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Protein Page:
TRIM25 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TRIM25 a ubiquitous protein that mediates estrogen action in various target organs. Contains one RING-type zinc finger and one SPRY domain.. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Transcription factor; EC 6.3.2.19; EC 6.3.2.-; Ubiquitin conjugating system; EC 6.3.2.n3; Ligase
Cellular Component: cytoplasm; nucleolus; nucleus; cytosol
Molecular Function: protein binding; zinc ion binding; ubiquitin-protein ligase activity; transcription factor activity
Biological Process: response to vitamin D; positive regulation of I-kappaB kinase/NF-kappaB cascade; viral reproduction; response to estrogen stimulus; innate immune response; positive regulation of transcription factor activity; regulation of virion penetration into host cell; defense response to virus; negative regulation of interferon type I production; activation of NF-kappaB transcription factor
Reference #:  Q14258 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin/ISG15 ligase TRIM25; EFP; Estrogen-responsive finger protein; RING finger protein 147; RNF147; TRI25; TRIM25; tripartite motif protein TRIM25; tripartite motif-containing 25; Tripartite motif-containing protein 25; Ubiquitin/ISG15-conjugating enzyme TRIM25; Z147; Zinc finger protein 147; zinc finger protein 147 (estrogen-responsive finger protein); zinc finger protein-147; ZNF147
Gene Symbols: TRIM25
Molecular weight: 70,973 Da
Basal Isoelectric point: 8.44  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TRIM25

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 2 Y48-p WAVQGSPyLCPQCRA
0 2 Y57-p CPQCRAVyQARPQLH
0 1 E84 LQADLAREPPADVWt
0 30 T91-p EPPADVWtPPARAsA
0 2 S97-p WtPPARAsAPsPNAQ
0 8 S100-p PARAsAPsPNAQVAC
0 26 K117-u CLKEAAVkTCLVCMA
0 1 T201 ASADLEATLRHkLTV
0 1 K205-u LEATLRHkLTVMYSQ
0 1 R226 ALDDVRNRQQDVRMT
0 1 - under review  
0 1 K237-u VRMTANRkVEQLQQE
0 15 Y245-p VEQLQQEyTEMkALL
0 1 K249-u QQEyTEMkALLDASE
0 6 K273-a EEKRVNSkFDtIyQI
0 3 K273-u EEKRVNSkFDtIyQI
0 20 T276-p RVNSkFDtIyQILLk
0 255 Y278-p NSkFDtIyQILLkkK
0 6 K283-u tIyQILLkkKSEIQt
0 3 K284-u IyQILLkkKSEIQtL
0 1 T290-p kkKSEIQtLkEEIEQ
0 1 K292-u KSEIQtLkEEIEQSL
0 1 K301-u EIEQSLTkRDEFEFL
0 2 K310-u DEFEFLEkASKLRGI
0 1 K313 EFLEkASKLRGISTk
0 1 K320-a KLRGISTkPVyIPEV
0 5 K320-u KLRGISTkPVyIPEV
0 4 Y323-p GISTkPVyIPEVELN
0 1 K335-u ELNHKLIkGIHQSTI
0 3 K345-u HQSTIDLkNELKQCI
0 1 - under review  
0 1 - under review  
0 2 K392-u KEEKKSKkPPPVPAL
0 1 L399 kPPPVPALPSkLPTF
0 5 K402-u PVPALPSkLPTFGAP
0 12 K416-u PEQLVDLkQAGLEAA
0 1 G419 LVDLkQAGLEAAAkA
0 7 K425-u AGLEAAAkATSSHPN
0 6 S435-p SSHPNSTsLkAkVLE
0 18 K437-u HPNSTsLkAkVLETF
0 20 K439-u NSTsLkAkVLETFLA
0 4 K447-u VLETFLAkSRPELLE
0 1 C475 NKVALSECYTVASVA
0 1 K509-u LGLHCYKkGIHYWEV
0 1 K567-a AWHNNVEkTLPSTkA
0 2 K567-u AWHNNVEkTLPSTkA
0 2 K573-u EkTLPSTkATRVGVL
  mouse

 
Y48 WVVQGPPYRCPQCRK
Y57 CPQCRKVYQVRPQLQ
T84-p LQAEQARtPVDDWtP
T90-p RtPVDDWtPPARFSA
S96 WtPPARFSASSAATQ
S99 PARFSASSAATQVAC
K116-u CLTEIAVkTCLVCMA
K200-u ASADLEYkLRNKLTI
K204 LEYkLRNKLTIMHSH
K225-u ALEDVRSkQQCVQDS
K234-u QCVQDSMkRKMEQLR
K236 VQDSMkRKMEQLRQE
Y244 MEQLRQEYMEMKAVI
K248 RQEYMEMKAVIDAAE
K272 EEKRVYGKFDTIyQV
K272 EEKRVYGKFDTIyQV
T275 RVYGKFDTIyQVLVk
Y277-p YGKFDTIyQVLVkKK
K282-u TIyQVLVkKKSEMQK
K283 IyQVLVkKKSEMQKL
K289 kKKSEMQKLKAEVEL
K291 KSEMQKLKAEVELIM
K300 EVELIMDKGDEFEFL
K309-u DEFEFLEkAAkLQGE
K312-u EFLEkAAkLQGESTk
K319 kLQGESTKPVYIPKI
K319-u kLQGESTkPVYIPKI
Y322 GESTkPVYIPKIDLD
M334 DLDHDLIMGIYQGAA
K344-u YQGAADLkSELKHSI
K376-u DQTQSTFkPVQPSkK
K382-u FkPVQPSkKTIQEKK
T393 QEKKTKKTPVAPGPP
S404-p PGPPSHFsPNkLPTF
K407-u PSHFsPNkLPTFGAP
K421-u PGQSLDSkATsPDAA
S424-p SLDSkATsPDAAPkA
K430-u TsPDAAPkASAAQPD
G440 AAQPDSVGVkAkVLE
K442-u QPDSVGVkAkVLENF
K444-u DSVGVkAkVLENFLT
K452 VLENFLTKSRTELLE
K480-u NKVSLSNkYTTASVS
N514 LGLHCYKNGIHYWEV
K572 AWHNNVEKTLPSTKA
K572 AWHNNVEKTLPSTKA
K578 EKTLPSTKATRVGVL
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