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O94972

- TRI37_HUMAN

UniProt

O94972 - TRI37_HUMAN

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Protein
E3 ubiquitin-protein ligase TRIM37
Gene
TRIM37, KIAA0898, MUL, POB1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication.2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5541RING-type; degenerate
Add
BLAST
Zinc fingeri90 – 13243B box-type
Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB
  4. tumor necrosis factor receptor binding Source: UniProtKB
  5. ubiquitin protein ligase binding Source: UniProtKB
  6. ubiquitin-protein transferase activity Source: UniProtKB
  7. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. aggresome assembly Source: UniProtKB
  2. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  3. negative regulation of centriole replication Source: UniProtKB
  4. positive regulation of NF-kappaB transcription factor activity Source: UniProt
  5. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProt
  6. protein autoubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiO94972.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM37 (EC:6.3.2.-)
Alternative name(s):
Mulibrey nanism protein
Tripartite motif-containing protein 37
Gene namesi
Name:TRIM37
Synonyms:KIAA0898, MUL, POB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7523. TRIM37.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. aggresome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761L → P in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication
VAR_060217
Natural varianti109 – 1091C → S in MUL; no effect on E3 ubiquitin-protein ligase activity. 1 Publication
VAR_060219
Natural varianti322 – 3221G → V in MUL; no effect on ubiquitination but affects subcellular localization. 2 Publications
VAR_060220

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 362CC → SS: Reduces ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication

Organism-specific databases

MIMi253250. phenotype.
Orphaneti2576. MULIBREY nanism.
PharmGKBiPA35497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 964964E3 ubiquitin-protein ligase TRIM37
PRO_0000056254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

Auto-ubiquitinated.

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiO94972.
PaxDbiO94972.
PRIDEiO94972.

PTM databases

PhosphoSiteiO94972.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiO94972.
BgeeiO94972.
CleanExiHS_TRIM37.
GenevestigatoriO94972.

Organism-specific databases

HPAiHPA021911.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRC1O436633EBI-741602,EBI-741137

Protein-protein interaction databases

BioGridi110678. 48 interactions.
DIPiDIP-34437N.
IntActiO94972. 29 interactions.
MINTiMINT-1433848.
STRINGi9606.ENSP00000262294.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1212
Turni16 – 183
Beta strandi23 – 275
Turni29 – 313
Beta strandi34 – 363
Helixi37 – 4610
Turni52 – 543
Helixi60 – 623
Helixi69 – 7911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRQX-ray2.29A/B/C/D1-90[»]
ProteinModelPortaliO94972.
SMRiO94972. Positions 1-84.

Miscellaneous databases

EvolutionaryTraceiO94972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini276 – 403128MATH
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 234103 Reviewed prediction
Add
BLAST
Coiled coili419 – 45032 Reviewed prediction
Add
BLAST
Coiled coili673 – 70028 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi534 – 5407Poly-Ser
Compositional biasi578 – 5814Poly-Ala

Sequence similaritiesi

Belongs to the TRIM/RBCC family.
Contains 1 MATH domain.

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG251245.
HOGENOMiHOG000013010.
HOVERGENiHBG057591.
InParanoidiO94972.
KOiK10608.
OMAiVRCMKTD.
OrthoDBiEOG7QG442.
PhylomeDBiO94972.
TreeFamiTF351092.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR002083. MATH.
IPR008974. TRAF-like.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00917. MATH. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
SMARTiSM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O94972-1) [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

MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ    50
CPHCRAPLQL RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE 100
KLSVFCWTCK KCICHQCALW GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL 150
RRRLMELISL VQEVERNVEA VRNAKDERVR EIRNAVEMMI ARLDTQLKNK 200
LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK SSEILMMFQQ 250
VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP 300
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ 350
SCNDPTKNII REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR 400
FQVRSPTFFQ KSRDQHWYIT QLEAAQTSYI QQINNLKERL TIELSRTQKS 450
RDLSPPDNHL SPQNDDALET RAKKSACSDM LLEGGPTTAS VREAKEDEED 500
EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS TATSNTEEND 550
IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR 600
THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA 650
SYSRKDKDQR KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK 700
SSSAASGDMQ TSLFSADQAA LAACGTENSG RLQDLGMELL AKSSVANCYI 750
RNSTNKKSNS PKPARSSVAG SLSLRRAVDP GENSRSKGDC QTLSEGSPGS 800
SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV AVFSGLPAVE 850
KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM 900
SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG 950
PEDLSFNTDE NSGR 964
Length:964
Mass (Da):107,906
Last modified:November 23, 2004 - v2
Checksum:iC0F08D5A5DC3B5AC
GO
Isoform 2 (identifier: O94972-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     899-937: Missing.

Note: No experimental confirmation available.

Show »
Length:803
Mass (Da):89,186
Checksum:i43486E1064478477
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761L → P in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication
VAR_060217
Natural varianti108 – 1081T → A.1 Publication
Corresponds to variant rs17853504 [ dbSNP | Ensembl ].
VAR_060218
Natural varianti109 – 1091C → S in MUL; no effect on E3 ubiquitin-protein ligase activity. 1 Publication
VAR_060219
Natural varianti322 – 3221G → V in MUL; no effect on ubiquitination but affects subcellular localization. 2 Publications
VAR_060220
Natural varianti838 – 8381V → I.
Corresponds to variant rs7222388 [ dbSNP | Ensembl ].
VAR_052142

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 122122Missing in isoform 2.
VSP_011919Add
BLAST
Alternative sequencei899 – 93739Missing in isoform 2.
VSP_011920Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti624 – 6241D → A in AAL36460. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF213365 mRNA. Translation: AAL36460.1.
AB020705 mRNA. Translation: BAA74921.1. Different initiation.
BX537955 mRNA. Translation: CAD97922.1.
BC036012 mRNA. Translation: AAH36012.1.
CCDSiCCDS32694.1. [O94972-1]
CCDS45746.1. [O94972-1]
RefSeqiNP_001005207.1. NM_001005207.2. [O94972-1]
NP_056109.1. NM_015294.3. [O94972-1]
UniGeneiHs.579079.

Genome annotation databases

EnsembliENST00000262294; ENSP00000262294; ENSG00000108395. [O94972-1]
ENST00000376149; ENSP00000365319; ENSG00000108395. [O94972-2]
ENST00000393066; ENSP00000376785; ENSG00000108395. [O94972-1]
GeneIDi4591.
KEGGihsa:4591.
UCSCiuc002iwy.4. human. [O94972-1]
uc002ixa.4. human. [O94972-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF213365 mRNA. Translation: AAL36460.1 .
AB020705 mRNA. Translation: BAA74921.1 . Different initiation.
BX537955 mRNA. Translation: CAD97922.1 .
BC036012 mRNA. Translation: AAH36012.1 .
CCDSi CCDS32694.1. [O94972-1 ]
CCDS45746.1. [O94972-1 ]
RefSeqi NP_001005207.1. NM_001005207.2. [O94972-1 ]
NP_056109.1. NM_015294.3. [O94972-1 ]
UniGenei Hs.579079.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LRQ X-ray 2.29 A/B/C/D 1-90 [» ]
ProteinModelPortali O94972.
SMRi O94972. Positions 1-84.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110678. 48 interactions.
DIPi DIP-34437N.
IntActi O94972. 29 interactions.
MINTi MINT-1433848.
STRINGi 9606.ENSP00000262294.

PTM databases

PhosphoSitei O94972.

Proteomic databases

MaxQBi O94972.
PaxDbi O94972.
PRIDEi O94972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262294 ; ENSP00000262294 ; ENSG00000108395 . [O94972-1 ]
ENST00000376149 ; ENSP00000365319 ; ENSG00000108395 . [O94972-2 ]
ENST00000393066 ; ENSP00000376785 ; ENSG00000108395 . [O94972-1 ]
GeneIDi 4591.
KEGGi hsa:4591.
UCSCi uc002iwy.4. human. [O94972-1 ]
uc002ixa.4. human. [O94972-2 ]

Organism-specific databases

CTDi 4591.
GeneCardsi GC17M057059.
H-InvDB HIX0014039.
HGNCi HGNC:7523. TRIM37.
HPAi HPA021911.
MIMi 253250. phenotype.
605073. gene.
neXtProti NX_O94972.
Orphaneti 2576. MULIBREY nanism.
PharmGKBi PA35497.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251245.
HOGENOMi HOG000013010.
HOVERGENi HBG057591.
InParanoidi O94972.
KOi K10608.
OMAi VRCMKTD.
OrthoDBi EOG7QG442.
PhylomeDBi O94972.
TreeFami TF351092.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki O94972.

Miscellaneous databases

ChiTaRSi TRIM37. human.
EvolutionaryTracei O94972.
GeneWikii TRIM37.
GenomeRNAii 4591.
NextBioi 17650.
PROi O94972.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94972.
Bgeei O94972.
CleanExi HS_TRIM37.
Genevestigatori O94972.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR003649. Bbox_C.
IPR002083. MATH.
IPR008974. TRAF-like.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00917. MATH. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view ]
SMARTi SM00502. BBC. 1 hit.
SM00336. BBOX. 1 hit.
SM00061. MATH. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiTRI37_HUMAN
AccessioniPrimary (citable) accession number: O94972
Secondary accession number(s): Q7Z3E6, Q8IYF7, Q8WYF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: September 3, 2014
This is version 131 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 17
    Human chromosome 17: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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