BACD2_HUMAN - dbPTM
BACD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BACD2_HUMAN
UniProt AC Q13829
Protein Name BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
Gene Name TNFAIP1
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Cytoplasm. Nucleus. Endosome. Colocalizes with RHOB in endosomes.
Protein Description Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(TNFAIP1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity..
Protein Sequence MSGDTCLCPASGAKPKLSGFKGGGLGNKYVQLNVGGSLYYTTVRALTRHDTMLKAMFSGRMEVLTDKEGWILIDRCGKHFGTILNYLRDDTITLPQNRQEIKELMAEAKYYLIQGLVNMCQSALQDKKDSYQPVCNIPIITSLKEEERLIESSTKPVVKLLYNRSNNKYSYTSNSDDHLLKNIELFDKLSLRFNGRVLFIKDVIGDEICCWSFYGQGRKLAEVCCTSIVYATEKKQTKVEFPEARIYEETLNVLLYETPRVPDNSLLEATSRSRSQASPSEDEETFELRDRVRRIHVKRYSTYDDRQLGHQSTHRD
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
11PhosphorylationDTCLCPASGAKPKLS
CCEEECCCCCCCCCC		25.1525159151
14UbiquitinationLCPASGAKPKLSGFK
EECCCCCCCCCCCCC		46.3333845483
16UbiquitinationPASGAKPKLSGFKGG
CCCCCCCCCCCCCCC		55.3623000965
21UbiquitinationKPKLSGFKGGGLGNK
CCCCCCCCCCCCCCC		61.2421890473
21UbiquitinationKPKLSGFKGGGLGNK
CCCCCCCCCCCCCCC		61.2421890473
21UbiquitinationKPKLSGFKGGGLGNK
CCCCCCCCCCCCCCC		61.2423000965
29PhosphorylationGGGLGNKYVQLNVGG
CCCCCCCEEEEECCC		9.4525072903
37PhosphorylationVQLNVGGSLYYTTVR
EEEECCCEEEHHHHH		13.7925072903
39PhosphorylationLNVGGSLYYTTVRAL
EECCCEEEHHHHHHH		10.6425072903
40PhosphorylationNVGGSLYYTTVRALT
ECCCEEEHHHHHHHH		10.9625072903
41PhosphorylationVGGSLYYTTVRALTR
CCCEEEHHHHHHHHC		12.7825072903
42PhosphorylationGGSLYYTTVRALTRH
CCEEEHHHHHHHHCC		7.5925072903
51UbiquitinationRALTRHDTMLKAMFS
HHHHCCHHHHHHHHH		20.48-
51PhosphorylationRALTRHDTMLKAMFS
HHHHCCHHHHHHHHH		20.48-
58PhosphorylationTMLKAMFSGRMEVLT
HHHHHHHHCCCEEEE		16.65-
64UbiquitinationFSGRMEVLTDKEGWI
HHCCCEEEECCCCEE		3.06-
67UbiquitinationRMEVLTDKEGWILID
CCEEEECCCCEEEEE		53.5521906983
78UbiquitinationILIDRCGKHFGTILN
EEEECCCCCHHHHHH		39.11-
102UbiquitinationPQNRQEIKELMAEAK
CCCHHHHHHHHHHHH		44.0032015554
127UbiquitinationCQSALQDKKDSYQPV
HHHHHHCCCCCCCCC		45.5832015554
130UbiquitinationALQDKKDSYQPVCNI
HHHCCCCCCCCCCCC		34.25-
131UbiquitinationLQDKKDSYQPVCNIP
HHCCCCCCCCCCCCC		27.28-
142PhosphorylationCNIPIITSLKEEERL
CCCCEEECCCHHHHH		27.34-
144UbiquitinationIPIITSLKEEERLIE
CCEEECCCHHHHHHH		63.9532015554
155UbiquitinationRLIESSTKPVVKLLY
HHHHCCCCCHHHHHE		37.4532015554
159UbiquitinationSSTKPVVKLLYNRSN
CCCCCHHHHHEECCC		32.7729967540
162PhosphorylationKPVVKLLYNRSNNKY
CCHHHHHEECCCCCE		20.97-
168UbiquitinationLYNRSNNKYSYTSNS
HEECCCCCEEECCCC		39.5632015554
169PhosphorylationYNRSNNKYSYTSNSD
EECCCCCEEECCCCC		14.7229496907
170PhosphorylationNRSNNKYSYTSNSDD
ECCCCCEEECCCCCC		24.4429496907
181UbiquitinationNSDDHLLKNIELFDK
CCCCCHHHHHHHHHH		63.3429967540
188UbiquitinationKNIELFDKLSLRFNG
HHHHHHHHHHHEECC		32.4221963094
190PhosphorylationIELFDKLSLRFNGRV
HHHHHHHHHEECCEE		24.2024719451
234UbiquitinationSIVYATEKKQTKVEF
HHHHHCCCCCCCCCC		45.9121963094
235UbiquitinationIVYATEKKQTKVEFP
HHHHCCCCCCCCCCC		57.9022817900
237PhosphorylationYATEKKQTKVEFPEA
HHCCCCCCCCCCCCH		46.03-
238UbiquitinationATEKKQTKVEFPEAR
HCCCCCCCCCCCCHH		36.9522817900
250PhosphorylationEARIYEETLNVLLYE
CHHHHHHHHHHHEEC		16.2222210691
256PhosphorylationETLNVLLYETPRVPD
HHHHHHEECCCCCCC		17.37-
265PhosphorylationTPRVPDNSLLEATSR
CCCCCCCCHHHHHHC		41.5328555341
270PhosphorylationDNSLLEATSRSRSQA
CCCHHHHHHCCCCCC		18.4622210691
271PhosphorylationNSLLEATSRSRSQAS
CCHHHHHHCCCCCCC		34.9922210691
273PhosphorylationLLEATSRSRSQASPS
HHHHHHCCCCCCCCC		35.7324732914
275PhosphorylationEATSRSRSQASPSED
HHHHCCCCCCCCCCC		31.2029255136
278PhosphorylationSRSRSQASPSEDEET
HCCCCCCCCCCCHHH		22.7129255136
280PhosphorylationSRSQASPSEDEETFE
CCCCCCCCCCHHHHH		56.0029255136
285PhosphorylationSPSEDEETFELRDRV
CCCCCHHHHHHHHHH		21.9923663014
301PhosphorylationRIHVKRYSTYDDRQL
EEEEEEECCCCCHHH		25.2330576142
302PhosphorylationIHVKRYSTYDDRQLG
EEEEEECCCCCHHHC		23.2627251275
303PhosphorylationHVKRYSTYDDRQLGH
EEEEECCCCCHHHCC		15.2029214152
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
278SPhosphorylationKinaseCSNK2A1P68400
GPS
280SPhosphorylationKinaseCSNK2A1P68400
GPS
280SPhosphorylationKinaseCK2-FAMILY-GPS
280SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
280SPhosphorylation

18669648
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 BACD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BACD3_HUMANKCTD10physical
22810651
RIN3_HUMANRIN3physical
22810651
CUL3_HUMANCUL3physical
22810651
CSK2B_HUMANCSNK2Bphysical
19851886
PCNA_HUMANPCNAphysical
19851886
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
RHOA_HUMANRHOAphysical
19782033
BACD2_HUMANTNFAIP1physical
25416956
CUL3_HUMANCUL3physical
25416956
HAT1_HUMANHAT1physical
25416956
STK16_HUMANSTK16physical
25416956
RPAC1_HUMANPOLR1Cphysical
25416956
EPMIP_HUMANEPM2AIP1physical
25416956
CAN7_HUMANCAPN7physical
25416956
EXOS5_HUMANEXOSC5physical
25416956
CARD9_HUMANCARD9physical
25416956
ARMC7_HUMANARMC7physical
25416956
BACD1_HUMANKCTD13physical
25416956
TBB4A_HUMANTUBB4Aphysical
23912453
HS71L_HUMANHSPA1Lphysical
26186194
FLNC_HUMANFLNCphysical
26186194
BAG3_HUMANBAG3physical
26186194
BACD3_HUMANKCTD10physical
26186194
BACD3_HUMANKCTD10physical
28514442
FLNC_HUMANFLNCphysical
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 BACD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"CK2 phosphorylates TNFAIP1 to affect its subcellular localization andinteraction with PCNA.";
Yang L., Liu N., Hu X., Zhang W., Wang T., Li H., Zhang B., Xiang S.,Zhou J., Zhang J.;
Mol. Biol. Rep. 37:2967-2973(2010).
Cited for: INTERACTION WITH CSNK2B AND PCNA, PHOSPHORYLATION AT SER-280,SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-142; THR-237; SER-265;SER-278 AND SER-280.
"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-278 AND SER-280, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285, AND MASSSPECTROMETRY.

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