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Protein

E3 ubiquitin-protein ligase TRIM37

Gene

TRIM37

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Has anti-HIV activity (PubMed:24317724).4 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5541RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • ligase activity Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • tumor necrosis factor receptor binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aggresome assembly Source: UniProtKB
  • histone H2A-K119 monoubiquitination Source: UniProtKB
  • histone H2A monoubiquitination Source: UniProtKB
  • negative regulation of centriole replication Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, 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 TRIM37Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
Mulibrey nanism protein1 Publication
Tripartite motif-containing protein 37Curated
Gene namesi
Name:TRIM37Imported
Synonyms:KIAA0898, MUL1 Publication, POB11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7523. TRIM37.

Subcellular locationi

GO - Cellular componenti

  • aggresome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Involvement in diseasei

Mulibrey nanism (MUL)8 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive growth disorder characterized by severe growth failure of prenatal onset, constrictive pericardium and progressive cardiomyopathy, facial dysmorphism, and failure of sexual maturation. Additional clinical features include hepatomegaly, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, hypoplasia of various endocrine glands, insulin resistance with type 2 diabetes, and an increased risk for Wilms' tumor.

See also OMIM:253250
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
Mutagenesisi18 – 181C → R: Abolishes ability to monoubiquitinate 'Lys-119' of histone H2A (H2AK119Ub). 1 Publication
Mutagenesisi35 – 362CC → SS: Reduces ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication

Keywords - Diseasei

Dwarfism, Proto-oncogene

Organism-specific databases

MIMi253250. phenotype.
Orphaneti2576. MULIBREY nanism.
PharmGKBiPA35497.

Polymorphism and mutation databases

BioMutaiTRIM37.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 964964E3 ubiquitin-protein ligase TRIM37PRO_0000056254Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Auto-ubiquitinated.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiO94972.
PaxDbiO94972.
PRIDEiO94972.

PTM databases

PhosphoSiteiO94972.

Expressioni

Tissue specificityi

Ubiquitous (PubMed:10888877). Highly expressed in testis, while it is weakly expressed in other tissues (PubMed:16310976).2 Publications

Inductioni

Overexpressed in a number of breast cancer cell lines.1 Publication

Gene expression databases

BgeeiO94972.
CleanExiHS_TRIM37.
ExpressionAtlasiO94972. baseline and differential.
GenevestigatoriO94972.

Organism-specific databases

HPAiHPA021911.

Interactioni

Subunit structurei

Associates with the PRC2/EED-EZH2 complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K9323EBI-741602,EBI-10174671
A8KAD63EBI-741602,EBI-10174974
BYSLQ138956EBI-741602,EBI-358049
CDC20BQ86Y333EBI-741602,EBI-10260504
DDX6P261963EBI-741602,EBI-351257
FAM107AO95990-33EBI-741602,EBI-10192902
FAM161AQ3B8203EBI-741602,EBI-719941
FAM50BQ9Y2473EBI-741602,EBI-742802
KAT5Q929933EBI-741602,EBI-399080
MCRS1Q96EZ84EBI-741602,EBI-348259
PRC1O436633EBI-741602,EBI-741137
RASD1Q9Y2723EBI-741602,EBI-740818
RPL9P9P329693EBI-741602,EBI-358122
SCNM1Q9BWG63EBI-741602,EBI-748391
SSX2IPQ9Y2D83EBI-741602,EBI-2212028
UBASH3AP570753EBI-741602,EBI-2105393
ZMAT2Q96NC03EBI-741602,EBI-2682299
ZNF329Q86UD43EBI-741602,EBI-7233259
ZNF417Q8TAU34EBI-741602,EBI-740727

Protein-protein interaction databases

BioGridi110678. 70 interactions.
DIPiDIP-34437N.
IntActiO94972. 44 interactions.
MINTiMINT-1433848.
STRINGi9606.ENSP00000262294.

Structurei

Secondary structure

964
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1212Combined sources
Turni16 – 183Combined sources
Beta strandi23 – 275Combined sources
Turni29 – 313Combined sources
Beta strandi34 – 363Combined sources
Helixi37 – 4610Combined sources
Turni52 – 543Combined sources
Helixi60 – 623Combined sources
Helixi69 – 7911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRQX-ray2.29A/B/C/D1-90[»]
ProteinModelPortaliO94972.
SMRiO94972. Positions 1-84, 88-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini276 – 403128MATHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili132 – 234103Sequence AnalysisAdd
BLAST
Coiled coili419 – 45032Sequence AnalysisAdd
BLAST
Coiled coili673 – 70028Sequence AnalysisAdd
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.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 MATH domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri15 – 5541RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG251245.
GeneTreeiENSGT00410000025800.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94972-1) [UniParc]FASTAAdd to basket

Also known as: TRIM37a1 Publication

, TRIM37b1 Publication

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

        10         20         30         40         50
MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ
60 70 80 90 100
CPHCRAPLQL RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE
110 120 130 140 150
KLSVFCWTCK KCICHQCALW GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL
160 170 180 190 200
RRRLMELISL VQEVERNVEA VRNAKDERVR EIRNAVEMMI ARLDTQLKNK
210 220 230 240 250
LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK SSEILMMFQQ
260 270 280 290 300
VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP
310 320 330 340 350
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ
360 370 380 390 400
SCNDPTKNII REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR
410 420 430 440 450
FQVRSPTFFQ KSRDQHWYIT QLEAAQTSYI QQINNLKERL TIELSRTQKS
460 470 480 490 500
RDLSPPDNHL SPQNDDALET RAKKSACSDM LLEGGPTTAS VREAKEDEED
510 520 530 540 550
EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS TATSNTEEND
560 570 580 590 600
IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR
610 620 630 640 650
THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA
660 670 680 690 700
SYSRKDKDQR KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK
710 720 730 740 750
SSSAASGDMQ TSLFSADQAA LAACGTENSG RLQDLGMELL AKSSVANCYI
760 770 780 790 800
RNSTNKKSNS PKPARSSVAG SLSLRRAVDP GENSRSKGDC QTLSEGSPGS
810 820 830 840 850
SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV AVFSGLPAVE
860 870 880 890 900
KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM
910 920 930 940 950
SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG
960
PEDLSFNTDE NSGR
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
Isoform 3 (identifier: O94972-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-41: Missing.

Show »
Length:930
Mass (Da):103,941
Checksum:i9AD3B427995A9961
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti620 – 6201I → M in BAF85148 (PubMed:14702039).Curated
Sequence conflicti624 – 6241D → A in AAL36460 (Ref. 1) Curated
Sequence conflicti916 – 9161E → G in BAG57954 (PubMed:10048485).Curated

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. 1 PublicationVSP_011919Add
BLAST
Alternative sequencei8 – 4134Missing in isoform 3. VSP_057468Add
BLAST
Alternative sequencei899 – 93739Missing in isoform 2. 1 PublicationVSP_011920Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF213365 mRNA. Translation: AAL36460.1.
AB020705 mRNA. Translation: BAA74921.1. Different initiation.
AK289674 mRNA. Translation: BAF82363.1.
AK294850 mRNA. Translation: BAG57954.1.
AK292459 mRNA. Translation: BAF85148.1.
BX537955 mRNA. Translation: CAD97922.1.
AC005207 Genomic DNA. No translation available.
AC036154 Genomic DNA. No translation available.
AC099850 Genomic DNA. No translation available.
AC100832 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94425.1.
CH471109 Genomic DNA. Translation: EAW94426.1.
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]
XP_005257444.1. XM_005257387.1. [O94972-3]
UniGeneiHs.579079.

Genome annotation databases

EnsembliENST00000262294; ENSP00000262294; ENSG00000108395. [O94972-1]
ENST00000393065; ENSP00000376784; ENSG00000108395. [O94972-3]
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF213365 mRNA. Translation: AAL36460.1.
AB020705 mRNA. Translation: BAA74921.1. Different initiation.
AK289674 mRNA. Translation: BAF82363.1.
AK294850 mRNA. Translation: BAG57954.1.
AK292459 mRNA. Translation: BAF85148.1.
BX537955 mRNA. Translation: CAD97922.1.
AC005207 Genomic DNA. No translation available.
AC036154 Genomic DNA. No translation available.
AC099850 Genomic DNA. No translation available.
AC100832 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94425.1.
CH471109 Genomic DNA. Translation: EAW94426.1.
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]
XP_005257444.1. XM_005257387.1. [O94972-3]
UniGeneiHs.579079.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LRQX-ray2.29A/B/C/D1-90[»]
ProteinModelPortaliO94972.
SMRiO94972. Positions 1-84, 88-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110678. 70 interactions.
DIPiDIP-34437N.
IntActiO94972. 44 interactions.
MINTiMINT-1433848.
STRINGi9606.ENSP00000262294.

PTM databases

PhosphoSiteiO94972.

Polymorphism and mutation databases

BioMutaiTRIM37.

Proteomic databases

MaxQBiO94972.
PaxDbiO94972.
PRIDEiO94972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262294; ENSP00000262294; ENSG00000108395. [O94972-1]
ENST00000393065; ENSP00000376784; ENSG00000108395. [O94972-3]
ENST00000393066; ENSP00000376785; ENSG00000108395. [O94972-1]
GeneIDi4591.
KEGGihsa:4591.
UCSCiuc002iwy.4. human. [O94972-1]
uc002ixa.4. human. [O94972-2]

Organism-specific databases

CTDi4591.
GeneCardsiGC17M057059.
H-InvDBHIX0014039.
HGNCiHGNC:7523. TRIM37.
HPAiHPA021911.
MIMi253250. phenotype.
605073. gene.
neXtProtiNX_O94972.
Orphaneti2576. MULIBREY nanism.
PharmGKBiPA35497.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG251245.
GeneTreeiENSGT00410000025800.
HOGENOMiHOG000013010.
HOVERGENiHBG057591.
InParanoidiO94972.
KOiK10608.
OMAiVRCMKTD.
OrthoDBiEOG7QG442.
PhylomeDBiO94972.
TreeFamiTF351092.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTRIM37. human.
EvolutionaryTraceiO94972.
GeneWikiiTRIM37.
GenomeRNAii4591.
NextBioi17650.
PROiO94972.
SOURCEiSearch...

Gene expression databases

BgeeiO94972.
CleanExiHS_TRIM37.
ExpressionAtlasiO94972. baseline and differential.
GenevestigatoriO94972.

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]
ProtoNetiSearch...

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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. Cited for: INVOLVEMENT IN MUL, TISSUE SPECIFICITY.
  9. "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.
  10. "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: INVOLVEMENT IN MUL.
  11. "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, PATHWAY, VARIANT MUL PRO-76, CHARACTERIZATION OF VARIANTS MUL PRO-76 AND MUL VAL-322.
  12. "Characterisation of the mulibrey nanism-associated TRIM37 gene: transcription initiation, promoter region and alternative splicing."
    Hamalainen R.H., Joensuu T., Kallijarvi J., Lehesjoki A.E.
    Gene 366:180-188(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "A novel mutation in TRIM37 is associated with mulibrey nanism in a Turkish boy."
    Doganc T., Yuksel Konuk B.E., Alpan N., Konuk O., Hamalainen R.H., Lehesjoki A.E., Tekin M.
    Clin. Dysmorphol. 16:173-176(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MUL.
  14. "Testicular failure and male infertility in the monogenic Mulibrey nanism disorder."
    Karlberg S., Toppari J., Karlberg N., Nurmio M., Karikoski R., Jalanko H., Lipsanen-Nyman M.
    J. Clin. Endocrinol. Metab. 96:3399-3407(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MUL.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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.
  17. "Refractory congestive heart failure following delayed pericardectomy in a 12-year-old child with Mulibrey nanism due to a novel mutation in TRIM37."
    Kumpf M., Hamalainen R.H., Hofbeck M., Baden W.
    Eur. J. Pediatr. 172:1415-1418(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MUL.
  18. Cited for: FUNCTION.
  19. "TRIM37 is a new histone H2A ubiquitin ligase and breast cancer oncoprotein."
    Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S., Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.
    Nature 516:116-120(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY, SUBUNIT, INDUCTION, MUTAGENESIS OF CYS-18.
  20. "E3 ubiquitin-protein ligase ring domain from human hr4604d."
    Northeast structural genomics consortium (NESG)
    Submitted (MAR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-90.
  21. Cited for: VARIANT MUL VAL-322, CHARACTERIZATION OF VARIANT MUL VAR-322.
  22. "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): A8K0V9
, A8K8U4, A8MZ79, B4DGZ3, F8WEE6, Q7Z3E6, Q8IYF7, Q8WYF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: April 29, 2015
This is version 139 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

Miscellaneous

Acts as a proto-oncogene via its ability to monoubiquinate 'Lys-119' of histone H2A (H2AK119Ub): overexpressed in a number of breast cancers and promotes transformation of cells by mediating silencing of tumor suppressor genes (PubMed:25470042).1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.