CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014211
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF123 
Protein Synonyms/Alias
 Kip1 ubiquitination-promoting complex protein 1; RING finger protein 123 
Gene Name
 RNF123 
Gene Synonyms/Alias
 KPC1; FP1477 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
467HCSSREGKESTEMKEubiquitination[1]
473GKESTEMKEETAEERubiquitination[1]
515LKLLLDNKDDNGGEAubiquitination[1]
530SRYIFLTKFRKFLQEubiquitination[1, 2]
533IFLTKFRKFLQENASubiquitination[1]
617SHLRKTLKDDLASKAubiquitination[1]
806DILAELTKSQKVFSEubiquitination[2]
814SQKVFSEKLDHLSRRubiquitination[1, 2]
906RLAAILAKHFADARIubiquitination[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] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Required for poly-ubiquitination and proteasome-mediated degradation of CDKN1B during G1 phase of the cell cycle. 
Sequence Annotation
 DOMAIN 74 254 B30.2/SPRY.
 ZN_FING 1254 1292 RING-type.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Ligase; Metal-binding; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1314 AA 
Protein Sequence
MASKGAGMSF SRKSYRLTSD AEKSRVTGIV QEKLLNDYLN RIFSSSEHAP PAATSRKPLN 60
FQNLPEHLDQ LLQVDNEEEE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN 120
FGTIRSTTCV YKGKWLYEVL ISSQGLMQIG WCTISCRFNQ EEGVGDTHNS YAYDGNRVRK 180
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS 240
FKESVAFNFG SRPLRYPVAG YRPLQDPPSA DLVRAQRLLG CFRAVLSVEL DPVEGRLLDK 300
ESSKWRLRGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGIVEKGT PTQAQSVVHQ 360
VLDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTIA ILRHEKSRKF 420
LLSNVLFDVL RSVVFFYIKS PLRVEEAGLQ ELIPTTWWPH CSSREGKEST EMKEETAEER 480
LRRRAYERGC QRLRKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS 540
GRGNMPMLCP PEYMVCFLHR LISALRYYWD EYKASNPHAS FSEEAYIPPQ VFYNGKVDYF 600
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQSTAMDD LDEDEEPAPA MAQRPMQALA 660
VGGPLPLPRP GWLSSPTLGR ANRFLSTAAV SLMTPRRPLS TSEKVKVRTL SVEQRTREDI 720
EGSHWNEGLL LGRPPEEPEQ PLTENSLLEV LDGAVMMYNL SVHQQLGKMV GVSDDVNEYA 780
MALRDTEDKL RRCPKRRKDI LAELTKSQKV FSEKLDHLSR RLAWVHATVY SQEKMLDIYW 840
LLRVCLRTIE HGDRTGSLFA FMPEFYLSVA INSYSALKNY FGPVHSMEEL PGYEETLTRL 900
AAILAKHFAD ARIVGTDIRD SLMQALASYV CYPHSLRAVE RIPEEQRIAM VRNLLAPYEQ 960
RPWAQTNWIL VRLWRGCGFG YRYTRLPHLL KTKLEDANLP SLQKPCPSTL LQQHMADLLQ 1020
QGPDVAPSFL NSVLNQLNWA FSEFIGMIQE IQQAAERLER NFVDSRQLKV CATCFDLSVS 1080
LLRVLEMTIT LVPEIFLDWT RPTSEMLLRR LAQLLNQVLN RVTAERNLFD RVVTLRLPGL 1140
ESVDHYPILV AVTGILVQLL VRGPASEREQ ATSVLLADPC FQLRSICYLL GQPEPPAPGT 1200
ALPAPDRKRF SLQSYADYIS ADELAQVEQM LAHLTSASAQ AAAASLPTSE EDLCPICYAH 1260
PISAVFQPCG HKSCKACINQ HLMNNKDCFF CKTTIVSVED WEKGANTSTT SSAA 1314 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:LIFEdb.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00622; SPRY 
SMART
 SM00184; RING
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS