CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000037
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF103 
Protein Synonyms/Alias
 KF-1; hKF-1; RING finger protein 103; Zinc finger protein 103 homolog; Zfp-103 
Gene Name
 RNF103 
Gene Synonyms/Alias
 ZFP103 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65GYSGLPEKKDVRELVubiquitination[1]
134DRSPLVGKIHWEKMVubiquitination[1]
190SKGKVMLKEYSGRKIubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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
 Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. 
Sequence Annotation
 ZN_FING 621 663 RING-type.  
Keyword
 Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 685 AA 
Protein Sequence
MWLKLFFLLL YFLVLFVLAR FFEAIVWYET GIFATQLVDP VALSFKKLKT ILECRGLGYS 60
GLPEKKDVRE LVEKSGDLME GELYSALKEE EASESVSSTN FSGEMHFYEL VEDTKDGIWL 120
VQVIANDRSP LVGKIHWEKM VKKVSRFGIR TGTFNCSSDP RYCRRRGWVR STLIMSVPQT 180
STSKGKVMLK EYSGRKIEVE HIFKWITAHA ASRIKTIYNA EHLKEEWNKS DQYWLKIYLF 240
ANLDQPPAFF SALSIKFTGR VEFIFVNVEN WDNKSYMTDI GIYNMPSYIL RTPEGIYRYG 300
NHTGEFISLQ AMDSFLRSLQ PEVNDLFVLS LVLVNLMAWM DLFITQGATI KRFVVLISTL 360
GTYNSLLIIS WLPVLGFLQL PYLDSFYEYS LKLLRYSNTT TLASWVRADW MFYSSHPALF 420
LSTYLGHGLL IDYFEKKRRR NNNNDEVNAN NLEWLSSLWD WYTSYLFHPI ASFQNFPVES 480
DWDEDPDLFL ERLAFPDLWL HPLIPTDYIK NLPMWRFKCL GVQSEEEMSE GSQDTENDSE 540
SENTDTLSSE KEVFEDKQSV LHNSPGTASH CDAEACSCAN KYCQTSPCER KGRSYGSYNT 600
NEDMEPDWLT WPADMLHCTE CVVCLENFEN GCLLMGLPCG HVFHQNCIVM WLAGGRHCCP 660
VCRWPSYKKK QPYAQHQPLS NDVPS 685 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007417; P:central nervous system development; TAS:ProtInc.
 GO:0030433; P:ER-associated protein catabolic process; IDA:UniProtKB. 
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