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Protein Page:
TRIM37 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TRIM37 E3 ubiquitin-protein ligase. Defects in TRIM37 are the cause of mulibrey nanism (MUL); also known as muscle-liver-brain-eye nanism. MUL is an autosomal recessive disorder that involves several tissues of mesodermal origin, implying a defect in a highly pleiotropic gene. Characteristic features include severe growth failure of prenatal onset and constrictive pericardium with consequent hepatomegaly. In addition, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, typical dysmorphic features and hypoplasia of various endocrine glands causing hormonal deficiency are common. Belongs to the TRIM/RBCC family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; Ubiquitin ligase; Ligase; EC 6.3.2.-
Chromosomal Location of Human Ortholog: 17q23.2
Cellular Component: perinuclear region of cytoplasm; cytoplasm; peroxisome; cytosol
Molecular Function: protein binding; protein homodimerization activity; zinc ion binding; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; tumor necrosis factor receptor binding; ligase activity
Biological Process: protein autoubiquitination; inhibition of NF-kappaB transcription factor; positive regulation of transcription factor activity; negative regulation of centriole replication; activation of NF-kappaB transcription factor
Reference #:  O94972 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase TRIM37; KIAA0898; MUL; Mulibrey nanism protein; POB1; RING-B-box-coiled-coil protein; TEF3; TRI37; TRIM37; tripartite motif-containing 37; Tripartite motif-containing protein 37
Gene Symbols: TRIM37
Molecular weight: 107,906 Da
Basal Isoelectric point: 5.04  Predict pI for various phosphorylation states
Select Structure to View Below

TRIM37

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S32-p ARLCPHCsKLCCFsC
0 1 S38-p CsKLCCFsCIRRWLT
0 5 T73 CRWAEEVTQQLDTLQ
0 1 T78 EVTQQLDTLQLCSLT
0 7 S83 LDTLQLCSLTKHEEN
0 7 T85 TLQLCSLTKHEENEK
0 1 T195-p MMIARLDtQLKNKLI
0 1 T203-p QLKNKLItLMGQKTS
0 1 S220 QETELLESLLQEVEH
0 1 S258-p VHRKPMAsFVttPVP
0 1 T261-p KPMAsFVttPVPPDF
0 1 T262-p PMAsFVttPVPPDFT
0 1 Y313-p LCWRLKVyPDGNGVV
0 1 K411 RSPTFFQKSRDQHWY
0 5 S454-p TQKSRDLsPPDNHLs
0 4 S461-p sPPDNHLsPQNDDAL
0 1 K693-ub RCMKTDVkNTLSEIK
0 1 S697 TDVkNTLSEIKSSSA
0 1 P763 KKSNSPKPARsSVAG
0 1 S766-p NSPKPARsSVAGSLs
0 1 S771 ARsSVAGSLsLRRAV
0 2 S773-p sSVAGSLsLRRAVDP
0 1 S784-p AVDPGENsRSKGDCQ
0 1 K787 PGENsRSKGDCQTLS
0 1 K824-ub SIGDILPkTEDRQCK
0 1 S844-p AVVVAVFsGLPAVEK
  mouse

 
S32 ARLCPHCSKLCCFSC
S38 CSKLCCFSCIRRWLT
T73-p CRWAEEVtQQLDtLQ
T78-p EVtQQLDtLQLCsLt
S83-p LDtLQLCsLtKHEEN
T85-p tLQLCsLtKHEENEK
T195 MMIARLDTQLKNKLI
T203 QLKNKLITLMGQKTS
S220-p QETELLEsLLQEVEH
S258 VHRKPMASFVTTPVP
T261 KPMASFVTTPVPPDF
T262 PMASFVTTPVPPDFT
Y313 LCWRLKVYPDGNGVV
K411-ub RSPTFFQkCRDQHWY
S454-p TQKSRDLsPPDNHLS
S461 sPPDNHLSPQNDDSP
K694 RCMKTDVKTTLsDIK
S698-p TDVKTTLsDIKGSSV
S763-p NKKNSPKsARAIAGs
- gap
S770-p sARAIAGsLsLRRAV
S772-p RAIAGsLsLRRAVDS
S783 AVDSGENSRSkGDCQ
K786-ub SGENSRSkGDCQVLA
K823 IIGDLLPKSEDRQCK
N843 AVVVAVFNGLPTVEK
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