CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023589
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RING finger protein 24 
Protein Synonyms/Alias
  
Gene Name
 RNF24 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82HKEFYAYKQVILKEKubiquitination[1, 2]
128FHRKCLIKWLEVRKVubiquitination[1, 3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 May play a role in TRPCs intracellular trafficking. 
Sequence Annotation
 ZN_FING 78 119 RING-type.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Golgi apparatus; Membrane; Metal-binding; Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 148 AA 
Protein Sequence
MLNKSGESRY PALFPVLGGS SMSSDFPHYN FRMPNIGFQN LPLNIYIVVF GTAIFVFILS 60
LLFCCYLIRL RHQAHKEFYA YKQVILKEKV KELNLHELCA VCLEDFKPRD ELGICPCKHA 120
FHRKCLIKWL EVRKVCPLCN MPVLQLAQLH SKQDRGPPQG PLPGAENIV 169 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS