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Protein

E3 ubiquitin-protein ligase TRIM31

Gene

Trim31

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May have E3 ubiquitin-protein ligase activity (By similarity). Regulator of Src-induced anchorage independent cell growth.By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
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 fingeri16 – 5641RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri89 – 13042B 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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM31 (EC:6.3.2.-)
Alternative name(s):
Tripartite motif-containing protein 31
Gene namesi
Name:Trim31
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2385051. Trim31.

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion By similarity

  • Note: Predomintanly expressed in the cytoplasm but a fraction is associated with the mitochondria.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507E3 ubiquitin-protein ligase TRIM31PRO_0000386639Add
BLAST

Post-translational modificationi

Auto-ubiquitinated (in vitro).By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ8R0K2.
PaxDbiQ8R0K2.
PRIDEiQ8R0K2.

PTM databases

iPTMnetiQ8R0K2.

Expressioni

Tissue specificityi

Highly expressed in the gastrointestrinal tract, with high expression in the small intestine, moderate in the large intestine and weak in the stomach and esophagus.1 Publication

Gene expression databases

BgeeiQ8R0K2.
GenevisibleiQ8R0K2. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with isoform p52shc of SHC1.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000077535.

Structurei

3D structure databases

ProteinModelPortaliQ8R0K2.
SMRiQ8R0K2. Positions 9-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini315 – 507193B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili176 – 24166Sequence analysisAdd
BLAST
Coiled coili269 – 29830Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5641RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri89 – 13042B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
InParanoidiQ8R0K2.
KOiK12011.
OMAiYFCEQDG.
OrthoDBiEOG71G9TQ.
PhylomeDBiQ8R0K2.
TreeFamiTF342569.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R0K2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGQPLACQL QEEVTCPICM EILQDPVTID CGHNFCLQCI SQVGKTSEKI
60 70 80 90 100
QCPLCKLSVN KNTFRPNKLL ASLAEKIQSM DPADIQAEKE DSRCQRHKEK
110 120 130 140 150
LHYFCEQDGA FLCVVCRDSK DHKSHNVTLI DEAAQNYKVQ IESQAQDLGQ
160 170 180 190 200
KDKKIIEEKK QGEGAIWAFR AQVDLEKLKI HEEFKLLRQR LDEEESFLLS
210 220 230 240 250
RLDWLEQQGA KQLRQYVTVT EKQLNSLRKL TKSLKIRLQS SSMELLKDIK
260 270 280 290 300
DALSRGKEFQ FLNPNPVPED LEKKCSEAKA RHESIIKTLT ELKDDMNAEG
310 320 330 340 350
KRDKSAFMNS LNKEEKESWS LLQKNNSVLP TSVPVTLDKS SADPDLTFSQ
360 370 380 390 400
DLKKVTLYIV AGKASNRQAK PRPFYPFHCV RGSPGLSSGR QVWEAEIRGP
410 420 430 440 450
SGGACIVGVV TELARGAQSQ TVSAQSYIWA LRISPSGCQP FTNCKAQEYL
460 470 480 490 500
QVCLKKVGVY VNHDCGEVVF YDAITSKHIY TFQTSFDGKV FPLFGLQVAC

SHITLSP
Length:507
Mass (Da):57,127
Last modified:June 1, 2002 - v1
Checksum:i086106A2E1BC31FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033650 mRNA. Translation: BAC28407.1.
CH466559 Genomic DNA. Translation: EDL23309.1.
BC026666 mRNA. Translation: AAH26666.1.
CCDSiCCDS28728.1.
RefSeqiNP_666189.1. NM_146077.2.
UniGeneiMm.213417.

Genome annotation databases

EnsembliENSMUST00000078438; ENSMUSP00000077535; ENSMUSG00000058063.
GeneIDi224762.
KEGGimmu:224762.
UCSCiuc008cll.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033650 mRNA. Translation: BAC28407.1.
CH466559 Genomic DNA. Translation: EDL23309.1.
BC026666 mRNA. Translation: AAH26666.1.
CCDSiCCDS28728.1.
RefSeqiNP_666189.1. NM_146077.2.
UniGeneiMm.213417.

3D structure databases

ProteinModelPortaliQ8R0K2.
SMRiQ8R0K2. Positions 9-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000077535.

PTM databases

iPTMnetiQ8R0K2.

Proteomic databases

MaxQBiQ8R0K2.
PaxDbiQ8R0K2.
PRIDEiQ8R0K2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000078438; ENSMUSP00000077535; ENSMUSG00000058063.
GeneIDi224762.
KEGGimmu:224762.
UCSCiuc008cll.1. mouse.

Organism-specific databases

CTDi11074.
MGIiMGI:2385051. Trim31.

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG4111G04. LUCA.
GeneTreeiENSGT00760000118893.
HOGENOMiHOG000234133.
InParanoidiQ8R0K2.
KOiK12011.
OMAiYFCEQDG.
OrthoDBiEOG71G9TQ.
PhylomeDBiQ8R0K2.
TreeFamiTF342569.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ8R0K2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0K2.
GenevisibleiQ8R0K2. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Cecum.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  4. "TRIM31 interacts with p52(Shc) and inhibits Src-induced anchorage-independent growth."
    Watanabe M., Tsukiyama T., Hatakeyama S.
    Biochem. Biophys. Res. Commun. 388:422-427(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SHC1.

Entry informationi

Entry nameiTRI31_MOUSE
AccessioniPrimary (citable) accession number: Q8R0K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: June 1, 2002
Last modified: June 8, 2016
This is version 119 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.