CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014210
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 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
33VTGIVQEKLLSDYLYubiquitination[1]
180YDGNRVRKWNVTTTNubiquitination[1]
450RVEEAGLKELIPTTWubiquitination[1]
515LKLLLDNKDDNGGEAubiquitination[1]
530SRYIFLTKFRKFLQEubiquitination[1]
533IFLTKFRKFLQENASubiquitination[1]
617SHLRKTLKDDLASKAubiquitination[1]
710RLLSTMEKVKVRSLNubiquitination[1]
795ALRDTEDKLRRCPKRubiquitination[1]
804RRCPKRRKDILAELTubiquitination[1]
812DILAELTKSQKVFSEubiquitination[1]
820SQKVFSEKLDHLSRRubiquitination[1]
912RLAAILAKHFADPRIubiquitination[1]
1010ANLPSLQKPCPSTLLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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 (By similarity). 
Sequence Annotation
 DOMAIN 74 254 B30.2/SPRY.
 ZN_FING 1254 1292 RING-type.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Ligase; Metal-binding; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1314 AA 
Protein Sequence
MASKGTGMSF SRKSYRLTSD AEKSRVTGIV QEKLLSDYLY RIFSPPDRGP AAATSRKPLN 60
FHNLPEHVDQ LLQVDSEDNE SQGQVEGRLG PSTVVLDHTG GFEGLLLVDD DLLGVIGHSN 120
FGTIRSTTCV YKGKWVYEVL ISSQGLMQIG WCTINCRFNQ EEGVGDTHNS YAYDGNRVRK 180
WNVTTTNYGK AWAAGDIVSC LIDLDDGTLS FCLNGVSLGT AFENLSRGLG MAYFPAISLS 240
FKESVAFNFG SRPLRYPVAG FRPLQDPPFA DLVRAQRLLG CFQAVLSVEL DPVEGRLVET 300
ESSEWQLQGQ PTVLLTLAHI FHHFAPLLRK VYLVEAVLMS FLLGVVEKGT PEQAQSVVHQ 360
ILDLLWLFME DYEVQDCLKQ LMMSLLRLYR FSPIVPDLGL QIHYLRLTMS ILRHEKSRKF 420
LLSNVLFDML RSVVFFYIKS PLRVEEAGLK ELIPTTWWPH RSSRESRDGK EAREETTEER 480
QRRRAYERGC QRLKKRIEVV EELQVQILKL LLDNKDDNGG EASRYIFLTK FRKFLQENAS 540
GRGNTPVLCP PEYMVCFLHR LVSALRFYWD EYKASNPRAS FSEEAYIPPQ IFYNGKVDYF 600
DLQRLGGLLS HLRKTLKDDL ASKANIVIDP LELQAATMDD LDEDEEPAPS AAQVWQEGQR 660
PMQALAIGGA LPLPRPGWLS SPTLGRANRF LSTAAVSLMT PRRLLSTMEK VKVRSLNVEQ 720
RTREDIEGSH WNEGLLLGRP PEEPEQPLTE NSLLEVLDGT VMMYNLSVHQ QLGKMVGVSD 780
DVNEYAMALR DTEDKLRRCP KRRKDILAEL TKSQKVFSEK LDHLSRRLAW VHATVYSQEK 840
MLDIYWLLRV CLRTIEHGDR TGSLFAFMPE FYLSVAINSY SALKNYFGPV HSMEELPGYE 900
ETLTRLAAIL AKHFADPRIV GTDIRDSLMQ ALASYVCYPH SLRAVERIPE EQRIAMVRNL 960
LAPYEQRPWA QTNWILVRLW RGCGFGYRYT RLPHLLKTKP EDANLPSLQK PCPSTLLQQH 1020
MADLLRQGSD VAPSFLNSVL NQLNWAFSEF IGMIQEIQQA AERLERNFVD SRQLKVCATC 1080
FDLSVSLLRV LEMTITLVPE IFLDWSRPTS EMLLRRLAQL LNQVLNRVTA ERNLFDRVVT 1140
LRLPGLESVD HYPILVAVTG ILVRLLVHGP TSETEQATSV LLADPCFQLR SICYLLGQPE 1200
PLAPGTTLPA PDRKRFSLQS YTDYISAEEL AQVEQMLAHL TAASAQAAAA SLPTNEEDLC 1260
PICYAHPISA VFQPCGHKSC KACINQHLMN NKDCFFCKAT IVSVEDWDKA ANTSAMSSAA 1320 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 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