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CAND1 (human)

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: Ubiquitin conjugating system; Transcription factor Cellular Component: nucleus; ubiquitin ligase complex Molecular Function: protein binding; TATA-binding protein binding Biological Process: transcription, DNA-dependent; negative regulation of catalytic activity; protein ubiquitination; cell differentiation; positive regulation of transcriptional preinitiation complex assembly 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®

Select Structure to View Below CAND1 1U6G - C=1-1230 (human) 4A0C - A/B=1-1230 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1U6G 4A0C  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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

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		K70-u	EVQNLAVkCLGPLVS
0	1		Y82	LVSKVKEYQVETIVD
0	1		S107-p	EQLRDISsIGLKTVI
0	1		T139	KKITGRLTSAIAKQE
0	1		S140	KITGRLTSAIAKQED
0	1		S227-p	SELSKNDsMsTTRTY
0	1		S229-p	LSKNDsMsTTRTYIQ
0	3		K255-u	RIGEYLEkIIPLVVK
0	1		S281-p	YCIQAFEsFVRRCPK
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	1		S381-p	TVSPALIsRFKEREE
0	1		K403-u	HAYLSLLkQTRPVQS
0	1		K548-u	LVTQQLVkVIRPLDQ
0	3		S558-p	RPLDQPSsFDATPYI
0	1		K577	TCTIKRLKAADIDQE
0	3		T624-p	ERLKNEItRLTTVkA
0	1		K630-u	ItRLTTVkALTLIAG
0	1		T670-p	QRALKLGtLsALDIL
0	1		S672-p	ALKLGtLsALDILIK
0	1		S725	TLAKVYPSSLSKISG
0	1		S728	KVYPSSLSKISGSIL
0	2		K826-u	GQFIQDVkNSRSTDS
0	3		K904	QEITSQPKRQYLLLH
0	1		S918-p	HSLKEIIssASVVGL
0	1		S919-p	SLKEIIssASVVGLK
0	1		Y928-p	SVVGLKPyVENIWAL
0	14		K957-u	VVAECLGkLTLIDPE
0	1		K971-a	ETLLPRLkGyLISGS
0	3		Y973-p	LLPRLkGyLISGSsy
0	1		S979-p	GyLISGSsyARSSVV
0	3		Y980-p	yLISGSsyARSSVVT
0	1		K1037-u	FNSAAHNkPSLIRDL
0	2		K1168-u	SVKQEFEkQDELkRs
0	1		K1173-a	FEkQDELkRsAMRAV
0	1		S1175-p	kQDELkRsAMRAVAA
0	1		K1191-a	LTIPEAEkSPLMSEF
0	1		T1229-p	TNLESMDtS______

	mouse
K14	HISNLLEKMTSSDKD
K40-u	ELQKDSIkLDDDSER
K51-u	DSERKVVkMILRLLE
R55	KVVkMILRLLEDkNG
R55	KVVkMILRLLEDkNG
K60-u	ILRLLEDkNGEVQNL
K70	EVQNLAVKCLGPLVS
Y82-p	LVSKVKEyQVETIVD
S107	EQLRDISSIGLKTVI
T139-p	KKITGRLtsAIAKQE
S140-p	KITGRLtsAIAKQED
S227	SELSKNDSMSTTRTY
S229	LSKNDSMSTTRTYIQ
K255-u	RIGEYLEkIIPLVVK
S281	YCIQAFESFVRRCPK
S295	KEVYPHVSTIINICL
T296	EVYPHVSTIINICLK
S335	GDDDDQGSDDEYSDD
S340	QGSDDEYSDDDDMSW
K373-u	EMLPEFYkTVSPALI
A381	TVSPALIARFKEREE
K403	HAYLSLLKQTRPVQS
K548	LVTQQLVKVIRPLDQ
S558-p	RPLDQPSsFDATPYI
K577-u	TCTIKRLkAADIDQE
T624-p	ERLKNEItRLTTVKA
K630	ItRLTTVKALTLIAG
T670	QRALKLGTLSALDIL
S672	ALKLGTLSALDILIK
S725-p	TLAKVYPsSLsKISG
S728-p	KVYPsSLsKISGSIL
K826-u	GQFIQDVkNSRSTDS
K904-u	QEITSQPkRQYLLLH
S918	HSLKEIISSASVAGL
S919	SLKEIISSASVAGLK
Y928	SVAGLKPYVENIWAL
K957-u	VVAECLGkLTLIDPE
K971	ETLLPRLKGYLISGS
Y973	LLPRLKGYLISGSSY
S979	GYLISGSSYARSSVV
Y980	YLISGSSYARSSVVT
K1037	FNSAAHNKPSLIRDL
K1168-u	SVKQEFEkQDELKRS
K1173	FEkQDELKRSAMRAV
S1175	kQDELKRSAMRAVAA
K1191	LTIPEAEKSPLMSEF
T1229	TNLESMDTS______

	rat
K14	HISNLLEKMTSSDKD
K40	ELQKDSIKLDDDSER
K51	DSERKVVKMILKLLE
K55	KVVKMILKLLEDKNG
K55	KVVKMILKLLEDKNG
K60	ILKLLEDKNGEVQNL
K70	EVQNLAVKCLGPLVS
Y82	LVSKVKEYQVETIVD
S107	EQLRDISSIGLKTVI
T139	KKITGRLTSAIAKQE
S140	KITGRLTSAIAKQED
S227	SELSKNDSMSTTRTY
S229	LSKNDSMSTTRTYIQ
K255	RIGEYLEKIIPLVVK
S281	YCIQAFESFVRRCPK
S295	KEVYPHVSTIINICL
T296	EVYPHVSTIINICLK
S335	GDDDDQGSDDEYSDD
S340	QGSDDEYSDDDDMSW
K373	EMLPEFYKTVSPALI
S381	TVSPALISRFKEREE
K403	HAYLSLLKQTRPVQS
K548	LVTQQLVKVIRPLDQ
S558	RPLDQPSSFDATPYI
K577	TCTIKRLKAADIDQE
T624	ERLKNEITRLTTVKA
K630	ITRLTTVKALTLIAG
T670	QRALKLGTLSALDIL
S672	ALKLGTLSALDILIK
S725	TLAKVYPSSLSKISG
S728	KVYPSSLSKISGSIL
K826	GQFIQDVKNSRSTDS
K904	QEITSQPKRQYLLLH
S918	HSLKEIISSASVVGL
S919	SLKEIISSASVVGLK
Y928	SVVGLKPYVENIWAL
K957-u	VVAECLGkLTLIDPE
K971	ETLLPRLKGYLISGS
Y973	LLPRLKGYLISGSSY
S979	GYLISGSSYARSSVV
Y980	YLISGSSYARSSVVT
K1037	FNSAAHNKPSLIRDL
K1168	SVKQEFEKQDELKRS
K1173	FEKQDELKRSAMRAV
S1175	KQDELKRSAMRAVAA
K1191	LTIPEAEKSPLMSEF
T1229	TNLESMDTS______

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