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Protein

Tripartite motif-containing protein 72

Gene

Trim72

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

Functioni

Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca2+-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri14 – 57RING-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri81 – 122B box-typePROSITE-ProRule annotationAdd BLAST42

GO - Molecular functioni

  • phosphatidylserine binding Source: UniProtKB
  • ubiquitin conjugating enzyme binding Source: MGI
  • ubiquitin protein ligase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Keywordsi

Biological processExocytosis, Transport
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-445355 Smooth Muscle Contraction

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 72
Alternative name(s):
Mitsugumin-53
Short name:
Mg53
Gene namesi
Name:Trim72Imported
Synonyms:Mg53Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:3612190 Trim72

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Viable until at least 11 months of age under unstressed conditions, and develop progressive muscle pathology with age. Mice show progressive myopathy and reduced exercise capability, associated with defective membrane-repair capacity.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi17C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi29C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi34C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi37C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi53C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi55C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi56C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi86C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi97C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi105C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi108C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi144C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi242C → A: Dominant-negative mutant that abolishes homooligomerization and function in membrane repair. 1 Publication1
Mutagenesisi313C → A: Does not affect homooligomerization. 1 Publication1
Mutagenesisi456C → A: Does not affect homooligomerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002781311 – 477Tripartite motif-containing protein 72Add BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei144S-nitrosocysteineBy similarity1
Disulfide bondi242Interchain1 Publication
Modified residuei255PhosphoserineBy similarity1

Post-translational modificationi

Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.
S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiQ1XH17
PaxDbiQ1XH17
PeptideAtlasiQ1XH17
PRIDEiQ1XH17

PTM databases

iPTMnetiQ1XH17
PhosphoSitePlusiQ1XH17

Expressioni

Tissue specificityi

Muscle-specific. Exclusively expressed in cardiac and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSMUSG00000042828 Expressed in 17 organ(s), highest expression level in skeletal muscle tissue
CleanExiMM_TRIM72

Interactioni

Subunit structurei

Homooligomer; disulfide-linked. Interacts with DYSF and CAV3.2 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi241694, 2 interactors
DIPiDIP-60129N
IntActiQ1XH17, 4 interactors
STRINGi10090.ENSMUSP00000079832

Structurei

3D structure databases

ProteinModelPortaliQ1XH17
SMRiQ1XH17
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini271 – 475B30.2/SPRYPROSITE-ProRule annotationAdd BLAST205

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili135 – 169Sequence analysisAdd BLAST35
Coiled coili204 – 232Sequence analysisAdd BLAST29

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Sequence analysis

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri14 – 57RING-typePROSITE-ProRule annotationAdd BLAST44
Zinc fingeri81 – 122B box-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2177 Eukaryota
ENOG4111G04 LUCA
GeneTreeiENSGT00760000118838
HOGENOMiHOG000234133
HOVERGENiHBG098570
InParanoidiQ1XH17
KOiK12036
OMAiSDGEHYW
OrthoDBiEOG091G06AH
PhylomeDBiQ1XH17
TreeFamiTF342569

Family and domain databases

CDDicd00021 BBOX, 1 hit
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR003879 Butyrophylin_SPRY
IPR013320 ConA-like_dom_sf
IPR006574 PRY
IPR003877 SPRY_dom
IPR035038 TRIM72
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
PANTHERiPTHR24103:SF11 PTHR24103:SF11, 1 hit
PfamiView protein in Pfam
PF13765 PRY, 1 hit
PF00622 SPRY, 1 hit
PF00643 zf-B_box, 1 hit
PRINTSiPR01407 BUTYPHLNCDUF
SMARTiView protein in SMART
SM00336 BBOX, 1 hit
SM00589 PRY, 1 hit
SM00184 RING, 1 hit
SM00449 SPRY, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 1 hit
PS50119 ZF_BBOX, 1 hit
PS00518 ZF_RING_1, 1 hit
PS50089 ZF_RING_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q1XH17-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT
60 70 80 90 100
VACPCCQAPT RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD
110 120 130 140 150
RTLVCGVCAS LGSHRGHRLL PAAEAQARLK TQLPQQKMQL QEACMRKEKT
160 170 180 190 200
VAVLEHQLVE VEETVRQFRG AVGEQLGKMR MFLAALESSL DREAERVRGD
210 220 230 240 250
AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK FCLVTSRLQK
260 270 280 290 300
ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP
310 320 330 340 350
SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE
360 370 380 390 400
VGDKPRWALG VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP
410 420 430 440 450
RALRTPERPP ARIGLYLSFA DGVLAFYDAS NPDVLTPIFS FHERLPGPVY
460 470
PIFDVCWHDK GKNAQPLLLV GPEQEQA
Length:477
Mass (Da):52,817
Last modified:May 2, 2006 - v1
Checksum:iDFB52299E5FFB66B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB231474 mRNA Translation: BAE93014.1
BC067209 mRNA Translation: AAH67209.1
BC147789 mRNA Translation: AAI47790.1
BC158111 mRNA Translation: AAI58112.1
BC158120 mRNA Translation: AAI58121.1
CCDSiCCDS40148.1
RefSeqiNP_001073401.1, NM_001079932.3
XP_006508065.1, XM_006508002.3
UniGeneiMm.389924

Genome annotation databases

EnsembliENSMUST00000081042; ENSMUSP00000079832; ENSMUSG00000042828
ENSMUST00000106248; ENSMUSP00000101855; ENSMUSG00000042828
GeneIDi434246
KEGGimmu:434246
UCSCiuc009jxv.2 mouse

Similar proteinsi

Entry informationi

Entry nameiTRI72_MOUSE
AccessioniPrimary (citable) accession number: Q1XH17
Secondary accession number(s): B2RWH7, Q6NX76
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 2, 2006
Last modified: September 12, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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