CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017027
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-9 
Protein Synonyms/Alias
 CUL-9; UbcH7-associated protein 1; p53-associated parkin-like cytoplasmic protein 
Gene Name
 CUL9 
Gene Synonyms/Alias
 H7AP1; KIAA0708; PARC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46LIRWSVLKCGEVGKVubiquitination[1]
87LGERALSKGLQHEPAubiquitination[1, 2]
188QIRRSAGKMLQALAAubiquitination[1]
627KTEAEPTKTRTETPMubiquitination[1]
986GAVRPLLKRLQQETQubiquitination[1]
1090ILSKVLDKHSAQLLLubiquitination[1]
1172KEDKCWEKVEVSSNPubiquitination[1]
1299GVEVLGPKPTFWPLFubiquitination[1]
1503DFVPRYCKLYEHLQRubiquitination[1]
1718CYLYHPRKCLPTEFCubiquitination[1]
1881CLLVRILKAHGEKGLubiquitination[2]
2007QEVEGLMKQTVRQVQubiquitination[1]
2141SSPEVISKYEKALLRubiquitination[1, 2]
2144EVISKYEKALLRGYVubiquitination[1, 2]
2230AQSKHLAKLISKRCPubiquitination[1]
2245SCQAPIEKNEGCLHMubiquitination[1]
2285NCSAMVSKAARQEKRubiquitination[3]
Reference
 [1] 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]
 [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]
 [3] 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
Functional Description
 Cytoplasmic anchor protein in p53-associated protein complex. Regulates the subcellular localization of p53 and subsequent function. Seems to be part of an atypical cullin-RING- based E3 ubiquitin-protein ligase complex. In vitro, complexes of CUL9/PARC with either CUL7 or TP53 contain E3 ubiquitin-protein ligase activity. 
Sequence Annotation
 DOMAIN 1143 1322 DOC.
 NP_BIND 1363 1370 ATP (Potential).
 ZN_FING 2070 2120 RING-type 1.
 ZN_FING 2140 2203 IBR-type.
 ZN_FING 2236 2265 RING-type 2.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2517 AA 
Protein Sequence
MVGERHAGDL MVPLGPRLQA YPEELIRQRP GHDGHPEYLI RWSVLKCGEV GKVGVEEGKA 60
EHILMWLSAP EVYANCPGLL GERALSKGLQ HEPAGVSGSF PRDPGGLDEV AMGEMEADVQ 120
ALVRRAARQL AESGTPSLTA AVLHTIHVLS AYASIGPLTG VFRETGALDL LMHMLCNPEP 180
QIRRSAGKML QALAAHDAGS RAHVLLSLSQ QDGIEQHMDF DSRYTLLELF AETTSSEEHC 240
MAFEGIHLPQ IPGKLLFSLV KRYLCVTSLL DQLNSSPELG AGDQSSPCAT REKSRGQREL 300
EFSMAVGNLI SELVRSMGWA RNLSEQGMSP PRPTRSIFQP YISGPSLLLP TIVTTPRRQG 360
WVFRQRSEFS SRSGYGEYVQ QTLQPGMRVR MLDDYEEISA GDEGEFRQSN NGIPPVQVFW 420
QSTGRTYWVH WHMLEILGPE EATEDKASAA VEKGAGATVL GTAFPSWDWN PMDGLYPLPY 480
LQPEPQKNER VGYLTQAEWW ELLFFIKKLD LCEQQPIFQN LWKNLDETLG EKALGEISVS 540
VEMAESLLQV LSSRFEGSTL NDLLNSQIYT KYGLLSNEPS SSSTSRNHSC TPDPEEESKS 600
EASFSEEETE SLKAKAEAPK TEAEPTKTRT ETPMAQSDSQ LFNQLLVTEG MTLPTEMKEA 660
ASEMARALRG PGPRSSLDQH VAAVVATVQI SSLDTNLQLS GLSALSQAVE EVTERDHPLV 720
RPDRSLREKL VKMLVELLTN QVGEKMVVVQ ALRLLYLLMT KHEWRPLFAR EGGIYAVLVC 780
MQEYKTSVLV QQAGLAALKM LAVASSSEIP TFVTGRDSIH SLFDAQMTRE IFASIDSATR 840
PGSESLLLTV PAAVILMLNT EGCSSAARNG LLLLNLLLCN HHTLGDQIIT QELRDTLFRH 900
SGIAPRTEPM PTTRTILMML LNRYSEPPGS PERAALETPI IQGQDGSPEL LIRSLVGGPS 960
AELLLDLERV LCREGSPGGA VRPLLKRLQQ ETQPFLLLLR TLDAPGPNKT LLLSVLRVIT 1020
RLLDFPEAMV LPWHEVLEPC LNCLSGPSSD SEIVQELTCF LHRLASMHKD YAVVLCCLGA 1080
KEILSKVLDK HSAQLLLGCE LRDLVTECEK YAQLYSNLTS SILAGCIQMV LGQIEDHRRT 1140
HQPINIPFFD VFLRHLCQGS SVEVKEDKCW EKVEVSSNPH RASKLTDHNP KTYWESNGST 1200
GSHYITLHMH RGVLVRQLTL LVASEDSSYM PARVVVFGGD STSCIGTELN TVNVMPSASR 1260
VILLENLNRF WPIIQIRIKR CQQGGIDTRV RGVEVLGPKP TFWPLFREQL CRRTCLFYTI 1320
RAQAWSRDIA EDHRRLLQLC PRLNRVLRHE QNFADRFLPD DEAAQALGKT CWEALVSPLV 1380
QNITSPDAEG VSALGWLLDQ YLEQRETSRN PLSRAASFAS RVRRLCHLLV HVEPPPGPSP 1440
EPSTRPFSKN SKGRDRSPAP SPVLPSSSLR NITQCWLSVV QEQVSRFLAA AWRAPDFVPR 1500
YCKLYEHLQR AGSELFGPRA AFMLALRSGF SGALLQQSFL TAAHMSEQFA RYIDQQIQGG 1560
LIGGAPGVEM LGQLQRHLEP IMVLSGLELA TTFEHFYQHY MADRLLSFGS SWLEGAVLEQ 1620
IGLCFPNRLP QLMLQSLSTS EELQRQFHLF QLQRLDKLFL EQEDEEEKRL EEEEEEEEEE 1680
EAEKELFIED PSPAISILVL SPRCWPVSPL CYLYHPRKCL PTEFCDALDR FSSFYSQSQN 1740
HPVLDMGPHR RLQWTWLGRA ELQFGKQILH VSTVQMWLLL KFNQTEEVSV ETLLKDSDLS 1800
PELLLQALVP LTSGNGPLTL HEGQDFPHGG VLRLHEPGPQ RSGEALWLIP PQAYLNVEKD 1860
EGRTLEQKRN LLSCLLVRIL KAHGEKGLHI DQLVCLVLEA WQKGPNPPGT LGHTVAGGVA 1920
CTSTDVLSCI LHLLGQGYVK RRDDRPQILM YAAPEPMGPC RGQADVPFCG SQSETSKPSP 1980
EAVATLASLQ LPAGRTMSPQ EVEGLMKQTV RQVQETLNLE PDVAQHLLAH SHWGAEQLLQ 2040
SYSEDPEPLL LAAGLCVHQA QAVPVRPDHC PVCVSPLGCD DDLPSLCCMH YCCKSCWNEY 2100
LTTRIEQNLV LNCTCPIADC PAQPTGAFIR AIVSSPEVIS KYEKALLRGY VESCSNLTWC 2160
TNPQGCDRIL CRQGLGCGTT CSKCGWASCF NCSFPEAHYP ASCGHMSQWV DDGGYYDGMS 2220
VEAQSKHLAK LISKRCPSCQ APIEKNEGCL HMTCAKCNHG FCWRCLKSWK PNHKDYYNCS 2280
AMVSKAARQE KRFQDYNERC TFHHQAREFA VNLRNRVSAI HEVPPPRSFT FLNDACQGLE 2340
QARKVLAYAC VYSFYSQDAE YMDVVEQQTE NLELHTNALQ ILLEETLLRC RDLASSLRLL 2400
RADCLSTGME LLRRIQERLL AILQHSAQDF RVGLQSPSVE AWEAKGPNMP GSQPQASSGP 2460
EAEEEEEDDE DDVPEWQQDE FDEELDNDSF SYDESENLDQ ETFFFGDEEE DEDEAYD 2517 
Gene Ontology
 GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR004939; APC_su10/DOC_dom.
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR021097; CPH_domain.
 IPR016157; Cullin_CS.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR019559; Cullin_neddylation_domain.
 IPR008979; Galactose-bd-like.
 IPR014722; Rib_L2_dom2.
 IPR011991; WHTH_DNA-bd_dom.
 IPR002867; Znf_C6HC.
 IPR001841; Znf_RING.
 IPR017907; Znf_RING_CS. 
Pfam
 PF03256; APC10
 PF11515; Cul7
 PF00888; Cullin
 PF01485; IBR 
SMART
 SM00884; Cullin_Nedd8
 SM00647; IBR
 SM00184; RING 
PROSITE
 PS01256; CULLIN_1
 PS50069; CULLIN_2
 PS51284; DOC
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS