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Protein

E3 ubiquitin-protein ligase TRIM69

Gene

Trim69

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in apoptosis.By similarity

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 fingeri41 – 8242RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM69 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 36
Tripartite motif-containing protein 69
Gene namesi
Name:Trim69
Synonyms:Rnf36
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1305074. Trim69.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499E3 ubiquitin-protein ligase TRIM69PRO_0000278238Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei341 – 3411PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Phosphorylation is necessary for nuclear localization (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5BK82.
PRIDEiQ5BK82.

Interactioni

Subunit structurei

Interacts with PML.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023209.

Structurei

3D structure databases

ProteinModelPortaliQ5BK82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini305 – 499195B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 152152Necessary for nuclear localizationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili160 – 265106Sequence analysisAdd
BLAST

Domaini

The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity and for nuclear localization and aggregation.By similarity

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
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 fingeri41 – 8242RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG410XWXM. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiQ5BK82.
KOiK12034.
OMAiASIQARM.
OrthoDBiEOG72RMXQ.
PhylomeDBiQ5BK82.
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.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5BK82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVSSRPPSN FDPGNYVEVS DPSTHLPSKV VIQDITTELH CPLCNDWFRD
60 70 80 90 100
PLMLTCGHNF CQACIQNYWK MQAKETFCPE CKMLCQYSNC TFNLVLEKLV
110 120 130 140 150
EKIKRLPLLK GHPQCPEHGE NLKLFSKPDG KMICFQCKDA RLSMGQSKDF
160 170 180 190 200
LQISEAVRFF TEELAIYQSQ LQTTLKELQS LRTMQKDAIA AYKDNKIQLQ
210 220 230 240 250
QNLSLEFLKL HQFLHNKEKD ILNDLRDEGK VLNEEMDANL NQIQEQCLLA
260 270 280 290 300
KDMLANIQAR MEQQNSFDFL TDITKLLENM EKGMKTLVPR QLISKKLSLG
310 320 330 340 350
RFKGPIQYTI WREMQSILSP GPSQLTLDPK TAHPNLVLSN SRTSVCHGDV
360 370 380 390 400
KQVMPDDPER FDSSVAVLGS KGFTSGKWYW EIEVAKKTKW TIGIVRESII
410 420 430 440 450
RKGSCPLTPE QGFWLLRLRN QTDLKALDLP SCSLNLGDLR RVGVYLDYEG
460 470 480 490
GQVSFYNATN MTHLYTFTSV FLEKLFPYLC PCLNDGGENK EPLHIVHPQ
Length:499
Mass (Da):57,215
Last modified:April 12, 2005 - v1
Checksum:i6050B9543D8E9A49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC091171 mRNA. Translation: AAH91171.1.
RefSeqiNP_001013178.1. NM_001013160.1.
UniGeneiRn.95375.

Genome annotation databases

EnsembliENSRNOT00000023209; ENSRNOP00000023209; ENSRNOG00000017157.
GeneIDi311373.
KEGGirno:311373.
UCSCiRGD:1305074. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC091171 mRNA. Translation: AAH91171.1.
RefSeqiNP_001013178.1. NM_001013160.1.
UniGeneiRn.95375.

3D structure databases

ProteinModelPortaliQ5BK82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023209.

Proteomic databases

PaxDbiQ5BK82.
PRIDEiQ5BK82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023209; ENSRNOP00000023209; ENSRNOG00000017157.
GeneIDi311373.
KEGGirno:311373.
UCSCiRGD:1305074. rat.

Organism-specific databases

CTDi140691.
RGDi1305074. Trim69.

Phylogenomic databases

eggNOGiKOG2177. Eukaryota.
ENOG410XWXM. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG001357.
InParanoidiQ5BK82.
KOiK12034.
OMAiASIQARM.
OrthoDBiEOG72RMXQ.
PhylomeDBiQ5BK82.
TreeFamiTF342569.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi663486.
PROiQ5BK82.

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.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRI69_RAT
AccessioniPrimary (citable) accession number: Q5BK82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: April 12, 2005
Last modified: December 9, 2015
This is version 90 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.