DCA16_HUMAN - dbPTM
DCA16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCA16_HUMAN
UniProt AC Q9NXF7
Protein Name DDB1- and CUL4-associated factor 16
Gene Name DCAF16
Organism Homo sapiens (Human).
Sequence Length 216
Subcellular Localization
Protein Description May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKCLLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLASCGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCCCGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL
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
61AcetylationWQVKCLLKYSTTWKP
HHHHHHHHCCCCCCC
24.9819608861
79UbiquitinationNSWLYHAKLLDPSTP
CCEEEEEECCCCCCC
35.95-
79UbiquitinationNSWLYHAKLLDPSTP
CCEEEEEECCCCCCC
35.9523000965
85PhosphorylationAKLLDPSTPVHILRE
EECCCCCCCHHHHHH
34.42-
129PhosphorylationPPFQKPLTSPSRLSR
CCCCCCCCCHHHHCC
47.3127067055
130PhosphorylationPFQKPLTSPSRLSRD
CCCCCCCCHHHHCCC
28.6727067055
135PhosphorylationLTSPSRLSRDHATLN
CCCHHHHCCCCHHHH
34.2526657352
150UbiquitinationGALQFATKQLSRTLS
HHHHHHHHHHHHHHH
45.9021890473
150UbiquitinationGALQFATKQLSRTLS
HHHHHHHHHHHHHHH
45.9022817900
165PhosphorylationRATPIPEYLKQIPNS
HCCCCHHHHHHCCCC
17.5327642862
167UbiquitinationTPIPEYLKQIPNSCV
CCCHHHHHHCCCCCH
45.3322505724
187UbiquitinationGWLTKTVKETTRTEP
HHHHHCCCCCCCCCC
55.3529967540
192PhosphorylationTVKETTRTEPINTTY
CCCCCCCCCCCCCCE
43.9824043423
197PhosphorylationTRTEPINTTYSYTDF
CCCCCCCCCEEHHHH
28.0324043423
198PhosphorylationRTEPINTTYSYTDFQ
CCCCCCCCEEHHHHH
13.1424043423
199PhosphorylationTEPINTTYSYTDFQK
CCCCCCCEEHHHHHH
9.5327642862
200PhosphorylationEPINTTYSYTDFQKA
CCCCCCEEHHHHHHH
21.3324043423
201PhosphorylationPINTTYSYTDFQKAV
CCCCCEEHHHHHHHH
10.4224043423
202PhosphorylationINTTYSYTDFQKAVN
CCCCEEHHHHHHHHH
25.1324043423
206UbiquitinationYSYTDFQKAVNKLLT
EEHHHHHHHHHHHHH
55.0521906983
210UbiquitinationDFQKAVNKLLTASL-
HHHHHHHHHHHHCC-
37.9722817900

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 DCA16_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCA16_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 DCA16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM1_HUMANPRMT1physical
23455924
ANM6_HUMANPRMT6physical
23455924
DDB1_HUMANDDB1physical
16949367
CUL4A_HUMANCUL4Aphysical
16949367

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 DCA16_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASS SPECTROMETRY.

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