publication
Modified residuei489 – 4891Phosphoserine1 Publication

Post-translational modificationi

Constitutively phosphorylated by PKC on serine/threonine in A431 cells.1 Publication

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

BgeeiQ14134.
CleanExiHS_TRIM29.
ExpressionAtlasiQ14134. baseline and differential.
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. 47 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 – 2215Combined sources
Turni226 – 2283Combined sources
Beta strandi234 – 2396Combined sources
Helixi245 – 2495Combined sources
Turni250 – 2523Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi257 – 2593Combined sources
Helixi260 – 2678Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSVNMR-A212-270[»]
ProteinModelPortaliQ14134.
SMRiQ14134. Positions 168-352.
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.
GeneTreeiENSGT00760000118995.
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. AlignAdd to basket

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

        10         20         30         40         50
MEAADASRSN GSSPEARDAR SPSGPSGSLE NGTKADGKDA KTTNGHGGEA
60 70 80 90 100
AEGKSLGSAL KPGEGRSALF AGNEWRRPII QFVESGDDKN SNYFSMDSME
110 120 130 140 150
GKRSPYAGLQ LGAAKKPPVT FAEKGELRKS IFSESRKPTV SIMEPGETRR
160 170 180 190 200
NSYPRADTGL FSRSKSGSEE VLCDSCIGNK QKAVKSCLVC QASFCELHLK
210 220 230 240 250
PHLEGAAFRD HQLLEPIRDF EARKCPVHGK TMELFCQTDQ TCICYLCMFQ
260 270 280 290 300
EHKNHSTVTV EEAKAEKETE LSLQKEQLQL KIIEIEDEAE KWQKEKDRIK
310 320 330 340 350
SFTTNEKAIL EQNFRDLVRD LEKQKEEVRA ALEQREQDAV DQVKVIMDAL
360 370 380 390 400
DERAKVLHED KQTREQLHSI SDSVLFLQEF GALMSNYSLP PPLPTYHVLL
410 420 430 440 450
EGEGLGQSLG NFKDDLLNVC MRHVEKMCKA DLSRNFIERN HMENGGDHRY
460 470 480 490 500
VNNYTNSFGG EWSAPDTMKR YSMYLTPKGG VRTSYQPSSP GRFTKETTQK
510 520 530 540 550
NFNNLYGTKG NYTSRVWEYS SSIQNSDNDL PVVQGSSSFS LKGYPSLMRS
560 570 580
QSPKAQPQTW KSGKQTMLSH YRPFYVNKGN GIGSNEAP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSVNMR-A212-270[»]
ProteinModelPortaliQ14134.
SMRiQ14134. Positions 168-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117177. 47 interactions.
IntActiQ14134. 20 interactions.
MINTiMINT-1183268.
STRINGi9606.ENSP00000343129.

PTM databases

PhosphoSiteiQ14134.

Polymorphism databases

DMDMi116242825.

Proteomic databases

MaxQBiQ14134.
PaxDbiQ14134.
PRIDEiQ14134.

Protocols and materials databases

DNASUi23650.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23650.
GeneCardsiGC11M119981.
HGNCiHGNC:17274. TRIM29.
HPAiHPA020053.
MIMi610658. gene.
neXtProtiNX_Q14134.
PharmGKBiPA38218.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149777.
GeneTreeiENSGT00760000118995.
HOGENOMiHOG000154677.
HOVERGENiHBG061597.
InParanoidiQ14134.
KOiK12010.
OMAiLEQNFRD.
OrthoDBiEOG7J446B.
PhylomeDBiQ14134.
TreeFamiTF351086.

Miscellaneous databases

ChiTaRSiTRIM29. human.
EvolutionaryTraceiQ14134.
GeneWikiiTRIM29.
GenomeRNAii23650.
NextBioi46485.
PROiQ14134.
SOURCEiSearch...

Gene expression databases

BgeeiQ14134.
CleanExiHS_TRIM29.
ExpressionAtlasiQ14134. baseline and differential.
GenevestigatoriQ14134.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.