CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016250
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
 KIAA0829; TIP120; TIP120A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
14HISNLLEKMTSSDKDacetylation[1]
14HISNLLEKMTSSDKDubiquitination[2, 3]
20EKMTSSDKDFRFMATubiquitination[2, 3, 4]
40ELQKDSIKLDDDSERubiquitination[5]
51DSERKVVKMILKLLEubiquitination[2, 3]
55KVVKMILKLLEDKNGacetylation[6]
55KVVKMILKLLEDKNGubiquitination[2, 3, 5]
60ILKLLEDKNGEVQNLubiquitination[4, 5]
132ALAANVCKKITGRLTubiquitination[2, 3]
255RIGEYLEKIIPLVVKubiquitination[2, 3, 7, 8]
355KVRRAAAKCLDAVVSubiquitination[4]
373EMLPEFYKTVSPALIubiquitination[2, 3, 4]
403HAYLSLLKQTRPVQSubiquitination[2, 3]
574DLFTCTIKRLKAADIubiquitination[4]
577TCTIKRLKAADIDQEubiquitination[9]
586ADIDQEVKERAISCMacetylation[9]
586ADIDQEVKERAISCMubiquitination[4]
630ITRLTTVKALTLIAGubiquitination[2, 3]
801QSYYSIAKCVAALTRubiquitination[4, 9]
812ALTRACPKEGPAVVGubiquitination[4]
826GQFIQDVKNSRSTDSubiquitination[2, 3, 9]
957VVAECLGKLTLIDPEubiquitination[4, 9]
971ETLLPRLKGYLISGSacetylation[1, 6]
1037FNSAAHNKPSLIRDLubiquitination[2, 3]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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. 
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.
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 971 971 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; 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
GDNLGSDLPN 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 IRDLLDTVLP 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; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0030154; P:cell differentiation; IDA:UniProtKB.
 GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
 GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Compara.
 GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
 GO:0010265; P:SCF complex assembly; IDA:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR013932; TATA-bd_TIP120. 
Pfam
 PF08623; TIP120 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS