Tag | Content |
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CPLM ID | CPLM-010665 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cullin-associated NEDD8-dissociated protein 1 |
Protein Synonyms/Alias | Cullin-associated and neddylation-dissociated protein 1; TBP-interacting protein of 120 kDa A; TBP-interacting protein 120A; p120 CAND1 |
Gene Name | Cand1 |
Gene Synonyms/Alias | Tip120; Tip120a |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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51 | DSERKVVKMILKLLE | acetylation | [1] | 55 | KVVKMILKLLEDKNG | acetylation | [1] | 60 | ILKLLEDKNGEVQNL | acetylation | [1] | 391 | KEREENVKADVFHAY | acetylation | [1] | 577 | TCTIKRLKAADIDQE | acetylation | [1] | 586 | ADIDQEVKERAISCM | acetylation | [1] | 971 | ETLLPRLKGYLISGS | acetylation | [1] | 1037 | FNSAAHNKPSLIRDL | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes (By similarity). May indirectly enhance transcription from various types of promoters. |
Sequence Annotation | REPEAT 2 39 HEAT 1. REPEAT 44 81 HEAT 2. REPEAT 83 119 HEAT 3. REPEAT 131 165 HEAT 4. REPEAT 171 208 HEAT 5. REPEAT 210 247 HEAT 6. REPEAT 248 282 HEAT 7. REPEAT 289 366 HEAT 8. REPEAT 370 407 HEAT 9. REPEAT 424 467 HEAT 10. REPEAT 471 510 HEAT 11. REPEAT 515 552 HEAT 12. REPEAT 563 602 HEAT 13. REPEAT 606 643 HEAT 14. REPEAT 646 683 HEAT 15. REPEAT 688 725 HEAT 16. REPEAT 729 768 HEAT 17. REPEAT 770 808 HEAT 18. REPEAT 809 845 HEAT 19. REPEAT 852 889 HEAT 20. REPEAT 890 927 HEAT 21. REPEAT 928 960 HEAT 22. REPEAT 961 998 HEAT 23. REPEAT 1002 1039 HEAT 24. REPEAT 1043 1097 HEAT 25. REPEAT 1099 1133 HEAT 26. REPEAT 1140 1189 HEAT 27. MOD_RES 2 2 N-acetylalanine (By similarity). MOD_RES 55 55 N6-acetyllysine (By similarity). MOD_RES 335 335 Phosphoserine (By similarity). MOD_RES 971 971 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1230 AA |
Protein Sequence | MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK 60 NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA 120 SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL 180 LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA 240 ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI 300 CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV 360 VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ 420 GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI 480 IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL 540 LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL 600 GDNLGPDLSN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR 660 KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA 720 KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT 780 GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL 840 SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT 900 SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL 960 IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL 1020 NVRRVALVTF NSAAHNKPSL IRDLLDSVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD 1080 IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ 1140 RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS 1200 QISSNPELAA IFESIQKDSS STNLESMDTS 1230 |
Gene Ontology | GO:0031461; C:cullin-RING ubiquitin ligase complex; ISS:UniProtKB. GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0017025; F:TBP-class protein binding; IDA:RGD. GO:0030154; P:cell differentiation; ISS:UniProtKB. GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB. GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:UniProtKB. GO:0016567; P:protein ubiquitination; ISS:UniProtKB. GO:0010265; P:SCF complex assembly; ISS:UniProtKB. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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