Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cullin-associated NEDD8-dissociated protein 1  

UniProtKB / Swiss-Prot ID :  CAND1_HUMAN

Gene Name (Synonyms) : 
CAND1, KIAA0829, TIP120, TIP120A  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins. 

Protein Sequence MASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKMILKLLEDKNGEVQNLAVK...
Predicted Secondary Structure CCCHHHHHHHHHHHHHCCCCCEEEEEHHHHHHHHHHHCCCCCCCHHHHHHHHHHHHHHCCCCCHHHHHHH...
Protein Variant
LocationDescription
803V -> A (in dbSNP:rs12580996). VAR_054041
952A -> V (in dbSNP:rs17854618). VAR_025327
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASASY
---CCCHHH
25.71UniProtKB
Link-
9PhosphoserineSYHISNLLE
HHHHHHHHH
14.23HPRD
Link
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NLLEKMTSS
HHHHHHHCC
47.66Phosphositeplus
Link
16PhosphothreonineLEKMTSSDK
HHHHHCCCC
35.83HPRD
Link
40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDSIKLDDD
HHCCCCCCC
50.22Phosphositeplus
Link
51Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RKVVKMILK
HHHHHHHHH
24.18Phosphositeplus
Link
55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KMILKLLED
HHHHHHHHC
39.85Phosphositeplus
Link
55N6-acetyllysineKMILKLLED
HHHHHHHHC
39.85HPRD
Link
55N6-acetyllysineKMILKLLED
HHHHHHHHC
39.85Phosphositeplus
Link
55N6-acetyllysine.KMILKLLED
HHHHHHHHC
39.85UniProtKB
Link
60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLEDKNGEV
HHHCCCCCH
58.43Phosphositeplus
Link
107PhosphoserineRDISSIGLK
HHHHHHHHH
22.47HPRD
Link
107PhosphoserineRDISSIGLK
HHHHHHHHH
22.47Phosphositeplus
Link
255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EYLEKIIPL
HHHHHHHHH
43.25Phosphositeplus
Link
295PhosphoserineYPHVSTIIN
CCCCHHHHH
15.74HPRD
Link
295PhosphoserineYPHVSTIIN
CCCCHHHHH
15.74Phosphositeplus
Link
296PhosphothreoninePHVSTIINI
CCCHHHHHH
25.45HPRD
Link
296PhosphothreoninePHVSTIINI
CCCHHHHHH
25.45Phosphositeplus
Link
335PhosphoserineDDQGSDDEY
CCCCCCCCC
35.93HPRD
Link-
335PhosphoserineDDQGSDDEY
CCCCCCCCC
35.93PhosphoELM
Link-
335PhosphoserineDDQGSDDEY
CCCCCCCCC
35.93Phosphositeplus
Link-
335PhosphoserineDDQGSDDEY
CCCCCCCCC
35.93SysPTM
Link-
335Phosphoserine.DDQGSDDEY
CCCCCCCCC
35.93UniProtKB
Link-
340PhosphoserineDDEYSDDDD
CCCCCCCCC
32.30HPRD
Link-
340PhosphoserineDDEYSDDDD
CCCCCCCCC
32.30PhosphoELM
Link-
340PhosphoserineDDEYSDDDD
CCCCCCCCC
32.30Phosphositeplus
Link-
340PhosphoserineDDEYSDDDD
CCCCCCCCC
32.30SysPTM
Link-
340Phosphoserine.DDEYSDDDD
CCCCCCCCC
32.30UniProtKB
Link-
373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEFYKTVSP
HHHHHHHHH
48.01Phosphositeplus
Link
381PhosphoserinePALISRFKE
HHHHHHHHH
32.30Phosphositeplus
Link
403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSLLKQTRP
HHHHHHCCC
55.72Phosphositeplus
Link
571S-nitrosocysteineDLFTCTIKR
HHHHHHHHH
2.65dbSNO
Link
624PhosphothreonineKNEITRLTT
HHHHCCCCH
17.28Phosphositeplus
Link
624Phosphothreonine.KNEITRLTT
HHHHCCCCH
17.28UniProtKB
Link
630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LTTVKALTL
CCHHHHHHH
35.27Phosphositeplus
Link
826Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQDVKNSRS
HHHHCCCCC
58.45Phosphositeplus
Link
866PhosphoserineLEAFSSPSE
HHHCCCCCC
48.68HPRD
Link
928PhosphotyrosineGLKPYVENI
CCCHHHHHH
20.86Phosphositeplus
Link
971N6-acetyllysineLPRLKGYLI
HHHHHHHHH
46.95HPRD
Link
971N6-acetyllysineLPRLKGYLI
HHHHHHHHH
46.95Phosphositeplus
Link
971N6-acetyllysine.LPRLKGYLI
HHHHHHHHH
46.95UniProtKB
Link
973PhosphotyrosineRLKGYLISG
HHHHHHHCC
10.16Phosphositeplus
Link
980PhosphotyrosineSGSSYARSS
CCCCHHHHH
14.02HPRD
Link
980PhosphotyrosineSGSSYARSS
CCCCHHHHH
14.02Phosphositeplus
Link
984PhosphoserineYARSSVVTA
HHHHHHHHH
18.30HPRD
Link
992PhosphothreonineAVKFTISDH
HHHHHHHCC
17.54HPRD
Link
1037Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AAHNKPSLI
HHCCCHHHH
26.56Phosphositeplus
Link
1134S-nitrosocysteineLSTLCPSAV
HHHHCCHHH
2.25dbSNO
Link
1168N6-acetyllysineQEFEKQDEL
HHHHHHHHH
69.26HPRD
Link
1219PhosphoserineIQKDSSSTN
HHHCCCCCC
32.97HPRD
Link-
1229PhosphothreonineESMDTS
CCCCCC
27.91HPRD
Link-
1229PhosphothreonineESMDTS
CCCCCC
27.91Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3318149MINT15161933
CUL1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-597772
EBI-597852
EBI-597
intact12504026
12504026
12504026
12504026
12504026
12504026
12504026
12504026
12504026
12504026
12504026
12504026
1
RBX1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-597847
EBI-595273
EBI-600
intact12504026
12504026
12504026
15537541
12609982
12609982
12609982
12609982
12609982
12609982
CUL3_HUMANphysical interaction
physical interaction
EBI-456121
EBI-456227
intact12609982
12609982
CUL4B_HUMANin vitroHPRD:06983HPRD12609982
CUL1_HUMANin vitroHPRD:06983HPRD12609982
CUL2_HUMANin vivoHPRD:06983HPRD12609982
RBX1_HUMANin vitroHPRD:06983HPRD12609982
RBX1_HUMANENSP00000299218STRING
TBP_HUMANENSP00000299218STRING
CUL1_HUMANENSP00000299218STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-624, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-340, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures