Tag | Content |
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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 |
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87 | LGERALSKGLQHEPA | ubiquitination | [1] | 188 | QIRRSAGKMLQALAA | ubiquitination | [1] | 461 | LNSQIYTKYGLLSNE | ubiquitination | [1] | 1771 | CLLVRILKAHGEKGL | ubiquitination | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |