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Q13049 (TRI32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM32

EC=6.3.2.-
Alternative name(s):
72 kDa Tat-interacting protein
Tripartite motif-containing protein 32
Zinc finger protein HT2A
Gene names
Name:TRIM32
Synonyms:HT2A
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with DTNBP1. It self-associates. Ref.7

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic bodies, often located around the nucleus.

Tissue specificity

Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle. Ref.10

Post-translational modification

Ubiquitinated. Ref.7

Involvement in disease

Defects in TRIM32 are the cause of limb-girdle muscular dystrophy type 2H (LGMD2H) [MIM:254110]; also known as muscular dystrophy Hutterite type. LGMD2H is an autosomal recessive degenerative myopathy characterized by pelvic girdle, shoulder girdle and quadriceps muscle weakness. Clinical phenotype and severity are highly variable. Disease progression is slow and most patients remain ambulatory into the sixth decade of life. Ref.10 Ref.12

Defects in TRIM32 are the cause of Bardet-Biedl syndrome type 11 (BBS11) [MIM:209900]. Bardet-Biedl syndrome (BBS) is a genetically heterogeneous, autosomal recessive disorder characterized by usually severe pigmentary retinopathy, early onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. A relatively high incidence of BBS is found in the mixed Arab populations of Kuwait and in Bedouin tribes throughout the Middle East, most likely due to the high rate of consaguinity in these populations and a founder effect. Ref.11

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 5 NHL repeats.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Limb-girdle muscular dystrophy
Mental retardation
Obesity
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processfat cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

innate immune response

Traceable author statement. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from direct assay. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell cycle

Inferred from direct assay. Source: BHF-UCL

positive regulation of cell growth

Inferred from direct assay. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay. Source: BHF-UCL

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of proteolysis

Inferred from direct assay. Source: BHF-UCL

protein polyubiquitination

Inferred from direct assay. Source: BHF-UCL

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.7. Source: UniProtKB

response to UV

Inferred from sequence or structural similarity. Source: BHF-UCL

response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular componentnucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular functionRNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Tat protein binding

Traceable author statement. Source: BHF-UCL

myosin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein self-association

Inferred from direct assay Ref.7. Source: UniProtKB

transcription coactivator activity

Traceable author statement. Source: ProtInc

translation initiation factor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ubiquitin binding

Inferred from direct assay Ref.7. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.7. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 653652E3 ubiquitin-protein ligase TRIM32
PRO_0000056246

Regions

Repeat358 – 40144NHL 1
Repeat415 – 45844NHL 2
Repeat459 – 49941NHL 3
Repeat562 – 60544NHL 4
Repeat606 – 64641NHL 5
Zinc finger20 – 6546RING-type
Zinc finger103 – 13331B box-type
Coiled coil138 – 19760 Potential
Compositional bias2 – 65Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.6
Modified residue3281Phosphoserine Ref.5
Modified residue3351Phosphoserine Ref.5 Ref.8
Modified residue3391Phosphoserine Ref.5 Ref.8

Natural variations

Natural variant1301P → S in BBS11. Ref.11
VAR_038807
Natural variant2571T → R.
Corresponds to variant rs3747834 [ dbSNP | Ensembl ].
VAR_038808
Natural variant2991R → Q in a patient with Bardet-Biedl syndrome; unknown pathological significance. Ref.13
VAR_066295
Natural variant3941R → H in LGMD2H. Ref.12
VAR_042939
Natural variant4081R → C.
Corresponds to variant rs3747835 [ dbSNP | Ensembl ].
VAR_038809
Natural variant4871D → N in LGMD2H. Ref.10
VAR_018725
Natural variant5881Missing in LGMD2H.
VAR_042940

Experimental info

Sequence conflict271F → I in AAA86474. Ref.1

Secondary structure

................. 653
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13049 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: D83B1595CA8378FD

FASTA65371,989
        10         20         30         40         50         60 
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR 

        70         80         90        100        110        120 
CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC 

       130        140        150        160        170        180 
EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR 

       190        200        210        220        230        240 
YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD 

       250        260        270        280        290        300 
YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT 

       310        320        330        340        350        360 
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK 

       370        380        390        400        410        420 
MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS 

       430        440        450        460        470        480 
FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS 

       490        500        510        520        530        540 
GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR 

       550        560        570        580        590        600 
QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL 

       610        620        630        640        650 
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins."
Fridell R.A., Harding L.S., Bogerd H.P., Cullen B.R.
Virology 209:347-357(1995) [PubMed: 7778269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[4]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-15; 51-60; 70-101; 205-238; 248-282; 345-359; 467-500; 587-596 AND 605-613, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[5]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-335 AND SER-339, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"TRIM32 is an E3 ubiquitin ligase for dysbindin."
Locke M., Tinsley C.L., Benson M.A., Blake D.J.
Hum. Mol. Genet. 18:2344-2358(2009) [PubMed: 19349376] [Abstract]
Cited for: FUNCTION AS A E3 UBIQUITIN-PROTEIN LIGASE, UBIQUITINATION, SELF-ASSOCIATION, INTERACTION WITH DTNBP1.
[8]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-339, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[9]"Solution structure of the RING domain of the tripartite motif protein 32."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 10-84.
[10]"Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene."
Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K., Fujiwara T.M., Wrogemann K.
Am. J. Hum. Genet. 70:663-672(2002) [PubMed: 11822024] [Abstract]
Cited for: VARIANT LGMD2H ASN-487, TISSUE SPECIFICITY.
[11]"Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11)."
Chiang A.P., Beck J.S., Yen H.-J., Tayeh M.K., Scheetz T.E., Swiderski R.E., Nishimura D.Y., Braun T.A., Kim K.-Y.A., Huang J., Elbedour K., Carmi R., Slusarski D.C., Casavant T.L., Stone E.M., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 103:6287-6292(2006) [PubMed: 16606853] [Abstract]
Cited for: VARIANT BBS11 SER-130.
[12]"Mutations that impair interaction properties of TRIM32 associated with limb-girdle muscular dystrophy 2H."
Saccone V., Palmieri M., Passamano L., Piluso G., Meroni G., Politano L., Nigro V.
Hum. Mutat. 29:240-247(2008) [PubMed: 17994549] [Abstract]
Cited for: VARIANTS LGMD2H HIS-394 AND ASP-588 DEL.
[13]"BBS genotype-phenotype assessment of a multiethnic patient cohort calls for a revision of the disease definition."
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., Jacobson S.G., Innes A.M. expand/collapse author list , Mitchell G.A., Boycott K., Heon E.
Hum. Mutat. 32:610-619(2011) [PubMed: 21344540] [Abstract]
Cited for: VARIANT GLN-299.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18543 mRNA. Translation: AAA86474.1.
AL133284 Genomic DNA. Translation: CAB92723.1.
BC003154 mRNA. Translation: AAH03154.1.
IPIIPI00297113.
RefSeqNP_001093149.1. NM_001099679.1.
NP_036342.2. NM_012210.3.
UniGeneHs.591910.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT2NMR-A10-84[»]
ProteinModelPortalQ13049.
SMRQ13049. Positions 3-90, 357-541.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13049. 7 interactions.
MINTMINT-2854880.
STRINGQ13049.

PTM databases

PhosphoSiteQ13049.

Polymorphism databases

DMDM20178303.

Proteomic databases

PRIDEQ13049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373983; ENSP00000363095; ENSG00000119401.
ENST00000394497; ENSP00000378006; ENSG00000119401.
ENST00000450136; ENSP00000408292; ENSG00000119401.
GeneID22954.
KEGGhsa:22954.
UCSCuc004bjw.2. human.

Organism-specific databases

CTD22954.
GeneCardsGC09P119449.
H-InvDBHIX0008331.
HGNCHGNC:16380. TRIM32.
MIM209900. phenotype.
254110. phenotype.
602290. gene.
neXtProtNX_Q13049.
Orphanet1878. Autosomal recessive limb-girdle muscular dystrophy type 2H.
110. Bardet-Biedl syndrome.
PharmGKBPA38130.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09747.
HOGENOMHBG447330.
HOVERGENHBG060344.
InParanoidQ13049.
OMAEHHLEGG.
OrthoDBEOG4QZ7KF.
PhylomeDBQ13049.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ13049.
BgeeQ13049.
CleanExHS_TRIM32.
GenevestigatorQ13049.
GermOnlineENSG00000119401. Homo sapiens.

Family and domain databases

InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR001258. NHL_repeat.
IPR013017. NHL_repeat_subgr.
IPR000315. Znf_B-box.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
Gene3DG3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
KOK10607.
PfamPF01436. NHL. 3 hits.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS51125. NHL. 5 hits.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio43741.
SOURCESearch...

Entry information

Entry nameTRI32_HUMAN
AccessionPrimary (citable) accession number: Q13049
Secondary accession number(s): Q9NQP8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: January 25, 2012
This is version 129 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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families