BACD3_HUMAN - dbPTM
BACD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BACD3_HUMAN
UniProt AC Q9H3F6
Protein Name BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3 {ECO:0000303|PubMed:19782033}
Gene Name KCTD10
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Nucleus .
Protein Description Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The BCR(BACURD3) E3 ubiquitin ligase complex mediates the ubiquitination of target proteins, leading to their degradation by the proteasome (By similarity)..
Protein Sequence MEEMSGESVVSSAVPAAATRTTSFKGTSPSSKYVKLNVGGALYYTTMQTLTKQDTMLKAMFSGRMEVLTDSEGWILIDRCGKHFGTILNYLRDGAVPLPESRREIEELLAEAKYYLVQGLVEECQAALQNKDTYEPFCKVPVITSSKEEQKLIATSNKPAVKLLYNRSNNKYSYTSNSDDNMLKNIELFDKLSLRFNGRVLFIKDVIGDEICCWSFYGQGRKIAEVCCTSIVYATEKKQTKVEFPEARIYEETLNILLYEAQDGRGPDNALLEATGGAAGRSHHLDEDEERERIERVRRIHIKRPDDRAHLHQ
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
1Acetylation-------MEEMSGES
-------CCCCCCCC		9.9322814378
5Phosphorylation---MEEMSGESVVSS
---CCCCCCCCHHHC		42.5629083192
8PhosphorylationMEEMSGESVVSSAVP
CCCCCCCCHHHCCCC		31.2025627689
21PhosphorylationVPAAATRTTSFKGTS
CCCCCCCCCCCCCCC		23.5719691289
22PhosphorylationPAAATRTTSFKGTSP
CCCCCCCCCCCCCCC		28.9519691289
23PhosphorylationAAATRTTSFKGTSPS
CCCCCCCCCCCCCCC		25.0926055452
25UbiquitinationATRTTSFKGTSPSSK
CCCCCCCCCCCCCCC		62.1321890473
25 (in isoform 2)Ubiquitination-62.1321890473
27PhosphorylationRTTSFKGTSPSSKYV
CCCCCCCCCCCCCEE		37.7519691289
28PhosphorylationTTSFKGTSPSSKYVK
CCCCCCCCCCCCEEE		31.3019691289
30PhosphorylationSFKGTSPSSKYVKLN
CCCCCCCCCCEEEEE		38.9519691289
31PhosphorylationFKGTSPSSKYVKLNV
CCCCCCCCCEEEEEE		31.2419691289
32 (in isoform 2)Ubiquitination-59.4021890473
32UbiquitinationKGTSPSSKYVKLNVG
CCCCCCCCEEEEEEC		59.4021890473
33 (in isoform 1)Ubiquitination-12.5521890473
40 (in isoform 1)Ubiquitination-14.2321890473
52 (in isoform 2)Ubiquitination-49.6521890473
52UbiquitinationTTMQTLTKQDTMLKA
ECCHHHCCHHHHHHH		49.6521906983
55PhosphorylationQTLTKQDTMLKAMFS
HHHCCHHHHHHHHHH		23.16-
58UbiquitinationTKQDTMLKAMFSGRM
CCHHHHHHHHHHCCC		27.3021890473
60 (in isoform 1)Ubiquitination-2.3421890473
62PhosphorylationTMLKAMFSGRMEVLT
HHHHHHHHCCCEEEE		16.65-
82UbiquitinationILIDRCGKHFGTILN
EEEECCCCCHHHHHH		39.11-
139UbiquitinationDTYEPFCKVPVITSS
CCCCCCCCCCEECCC		50.37-
147UbiquitinationVPVITSSKEEQKLIA
CCEECCCHHHHHHHC		66.1021906983
147 (in isoform 2)Ubiquitination-66.1021890473
151UbiquitinationTSSKEEQKLIATSNK
CCCHHHHHHHCCCCC		45.18-
155 (in isoform 1)Ubiquitination-26.3221890473
158UbiquitinationKLIATSNKPAVKLLY
HHHCCCCCCCHHHEE		33.8421906983
158 (in isoform 2)Ubiquitination-33.8421890473
162 (in isoform 2)Ubiquitination-34.5821890473
162UbiquitinationTSNKPAVKLLYNRSN
CCCCCCHHHEEECCC		34.5821890473
165PhosphorylationKPAVKLLYNRSNNKY
CCCHHHEEECCCCCE		20.97-
166 (in isoform 1)Ubiquitination-40.6521890473
168PhosphorylationVKLLYNRSNNKYSYT
HHHEEECCCCCEEEC		40.9129083192
170 (in isoform 1)Ubiquitination-45.9821890473
171UbiquitinationLYNRSNNKYSYTSNS
EEECCCCCEEECCCC		39.5621890473
172PhosphorylationYNRSNNKYSYTSNSD
EECCCCCEEECCCCC		14.7229083192
173PhosphorylationNRSNNKYSYTSNSDD
ECCCCCEEECCCCCC		24.4429083192
174PhosphorylationRSNNKYSYTSNSDDN
CCCCCEEECCCCCCC		15.8829083192
175PhosphorylationSNNKYSYTSNSDDNM
CCCCEEECCCCCCCC		18.5829083192
176PhosphorylationNNKYSYTSNSDDNML
CCCEEECCCCCCCCH		26.5529083192
179 (in isoform 1)Ubiquitination-56.4021890473
184UbiquitinationNSDDNMLKNIELFDK
CCCCCCHHHHHHHHH		45.142190698
191UbiquitinationKNIELFDKLSLRFNG
HHHHHHHHHHHEECC		32.42-
192 (in isoform 1)Ubiquitination-6.6621890473
193PhosphorylationIELFDKLSLRFNGRV
HHHHHHHHHEECCEE		24.2024719451
240PhosphorylationYATEKKQTKVEFPEA
HHCCCCCCCCCCCCH		46.03-
241UbiquitinationATEKKQTKVEFPEAR
HCCCCCCCCCCCCHH		36.95-
303UbiquitinationRVRRIHIKRPDDRAH
HHHHHEECCCCCCCC		43.65-
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 BACD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BACD3_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 BACD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BACD2_HUMANTNFAIP1physical
22810651
PCNA_HUMANPCNAphysical
19125419
NOTC1_HUMANNOTCH1physical
25401743
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 BACD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-23, AND MASSSPECTROMETRY.

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