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Protein Page:
TRIM27 (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
TRIM27 Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Defects in TRIM27 are a cause of thyroid papillary carcinoma (TPC). TPC is a common tumor of the thyroid that typically arises as an irregular, solid or cystic mass from otherwise normal thyroid tissue. Papillary carcinomas are malignant neoplasm characterized by the formation of numerous, irregular, finger-like projections of fibrous stroma that is covered with a surface layer of neoplastic epithelial cells. A chromosomal aberration involving TRIM27/RFP is found in thyroid papillary carcinomas. Translocation t(6;10)(p21.3;q11.2) with RET. The translocation generates TRIM27/RET and delta TRIM27/RET oncogenes. 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: Motility/polarity/chemotaxis; Ubiquitin conjugating system; EC 6.3.2.-
Cellular Component: nucleoplasm; PML body; nuclear membrane; membrane; integral to plasma membrane; retromer complex; cytoplasm; early endosome; nucleus; endosome
Molecular Function: protein binding; nucleic acid binding; DNA binding; zinc ion binding; metal ion binding; ubiquitin-protein ligase activity; transmembrane receptor protein tyrosine kinase activity; ligase activity
Biological Process: cell proliferation; negative regulation of viral transcription; peptidyl-tyrosine phosphorylation; transcription, DNA-dependent; negative regulation of gene expression, epigenetic; negative regulation of adaptive immune response; negative regulation of protein kinase activity; innate immune response; positive regulation of transcription factor activity; spermatogenesis; negative regulation of transcription from RNA polymerase II promoter; negative regulation of tumor necrosis factor production; retrograde transport, endosome to Golgi
Reference #:  P14373 (UniProtKB)
Alt. Names/Synonyms: Ret finger protein; RFP; RFP transforming protein; RING finger protein 76; RNF76; TRI27; TRIM27; tripartite motif protein TRIM27; tripartite motif-containing 27; Tripartite motif-containing protein 27; Zinc finger protein RFP
Gene Symbols: TRIM27
Molecular weight: 58,490 Da
Basal Isoelectric point: 5.83  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TRIM27

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 K79-ub ANVTQLVkQLRTERP
0 1 T269-p RIPEPWItPPDLQEK
0 2 K292-ub LFLTESLkQFTEKMQ
0 1 K304-ub KMQSDMEkIQELREA
0 1 S341-p NLRQVRYsYLQQDLP
0 9 K380-ub WEVEVGDkAkWTIGV
0 1 K382-ub VEVGDkAkWTIGVCE
0 1 S493-p PLIICPMsGIDGFsG
0 1 S499-p MsGIDGFsGHVGNHG
  mouse

 
K79 ANVTQLVKQLRTERP
T269 RIPEPWITPPDLQEK
K292 LFLTESLKQFTEKMQ
K304 KMQSDMEKIQELREA
S341 NLRQVRYSYLQQDLP
K380-ub WEVEVGDkAKWTIGV
K382 VEVGDkAKWTIGVCE
S493 PLIICPMSGIDGFSG
S499 MSGIDGFSGHVGNHG
  rat

 
K79 ANVTQLVKQLRTERP
T269 RIPEPWITPPDLQEK
K292 LFLTESLKQFTEKMQ
K304 KMQSDMEKIQELREA
S341 NLRQVRYSYLQQDLP
K380 WEVEVGDKAKWTIGV
K382 VEVGDKAKWTIGVCE
S493 PLIICPMSGIDGFSG
S499 MSGIDGFSGHVGNHG
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