DCAF4_HUMAN - dbPTM
DCAF4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCAF4_HUMAN
UniProt AC Q8WV16
Protein Name DDB1- and CUL4-associated factor 4
Gene Name DCAF4
Organism Homo sapiens (Human).
Sequence Length 495
Subcellular Localization
Protein Description May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MNKSRWQSRRRHGRRSHQQNPWFRLRDSEDRSDSRAAQPAHDSGHGDDESPSTSSGTAGTSSVPELPGFYFDPEKKRYFRLLPGHNNCNPLTKESIRQKEMESKRLRLLQEEDRRKKIARMGFNASSMLRKSQLGFLNVTNYCHLAHELRLSCMERKKVQIRSMDPSALASDRFNLILADTNSDRLFTVNDVKVGGSKYGIINLQSLKTPTLKVFMHENLYFTNRKVNSVCWASLNHLDSHILLCLMGLAETPGCATLLPASLFVNSHPGIDRPGMLCSFRIPGAWSCAWSLNIQANNCFSTGLSRRVLLTNVVTGHRQSFGTNSDVLAQQFALMAPLLFNGCRSGEIFAIDLRCGNQGKGWKATRLFHDSAVTSVRILQDEQYLMASDMAGKIKLWDLRTTKCVRQYEGHVNEYAYLPLHVHEEEGILVAVGQDCYTRIWSLHDARLLRTIPSPYPASKADIPSVAFSSRLGGSRGAPGLLMAVGQDLYCYSYS
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
16PhosphorylationRRRHGRRSHQQNPWF
HHHHCCCCCCCCCCC
25.0428555341
108UbiquitinationMESKRLRLLQEEDRR
HHHHHHHHHHHHHHH
7.3821890473
127PhosphorylationRMGFNASSMLRKSQL
HCCCCHHHHHHHHHC
21.3019664995
147UbiquitinationTNYCHLAHELRLSCM
HCHHHHHHHHHHHHH
40.7721890473
163PhosphorylationRKKVQIRSMDPSALA
HCCCEEECCCHHHHH
29.2125404012
167PhosphorylationQIRSMDPSALASDRF
EEECCCHHHHHCCCC
31.4825404012
171PhosphorylationMDPSALASDRFNLIL
CCHHHHHCCCCCEEE
30.1225404012
208 (in isoform 2)Ubiquitination-58.6721890473
208 (in isoform 1)Ubiquitination-58.6721890473
208UbiquitinationIINLQSLKTPTLKVF
EEECHHCCCCCEEEE
58.67-
279PhosphorylationDRPGMLCSFRIPGAW
CCCCEEEEEECCCCE
17.3824719451
360AcetylationLRCGNQGKGWKATRL
EECCCCCCCCEEEEE
52.4025953088
384PhosphorylationRILQDEQYLMASDMA
EEECCHHHHHHCCCC
9.0822817900
388PhosphorylationDEQYLMASDMAGKIK
CHHHHHHCCCCCCEE
17.6022964224
460UbiquitinationPSPYPASKADIPSVA
CCCCCCCCCCCCCHH
52.782190698
460 (in isoform 1)Ubiquitination-52.7821890473
465PhosphorylationASKADIPSVAFSSRL
CCCCCCCCHHCCCCC
26.8126270265
465O-linked_GlycosylationASKADIPSVAFSSRL
CCCCCCCCHHCCCCC
26.8130379171
469PhosphorylationDIPSVAFSSRLGGSR
CCCCHHCCCCCCCCC
12.5724719451
470PhosphorylationIPSVAFSSRLGGSRG
CCCHHCCCCCCCCCC
25.6826270265

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 DCAF4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCAF4_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 DCAF4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOX30_HUMANSOX30physical
21988832
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367
CUL4B_HUMANCUL4Bphysical
16949367
CUL4A_HUMANCUL4Aphysical
28514442
CUL4B_HUMANCUL4Bphysical
28514442
CH60_HUMANHSPD1physical
28514442
TCPG_HUMANCCT3physical
28514442
CSN7B_HUMANCOPS7Bphysical
28514442
CSN1_HUMANGPS1physical
28514442
CSN5_HUMANCOPS5physical
28514442
DDB1_HUMANDDB1physical
28514442
CSN4_HUMANCOPS4physical
28514442
LONM_HUMANLONP1physical
28514442
CLU_HUMANCLUHphysical
28514442
TCPB_HUMANCCT2physical
28514442

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 DCAF4_HUMAN

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Related Literatures of Post-Translational Modification

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