FA53B_HUMAN - dbPTM
FA53B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA53B_HUMAN
UniProt AC Q14153
Protein Name Protein FAM53B {ECO:0000305}
Gene Name FAM53B {ECO:0000312|HGNC:HGNC:28968}
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Nucleus .
Protein Description Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) nuclear localization..
Protein Sequence MVMVLSESLSTRGADSIACGTFSRELHTPKKMSQGPTLFSCGIMENDRWRDLDRKCPLQIDQPSTSIWECLPEKDSSLWHREAVTACAVTSLIKDLSISDHNGNPSAPPSKRQCRSLSFSDEMSSCRTSWRPLGSKVWTPVEKRRCYSGGSVQRYSNGFSTMQRSSSFSLPSRANVLSSPCDQAGLHHRFGGQPCQGVPGSAPCGQAGDTWSPDLHPVGGGRLDLQRSLSCSHEQFSFVEYCPPSANSTPASTPELARRSSGLSRSRSQPCVLNDKKVGVKRRRPEEVQEQRPSLDLAKMAQNCQTFSSLSCLSAGTEDCGPQSPFARHVSNTRAWTALLSASGPGGRTPAGTPVPEPLPPSFDDHLACQEDLSCEESDSCALDEDCGRRAEPAAAWRDRGAPGNSLCSLDGELDIEQIEKN
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
6Phosphorylation--MVMVLSESLSTRG
--CEEEECCCCCCCC		17.4628450419
8PhosphorylationMVMVLSESLSTRGAD
CEEEECCCCCCCCCC		25.0128450419
10PhosphorylationMVLSESLSTRGADSI
EEECCCCCCCCCCCE		25.9028450419
11PhosphorylationVLSESLSTRGADSIA
EECCCCCCCCCCCEE		38.1128450419
16PhosphorylationLSTRGADSIACGTFS
CCCCCCCCEEECCCC		16.1430206219
21PhosphorylationADSIACGTFSRELHT
CCCEEECCCCCCCCC		20.5130206219
23PhosphorylationSIACGTFSRELHTPK
CEEECCCCCCCCCCC		25.3630206219
55UbiquitinationRWRDLDRKCPLQIDQ
HHCCCCCCCCCCCCC		39.6129967540
74UbiquitinationIWECLPEKDSSLWHR
HHHHCCCCCCCCHHH		62.0529967540
91PhosphorylationVTACAVTSLIKDLSI
HHHHHHHHHHHHCCC		22.8424719451
97PhosphorylationTSLIKDLSISDHNGN
HHHHHHCCCCCCCCC		30.1328348404
99PhosphorylationLIKDLSISDHNGNPS
HHHHCCCCCCCCCCC		29.4628348404
116PhosphorylationPSKRQCRSLSFSDEM
CCHHHHCCCCCCHHH		35.6723927012
118PhosphorylationKRQCRSLSFSDEMSS
HHHHCCCCCCHHHHH		24.7723927012
120PhosphorylationQCRSLSFSDEMSSCR
HHCCCCCCHHHHHCC		29.3223927012
124PhosphorylationLSFSDEMSSCRTSWR
CCCCHHHHHCCCCCC		25.0023403867
125PhosphorylationSFSDEMSSCRTSWRP
CCCHHHHHCCCCCCC		13.3023403867
128PhosphorylationDEMSSCRTSWRPLGS
HHHHHCCCCCCCCCC		36.6523186163
135PhosphorylationTSWRPLGSKVWTPVE
CCCCCCCCCCCCCCC		31.5523186163
139PhosphorylationPLGSKVWTPVEKRRC
CCCCCCCCCCCEECC		22.0523186163
143UbiquitinationKVWTPVEKRRCYSGG
CCCCCCCEECCCCCC		45.43-
147PhosphorylationPVEKRRCYSGGSVQR
CCCEECCCCCCCCEE		14.4526552605
148PhosphorylationVEKRRCYSGGSVQRY
CCEECCCCCCCCEEE		40.0622115753
151PhosphorylationRRCYSGGSVQRYSNG
ECCCCCCCCEEECCC		20.7128450419
165PhosphorylationGFSTMQRSSSFSLPS
CCCCCCCCCCCCCCC		17.2830278072
166PhosphorylationFSTMQRSSSFSLPSR
CCCCCCCCCCCCCCC		37.2830278072
167PhosphorylationSTMQRSSSFSLPSRA
CCCCCCCCCCCCCCC		21.7925159151
169PhosphorylationMQRSSSFSLPSRANV
CCCCCCCCCCCCCCC		41.1223927012
172PhosphorylationSSSFSLPSRANVLSS
CCCCCCCCCCCCCCC		49.6823403867
178PhosphorylationPSRANVLSSPCDQAG
CCCCCCCCCCCCCCC		28.1423927012
179PhosphorylationSRANVLSSPCDQAGL
CCCCCCCCCCCCCCC		25.9523401153
201PhosphorylationPCQGVPGSAPCGQAG
CCCCCCCCCCCCCCC		23.9826074081
210PhosphorylationPCGQAGDTWSPDLHP
CCCCCCCCCCCCCCC		27.2426074081
212PhosphorylationGQAGDTWSPDLHPVG
CCCCCCCCCCCCCCC		15.6128464451
228PhosphorylationGRLDLQRSLSCSHEQ
CCCCCHHHEECCCCE		16.2128450419
230PhosphorylationLDLQRSLSCSHEQFS
CCCHHHEECCCCEEE		18.1528450419
232PhosphorylationLQRSLSCSHEQFSFV
CHHHEECCCCEEEEE		27.0428450419
237PhosphorylationSCSHEQFSFVEYCPP
ECCCCEEEEEEECCC		28.2528387310
241PhosphorylationEQFSFVEYCPPSANS
CEEEEEEECCCCCCC		12.6427080861
245PhosphorylationFVEYCPPSANSTPAS
EEEECCCCCCCCCCC		25.8130576142
248PhosphorylationYCPPSANSTPASTPE
ECCCCCCCCCCCCHH		35.1728450419
249PhosphorylationCPPSANSTPASTPEL
CCCCCCCCCCCCHHH		23.7627080861
252PhosphorylationSANSTPASTPELARR
CCCCCCCCCHHHHHH		45.7827080861
253PhosphorylationANSTPASTPELARRS
CCCCCCCCHHHHHHC		23.9227080861
261PhosphorylationPELARRSSGLSRSRS
HHHHHHCCCCCCCCC		41.77-
266PhosphorylationRSSGLSRSRSQPCVL
HCCCCCCCCCCCCCC		32.6723401153
268PhosphorylationSGLSRSRSQPCVLND
CCCCCCCCCCCCCCC		39.4623401153
294PhosphorylationEVQEQRPSLDLAKMA
HHHHHCCCCCHHHHH		36.3823312004
308PhosphorylationAQNCQTFSSLSCLSA
HHHCCCHHHHHHHHC		33.4827251275
309PhosphorylationQNCQTFSSLSCLSAG
HHCCCHHHHHHHHCC		21.8027251275
311PhosphorylationCQTFSSLSCLSAGTE
CCCHHHHHHHHCCCC		18.2427251275
314PhosphorylationFSSLSCLSAGTEDCG
HHHHHHHHCCCCCCC		29.0428348404
317PhosphorylationLSCLSAGTEDCGPQS
HHHHHCCCCCCCCCC		28.5024719451
324PhosphorylationTEDCGPQSPFARHVS
CCCCCCCCCCHHHCC		25.7227251275
343PhosphorylationWTALLSASGPGGRTP
HHHHHHCCCCCCCCC		41.9927251275
406PhosphorylationDRGAPGNSLCSLDGE
CCCCCCCCCCCCCCC		36.3528634120
409PhosphorylationAPGNSLCSLDGELDI
CCCCCCCCCCCCCCH		34.4927251275
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 FA53B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA53B_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 FA53B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBY1_HUMANCBY1physical
27173435
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 FA53B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-167, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASSSPECTROMETRY.
"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-167, AND MASSSPECTROMETRY.

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