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Q14134 (TRI29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tripartite motif-containing protein 29
Alternative name(s):
Ataxia telangiectasia group D-associated protein
Gene names
Name:TRIM29
Synonyms:ATDC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with VIM and HINT1. Ref.4

Subcellular location

Cytoplasm. Note: Colocalizes with intermediate filaments. Ref.4

Tissue specificity

Expressed in placenta, prostate and thymus. Ref.2

Post-translational modification

Constitutively phosphorylated by PKC on serine/threonine in A431 cells. Ref.5

Sequence similarities

Contains 1 B box-type zinc finger.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q14134-1)

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.
Isoform Beta (identifier: Q14134-2)

The sequence of this isoform differs from the canonical sequence as follows:
     569-588: SHYRPFYVNKGNGIGSNEAP → VV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 588588Tripartite motif-containing protein 29
PRO_0000056242

Regions

Zinc finger220 – 26041B box-type
Coiled coil259 – 35294 Potential

Amino acid modifications

Modified residue211Phosphoserine Ref.8 Ref.9
Modified residue1041Phosphoserine Ref.6 Ref.8 Ref.9
Modified residue4761Phosphothreonine Ref.8
Modified residue4891Phosphoserine Ref.8

Natural variations

Alternative sequence569 – 58820SHYRP…SNEAP → VV in isoform Beta.
VSP_011999
Natural variant5141S → F in a breast cancer sample; somatic mutation. Ref.12
VAR_035962

Experimental info

Sequence conflict126 – 1272EL → DV Ref.1
Sequence conflict126 – 1272EL → DV Ref.2

Secondary structure

.............. 588
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 7CBAD7A4C43A311C

FASTA58865,835
        10         20         30         40         50         60 
MEAADASRSN GSSPEARDAR SPSGPSGSLE NGTKADGKDA KTTNGHGGEA AEGKSLGSAL 

        70         80         90        100        110        120 
KPGEGRSALF AGNEWRRPII QFVESGDDKN SNYFSMDSME GKRSPYAGLQ LGAAKKPPVT 

       130        140        150        160        170        180 
FAEKGELRKS IFSESRKPTV SIMEPGETRR NSYPRADTGL FSRSKSGSEE VLCDSCIGNK 

       190        200        210        220        230        240 
QKAVKSCLVC QASFCELHLK PHLEGAAFRD HQLLEPIRDF EARKCPVHGK TMELFCQTDQ 

       250        260        270        280        290        300 
TCICYLCMFQ EHKNHSTVTV EEAKAEKETE LSLQKEQLQL KIIEIEDEAE KWQKEKDRIK 

       310        320        330        340        350        360 
SFTTNEKAIL EQNFRDLVRD LEKQKEEVRA ALEQREQDAV DQVKVIMDAL DERAKVLHED 

       370        380        390        400        410        420 
KQTREQLHSI SDSVLFLQEF GALMSNYSLP PPLPTYHVLL EGEGLGQSLG NFKDDLLNVC 

       430        440        450        460        470        480 
MRHVEKMCKA DLSRNFIERN HMENGGDHRY VNNYTNSFGG EWSAPDTMKR YSMYLTPKGG 

       490        500        510        520        530        540 
VRTSYQPSSP GRFTKETTQK NFNNLYGTKG NYTSRVWEYS SSIQNSDNDL PVVQGSSSFS 

       550        560        570        580 
LKGYPSLMRS QSPKAQPQTW KSGKQTMLSH YRPFYVNKGN GIGSNEAP 

« Hide

Isoform Beta [UniParc].

Checksum: D5A14625B49E5FAC
Show »

FASTA57063,844

References

« Hide 'large scale' references
[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]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-514.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L24203 mRNA. Translation: AAA35762.1.
AF230388 mRNA. Translation: AAG50167.1.
AF230389 mRNA. Translation: AAG50168.1.
BC017352 mRNA. Translation: AAH17352.1.
PIRA49618.
RefSeqNP_036233.2. NM_012101.3.
XP_005271544.1. XM_005271487.1.
UniGeneHs.504115.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSVNMR-A212-270[»]
ProteinModelPortalQ14134.
SMRQ14134. Positions 168-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117177. 39 interactions.
IntActQ14134. 20 interactions.
MINTMINT-1183268.
STRING9606.ENSP00000343129.

PTM databases

PhosphoSiteQ14134.

Polymorphism databases

DMDM116242825.

Proteomic databases

PaxDbQ14134.
PRIDEQ14134.

Protocols and materials databases

DNASU23650.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341846; ENSP00000343129; ENSG00000137699. [Q14134-1]
GeneID23650.
KEGGhsa:23650.
UCSCuc001pwz.3. human. [Q14134-1]

Organism-specific databases

CTD23650.
GeneCardsGC11M120015.
HGNCHGNC:17274. TRIM29.
HPAHPA020053.
MIM610658. gene.
neXtProtNX_Q14134.
PharmGKBPA38218.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149777.
HOGENOMHOG000154677.
HOVERGENHBG061597.
InParanoidQ14134.
KOK12010.
OMALEQNFRD.
OrthoDBEOG7J446B.
PhylomeDBQ14134.
TreeFamTF351086.

Gene expression databases

ArrayExpressQ14134.
BgeeQ14134.
CleanExHS_TRIM29.
GenevestigatorQ14134.

Family and domain databases

Gene3D4.10.45.10. 1 hit.
InterProIPR000315. Znf_B-box.
[Graphical view]
PfamPF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
[Graphical view]
PROSITEPS50119. ZF_BBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM29. human.
EvolutionaryTraceQ14134.
GeneWikiTRIM29.
GenomeRNAi23650.
NextBio46485.
PROQ14134.
SOURCESearch...

Entry information

Entry nameTRI29_HUMAN
AccessionPrimary (citable) accession number: Q14134
Secondary accession number(s): Q96AA9, Q9BZY7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM