CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017028
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
87LGERALSKGLQHEPAubiquitination[1]
188QIRRSAGKMLQALAAubiquitination[1]
461LNSQIYTKYGLLSNEubiquitination[1]
1771CLLVRILKAHGEKGLubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
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 NGIPPVQTLG 420
EKALGEISVS VEMAESLLQV LSSRFEGSTL NDLLNSQIYT KYGLLSNEPS SSSTSRNHSC 480
TPDPEEESKS EASFSEEETE SLKAKAEAPK TEAEPTKTRT ETPMAQSDSQ LFNQLLVTEG 540
MTLPTEMKEA ASEMARALRG PGPRSSLDQH VAAVVATVQI SSLDTNLQLS GLSALSQAVE 600
EVTERDHPLV RPDRSLREKL VKMLVELLTN QVGEKMVVVQ ALRLLYLLMT KHEWRPLFAR 660
EGGIYAVLVC MQEYKTSVLV QQAGLAALKM LAVASSSEIP TFVTGRDSIH SLFDAQMTRE 720
IFASIDSATR PGSESLLLTV PAAVILMLNT EGCSSAARNG LLLLNLLLCN HHTLGDQIIT 780
QELRDTLFRH SGIAPRTEPM PTTRTILMML LNRYSEPPGS PERAALETPI IQGQDGSPEL 840
LIRSLVGGPS AELLLDLERV LCREGSPGGA VRPLLKRLQQ ETQPFLLLLR TLDAPGPNKT 900
LLLSVLRVIT RLLDFPEAMV LPWHEVLEPC LNCLSGPSSD SEIVQELTCF LHRLASMHKD 960
YAVVLCCLGA KEILSKVLDK HSAQLLLGCE LRDLVTECEK YAQLYSNLTS SILAGCIQMV 1020
LGQIEDHRRT HQPINIPFFD VFLRHLCQGS SVEVKEDKCW EKVEVSSNPH RASKLTDHNP 1080
KTYWESNGST GSHYITLHMH RGVLVRQLTL LVASEDSSYM PARVVVFGGD STSCIGTELN 1140
TVNVMPSASR VILLENLNRF WPIIQIRIKR CQQGGIDTRV RGVEVLGPKP TFWPLFREQL 1200
CRRTCLFYTI RAQAWSRDIA EDHRRLLQLC PRLNRVLRHE QNFADRFLPD DEAAQALGKT 1260
CWEALVSPLV QNITSPDAEG VSALGWLLDQ YLEQRETSRN PLSRAASFAS RVRRLCHLLV 1320
HVEPPPGPSP EPSTRPFSKN SKGRDRSPAP SPVLPSSSLR NITQCWLSVV QEQVSRFLAA 1380
AWRAPDFVPR YCKLYEHLQR AGSELFGPRA AFMLALRSGF SGALLQQSFL TAAHMSEQFA 1440
RYIDQQIQGG LIGGAPGVEM LGQLQRHLEP IMVLSGLELA TTFEHFYQHY MADRLLSFGS 1500
SWLEGAVLEQ IGLCFPNRLP QLMLQSLSTS EELQRQFHLF QLQRLDKLFL EQEDEEEKRL 1560
EEEEEEEEEE EAEKELFIED PSPAISILVL SPRCWPVSPL CYLYHPRKCL PTEFCDALDR 1620
FSSFYSQSQN HPVLDMGPHR RLQWTWLGRA ELQFGKQILH VSTVQMWLLL KFNQTEEVSV 1680
ETLLKDSDLS PELLLQALVP LTSGNGPLTL HEGQDFPHGG VLRLHEPGPQ RSGEALWLIP 1740
PQAYLNVEKD EGRTLEQKRN LLSCLLVRIL KAHGEKGLHI DQLVCLVLEA WQKGPNPPGT 1800
LGHTVAGGVA CTSTDVLSCI LHLLGQGYVK RRDDRPQILM YAAPEPMGPC RGQADVPFCG 1860
SQSETSKPSP EAVATLASLQ LPAGRTMSPQ EVEGLMKQTV RQVQETLNLE PDVAQHLLAH 1920
SHWGAEQLLQ SYSEDPEPLL LAAGLCVHQA QAVPVRPDHC PVCVSPLGCD DDLPSLCCMH 1980
YCCKSCWNEY LTTRIEQNLV LNCTCPIADC PAQPTGAFIR AIVSSPEVIS KYEKALLRGY 2040
VESCSNLTWC TNPQGCDRIL CRQGLGCGTT CSKCGWASCF NCSFPEAHYP ASCGHMSQWV 2100
DDGGYYDGMS VEAQSKHLAK LISKRCPSCQ APIEKNEGCL HMTCAKCNHG FCWRCLKSWK 2160
PNHKDYYNCS AMVSKAARQE KRFQDYNERC TFHHQAREFA VNLRNRVSAI HEVPPPRSFT 2220
FLNDACQGLE QARKVLAYAC VYSFYSQDAE YMDVVEQQTE NLELHTNALQ ILLEETLLRC 2280
RDLASSLRLL RADCLSTGME LLRRIQERLL AILQHSAQDF RVGLQSPSVE AWEAKGPNMP 2340
GSQPQASSGP EAEEEEEDDE DDVPEWQQDE FDEELDNDSF SYDESENLDQ ETFFFGDEEE 2400
DEDEAYD 2407 
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