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Protein

E3 ubiquitin-protein ligase TRIM63

Gene

Trim63

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

Functioni

E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.2 Publications

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 fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • muscle contraction Source: MGI
  • response to electrical stimulus involved in regulation of muscle adaptation Source: UniProtKB
  • response to glucocorticoid Source: RGD
  • response to interleukin-1 Source: RGD
  • skeletal muscle atrophy Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Muscle protein

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.2.19. 5301.
ReactomeiR-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM63 (EC:6.3.2.-)
Alternative name(s):
Muscle-specific RING finger protein 1
Short name:
MuRF-1
Short name:
MuRF1
Tripartite motif-containing protein 63
Gene namesi
Name:Trim63
Synonyms:Murf1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi619964. Trim63.

Subcellular locationi

GO - Cellular componenti

  • contractile fiber Source: MGI
  • M band Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351E3 ubiquitin-protein ligase TRIM63PRO_0000056292Add
BLAST

Proteomic databases

PaxDbiQ91Z63.
PRIDEiQ91Z63.

Expressioni

Tissue specificityi

Muscle specific. Selectively expressed in heart and skeletal muscle.1 Publication

Inductioni

By interleukin-1, dexamethasone, lipolysaccharide and indinavir. Up-regulated upon muscle denervation, immobilization and unweighting and more generally upon muscle atrophy. Up-regulated upon sepsis. Down-regulated upon aging.6 Publications

Gene expression databases

GenevisibleiQ91Z63. RN.

Interactioni

Subunit structurei

Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 and TNNI3. Forms a ternary complex with RACK1 and PRKCE. Interacts with CKM (By similarity).By similarity

Protein-protein interaction databases

BioGridi250873. 1 interaction.
STRINGi10116.ENSRNOP00000058869.

Structurei

3D structure databases

ProteinModelPortaliQ91Z63.
SMRiQ91Z63. Positions 119-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 32559COSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni74 – 218145Interaction with TTNBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili189 – 26981Sequence analysisAdd
BLAST

Domaini

The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus. Also required for the E3 ubiquitin ligase activity (By similarity).By similarity
The B box-type zinc finger mediates homodimerization.By similarity

Sequence similaritiesi

Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 COS domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri23 – 7957RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 15943B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITEN. Eukaryota.
ENOG4110918. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231156.
HOVERGENiHBG071242.
InParanoidiQ91Z63.
KOiK10655.
OMAiDGNPMEN.
OrthoDBiEOG7VDXPK.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR017903. COS_domain.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51262. COS. 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.

Q91Z63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYKSGLIPD GNAMENLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND
60 70 80 90 100
IFQAANPYWT NRGGSVSMSG GRFRCPSCRH EVIMDRHGVY GLQRNLLVEN
110 120 130 140 150
IIDIYKQECS SRPLQKGSHP MCKEHEDEKI NIYCLTCEVP TCSLCKVFGA
160 170 180 190 200
HQACEVAPLQ SIFQGQKTEL SNCISMLVAG NDRVQTIISQ LEDSCRVTKE
210 220 230 240 250
NSHQVKEELS HKFDALYAIL DEKKSELLQR ITQEQEEKLD FIEALILQYR
260 270 280 290 300
EQLEKSTKLV ETAIQSLDEP GGATFLLSAK PLIKSIVEAS KGCQLGKTEQ
310 320 330 340 350
GFENMDYFTL NLEHIAEALR AIDFGTDEEE EFTEEEEEED QEEGVSTEGH

Q
Length:351
Mass (Da):39,723
Last modified:December 1, 2001 - v1
Checksum:iBF906A21340C4D97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY059627 mRNA. Translation: AAL16405.1.
BC061824 mRNA. Translation: AAH61824.1.
RefSeqiNP_543179.1. NM_080903.1.
UniGeneiRn.40636.

Genome annotation databases

EnsembliENSRNOT00000067524; ENSRNOP00000058869; ENSRNOG00000016543.
GeneIDi140939.
KEGGirno:140939.
UCSCiRGD:619964. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY059627 mRNA. Translation: AAL16405.1.
BC061824 mRNA. Translation: AAH61824.1.
RefSeqiNP_543179.1. NM_080903.1.
UniGeneiRn.40636.

3D structure databases

ProteinModelPortaliQ91Z63.
SMRiQ91Z63. Positions 119-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250873. 1 interaction.
STRINGi10116.ENSRNOP00000058869.

Proteomic databases

PaxDbiQ91Z63.
PRIDEiQ91Z63.

Protocols and materials databases

DNASUi140939.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000067524; ENSRNOP00000058869; ENSRNOG00000016543.
GeneIDi140939.
KEGGirno:140939.
UCSCiRGD:619964. rat.

Organism-specific databases

CTDi84676.
RGDi619964. Trim63.

Phylogenomic databases

eggNOGiENOG410ITEN. Eukaryota.
ENOG4110918. LUCA.
GeneTreeiENSGT00760000118878.
HOGENOMiHOG000231156.
HOVERGENiHBG071242.
InParanoidiQ91Z63.
KOiK10655.
OMAiDGNPMEN.
OrthoDBiEOG7VDXPK.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 5301.
ReactomeiR-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi620830.
PROiQ91Z63.

Gene expression databases

GenevisibleiQ91Z63. RN.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR017903. COS_domain.
IPR027370. Znf-RING_LisH.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
PF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS51262. COS. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, FUNCTION.
    Strain: Sprague-Dawley.
  2. "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: Prostate.
  3. "Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1."
    McElhinny A.S., Kakinuma K., Sorimachi H., Labeit S., Gregorio C.C.
    J. Cell Biol. 157:125-136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Induction of MafBx and Murf ubiquitin ligase mRNAs in rat skeletal muscle after LPS injection."
    Dehoux M.J.M., van Beneden R.P., Fernandez-Celemin L., Lause P.L., Thissen J.-P.M.
    FEBS Lett. 544:214-217(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle."
    Wray C.J., Mammen J.M.V., Hershko D.D., Hasselgren P.-O.
    Int. J. Biochem. Cell Biol. 35:698-705(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression."
    Lecker S.H., Jagoe R.T., Gilbert A., Gomes M., Baracos V., Bailey J., Price S.R., Mitch W.E., Goldberg A.L.
    FASEB J. 18:39-51(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents cardiomyocyte hypertrophy."
    Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., Patterson C.
    J. Cell Biol. 167:1147-1159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Indinavir alters regulators of protein anabolism and catabolism in skeletal muscle."
    Hong-Brown L.Q., Pruznak A.M., Frost R.A., Vary T.C., Lang C.H.
    Am. J. Physiol. 289:E382-E390(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Selective downregulation of ubiquitin conjugation cascade mRNA occurs in the senescent rat soleus muscle."
    DeRuisseau K.C., Kavazis A.N., Powers S.K.
    Exp. Gerontol. 40:526-531(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiTRI63_RAT
AccessioniPrimary (citable) accession number: Q91Z63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 112 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.