Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  E3 ubiquitin-protein ligase RNF138  

UniProtKB / Swiss-Prot ID :  RN138_HUMAN

Gene Name (Synonyms) : 
RNF138, NARF HSD-4, HSD4  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  E3 ubiquitin-protein ligase. Together with NLK, involved in the ubiquitination and degradation of TCF/LEF. Also exhibits auto-ubiquitination activity in combination with UBE2K. May act as a negative regulator in the Wnt/beta-catenin-mediated signaling pathway. 

Protein Sequence MAEDLSAATSYTEDDFYCPVCQEVLKTPVRTTACQHVFCRKCFLTAMRESGAHCPLCRGNVTRRERACPE...
Predicted Secondary Structure CCCCCCCCCCCCCCCEEEECCCHHHHHHHHHCCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCH...
Protein Variant
LocationDescription
81K -> R (in dbSNP:rs7229690). VAR_052109
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEDLS
---CCCCCC
21.00UniProtKB
Link-
41N6-acetyllysineVFCRKCFLT
HHHHHHHHH
30.44Phosphositeplus
Link-
108PhosphotyrosineSCKKYQDEY
HHHHHHHHC
13.49Phosphositeplus
Link-
112PhosphotyrosineYQDEYGVSS
HHHHCCCCC
30.99Phosphositeplus
Link-
124PhosphoserineNFQISQDSV
CCCCCCCCC
19.70HPRD
Link-
124PhosphoserineNFQISQDSV
CCCCCCCCC
19.70PhosphoELM
Link-
124PhosphoserineNFQISQDSV
CCCCCCCCC
19.70Phosphositeplus
Link-
124Phosphoserine.NFQISQDSV
CCCCCCCCC
19.70UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CF165_HUMANphysical interactionEBI-756970
intact16189514
PCBP4_HUMANphysical interactionEBI-955886
intact16713569
TAF9_HUMANphysical interactionEBI-956062
intact16713569
CF165_HUMANyeast 2-hybridHPRD:11508HPRD16189514
PCBP4_HUMANyeast 2-hybridHPRD:11508HPRD16713569
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures