DCA12_HUMAN - dbPTM
DCA12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCA12_HUMAN
UniProt AC Q5T6F0
Protein Name DDB1- and CUL4-associated factor 12
Gene Name DCAF12
Organism Homo sapiens (Human).
Sequence Length 453
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MARKVVSRKRKAPASPGAGSDAQGPQFGWDHSLHKRKRLPPVKRSLVYYLKNREVRLQNETSYSRVLHGYAAQQLPSLLKEREFHLGTLNKVFASQWLNHRQVVCGTKCNTLFVVDVQTSQITKIPILKDREPGGVTQQGCGIHAIELNPSRTLLATGGDNPNSLAIYRLPTLDPVCVGDDGHKDWIFSIAWISDTMAVSGSRDGSMGLWEVTDDVLTKSDARHNVSRVPVYAHITHKALKDIPKEDTNPDNCKVRALAFNNKNKELGAVSLDGYFHLWKAENTLSKLLSTKLPYCRENVCLAYGSEWSVYAVGSQAHVSFLDPRQPSYNVKSVCSRERGSGIRSVSFYEHIITVGTGQGSLLFYDIRAQRFLEERLSACYGSKPRLAGENLKLTTGKGWLNHDETWRNYFSDIDFFPNAVYTHCYDSSGTKLFVAGGPLPSGLHGNYAGLWS
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
15PhosphorylationRKRKAPASPGAGSDA
CCCCCCCCCCCCCCC
23.8623401153
20PhosphorylationPASPGAGSDAQGPQF
CCCCCCCCCCCCCCC
29.2823927012
32PhosphorylationPQFGWDHSLHKRKRL
CCCCCCCCCCCCCCC
29.6923927012
35UbiquitinationGWDHSLHKRKRLPPV
CCCCCCCCCCCCCCC
65.9829967540
77PhosphorylationYAAQQLPSLLKEREF
HHHHHHHHHHHHCCC
55.7318491316
80UbiquitinationQQLPSLLKEREFHLG
HHHHHHHHHCCCHHH
61.0829967540
107PhosphorylationHRQVVCGTKCNTLFV
CCEEEECCCCCEEEE
27.57-
219UbiquitinationVTDDVLTKSDARHNV
ECCCEECHHHHCCCC
42.022190698
232PhosphorylationNVSRVPVYAHITHKA
CCCCCCEEEEHHHHH
6.0827642862
238UbiquitinationVYAHITHKALKDIPK
EEEEHHHHHHCCCCC
46.9229967540
241UbiquitinationHITHKALKDIPKEDT
EHHHHHHCCCCCCCC
59.48-
254UbiquitinationDTNPDNCKVRALAFN
CCCCCCCEEEEEEEC
40.8029967540
263UbiquitinationRALAFNNKNKELGAV
EEEEECCCCCCCCEE
71.1929967540
265UbiquitinationLAFNNKNKELGAVSL
EEECCCCCCCCEEEE
56.79-
271PhosphorylationNKELGAVSLDGYFHL
CCCCCEEEECCHHHH
21.87-
275PhosphorylationGAVSLDGYFHLWKAE
CEEEECCHHHHHHHH
6.36-
287UbiquitinationKAENTLSKLLSTKLP
HHHHHHHHHHHCCCC
57.4729967540
290PhosphorylationNTLSKLLSTKLPYCR
HHHHHHHHCCCCCCC
33.6524719451
292UbiquitinationLSKLLSTKLPYCREN
HHHHHHCCCCCCCCC
44.05-
292AcetylationLSKLLSTKLPYCREN
HHHHHHCCCCCCCCC
44.0525953088
383PhosphorylationRLSACYGSKPRLAGE
HHHHHHCCCCCCCCC
17.01-
384AcetylationLSACYGSKPRLAGEN
HHHHHCCCCCCCCCC
29.7825953088
384UbiquitinationLSACYGSKPRLAGEN
HHHHHCCCCCCCCCC
29.78-
393UbiquitinationRLAGENLKLTTGKGW
CCCCCCCEECCCCCC
56.2033845483
398UbiquitinationNLKLTTGKGWLNHDE
CCEECCCCCCCCCCH
44.83-

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 DCA12_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCA12_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 DCA12_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
16949367
TBA3C_HUMANTUBA3Cphysical
28514442
MCMBP_HUMANMCMBPphysical
28514442
GOLI4_HUMANGOLIM4physical
28514442
XIAP_HUMANXIAPphysical
28514442
BIRC2_HUMANBIRC2physical
28514442
BIRC6_HUMANBIRC6physical
28514442
YYAP1_HUMANYY1AP1physical
28514442
ZZEF1_HUMANZZEF1physical
28514442
MOV10_HUMANMOV10physical
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 DCA12_HUMAN

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Related Literatures of Post-Translational Modification

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