Version 5.4
Homo sapiens Protein: RNF144A
Summary
InnateDB Protein IDBP-26992.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RNF144A
Protein Name ring finger protein 144A
Synonyms RNF144; UBCE7IP4;
Species Homo sapiens
Ensembl Protein ENSP00000321330
InnateDB Gene IDBG-26990 (RNF144A)
Protein Structure
UniProt Annotation
Function E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 14 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 14 [view]
Protein-Protein 14 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
Biological Process
GO:0016567 protein ubiquitination
Cellular Component
GO:0005794 Golgi apparatus
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID
InterPro IPR001841 Zinc finger, RING-type
IPR002867 Zinc finger, C6HC-type
PFAM PF13639
PF14634
PF01485
PRINTS
PIRSF
SMART SM00184
SM00647
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P50876
PhosphoSite PhosphoSite-
TrEMBL C9JLH4
UniProt Splice Variant
Entrez Gene 9781
UniGene Hs.22146
RefSeq NP_055561
HUGO HGNC:20457
OMIM
CCDS CCDS1657
HPRD 11510
IMGT
EMBL AC017076 AC068481 BC050373 CH471053 D79983
GenPept AAH50373 AAX82010 BAA11478 EAX01030 EAX01031

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca