DCA13_HUMAN - dbPTM
DCA13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCA13_HUMAN
UniProt AC Q9NV06
Protein Name DDB1- and CUL4-associated factor 13
Gene Name DCAF13
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Nucleus, nucleolus . In the nucleolus, localizes predominantly in the granular component, but also detected in the fibrillar center and dense fibrillar component.
Protein Description Possible role in ribosomal RNA processing (By similarity). May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex..
Protein Sequence MKVKMLSRNPDNYVRETKLDLQRVPRNYDPALHPFEVPREYIRALNATKLERVFAKPFLASLDGHRDGVNCLAKHPEKLATVLSGACDGEVRIWNLTQRNCIRTIQAHEGFVRGICTRFCGTSFFTVGDDKTVKQWKMDGPGYGDEEEPLHTILGKTVYTGIDHHWKEAVFATCGQQVDIWDEQRTNPICSMTWGFDSISSVKFNPIETFLLGSCASDRNIVLYDMRQATPLKKVILDMRTNTICWNPMEAFIFTAANEDYNLYTFDMRALDTPVMVHMDHVSAVLDVDYSPTGKEFVSASFDKSIRIFPVDKSRSREVYHTKRMQHVICVKWTSDSKYIMCGSDEMNIRLWKANASEKLGVLTSREKAAKDYNQKLKEKFQHYPHIKRIARHRHLPKSIYSQIQEQRIMKEARRRKEVNRIKHSKPGSVPLVSEKKKHVVAVVK
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
4Sumoylation----MKVKMLSRNPD
----CCCCCCCCCCC		28.71-
7Phosphorylation-MKVKMLSRNPDNYV
-CCCCCCCCCCCCHH		26.8924719451
13PhosphorylationLSRNPDNYVRETKLD
CCCCCCCHHHHHCCC		14.3127067055
17PhosphorylationPDNYVRETKLDLQRV
CCCHHHHHCCCHHCC		26.7527067055
18SumoylationDNYVRETKLDLQRVP
CCHHHHHCCCHHCCC		34.94-
18UbiquitinationDNYVRETKLDLQRVP
CCHHHHHCCCHHCCC		34.94-
18AcetylationDNYVRETKLDLQRVP
CCHHHHHCCCHHCCC		34.9425953088
28PhosphorylationLQRVPRNYDPALHPF
HHCCCCCCCCCCCCC		25.2827642862
48PhosphorylationYIRALNATKLERVFA
HHHHHCCHHHHHHHC		34.7822617229
49SumoylationIRALNATKLERVFAK
HHHHCCHHHHHHHCH		46.04-
49 (in isoform 2)Ubiquitination-46.0421890473
49AcetylationIRALNATKLERVFAK
HHHHCCHHHHHHHCH		46.0419608861
49UbiquitinationIRALNATKLERVFAK
HHHHCCHHHHHHHCH		46.04-
56 (in isoform 2)Ubiquitination-25.4921890473
56UbiquitinationKLERVFAKPFLASLD
HHHHHHCHHHHHHCC		25.4921890473
56AcetylationKLERVFAKPFLASLD
HHHHHHCHHHHHHCC		25.4923749302
74UbiquitinationDGVNCLAKHPEKLAT
CCCCHHHCCHHHHHH		46.90-
78UbiquitinationCLAKHPEKLATVLSG
HHHCCHHHHHHHHHC		48.12-
78AcetylationCLAKHPEKLATVLSG
HHHCCHHHHHHHHHC		48.1226051181
131UbiquitinationFFTVGDDKTVKQWKM
EEEECCCCCEEEEEC		61.02-
134UbiquitinationVGDDKTVKQWKMDGP
ECCCCCEEEEECCCC		56.52-
137UbiquitinationDKTVKQWKMDGPGYG
CCCEEEEECCCCCCC		25.31-
170SumoylationDHHWKEAVFATCGQQ
CHHHHHHHHHHCCCE		3.35-
170UbiquitinationDHHWKEAVFATCGQQ
CHHHHHHHHHHCCCE		3.35-
200PhosphorylationTWGFDSISSVKFNPI
ECCCCCCEEEECCCC		32.79-
201AcetylationWGFDSISSVKFNPIE
CCCCCCEEEECCCCC		27.8819608861
201SumoylationWGFDSISSVKFNPIE
CCCCCCEEEECCCCC		27.8819608861
201UbiquitinationWGFDSISSVKFNPIE
CCCCCCEEEECCCCC		27.8819608861
201 (in isoform 1)Ubiquitination-27.8821890473
208UbiquitinationSVKFNPIETFLLGSC
EEECCCCCEEEECCC		34.46-
208AcetylationSVKFNPIETFLLGSC
EEECCCCCEEEECCC		34.46-
208 (in isoform 1)Ubiquitination-34.4621890473
224PhosphorylationSDRNIVLYDMRQATP
CCCCEEEEECCCCCC		9.2222817900
226UbiquitinationRNIVLYDMRQATPLK
CCEEEEECCCCCCCC		1.85-
227MethylationNIVLYDMRQATPLKK
CEEEEECCCCCCCCE		21.78115920045
230UbiquitinationLYDMRQATPLKKVIL
EEECCCCCCCCEEEE		22.33-
234UbiquitinationRQATPLKKVILDMRT
CCCCCCCEEEEECCC		42.04-
283UbiquitinationMVHMDHVSAVLDVDY
EEECCCEEEEEEECC		14.83-
289 (in isoform 1)Ubiquitination-37.5521890473
289UbiquitinationVSAVLDVDYSPTGKE
EEEEEEECCCCCCCC		37.55-
304UbiquitinationFVSASFDKSIRIFPV
EEEEECCCEEEEEEC		45.8521890473
313UbiquitinationIRIFPVDKSRSREVY
EEEEECCCCCCCCEE		48.26-
320PhosphorylationKSRSREVYHTKRMQH
CCCCCCEECCCCCCE		10.06-
332AcetylationMQHVICVKWTSDSKY
CCEEEEEEECCCCCE		40.1026051181
353MethylationEMNIRLWKANASEKL
HHHHEEEECCHHHHH		36.03115978595
353UbiquitinationEMNIRLWKANASEKL
HHHHEEEECCHHHHH		36.03-
359UbiquitinationWKANASEKLGVLTSR
EECCHHHHHCCCCCH		48.3121890473
359SumoylationWKANASEKLGVLTSR
EECCHHHHHCCCCCH		48.31-
376UbiquitinationAAKDYNQKLKEKFQH
HHHHHHHHHHHHHCC		58.87-
379MethylationDYNQKLKEKFQHYPH
HHHHHHHHHHCCCHH		70.33-
386UbiquitinationEKFQHYPHIKRIARH
HHHCCCHHHHHHHHH		30.91-
398UbiquitinationARHRHLPKSIYSQIQ
HHHCCCCHHHHHHHH		56.7121890473
398AcetylationARHRHLPKSIYSQIQ
HHHCCCCHHHHHHHH		56.7126051181
399PhosphorylationRHRHLPKSIYSQIQE
HHCCCCHHHHHHHHH		25.4829978859
401PhosphorylationRHLPKSIYSQIQEQR
CCCCHHHHHHHHHHH		11.1228152594
402PhosphorylationHLPKSIYSQIQEQRI
CCCHHHHHHHHHHHH		21.0928152594
423AcetylationRKEVNRIKHSKPGSV
HHHHHCCCCCCCCCC		38.297364639
434PhosphorylationPGSVPLVSEKKKHVV
CCCCCCCCCCCCEEE		51.9225159151
436AcetylationSVPLVSEKKKHVVAV
CCCCCCCCCCEEEEE		60.667364647
456Ubiquitination------------------
------------------		-
456 (in isoform 1)Ubiquitination-21890473
465Ubiquitination---------------------------
---------------------------		-
505Ubiquitination-------------------------------------------------------------------
-------------------------------------------------------------------		-
505Methylation-------------------------------------------------------------------
-------------------------------------------------------------------		-
511Ubiquitination-------------------------------------------------------------------------
-------------------------------------------------------------------------		-
511 (in isoform 1)Ubiquitination-21890473
511Sumoylation-------------------------------------------------------------------------
-------------------------------------------------------------------------		-
528Ubiquitination------------------------------------------------------------------------------------------
------------------------------------------------------------------------------------------		-
532Ubiquitination----------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------		-
550Ubiquitination----------------------------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------------------------		-
550 (in isoform 1)Ubiquitination-21890473
575Ubiquitination-----------------------------------------------------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------------------------------------------------		-
578Ubiquitination--------------------------------------------------------------------------------------------------------------------------------------------
--------------------------------------------------------------------------------------------------------------------------------------------		-
586Phosphorylation----------------------------------------------------------------------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------------------------------------------------------------------		-
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 DCA13_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCA13_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 DCA13_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBL3_HUMANTBL3physical
26344197
UT14A_HUMANUTP14Aphysical
26344197
WDR36_HUMANWDR36physical
26344197
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 DCA13_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-49, AND MASS SPECTROMETRY.

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