CAND1_MOUSE - dbPTM
CAND1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAND1_MOUSE
UniProt AC Q6ZQ38
Protein Name Cullin-associated NEDD8-dissociated protein 1
Gene Name Cand1
Organism Mus musculus (Mouse).
Sequence Length 1230
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic..
Protein 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)..
Protein Sequence MASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKMILRLLEDKNGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLSDKEQLRDISSIGLKTVIGELPPASSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDIMADMLSRQGGLLVNFHPSILTCLLPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEHLLSELSKNDSMSTTRTYIQCIAAISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQAFESFVRRCPKEVYPHVSTIINICLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDDEYSDDDDMSWKVRRAAAKCLDAVVSTRHEMLPEFYKTVSPALIARFKEREENVKADVFHAYLSLLKQTRPVQSWLCDPDAMEQGDTPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNMLTELVNVLPGALTQHIPVLVPGIIFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHVQALVPPVVACVGDPFYKITSEALLVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLKAADIDQEVKERAISCMGQIICNLGDNLGPDLSNTLQIFLERLKNEITRLTTVKALTLIAGSPLKIDLRPVLGEGVPILASFLRKNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDELPPLISESDMHVSQMAISFLTTLAKVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLDFFQALVVTGTNNLGYMDLLRMLTGPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAVVGQFIQDVKNSRSTDSIRLLALLSLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAASYALGSISVGNLPEYLPFVLQEITSQPKRQYLLLHSLKEIISSASVAGLKPYVENIWALLLKHCECAEEGTRNVVAECLGKLTLIDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHPQPIDPLLKNCIGDFLKTLEDPDLNVRRVALVTFNSAAHNKPSLIRDLLDSVLPHLYNETKVRKELIREVEMGPFKHTVDDGLDIRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHYDIKMLTFLMLVRLSTLCPSAVLQRLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAMRAVAALLTIPEAEKSPLMSEFQSQISSNPELAAIFESIQKDSSSTNLESMDTS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MASASYHIS
------CCCHHHHHH		25.71-
3Phosphorylation-----MASASYHISN
-----CCCHHHHHHH		29.6120415495
5Phosphorylation---MASASYHISNLL
---CCCHHHHHHHHH		18.1020415495
6Phosphorylation--MASASYHISNLLE
--CCCHHHHHHHHHH		11.6829514104
20AcetylationEKMTSSDKDFRFMAT
HHHCCCCCCCHHHHH		61.7923806337
40UbiquitinationELQKDSIKLDDDSER
HHHHCCCCCCCHHHH		50.2222790023
51UbiquitinationDSERKVVKMILRLLE
HHHHHHHHHHHHHHH		24.1822790023
51AcetylationDSERKVVKMILRLLE
HHHHHHHHHHHHHHH		24.1822826441
60UbiquitinationILRLLEDKNGEVQNL
HHHHHHCCCCCHHHH		58.4322790023
60AcetylationILRLLEDKNGEVQNL
HHHHHHCCCCCHHHH		58.4323236377
80AcetylationGPLVSKVKEYQVETI
HHHHHHHHHHHHHHH		55.2122826441
82PhosphorylationLVSKVKEYQVETIVD
HHHHHHHHHHHHHHH		16.4920116462
139PhosphorylationKKITGRLTSAIAKQE
HHHHCHHHHHHHCCC		18.1018779572
140PhosphorylationKITGRLTSAIAKQED
HHHCHHHHHHHCCCC		23.4425521595
255AcetylationRIGEYLEKIIPLVVK
HHHHHHHHHHHHHHH		43.2522826441
255UbiquitinationRIGEYLEKIIPLVVK
HHHHHHHHHHHHHHH		43.2522790023
264S-palmitoylationIPLVVKFCNVDDDEL
HHHHHHHCCCCHHHH		3.9328526873
296PhosphorylationEVYPHVSTIINICLK
HHHCCHHHHHHHHHH		25.4522705319
304PhosphorylationIINICLKYLTYDPNY
HHHHHHHHHCCCCCC		7.4223737553
306PhosphorylationNICLKYLTYDPNYNY
HHHHHHHCCCCCCCC		23.8423737553
307PhosphorylationICLKYLTYDPNYNYD
HHHHHHCCCCCCCCC		27.1523737553
311PhosphorylationYLTYDPNYNYDDEDE
HHCCCCCCCCCCCCC		22.0823737553
313PhosphorylationTYDPNYNYDDEDEDE
CCCCCCCCCCCCCCC		17.8923737553
335PhosphorylationGDDDDQGSDDEYSDD
CCCCCCCCCCCCCCC		35.9323737553
339PhosphorylationDQGSDDEYSDDDDMS
CCCCCCCCCCCHHHH		25.1323737553
340PhosphorylationQGSDDEYSDDDDMSW
CCCCCCCCCCHHHHH		32.3023737553
346PhosphorylationYSDDDDMSWKVRRAA
CCCCHHHHHHHHHHH		30.6423737553
373UbiquitinationEMLPEFYKTVSPALI
HHCHHHHHHCCHHHH		48.0122790023
557PhosphorylationIRPLDQPSSFDATPY
HCCCCCCCCCCCCHH		37.6924925903
558PhosphorylationRPLDQPSSFDATPYI
CCCCCCCCCCCCHHH		33.5525521595
562PhosphorylationQPSSFDATPYIKDLF
CCCCCCCCHHHHHHH		20.6124925903
564PhosphorylationSSFDATPYIKDLFTC
CCCCCCHHHHHHHHH		19.0929550500
566AcetylationFDATPYIKDLFTCTI
CCCCHHHHHHHHHHH		42.4022826441
574SuccinylationDLFTCTIKRLKAADI
HHHHHHHHHHHHCCC		33.2623806337
574AcetylationDLFTCTIKRLKAADI
HHHHHHHHHHHHCCC		33.2623806337
574MalonylationDLFTCTIKRLKAADI
HHHHHHHHHHHHCCC		33.2626320211
577UbiquitinationTCTIKRLKAADIDQE
HHHHHHHHHCCCCHH		45.6327667366
577MalonylationTCTIKRLKAADIDQE
HHHHHHHHHCCCCHH		45.6326320211
586AcetylationADIDQEVKERAISCM
CCCCHHHHHHHHHHH		40.5023954790
586UbiquitinationADIDQEVKERAISCM
CCCCHHHHHHHHHHH		40.5027667366
624PhosphorylationERLKNEITRLTTVKA
HHHHHHHHHHHHHHH		17.2822817900
630AcetylationITRLTTVKALTLIAG
HHHHHHHHHHHHHCC		35.2722826441
638PhosphorylationALTLIAGSPLKIDLR
HHHHHCCCCCEEECC		20.3128066266
725PhosphorylationTLAKVYPSSLSKISG
HHHHHCHHHHHHHCH		26.6518779572
728PhosphorylationKVYPSSLSKISGSIL
HHCHHHHHHHCHHHH		29.8618779572
801AcetylationQSYYSIAKCVAALTR
HHHHHHHHHHHHHHH		27.8022826441
826UbiquitinationGQFIQDVKNSRSTDS
HHHHHHHHCCCCCHH		58.4522790023
828PhosphorylationFIQDVKNSRSTDSIR
HHHHHHCCCCCHHHH		23.1423684622
830PhosphorylationQDVKNSRSTDSIRLL
HHHHCCCCCHHHHHH		36.0718779572
831PhosphorylationDVKNSRSTDSIRLLA
HHHCCCCCHHHHHHH		32.4318779572
833PhosphorylationKNSRSTDSIRLLALL
HCCCCCHHHHHHHHH		15.0818779572
904UbiquitinationQEITSQPKRQYLLLH
HHHCCCCHHHHHHHH		44.49-
928PhosphorylationSVAGLKPYVENIWAL
CCCCCHHHHHHHHHH		20.8626487105
957UbiquitinationVVAECLGKLTLIDPE
HHHHHHCCCCCCCHH		25.9122790023
971AcetylationETLLPRLKGYLISGS
HHHHHHHCCEEECCC		46.9523806337
992PhosphorylationVVTAVKFTISDHPQP
CEEEEEEECCCCCCC		17.5426643407
994PhosphorylationTAVKFTISDHPQPID
EEEEEECCCCCCCCC		27.1526643407
1134S-palmitoylationLVRLSTLCPSAVLQR
HHHHHCCCHHHHHHH		2.2528526873
1163MalonylationKVKANSVKQEFEKQD
HHHHHHHHHHHHCHH		43.8826320211
1168AcetylationSVKQEFEKQDELKRS
HHHHHHHCHHHHHHH		69.2623954790
1168UbiquitinationSVKQEFEKQDELKRS
HHHHHHHCHHHHHHH		69.2622790023
1219PhosphorylationFESIQKDSSSTNLES
HHHHHCCCCCCCHHH		32.9729899451
1220PhosphorylationESIQKDSSSTNLESM
HHHHCCCCCCCHHHC		51.8425521595
1221PhosphorylationSIQKDSSSTNLESMD
HHHCCCCCCCHHHCC		25.8525521595
1222PhosphorylationIQKDSSSTNLESMDT
HHCCCCCCCHHHCCC		45.8520415495
1226PhosphorylationSSSTNLESMDTS---
CCCCCHHHCCCC---		25.7325521595
1229PhosphorylationTNLESMDTS------
CCHHHCCCC------		27.9121743459
1230PhosphorylationNLESMDTS-------
CHHHCCCC-------		33.6827087446
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CAND1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAND1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CAND1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAND1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAND1_MOUSE

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Related Literatures of Post-Translational Modification

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