Q14134 (TRI29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tripartite motif-containing protein 29

Alternative name(s):
Ataxia telangiectasia group D-associated protein

Gene names

Name:	TRIM29
Synonyms:	ATDC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of protein localization to nucleus Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AXIN1	O15169	2	EBI-702370,EBI-710484
DVL2	O14641	5	EBI-702370,EBI-740850
GCC1	Q96CN9	2	EBI-702370,EBI-746252
GSK3B	P49841	2	EBI-702370,EBI-373586

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 588

588

Tripartite motif-containing protein 29

PRO_0000056242

Regions

Zinc finger

220 – 260

41

B box-type

Coiled coil

259 – 352

94

Potential

Amino acid modifications

Modified residue

9

1

Phosphoserine By similarity

Modified residue

13

1

Phosphoserine By similarity

Modified residue

21

1

Phosphoserine Ref.8 Ref.9

Modified residue

104

1

Phosphoserine Ref.6 Ref.8 Ref.9

Modified residue

476

1

Phosphothreonine Ref.8

Modified residue

489

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

569 – 588

20

SHYRP…SNEAP → VV in isoform Beta.

VSP_011999

Natural variant

514

1

S → F in a breast cancer sample; somatic mutation. Ref.12

VAR_035962

Experimental info

Sequence conflict

126 – 127

2

EL → DV Ref.1

Sequence conflict

126 – 127

2

EL → DV Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

588

Helix Strand Turn

Details...

Beta strand

217 – 221

5

Turn

226 – 228

3

Beta strand

234 – 239

6

Helix

245 – 249

5

Turn

250 – 252

3

Beta strand

253 – 255

3

Beta strand

257 – 259

3

Helix

260 – 267

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 7CBAD7A4C43A311C	FASTA	588	65,835
	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
	Isoform Beta [UniParc]. Checksum: D5A14625B49E5FAC	FASTA	570	63,844
	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 LKGYPSLMRS QSPKAQPQTW KSGKQTMLVV

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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. , 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.

IPI

IPI00073096.
IPI00232492.

PIR

A49618.

RefSeq

NP_036233.2. NM_012101.3.

UniGene

Hs.504115.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CSV	NMR	-	A	212-270	[»]

ProteinModelPortal

Q14134.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14134. 18 interactions.

MINT

MINT-1183268.

STRING

9606.ENSP00000343129.

PTM databases

PhosphoSite

Q14134.

Polymorphism databases

DMDM

116242825.

Proteomic databases

PaxDb

Q14134.

PRIDE

Q14134.

Protocols and materials databases

DNASU

23650.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341846; ENSP00000343129; ENSG00000137699.

GeneID

23650.

KEGG

hsa:23650.

UCSC

uc001pwz.3. human.

Organism-specific databases

CTD

23650.

GeneCards

GC11M120015.

HGNC

HGNC:17274. TRIM29.

HPA

HPA020053.

MIM

610658. gene.

neXtProt

NX_Q14134.

PharmGKB

PA38218.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG149777.

HOGENOM

HOG000154677.

HOVERGEN

HBG061597.

InParanoid

Q14134.

KO

K12010.

OMA

LEQNFRD.

OrthoDB

EOG45B1F5.

PhylomeDB

Q14134.

Gene expression databases

ArrayExpress

Q14134.

Bgee

Q14134.

CleanEx

HS_TRIM29.

Genevestigator

Q14134.

GermOnline

ENSG00000137699. Homo sapiens.

Family and domain databases

InterPro

IPR000315. Znf_B-box.
[Graphical view]

Pfam

PF00643. zf-B_box. 1 hit.
[Graphical view]

SMART

SM00336. BBOX. 1 hit.
[Graphical view]

PROSITE

PS50119. ZF_BBOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TRIM29. human.

EvolutionaryTrace

Q14134.

GenomeRNAi

23650.

NextBio

46485.

SOURCE

Search...

Entry information

Entry name

TRI29_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.