CUL4A_MOUSE - dbPTM
CUL4A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUL4A_MOUSE
UniProt AC Q3TCH7
Protein Name Cullin-4A
Gene Name Cul4a
Organism Mus musculus (Mouse).
Sequence Length 759
Subcellular Localization
Protein Description Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. In association with RBX1, DDB1 and DDB2 is required for histone H3 and histone H4 ubiquitination in response to ultraviolet and may be important for subsequent DNA repair. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL (By similarity)..
Protein Sequence MADEGPRKGSVSALMGRTNGLTKPAALAGGPAKPGGTGGSRKLVIKNFRDRPRLPDNYTQDTWRKLHEAVKAIQSSTSIRYNLEELYQAVENLCSHKVSPTLYKQLRQVCEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRNHIISDRMVQSKTIDGILLLIGRERSGEAVDRSLLRSLLSMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLEHLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVINPEKDKDMVQDLLDFKDKVDHVVEVCFQRNERFINLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERILDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSAPGPIDLTVNILTMGYWPTYTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNADFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDSPNQYHYVA
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
10PhosphorylationDEGPRKGSVSALMGR
CCCCCCCCHHHHCCC		18.8826824392
12PhosphorylationGPRKGSVSALMGRTN
CCCCCCHHHHCCCCC		19.8628833060
18PhosphorylationVSALMGRTNGLTKPA
HHHHCCCCCCCCCCH		28.1028576409
75PhosphorylationEAVKAIQSSTSIRYN
HHHHHHHCCCCCCCC		29.4825159016
76PhosphorylationAVKAIQSSTSIRYNL
HHHHHHCCCCCCCCH		15.1425159016
77PhosphorylationVKAIQSSTSIRYNLE
HHHHHCCCCCCCCHH		33.1625159016
78PhosphorylationKAIQSSTSIRYNLEE
HHHHCCCCCCCCHHH		13.6625159016
81PhosphorylationQSSTSIRYNLEELYQ
HCCCCCCCCHHHHHH		23.5625159016
95PhosphorylationQAVENLCSHKVSPTL
HHHHHHHHCCCCHHH		29.5225159016
104UbiquitinationKVSPTLYKQLRQVCE
CCCHHHHHHHHHHHH		46.0722790023
125PhosphorylationILPFREDSLDSVLFL
HCCCCCCCCHHHHHH		29.35-
190PhosphorylationISDRMVQSKTIDGIL
CCCCHHCCCCCCEEE		21.9826239621
192PhosphorylationDRMVQSKTIDGILLL
CCHHCCCCCCEEEEE		29.5526239621
227PhosphorylationMLSDLQVYKDSFELK
HHHCCCHHHCCEEEE		8.9825159016
277PhosphorylationEADRVITYLDHSTQK
HHHHHHHHCCCCCCC		10.0624759943
309UbiquitinationILQKGLEHLLDENRV
HHHHHHHHHHCCCCC		36.4127667366
369UbiquitinationVQDLLDFKDKVDHVV
HHHHHHHHHHCCHHH		57.2022790023
371UbiquitinationDLLDFKDKVDHVVEV
HHHHHHHHCCHHHHH		50.5922790023
396UbiquitinationLMKESFETFINKRPN
HHHHHHHHHHHCCCC		28.0127667366
422UbiquitinationSKLRAGNKEATDEEL
HHHHCCCCCCCHHHH		48.0522790023
422AcetylationSKLRAGNKEATDEEL
HHHHCCCCCCCHHHH		48.0523954790
454UbiquitinationDVFEAFYKKDLAKRL
HHHHHHHCHHHHHHH		33.1022790023
465MalonylationAKRLLVGKSASVDAE
HHHHHCCCCCCCHHH		35.0626320211
465UbiquitinationAKRLLVGKSASVDAE
HHHHHCCCCCCCHHH		35.06-
480AcetylationKSMLSKLKHECGAAF
HHHHHHHHHHHCHHH		40.8822826441
496UbiquitinationSKLEGMFKDMELSKD
HHHHHHHCCCHHCHH		47.4722790023
635MalonylationLQSLACGKARVLIKS
HHHHHCCCEEEEEEC		32.6726320211
635UbiquitinationLQSLACGKARVLIKS
HHHHHCCCEEEEEEC		32.67-
642PhosphorylationKARVLIKSPKGKEVE
CEEEEEECCCCCCCC		25.5028066266
705UbiquitinationAAIVRIMKMRKTLGH
HHHHHHHHHHHHHCC		32.93-
738PhosphorylationDLKKRIESLIDRDYM
CHHHHHHHHHCHHHH		28.4028066266
751PhosphorylationYMERDKDSPNQYHYV
HHHHCCCCCCCCCCC		31.3323684622
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 CUL4A_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CUL4A_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 CUL4A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBX2_MOUSERnf7physical
19037258
ELOB_RATTceb2physical
19037258
ELOC_RATTceb1physical
19037258
RBX1_MOUSERbx1physical
19037258
CTNB1_MOUSECtnnb1physical
17954973
LST8_HUMANMLST8physical
18235224
DDB1_HUMANDDB1physical
18235224
CDT1_MOUSECdt1physical
14578910
TTP_MOUSEZfp36physical
22262661
ATRX_HUMANATRXphysical
26496610
CHD1_HUMANCHD1physical
26496610
CSN1_HUMANGPS1physical
26496610
NEDD8_HUMANNEDD8physical
26496610
UBF1_HUMANUBTFphysical
26496610
ZNF35_HUMANZNF35physical
26496610
S39A7_HUMANSLC39A7physical
26496610
CSN3_HUMANCOPS3physical
26496610
U3IP2_HUMANRRP9physical
26496610
CSN2_HUMANCOPS2physical
26496610
MDC1_HUMANMDC1physical
26496610
DCAF1_HUMANVPRBPphysical
26496610
RBX1_HUMANRBX1physical
26496610
CSN8_HUMANCOPS8physical
26496610
CSN6_HUMANCOPS6physical
26496610
NECT3_HUMANPVRL3physical
26496610
CSN7A_HUMANCOPS7Aphysical
26496610
CSN4_HUMANCOPS4physical
26496610
DTL_HUMANDTLphysical
26496610
BRWD1_HUMANBRWD1physical
26496610
PHIP_HUMANPHIPphysical
26496610
CAND1_HUMANCAND1physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
DDA1_HUMANDDA1physical
26496610
DCA10_HUMANDCAF10physical
26496610
DCA11_HUMANDCAF11physical
26496610
H2AV_HUMANH2AFVphysical
26496610
AHNK2_HUMANAHNAK2physical
26496610
SOGA1_HUMANSOGA1physical
26496610
BRWD3_HUMANBRWD3physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUL4A_MOUSE

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Related Literatures of Post-Translational Modification

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