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O94972 (TRI37_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM37

EC=6.3.2.-
Alternative name(s):
Mulibrey nanism protein
Tripartite motif-containing protein 37
Gene names
Name:TRIM37
Synonyms:KIAA0898, MUL, POB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length964 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication. Ref.8 Ref.10

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasmperinuclear region. Peroxisome. Note: Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. Ref.6 Ref.8 Ref.10

Tissue specificity

Ubiquitous. Ref.5

Post-translational modification

Auto-ubiquitinated.

Involvement in disease

Mulibrey nanism (MUL) [MIM:253250]: Autosomal recessive disorder that involves several tissues of mesodermal origin, implying a defect in a highly pleiotropic gene. Characteristic features include severe growth failure of prenatal onset and constrictive pericardium with consequent hepatomegaly. In addition, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, typical dysmorphic features and hypoplasia of various endocrine glands causing hormonal deficiency are common.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.7 Ref.8 Ref.11 Ref.12

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 1 MATH domain.

Contains 1 RING-type zinc finger.

Sequence caution

The sequence BAA74921.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaggresome assembly

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 11279055. Source: UniProtKB

negative regulation of centriole replication

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 23077300. Source: UniProt

protein autoubiquitination

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentaggresome

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 11279055. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

peroxisome

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 11279055. Source: UniProtKB

tumor necrosis factor receptor binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 11279055. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.8. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRC1O436633EBI-741602,EBI-741137

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94972-1)

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 2 (identifier: O94972-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     899-937: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 964964E3 ubiquitin-protein ligase TRIM37
PRO_0000056254

Regions

Domain276 – 403128MATH
Zinc finger15 – 5541RING-type; degenerate
Zinc finger90 – 13243B box-type
Coiled coil132 – 234103 Potential
Coiled coil419 – 45032 Potential
Coiled coil673 – 70028 Potential
Compositional bias534 – 5407Poly-Ser
Compositional bias578 – 5814Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9

Natural variations

Alternative sequence1 – 122122Missing in isoform 2.
VSP_011919
Alternative sequence899 – 93739Missing in isoform 2.
VSP_011920
Natural variant761L → P in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates. Ref.8
VAR_060217
Natural variant1081T → A. Ref.4
Corresponds to variant rs17853504 [ dbSNP | Ensembl ].
VAR_060218
Natural variant1091C → S in MUL; no effect on E3 ubiquitin-protein ligase activity. Ref.12
VAR_060219
Natural variant3221G → V in MUL; no effect on ubiquitination but affects subcellular localization. Ref.8 Ref.11
VAR_060220
Natural variant8381V → I.
Corresponds to variant rs7222388 [ dbSNP | Ensembl ].
VAR_052142

Experimental info

Mutagenesis35 – 362CC → SS: Reduces ubiquitination and abolishes the formation of perinuclear aggregates. Ref.8
Sequence conflict6241D → A in AAL36460. Ref.1

Secondary structure

................. 964
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: C0F08D5A5DC3B5AC

FASTA964107,906
        10         20         30         40         50         60 
MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL 

        70         80         90        100        110        120 
RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW 

       130        140        150        160        170        180 
GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR 

       190        200        210        220        230        240 
EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK 

       250        260        270        280        290        300 
SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP 

       310        320        330        340        350        360 
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII 

       370        380        390        400        410        420 
REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR FQVRSPTFFQ KSRDQHWYIT 

       430        440        450        460        470        480 
QLEAAQTSYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDALET RAKKSACSDM 

       490        500        510        520        530        540 
LLEGGPTTAS VREAKEDEED EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS 

       550        560        570        580        590        600 
TATSNTEEND IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR 

       610        620        630        640        650        660 
THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA SYSRKDKDQR 

       670        680        690        700        710        720 
KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK SSSAASGDMQ TSLFSADQAA 

       730        740        750        760        770        780 
LAACGTENSG RLQDLGMELL AKSSVANCYI RNSTNKKSNS PKPARSSVAG SLSLRRAVDP 

       790        800        810        820        830        840 
GENSRSKGDC QTLSEGSPGS SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV 

       850        860        870        880        890        900 
AVFSGLPAVE KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM 

       910        920        930        940        950        960 
SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG PEDLSFNTDE 


NSGR 

« Hide

Isoform 2 [UniParc].

Checksum: 43486E1064478477
Show »

FASTA80389,186

References

« Hide 'large scale' references
[1]"Gene POB1 is amplified and overexpressed in human breast cancer."
Wu G., Couch F.J.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[4]"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 1), VARIANT ALA-108.
Tissue: Testis.
[5]"Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey nanism."
Avela K., Lipsanen-Nyman M., Idanheimo N., Seemanova E., Rosengren S., Makela T.P., Perheentupa J., Chapelle A.D., Lehesjoki A.E.
Nat. Genet. 25:298-301(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, TISSUE SPECIFICITY.
[6]"The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein: classification of mulibrey nanism as a new peroxisomal disorder."
Kallijarvi J., Avela K., Lipsanen-Nyman M., Ulmanen I., Lehesjoki A.E.
Am. J. Hum. Genet. 70:1215-1228(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"A novel splice site mutation in the TRIM37 gene causes mulibrey nanism in a Turkish family with phenotypic heterogeneity."
Jagiello P., Hammans C., Wieczorek S., Arning L., Stefanski A., Strehl H., Epplen J.T., Gencik M.
Hum. Mutat. 21:630-635(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[8]"TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase."
Kallijaervi J., Lahtinen U., Haemaelaeinen R., Lipsanen-Nyman M., Palvimo J.J., Lehesjoki A.-E.
Exp. Cell Res. 308:146-155(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, MUTAGENESIS OF 35-CYS-CYS-36, VARIANT MUL PRO-76, CHARACTERIZATION OF VARIANTS MUL PRO-76 AND MUL VAL-322.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Discovering regulators of centriole biogenesis through siRNA-based functional genomics in human cells."
Balestra F.R., Strnad P., Fluckiger I., Gonczy P.
Dev. Cell 25:555-571(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Novel mutations in the TRIM37 gene in Mulibrey Nanism."
Haemaelaeinen R.H., Avela K., Lambert J.A., Kallijaervi J., Eyaid W., Gronau J., Ignaszewski A.P., McFadden D., Sorge G., Lipsanen-Nyman M., Lehesjoki A.E.
Hum. Mutat. 23:522-522(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MUL VAL-322, CHARACTERIZATION OF VARIANT MUL VAR-322.
[12]"Wilms' tumor and novel TRIM37 mutations in an Australian patient with mulibrey nanism."
Haemaelaeinen R.H., Mowat D., Gabbett M.T., O'brien T.A., Kallijaervi J., Lehesjoki A.-E.
Clin. Genet. 70:473-479(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MUL SER-109, CHARACTERIZATION OF VARIANT MUL SER-109.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF213365 mRNA. Translation: AAL36460.1.
AB020705 mRNA. Translation: BAA74921.1. Different initiation.
BX537955 mRNA. Translation: CAD97922.1.
BC036012 mRNA. Translation: AAH36012.1.
CCDSCCDS32694.1. [O94972-1]
CCDS45746.1. [O94972-1]
RefSeqNP_001005207.1. NM_001005207.2. [O94972-1]
NP_056109.1. NM_015294.3. [O94972-1]
UniGeneHs.579079.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRQX-ray2.29A/B/C/D1-90[»]
ProteinModelPortalO94972.
SMRO94972. Positions 1-84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110678. 48 interactions.
DIPDIP-34437N.
IntActO94972. 29 interactions.
MINTMINT-1433848.
STRING9606.ENSP00000262294.

PTM databases

PhosphoSiteO94972.

Proteomic databases

MaxQBO94972.
PaxDbO94972.
PRIDEO94972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262294; ENSP00000262294; ENSG00000108395. [O94972-1]
ENST00000376149; ENSP00000365319; ENSG00000108395. [O94972-2]
ENST00000393066; ENSP00000376785; ENSG00000108395. [O94972-1]
GeneID4591.
KEGGhsa:4591.
UCSCuc002iwy.4. human. [O94972-1]
uc002ixa.4. human. [O94972-2]

Organism-specific databases

CTD4591.
GeneCardsGC17M057059.
H-InvDBHIX0014039.
HGNCHGNC:7523. TRIM37.
HPAHPA021911.
MIM253250. phenotype.
605073. gene.
neXtProtNX_O94972.
Orphanet2576. MULIBREY nanism.
PharmGKBPA35497.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251245.
HOGENOMHOG000013010.
HOVERGENHBG057591.
InParanoidO94972.
KOK10608.
OMAVRCMKTD.
OrthoDBEOG7QG442.
PhylomeDBO94972.
TreeFamTF351092.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkO94972.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO94972.
BgeeO94972.
CleanExHS_TRIM37.
GenevestigatorO94972.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR003649. Bbox_C.
IPR002083. MATH.
IPR008974. TRAF-like.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00917. MATH. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49599. SSF49599. 1 hit.
PROSITEPS50144. MATH. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIM37. human.
EvolutionaryTraceO94972.
GeneWikiTRIM37.
GenomeRNAi4591.
NextBio17650.
PROO94972.
SOURCESearch...

Entry information

Entry nameTRI37_HUMAN
AccessionPrimary (citable) accession number: O94972
Secondary accession number(s): Q7Z3E6, Q8IYF7, Q8WYF7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 130 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 17

Human chromosome 17: entries, gene names and cross-references to MIM