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Protein Page:
CAND1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CAND1 Enhances transcription from various types of promoters. 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. Binds TBP. Part of a complex that contains CUL1 and RBX1. Binds unneddylated CUL1, but cannot bind CUL1 once it has been neddylated. Binds CUL2, CUL3, CUL4A, CUL4B and CUL5. Belongs to the CAND family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; Ubiquitin conjugating system
Cellular Component: cullin-RING ubiquitin ligase complex; intracellular membrane-bound organelle; cytoplasm; nucleolus; nucleus; ubiquitin ligase complex
Molecular Function: protein binding; TATA-binding protein binding
Biological Process: SCF complex assembly; negative regulation of catalytic activity; protein ubiquitination; positive regulation of transcriptional preinitiation complex assembly; cell differentiation
Reference #:  Q86VP6 (UniProtKB)
Alt. Names/Synonyms: CAND1; cullin-associated and neddylation-dissociated 1; Cullin-associated and neddylation-dissociated protein 1; Cullin-associated NEDD8-dissociated protein 1; DKFZp434M1414; FLJ10114; FLJ10929; FLJ38691; FLJ90441; KIAA0829; p120 CAND1; TBP interacting protein; TBP-interacting protein 120A; TBP-interacting protein of 120 kDa A; TIP120; TIP120A
Gene Symbols: CAND1
Molecular weight: 136,376 Da
Basal Isoelectric point: 5.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CAND1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K14-u HISNLLEkMTSSDKD
0 2 K40-u ELQKDSIkLDDDSER
0 2 K51-u DSERKVVkMILkLLE
0 1 K55-a KVVkMILkLLEDkNG
0 2 K55-u KVVkMILkLLEDkNG
0 3 K60-u ILkLLEDkNGEVQNL
0 1 Y82 LVSKVKEYQVETIVD
0 1 S107-p EQLRDISsIGLKTVI
0 1 T139 KKITGRLTSAIAKQE
0 1 S140 KITGRLTSAIAKQED
0 3 K255-u RIGEYLEkIIPLVVK
0 1 S295-p KEVYPHVstIINICL
0 1 T296-p EVYPHVstIINICLK
0 1 S335-p GDDDDQGsDDEYsDD
0 1 S340-p QGsDDEYsDDDDMSW
0 2 K373-u EMLPEFYkTVSPALI
0 2 S381-p TVSPALIsRFKEREE
0 1 K403-u HAYLSLLkQTRPVQS
0 4 S558-p RPLDQPSsFDATPYI
0 1 K577 TCTIKRLKAADIDQE
0 3 T624-p ERLKNEItRLTTVkA
0 1 K630-u ItRLTTVkALTLIAG
0 1 S725 TLAKVYPSSLSKISG
0 1 S728 KVYPSSLSKISGSIL
0 2 K826-u GQFIQDVkNSRSTDS
0 3 K904 QEITSQPKRQYLLLH
0 1 Y928-p SVVGLKPyVENIWAL
0 14 K957-u VVAECLGkLTLIDPE
0 1 K971-a ETLLPRLkGyLISGS
0 3 Y973-p LLPRLkGyLISGSSy
0 3 Y980-p yLISGSSyARSSVVT
0 1 K1037-u FNSAAHNkPSLIRDL
0 2 K1168-u SVKQEFEkQDELKRS
0 1 T1229-p TNLESMDtS______
  mouse

 
K14 HISNLLEKMTSSDKD
K40-u ELQKDSIkLDDDSER
K51-u DSERKVVkMILRLLE
R55 KVVkMILRLLEDkNG
R55 KVVkMILRLLEDkNG
K60-u ILRLLEDkNGEVQNL
Y82-p LVSKVKEyQVETIVD
S107 EQLRDISSIGLKTVI
T139-p KKITGRLtsAIAKQE
S140-p KITGRLtsAIAKQED
K255-u RIGEYLEkIIPLVVK
S295 KEVYPHVSTIINICL
T296 EVYPHVSTIINICLK
S335 GDDDDQGSDDEYSDD
S340 QGSDDEYSDDDDMSW
K373-u EMLPEFYkTVSPALI
A381 TVSPALIARFKEREE
K403 HAYLSLLKQTRPVQS
S558-p RPLDQPSsFDATPYI
K577-u TCTIKRLkAADIDQE
T624-p ERLKNEItRLTTVKA
K630 ItRLTTVKALTLIAG
S725-p TLAKVYPsSLsKISG
S728-p KVYPsSLsKISGSIL
K826-u GQFIQDVkNSRSTDS
K904-u QEITSQPkRQYLLLH
Y928 SVAGLKPYVENIWAL
K957-u VVAECLGkLTLIDPE
K971 ETLLPRLKGYLISGS
Y973 LLPRLKGYLISGSSY
Y980 YLISGSSYARSSVVT
K1037 FNSAAHNKPSLIRDL
K1168-u SVKQEFEkQDELKRS
T1229 TNLESMDTS______
  rat

 
K14 HISNLLEKMTSSDKD
K40 ELQKDSIKLDDDSER
K51 DSERKVVKMILKLLE
K55 KVVKMILKLLEDKNG
K55 KVVKMILKLLEDKNG
K60 ILKLLEDKNGEVQNL
Y82 LVSKVKEYQVETIVD
S107 EQLRDISSIGLKTVI
T139 KKITGRLTSAIAKQE
S140 KITGRLTSAIAKQED
K255 RIGEYLEKIIPLVVK
S295 KEVYPHVSTIINICL
T296 EVYPHVSTIINICLK
S335 GDDDDQGSDDEYSDD
S340 QGSDDEYSDDDDMSW
K373 EMLPEFYKTVSPALI
S381 TVSPALISRFKEREE
K403 HAYLSLLKQTRPVQS
S558 RPLDQPSSFDATPYI
K577 TCTIKRLKAADIDQE
T624 ERLKNEITRLTTVKA
K630 ITRLTTVKALTLIAG
S725 TLAKVYPSSLSKISG
S728 KVYPSSLSKISGSIL
K826 GQFIQDVKNSRSTDS
K904 QEITSQPKRQYLLLH
Y928 SVVGLKPYVENIWAL
K957-u VVAECLGkLTLIDPE
K971 ETLLPRLKGYLISGS
Y973 LLPRLKGYLISGSSY
Y980 YLISGSSYARSSVVT
K1037 FNSAAHNKPSLIRDL
K1168 SVKQEFEKQDELKRS
T1229 TNLESMDTS______
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