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Protein

E3 ubiquitin-protein ligase TRIM37

Gene

Trim37

Organism
Mus musculus (Mouse)
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 (By similarity). Probably acts by ubiquitinating positive regulators of centriole reduplication (By similarity). 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).By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM37Curated (EC:6.3.2.-By similarity)
Alternative name(s):
Tripartite motif-containing protein 37Curated
Gene namesi
Name:Trim37Imported
Synonyms:Kiaa08981 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2153072. Trim37.

Subcellular locationi

  • Cytoplasmperinuclear region By similarity
  • Peroxisome By similarity

  • Note: Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961E3 ubiquitin-protein ligase TRIM37PRO_0000056255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

Auto-ubiquitinated.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ6PCX9.
PaxDbiQ6PCX9.
PRIDEiQ6PCX9.

PTM databases

iPTMnetiQ6PCX9.
PhosphoSiteiQ6PCX9.

Expressioni

Tissue specificityi

Highly expressed in testis and brain. In embryonic tissues, expressed in epithelia, including ducts of the developing pancreas, epithelium of the midgut and nasal epithelium. In adult, detected in the central and peripheral nervous systems, including enteric ganglia, retina and the adrenal medulla (at protein level).1 Publication

Gene expression databases

BgeeiQ6PCX9.
CleanExiMM_TRIM37.
ExpressionAtlasiQ6PCX9. baseline and differential.
GenevisibleiQ6PCX9. MM.

Interactioni

Subunit structurei

Associates with the PRC2/EED-EZH2 complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049057.

Structurei

3D structure databases

ProteinModelPortaliQ6PCX9.
SMRiQ6PCX9. Positions 1-84, 88-230.
ModBaseiSearch...
MobiDBiSearch...

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi535 – 5417Poly-Ser
Compositional biasi579 – 5824Poly-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

eggNOGiENOG410ITG1. Eukaryota.
ENOG410YSD5. LUCA.
GeneTreeiENSGT00410000025800.
HOGENOMiHOG000013010.
HOVERGENiHBG057591.
InParanoidiQ6PCX9.
KOiK10608.
OMAiCYIRNST.
OrthoDBiEOG7QG442.
PhylomeDBiQ6PCX9.
TreeFamiTF351092.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR002083. MATH/TRAF_dom.
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.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PCX9-1 [UniParc]FASTAAdd to basket

« 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 NRQNDTVILR
410 420 430 440 450
FQVRSPTFFQ KCRDQHWYIT QLEAAQTGYI QQINNLKERL TIELSRTQKS
460 470 480 490 500
RDLSPPDNHL SPQNDDSPET RTKKAGSCSD MLLEGGPTCA SVRETKEDED
510 520 530 540 550
EEEKIQNEDY HHELSDGDLD LDLVGEDEVN HLDGSSSSAS STATSNTEEN
560 570 580 590 600
DIDEETMSGE NDVEYNSMEL EEGELMEDAA AAGPPGSSHS YVGASSRMSR
610 620 630 640 650
RTHLCSAATS SLLDIDPLIL IHLLDLKDRS SMENLWGLQP RPSASLLQPT
660 670 680 690 700
ASYSRKDKDQ RKQQAMWRVP SDLKMLKRLK TQMAEVRCMK TDVKTTLSDI
710 720 730 740 750
KGSSVASTDM QTNLFCADQA ALTTCGPENS GRLQDLGMEL LAKSSVAGCY
760 770 780 790 800
IRNPTNKKNS PKSARAIAGS LSLRRAVDSG ENSRSKGDCQ VLAEGSSGSS
810 820 830 840 850
QSGSRHSSPR ALTHGIIGDL LPKSEDRQCK ALDSDAVVVA VFNGLPTVEK
860 870 880 890 900
RRKMVTLGTN AKGGRLEGMQ MADLESHSEA GEVQPTLPEG ASAAPEEGMS
910 920 930 940 950
SDSDIECDTE NEEQEEHTSM GAFNDPFLAQ PPDEDSHSSF PDGEQIDPEN
960
LHFNPDEGGG R
Length:961
Mass (Da):107,660
Last modified:July 5, 2004 - v1
Checksum:i85629CEFE0A1D6EA
GO

Sequence cautioni

The sequence BAC41455.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2326Missing in BAC41455 (PubMed:12465718).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093271 Transcribed RNA. Translation: BAC41455.1. Different initiation.
AK140822 mRNA. Translation: BAE24489.1.
BC058678 mRNA. Translation: AAH58678.1.
BC059070 mRNA. Translation: AAH59070.1.
CCDSiCCDS25210.1.
RefSeqiNP_932104.1. NM_197987.2.
UniGeneiMm.17436.

Genome annotation databases

EnsembliENSMUST00000041282; ENSMUSP00000049057; ENSMUSG00000018548.
GeneIDi68729.
KEGGimmu:68729.
UCSCiuc007ktm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093271 Transcribed RNA. Translation: BAC41455.1. Different initiation.
AK140822 mRNA. Translation: BAE24489.1.
BC058678 mRNA. Translation: AAH58678.1.
BC059070 mRNA. Translation: AAH59070.1.
CCDSiCCDS25210.1.
RefSeqiNP_932104.1. NM_197987.2.
UniGeneiMm.17436.

3D structure databases

ProteinModelPortaliQ6PCX9.
SMRiQ6PCX9. Positions 1-84, 88-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000049057.

PTM databases

iPTMnetiQ6PCX9.
PhosphoSiteiQ6PCX9.

Proteomic databases

MaxQBiQ6PCX9.
PaxDbiQ6PCX9.
PRIDEiQ6PCX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041282; ENSMUSP00000049057; ENSMUSG00000018548.
GeneIDi68729.
KEGGimmu:68729.
UCSCiuc007ktm.2. mouse.

Organism-specific databases

CTDi4591.
MGIiMGI:2153072. Trim37.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410ITG1. Eukaryota.
ENOG410YSD5. LUCA.
GeneTreeiENSGT00410000025800.
HOGENOMiHOG000013010.
HOVERGENiHBG057591.
InParanoidiQ6PCX9.
KOiK10608.
OMAiCYIRNST.
OrthoDBiEOG7QG442.
PhylomeDBiQ6PCX9.
TreeFamiTF351092.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiTrim37. mouse.
NextBioi327786.
PROiQ6PCX9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PCX9.
CleanExiMM_TRIM37.
ExpressionAtlasiQ6PCX9. baseline and differential.
GenevisibleiQ6PCX9. MM.

Family and domain databases

Gene3Di2.60.210.10. 1 hit.
3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR003649. Bbox_C.
IPR002083. MATH/TRAF_dom.
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.
[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. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
    DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Tissue expression of the mulibrey nanism-associated Trim37 protein in embryonic and adult mouse tissues."
    Kallijarvi J., Hamalainen R.H., Karlberg N., Sainio K., Lehesjoki A.E.
    Histochem. Cell Biol. 126:325-334(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  6. "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.

Entry informationi

Entry nameiTRI37_MOUSE
AccessioniPrimary (citable) accession number: Q6PCX9
Secondary accession number(s): Q5SX31, Q8CHC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.