CUL4A_HUMAN - dbPTM
CUL4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUL4A_HUMAN
UniProt AC Q13619
Protein Name Cullin-4A
Gene Name CUL4A
Organism Homo sapiens (Human).
Sequence Length 759
Subcellular Localization
Protein Description Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination 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. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. 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..
Protein Sequence MADEAPRKGSFSALVGRTNGLTKPAALAAAPAKPGGAGGSKKLVIKNFRDRPRLPDNYTQDTWRKLHEAVRAVQSSTSIRYNLEELYQAVENLCSHKVSPMLYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSTLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIVINPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDNPNQYHYVA
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
8AcetylationMADEAPRKGSFSALV
CCCCCCCCCCHHHHH
58.8226051181
8SumoylationMADEAPRKGSFSALV
CCCCCCCCCCHHHHH
58.8228112733
8UbiquitinationMADEAPRKGSFSALV
CCCCCCCCCCHHHHH
58.82-
10PhosphorylationDEAPRKGSFSALVGR
CCCCCCCCHHHHHCC
21.0429255136
12PhosphorylationAPRKGSFSALVGRTN
CCCCCCHHHHHCCCC
23.5330266825
22PhosphorylationVGRTNGLTKPAALAA
HCCCCCCCCHHHHHC
36.0622817900
23AcetylationGRTNGLTKPAALAAA
CCCCCCCCHHHHHCC
37.3926051181
33AcetylationALAAAPAKPGGAGGS
HHHCCCCCCCCCCCC
43.0426051181
33UbiquitinationALAAAPAKPGGAGGS
HHHCCCCCCCCCCCC
43.0418781797
40PhosphorylationKPGGAGGSKKLVIKN
CCCCCCCCCEEEEEC
26.2129514088
41AcetylationPGGAGGSKKLVIKNF
CCCCCCCCEEEEECC
54.0912435295
42AcetylationGGAGGSKKLVIKNFR
CCCCCCCEEEEECCC
50.0812436343
58PhosphorylationRPRLPDNYTQDTWRK
CCCCCCCCCHHHHHH
17.1027642862
75PhosphorylationEAVRAVQSSTSIRYN
HHHHHHHCCCCCCCC
29.0520860994
76PhosphorylationAVRAVQSSTSIRYNL
HHHHHHCCCCCCCCH
14.7521406692
77PhosphorylationVRAVQSSTSIRYNLE
HHHHHCCCCCCCCHH
33.1621406692
78PhosphorylationRAVQSSTSIRYNLEE
HHHHCCCCCCCCHHH
13.6621406692
99PhosphorylationNLCSHKVSPMLYKQL
HHHHCCCCHHHHHHH
14.9219413330
104AcetylationKVSPMLYKQLRQACE
CCCHHHHHHHHHHHH
38.6025953088
104MalonylationKVSPMLYKQLRQACE
CCCHHHHHHHHHHHH
38.6026320211
104UbiquitinationKVSPMLYKQLRQACE
CCCHHHHHHHHHHHH
38.60-
104 (in isoform 1)Ubiquitination-38.6021890473
133AcetylationLDSVLFLKKINTCWQ
CHHHHHHHHHHHHCH
44.2527452117
133UbiquitinationLDSVLFLKKINTCWQ
CHHHHHHHHHHHHCH
44.25-
151PhosphorylationRQMIMIRSIFLFLDR
HHHHHHHHHHHHCCC
13.5321712546
159PhosphorylationIFLFLDRTYVLQNST
HHHHCCCCHHHCCCC
20.0423898821
160PhosphorylationFLFLDRTYVLQNSTL
HHHCCCCHHHCCCCC
10.4823898821
165PhosphorylationRTYVLQNSTLPSIWD
CCHHHCCCCCCCHHH
20.5423898821
166PhosphorylationTYVLQNSTLPSIWDM
CHHHCCCCCCCHHHH
50.6823898821
169PhosphorylationLQNSTLPSIWDMGLE
HCCCCCCCHHHHHHH
39.1523898821
180PhosphorylationMGLELFRTHIISDKM
HHHHHHHHHHCCCHH
15.3023898821
184PhosphorylationLFRTHIISDKMVQSK
HHHHHHCCCHHHCCC
30.4923898821
186UbiquitinationRTHIISDKMVQSKTI
HHHHCCCHHHCCCCC
33.89-
216PhosphorylationVDRSLLRSLLGMLSD
HCHHHHHHHHHHHCC
28.1020068231
227PhosphorylationMLSDLQVYKDSFELK
HHCCHHHHHCCEEEE
8.9822817900
234UbiquitinationYKDSFELKFLEETNC
HHCCEEEEEHHHHCC
40.48-
259PhosphorylationQEREVPEYLNHVSKR
HHHCHHHHHHHHHHH
13.51-
265UbiquitinationEYLNHVSKRLEEEGD
HHHHHHHHHHHHCCC
60.97-
276O-linked_GlycosylationEEGDRVITYLDHSTQ
HCCCCEEEEEECCCC
18.3828510447
284AcetylationYLDHSTQKPLIACVE
EEECCCCCCHHHHHH
41.7126051181
284MalonylationYLDHSTQKPLIACVE
EEECCCCCCHHHHHH
41.7126320211
284UbiquitinationYLDHSTQKPLIACVE
EEECCCCCCHHHHHH
41.71-
292AcetylationPLIACVEKQLLGEHL
CHHHHHHHHHHHHHH
26.3326051181
322 (in isoform 2)Ubiquitination-1.5921890473
330MethylationYQLFSRVRGGQQALL
HHHHHHHHHHHHHHH
42.27-
354 (in isoform 2)Ubiquitination-27.9921890473
357UbiquitinationAIVINPEKDKDMVQD
EEEECCCCCHHHHHH
71.92-
359UbiquitinationVINPEKDKDMVQDLL
EECCCCCHHHHHHHH
59.81-
369UbiquitinationVQDLLDFKDKVDHVI
HHHHHHHHHHHCHHH
57.20-
391UbiquitinationERFVNLMKESFETFI
HHHHHHHHHHHHHHH
54.06-
396 (in isoform 2)Ubiquitination-28.0121890473
404UbiquitinationFINKRPNKPAELIAK
HHHCCCCCCHHHHHH
48.57-
411UbiquitinationKPAELIAKHVDSKLR
CCHHHHHHHHHHHHH
36.85-
416UbiquitinationIAKHVDSKLRAGNKE
HHHHHHHHHHCCCCC
37.21-
422AcetylationSKLRAGNKEATDEEL
HHHHCCCCCCCHHHH
48.0526051181
422UbiquitinationSKLRAGNKEATDEEL
HHHHCCCCCCCHHHH
48.0521906983
422 (in isoform 1)Ubiquitination-48.0521890473
425PhosphorylationRAGNKEATDEELERT
HCCCCCCCHHHHHHH
45.0620860994
453PhosphorylationKDVFEAFYKKDLAKR
HHHHHHHHCHHHHHH
24.95-
454UbiquitinationDVFEAFYKKDLAKRL
HHHHHHHCHHHHHHH
33.102190698
454 (in isoform 1)Ubiquitination-33.1021890473
465AcetylationAKRLLVGKSASVDAE
HHHHHCCCCCCCHHH
35.0625953088
465MalonylationAKRLLVGKSASVDAE
HHHHHCCCCCCCHHH
35.0626320211
465UbiquitinationAKRLLVGKSASVDAE
HHHHHCCCCCCCHHH
35.06-
473AcetylationSASVDAEKSMLSKLK
CCCCHHHHHHHHHHH
42.7725953088
477PhosphorylationDAEKSMLSKLKHECG
HHHHHHHHHHHHHHC
27.5724260401
480AcetylationKSMLSKLKHECGAAF
HHHHHHHHHHHCHHH
40.8826051181
480UbiquitinationKSMLSKLKHECGAAF
HHHHHHHHHHHCHHH
40.88-
490UbiquitinationCGAAFTSKLEGMFKD
HCHHHHHHHHHHHCC
47.72-
496AcetylationSKLEGMFKDMELSKD
HHHHHHHCCCCCCHH
47.4726051181
496UbiquitinationSKLEGMFKDMELSKD
HHHHHHHCCCCCCHH
47.47-
496 (in isoform 1)Ubiquitination-47.4721890473
502UbiquitinationFKDMELSKDIMVHFK
HCCCCCCHHHHHHHH
64.99-
541AcetylationPTYTPMEVHLTPEMI
CCCCCCEEECCHHHH
3.4919608861
541 (in isoform 2)Acetylation-3.49-
555AcetylationIKLQEVFKAFYLGKH
HHHHHHHHHHHCCCC
42.64129845
561AcetylationFKAFYLGKHSGRKLQ
HHHHHCCCCCCCCEE
31.8125953088
561UbiquitinationFKAFYLGKHSGRKLQ
HHHHHCCCCCCCCEE
31.81-
615SulfoxidationFSFEEIKMATGIEDS
CCHHHHHHHHCCCHH
5.0521406390
633S-nitrosylationRTLQSLACGKARVLI
HHHHHHHCCCEEEEE
7.5322126794
635AcetylationLQSLACGKARVLIKS
HHHHHCCCEEEEEEC
32.6725953088
635MalonylationLQSLACGKARVLIKS
HHHHHCCCEEEEEEC
32.6726320211
635UbiquitinationLQSLACGKARVLIKS
HHHHHCCCEEEEEEC
32.67-
641AcetylationGKARVLIKSPKGKEV
CCEEEEEECCCCCCC
57.4519608861
642PhosphorylationKARVLIKSPKGKEVE
CEEEEEECCCCCCCC
25.5023911959
646AcetylationLIKSPKGKEVEDGDK
EEECCCCCCCCCCCE
65.7926051181
646UbiquitinationLIKSPKGKEVEDGDK
EEECCCCCCCCCCCE
65.79-
661UbiquitinationFIFNGEFKHKLFRIK
EEECCCCCCEEEEEE
35.21-
683PhosphorylationETVEEQVSTTERVFQ
HHHHHHHHHHHHHHH
29.3424719451
684PhosphorylationTVEEQVSTTERVFQD
HHHHHHHHHHHHHHH
33.5425627689
692MethylationTERVFQDRQYQIDAA
HHHHHHHHHHHHHHH
26.73-
702DimethylationQIDAAIVRIMKMRKT
HHHHHHHHHHHHHHH
19.71-
705UbiquitinationAAIVRIMKMRKTLGH
HHHHHHHHHHHHHCC
32.93-
708UbiquitinationVRIMKMRKTLGHNLL
HHHHHHHHHHCCCHH
44.60-
724UbiquitinationSELYNQLKFPVKPGD
HHHHHHCCCCCCCCC
37.55-
728AcetylationNQLKFPVKPGDLKKR
HHCCCCCCCCCHHHH
43.4525953088
728UbiquitinationNQLKFPVKPGDLKKR
HHCCCCCCCCCHHHH
43.45-
733MalonylationPVKPGDLKKRIESLI
CCCCCCHHHHHHHHH
44.7526320211
733UbiquitinationPVKPGDLKKRIESLI
CCCCCCHHHHHHHHH
44.75-
738PhosphorylationDLKKRIESLIDRDYM
CHHHHHHHHHCHHHH
28.4026074081
742MethylationRIESLIDRDYMERDK
HHHHHHCHHHHHHCC
29.93-
744PhosphorylationESLIDRDYMERDKDN
HHHHCHHHHHHCCCC
11.1926074081
749UbiquitinationRDYMERDKDNPNQYH
HHHHHHCCCCCCCCC
66.67-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CUL4A_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAND1_HUMANCAND1physical
12609982
HS90A_HUMANHSP90AA1physical
12481031
NEDD8_HUMANNEDD8physical
12481031
TBA1B_HUMANTUBA1Bphysical
12481031
CDN1A_HUMANCDKN1Aphysical
18794347
DDB1_HUMANDDB1physical
18593899
DDB2_HUMANDDB2physical
18593899
RBX1_HUMANRBX1physical
18593899
CUL4B_HUMANCUL4Bphysical
18593899
MERL_HUMANNF2physical
18332868
UBC_HUMANUBCphysical
16964240
PCNA_HUMANPCNAphysical
16964240
CUL4B_HUMANCUL4Bphysical
16964240
TP4AP_HUMANTRPC4APphysical
16964240
DET1_HUMANDET1physical
16964240
DDA1_HUMANDDA1physical
16964240
NEDD8_HUMANNEDD8physical
16964240
CRBN_HUMANCRBNphysical
16964240
CSN3_HUMANCOPS3physical
16964240
CSN4_HUMANCOPS4physical
16964240
CSN5_HUMANCOPS5physical
16964240
CSN2_HUMANCOPS2physical
16964240
CSN8_HUMANCOPS8physical
16964240
CSN7B_HUMANCOPS7Bphysical
16964240
CSN7A_HUMANCOPS7Aphysical
16964240
CSN6_HUMANCOPS6physical
16964240
DDB1_HUMANDDB1physical
16964240
DDB2_HUMANDDB2physical
16964240
DCA11_HUMANDCAF11physical
16964240
DCAF5_HUMANDCAF5physical
16964240
BRWD1_HUMANBRWD1physical
16964240
PHIP_HUMANPHIPphysical
16964240
DCAF6_HUMANDCAF6physical
16964240
DCA12_HUMANDCAF12physical
16964240
DCA10_HUMANDCAF10physical
16964240
DCAF4_HUMANDCAF4physical
16964240
WDTC1_HUMANWDTC1physical
16964240
CAND1_HUMANCAND1physical
16964240
SKP2_HUMANSKP2physical
16537899
CDN1B_HUMANCDKN1Bphysical
16537899
TOIP2_HUMANTOR1AIP2physical
16964240
IFG15_HUMANTOR1AIP2physical
16964240
BAF_HUMANBANF1physical
19759913
EMD_HUMANEMDphysical
19759913
DDB1_HUMANDDB1physical
15811626
DDB2_HUMANDDB2physical
17041588
DTL_HUMANDTLphysical
17041588
WDR26_HUMANWDR26physical
17041588
GRWD1_HUMANGRWD1physical
17041588
RBBP5_HUMANRBBP5physical
17041588
RFWD2_HUMANRFWD2physical
17041588
WDR5B_HUMANWDR5Bphysical
17041588
POC1B_HUMANPOC1Bphysical
17041588
SNR40_HUMANSNRNP40physical
17041588
WDR61_HUMANWDR61physical
17041588
WDR76_HUMANWDR76physical
17041588
WDR82_HUMANWDR82physical
17041588
WDR5_HUMANWDR5physical
17041588
TLE2_HUMANTLE2physical
17041588
EED_HUMANEEDphysical
17041588
DDB1_HUMANDDB1physical
15448697
CAND1_HUMANCAND1physical
15448697
RBX1_HUMANRBX1physical
15448697
CDT1_HUMANCDT1physical
15448697
RBX1_HUMANRBX1physical
11861641
DDB2_HUMANDDB2physical
11564859
COMD1_HUMANCOMMD1physical
21778237
RBX1_HUMANRBX1physical
19287380
RASF1_HUMANRASSF1physical
21205828
CAND1_HUMANCAND1physical
21249194
DCAF1_HUMANVPRBPphysical
17630831
GLMN_HUMANGLMNphysical
22405651
RBX1_HUMANRBX1physical
22405651
CAND1_HUMANCAND1physical
22405651
CTNB1_HUMANCTNNB1physical
17954973
CDN1B_HUMANCDKN1Bphysical
16467204
CDT1_HUMANCDT1physical
14578910
CAND1_HUMANCAND1physical
12504026
P53_HUMANTP53physical
16861890
MDM2_HUMANMDM2physical
16861890
PCNA_HUMANPCNAphysical
16861890
DDB1_HUMANDDB1physical
17079684
RBX1_HUMANRBX1physical
17079684
DDB2_HUMANDDB2physical
17079684
CDT1_HUMANCDT1physical
17079684
CUL1_HUMANCUL1physical
17079684
CAND1_HUMANCAND1physical
17079684
DCAF1_HUMANVPRBPphysical
17079684
DCA11_HUMANDCAF11physical
17079684
CSN1_HUMANGPS1physical
17079684
CSN3_HUMANCOPS3physical
17079684
CSN4_HUMANCOPS4physical
17079684
CSN5_HUMANCOPS5physical
17079684
CSN6_HUMANCOPS6physical
17079684
CSN7A_HUMANCOPS7Aphysical
17079684
CSN7B_HUMANCOPS7Bphysical
17079684
CSN8_HUMANCOPS8physical
17079684
RBBP7_HUMANRBBP7physical
17079684
FBXW5_HUMANFBXW5physical
17079684
FBXW8_HUMANFBXW8physical
17079684
RFWD2_HUMANRFWD2physical
17079684
WSB1_HUMANWSB1physical
17079684
WSB2_HUMANWSB2physical
17079684
NUP43_HUMANNUP43physical
17079684
FBW1A_HUMANBTRCphysical
17079684
PWP1_HUMANPWP1physical
17079684
RBBP4_HUMANRBBP4physical
17079684
GRWD1_HUMANGRWD1physical
17079684
CHK1_HUMANCHEK1physical
19808933
DCAF1_HUMANVPRBPphysical
18606781
CAND1_HUMANCAND1physical
18606781
DDB1_HUMANDDB1physical
18606781
CSN1_HUMANGPS1physical
18606781
CSN2_HUMANCOPS2physical
18606781
CSN3_HUMANCOPS3physical
18606781
CSN4_HUMANCOPS4physical
18606781
CSN5_HUMANCOPS5physical
18606781
CSN6_HUMANCOPS6physical
18606781
CSN7A_HUMANCOPS7Aphysical
18606781
CSN7B_HUMANCOPS7Bphysical
18606781
CSN8_HUMANCOPS8physical
18606781
UBXN7_HUMANUBXN7physical
22466964
DCAF6_HUMANDCAF6physical
21145461
CUL4A_HUMANCUL4Aphysical
21145461
DCNL1_HUMANDCUN1D1physical
21145461
KAD9_HUMANAK9physical
21145461
DCST1_HUMANDCST1physical
21145461
WDTC1_HUMANWDTC1physical
21145461
TP4AP_HUMANTRPC4APphysical
21145461
DCA12_HUMANDCAF12physical
21145461
CSN4_HUMANCOPS4physical
21145461
PHIP_HUMANPHIPphysical
21145461
DCAF8_HUMANDCAF8physical
21145461
AMRA1_HUMANAMBRA1physical
21145461
DCAF1_HUMANVPRBPphysical
21145461
DDB2_HUMANDDB2physical
21145461
DCAF4_HUMANDCAF4physical
21145461
CSN3_HUMANCOPS3physical
21145461
CSN1_HUMANGPS1physical
21145461
DCA11_HUMANDCAF11physical
21145461
DDB1_HUMANDDB1physical
21145461
CSN5_HUMANCOPS5physical
21145461
DC122_HUMANDCAF12L2physical
21145461
CSN2_HUMANCOPS2physical
21145461
CRBN_HUMANCRBNphysical
21145461
CSN7A_HUMANCOPS7Aphysical
21145461
DCA16_HUMANDCAF16physical
21145461
ERCC8_HUMANERCC8physical
21145461
BRWD1_HUMANBRWD1physical
21145461
DTL_HUMANDTLphysical
21145461
CUL4B_HUMANCUL4Bphysical
21145461
CSN6_HUMANCOPS6physical
21145461
CUL5_HUMANCUL5physical
21145461
DC4L1_HUMANDCAF4L1physical
21145461
CAND1_HUMANCAND1physical
21145461
CSN7B_HUMANCOPS7Bphysical
21145461
DDA1_HUMANDDA1physical
21145461
TOIP2_HUMANTOR1AIP2physical
21145461
IFG15_HUMANTOR1AIP2physical
21145461
CSN8_HUMANCOPS8physical
21145461
IF2B1_HUMANIGF2BP1physical
21145461
CSN9_HUMANMYEOV2physical
21145461
DCAF5_HUMANDCAF5physical
21145461
NEDD8_HUMANNEDD8physical
21145461
APC5_HUMANANAPC5physical
21145461
CDY2_HUMANCDY2Aphysical
21145461
OTUL_HUMANOTULINphysical
21145461
NXPH3_HUMANNXPH3physical
21145461
RFWD2_HUMANRFWD2physical
21145461
RGS12_HUMANRGS12physical
21145461
SCAFB_HUMANSCAF11physical
21145461
SH3R2_HUMANSH3RF2physical
21145461
SLAP1_HUMANSLAphysical
21145461
TCHP_HUMANTCHPphysical
21145461
DCA10_HUMANDCAF10physical
21145461
UBP7_HUMANUSP7physical
21145461
MAP4_HUMANMAP4physical
21145461
ABCAA_HUMANABCA10physical
21145461
XXLT1_HUMANXXYLT1physical
21145461
SYNEM_HUMANSYNMphysical
21145461
ZN407_HUMANZNF407physical
21145461
CSR2B_HUMANCSRP2BPphysical
21145461
RL26_HUMANRPL26physical
21145461
GHC1_HUMANSLC25A22physical
21145461
SFXN1_HUMANSFXN1physical
21145461
HSP7C_HUMANHSPA8physical
21145461
TFG_HUMANTFGphysical
21145461
CUL3_HUMANCUL3physical
21145461
K1C10_HUMANKRT10physical
21145461
DCAF7_HUMANDCAF7physical
21145461
CAH2_HUMANCA2physical
21145461
KLHL9_HUMANKLHL9physical
21145461
K2C1_HUMANKRT1physical
21145461
FUS_HUMANFUSphysical
21145461
K1C9_HUMANKRT9physical
21145461
TBB4B_HUMANTUBB4Bphysical
21145461
ENPL_HUMANHSP90B1physical
21145461
PRS10_HUMANPSMC6physical
21145461
SKP1_HUMANSKP1physical
21145461
TBA4A_HUMANTUBA4Aphysical
21145461
UBC_HUMANUBCphysical
21145461
EWS_HUMANEWSR1physical
21145461
H2AV_HUMANH2AFVphysical
21145461
HAX1_HUMANHAX1physical
21145461
ROA2_HUMANHNRNPA2B1physical
21145461
HNRL1_HUMANHNRNPUL1physical
21145461
HS71L_HUMANHSPA1Lphysical
21145461
SYIC_HUMANIARSphysical
21145461
K22E_HUMANKRT2physical
21145461
K1C24_HUMANKRT24physical
21145461
PHS_HUMANPCBD1physical
21145461
PWP1_HUMANPWP1physical
21145461
SMD1_HUMANSNRPD1physical
21145461
TBA1C_HUMANTUBA1Cphysical
21145461
TBB1_HUMANTUBB1physical
21145461
HNRH1_HUMANHNRNPH1physical
21145461
HNRH3_HUMANHNRNPH3physical
21145461
GRP78_HUMANHSPA5physical
21145461
LG3BP_HUMANLGALS3BPphysical
21145461
NUCL_HUMANNCLphysical
21145461
PABP1_HUMANPABPC1physical
21145461
2AAA_HUMANPPP2R1Aphysical
21145461
SNRPA_HUMANSNRPAphysical
21145461
RSMB_HUMANSNRPBphysical
21145461
TCPE_HUMANCCT5physical
21145461
DJC10_HUMANDNAJC10physical
21145461
EF1A1_HUMANEEF1A1physical
21145461
EF1A2_HUMANEEF1A2physical
21145461
ENOA_HUMANENO1physical
21145461
ROAA_HUMANHNRNPABphysical
21145461
HNRPF_HUMANHNRNPFphysical
21145461
HNRDL_HUMANHNRNPDLphysical
21145461
GRP75_HUMANHSPA9physical
21145461
K22O_HUMANKRT76physical
21145461
PRDX1_HUMANPRDX1physical
21145461
QPCT_HUMANQPCTphysical
21145461
RL15_HUMANRPL15physical
21145461
RL7A_HUMANRPL7Aphysical
21145461
RLA2_HUMANRPLP2physical
21145461
RS2_HUMANRPS2physical
21145461
SRSF3_HUMANSRSF3physical
21145461
ADT2_HUMANSLC25A5physical
21145461
ADT3_HUMANSLC25A6physical
21145461
SSBP_HUMANSSBP1physical
21145461
RBP56_HUMANTAF15physical
21145461
TBB5_HUMANTUBBphysical
21145461
BAG4_HUMANBAG4physical
21145461
C1QBP_HUMANC1QBPphysical
21145461
DDX21_HUMANDDX21physical
21145461
DDX5_HUMANDDX5physical
21145461
DHX15_HUMANDHX15physical
21145461
DHX9_HUMANDHX9physical
21145461
H2A1B_HUMANHIST1H2AEphysical
21145461
H2A1J_HUMANHIST1H2AJphysical
21145461
H2A1_HUMANHIST1H2AIphysical
21145461
HNRPD_HUMANHNRNPDphysical
21145461
HS90A_HUMANHSP90AA1physical
21145461
HS90B_HUMANHSP90AB1physical
21145461
CH60_HUMANHSPD1physical
21145461
K2C75_HUMANKRT75physical
21145461
NFKB1_HUMANNFKB1physical
21145461
NPM_HUMANNPM1physical
21145461
PABP4_HUMANPABPC4physical
21145461
RL10A_HUMANRPL10Aphysical
21145461
RL11_HUMANRPL11physical
21145461
RL19_HUMANRPL19physical
21145461
RL22_HUMANRPL22physical
21145461
RL23A_HUMANRPL23Aphysical
21145461
RL38_HUMANRPL38physical
21145461
RL4_HUMANRPL4physical
21145461
RLA1_HUMANRPLP1physical
21145461
RS14_HUMANRPS14physical
21145461
RS15A_HUMANRPS15Aphysical
21145461
RS18_HUMANRPS18physical
21145461
RS20_HUMANRPS20physical
21145461
RS3_HUMANRPS3physical
21145461
SDHA_HUMANSDHAphysical
21145461
RU17_HUMANSNRNP70physical
21145461
SMD3_HUMANSNRPD3physical
21145461
RUXE_HUMANSNRPEphysical
21145461
TIA1_HUMANTIA1physical
21145461
TIAR_HUMANTIAL1physical
21145461
NEDD8_HUMANNEDD8physical
22474075
SKP1_HUMANSKP1physical
22474075
DDB1_HUMANDDB1physical
22474075
RBX1_HUMANRBX1physical
22474075
CASA1_HUMANCSN1S1physical
22474075
CSN6_HUMANCOPS6physical
22474075
CSN5_HUMANCOPS5physical
22474075
CAND1_HUMANCAND1physical
22474075
FBXW5_HUMANFBXW5physical
22910413
LRWD1_HUMANLRWD1physical
22935713
DDB1_HUMANDDB1physical
22342275
DDB1_HUMANDDB1physical
16260596
DDB2_HUMANDDB2physical
16260596
DDB1_HUMANDDB1physical
22952844
GRK5_HUMANGRK5physical
22952844
LTP_EBVB9BPLF1physical
20190741
SENP8_HUMANSENP8physical
20190741
RFWD2_HUMANRFWD2physical
19295130
CSN2_HUMANCOPS2physical
19295130
CSN3_HUMANCOPS3physical
19295130
CSN4_HUMANCOPS4physical
19295130
CSN5_HUMANCOPS5physical
19295130
CSN6_HUMANCOPS6physical
19295130
CSN7A_HUMANCOPS7Aphysical
19295130
CSN7B_HUMANCOPS7Bphysical
19295130
CSN8_HUMANCOPS8physical
19295130
UBC_HUMANUBCphysical
19295130
NEDD8_HUMANNEDD8physical
19295130
RBX1_HUMANRBX1physical
19295130
DDB1_HUMANDDB1physical
19295130
DDB2_HUMANDDB2physical
19295130
DCAF6_HUMANDCAF6physical
19295130
DCAF1_HUMANVPRBPphysical
19295130
AMRA1_HUMANAMBRA1physical
19295130
DCA11_HUMANDCAF11physical
19295130
DCAF8_HUMANDCAF8physical
19295130
PWP1_HUMANPWP1physical
19295130
PHIP_HUMANPHIPphysical
19295130
DDA1_HUMANDDA1physical
19295130
DCA15_HUMANDCAF15physical
19295130
DCA16_HUMANDCAF16physical
19295130
CAND1_HUMANCAND1physical
19295130
DDB1_HUMANDDB1physical
22939629
SGT1_HUMANSUGT1physical
22939629
CUL4B_HUMANCUL4Bphysical
23555860
SF3B3_HUMANSF3B3physical
23951410
DICER_HUMANDICER1physical
23849790
RHG07_HUMANDLC1physical
24082123
ICAL_HUMANCASTphysical
22863883
ANM5_HUMANPRMT5physical
22863883
RBX1_HUMANRBX1physical
22863883
CSN2_HUMANCOPS2physical
25349427
CSN5_HUMANCOPS5physical
25349427
DDB1_HUMANDDB1physical
25349427
RBX1_HUMANRBX1physical
17452440
LTP_EBVB9BPLF1physical
22474075
LTP_HHV8PORF64physical
22474075
TERA_HUMANVCPphysical
22466964
CLCN1_HUMANCLCN1physical
26021757
TBG1_HUMANTUBG1physical
25542213
AMRA1_HUMANAMBRA1physical
25499913
DDB1_HUMANDDB1physical
26344197
CENPA_HUMANCENPAphysical
25727006
CRBN_HUMANCRBNphysical
26231201
DDB1_HUMANDDB1physical
26231201
GBB2_HUMANGNB2physical
25982117
DDB1_HUMANDDB1physical
25982117
GBB1_HUMANGNB1physical
25982117
GBB3_HUMANGNB3physical
25982117
GBB4_HUMANGNB4physical
25982117
GNB5_HUMANGNB5physical
25982117
DDB1_HUMANDDB1physical
25795299
RBBP7_HUMANRBBP7physical
25795299
DDB1_HUMANDDB1physical
26613412
CDN1A_HUMANCDKN1Aphysical
26613412
CDN1B_HUMANCDKN1Bphysical
26613412
UBC_HUMANUBCphysical
27001857
CUL4A_HUMANCUL4Aphysical
17254749
CUL4A_HUMANCUL4Aphysical
16751180
DDB1_HUMANDDB1physical
27203177
CAND1_HUMANCAND1physical
27203177
UVRAG_HUMANUVRAGphysical
27203177
CSN2_HUMANCOPS2physical
26976604
CSN5_HUMANCOPS5physical
26976604
DDB1_HUMANDDB1physical
26976604
RBX1_HUMANRBX1physical
26976604
CSN1_HUMANGPS1physical
26976604
RBX1_HUMANRBX1physical
26990986
SLBP_HUMANSLBPphysical
27254819
FKBP8_HUMANFKBP8physical
27580824
CRBN_HUMANCRBNphysical
27294876
IKZF3_HUMANIKZF3physical
27294876
DDB1_HUMANDDB1physical
27294876
LATS1_HUMANLATS1physical
28420424
DDB1_HUMANDDB1physical
28886238

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUL4A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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-10, AND MASSSPECTROMETRY.
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.
"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 TYR-227, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22, UBIQUITINATION[LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.

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