FA53C_HUMAN - dbPTM
FA53C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FA53C_HUMAN
UniProt AC Q9NYF3
Protein Name Protein FAM53C {ECO:0000305}
Gene Name FAM53C {ECO:0000312|HGNC:HGNC:1336}
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization
Protein Description
Protein Sequence MITLITEQLQKQTLDELKCTRFSISLPLPDHADISNCGNSFQLVSEGASWRGLPHCSCAEFQDSLNFSYHPSGLSLHLRPPSRGNSPKEQPFSQVLRPEPPDPEKLPVPPAPPSKRHCRSLSVPVDLSRWQPVWRPAPSKLWTPIKHRGSGGGGGPQVPHQSPPKRVSSLRFLQAPSASSQCAPAHRPYSPPFFSLALAQDSSRPCAASPQSGSWESDAESLSPCPPQRRFSLSPSLGPQASRFLPSARSSPASSPELPWRPRGLRNLPRSRSQPCDLDARKTGVKRRHEEDPRRLRPSLDFDKMNQKPYSGGLCLQETAREGSSISPPWFMACSPPPLSASCSPTGGSSQVLSESEEEEEGAVRWGRQALSKRTLCQRDFGDLDLNLIEEN
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-------MITLITEQ
-------CCCHHHHH		4.8222223895
3Phosphorylation-----MITLITEQLQ
-----CCCHHHHHHH		15.7124043423
6Phosphorylation--MITLITEQLQKQT
--CCCHHHHHHHHCC		22.3124043423
13PhosphorylationTEQLQKQTLDELKCT
HHHHHHCCHHHHCCC		43.1222817900
25PhosphorylationKCTRFSISLPLPDHA
CCCEEEEECCCCCCC		23.8028464451
62PhosphorylationHCSCAEFQDSLNFSY
CCCHHHHHCCCCEEE		30.7832645325
88PhosphorylationPSRGNSPKEQPFSQV
CCCCCCCCCCCHHHH		69.6632142685
112PhosphorylationKLPVPPAPPSKRHCR
HCCCCCCCCCCCCCC		39.2032142685
120PhosphorylationPSKRHCRSLSVPVDL
CCCCCCCCEECCCCH		30.3230266825
122PhosphorylationKRHCRSLSVPVDLSR
CCCCCCEECCCCHHH		26.1419664994
128O-linked_GlycosylationLSVPVDLSRWQPVWR
EECCCCHHHCCCCCC		27.3230379171
128PhosphorylationLSVPVDLSRWQPVWR
EECCCCHHHCCCCCC		27.3223403867
143PhosphorylationPAPSKLWTPIKHRGS
CCCCCCCCCCCCCCC		26.1021815630
146UbiquitinationSKLWTPIKHRGSGGG
CCCCCCCCCCCCCCC		28.5829967540
150PhosphorylationTPIKHRGSGGGGGPQ
CCCCCCCCCCCCCCC		33.9329396449
152PhosphorylationIKHRGSGGGGGPQVP
CCCCCCCCCCCCCCC		33.0232142685
162PhosphorylationGPQVPHQSPPKRVSS
CCCCCCCCCCCCCCE		39.8923401153
168PhosphorylationQSPPKRVSSLRFLQA
CCCCCCCCEEEECCC		27.9124719451
169PhosphorylationSPPKRVSSLRFLQAP
CCCCCCCEEEECCCC		22.2524719451
189PhosphorylationCAPAHRPYSPPFFSL
CCCCCCCCCCCCHHH		33.4926657352
190PhosphorylationAPAHRPYSPPFFSLA
CCCCCCCCCCCHHHH		28.87-
222PhosphorylationWESDAESLSPCPPQR
CCCCHHHCCCCCCCC		5.0832142685
224PhosphorylationSDAESLSPCPPQRRF
CCHHHCCCCCCCCCC		39.6732142685
232PhosphorylationCPPQRRFSLSPSLGP
CCCCCCCCCCCCCCH		26.5722167270
234PhosphorylationPQRRFSLSPSLGPQA
CCCCCCCCCCCCHHH		15.9619664994
236PhosphorylationRRFSLSPSLGPQASR
CCCCCCCCCCHHHHH		42.4522167270
242PhosphorylationPSLGPQASRFLPSAR
CCCCHHHHHCCCCCC		20.5122167270
244PhosphorylationLGPQASRFLPSARSS
CCHHHHHCCCCCCCC		12.4733259812
247PhosphorylationQASRFLPSARSSPAS
HHHHCCCCCCCCCCC		38.1623403867
250PhosphorylationRFLPSARSSPASSPE
HCCCCCCCCCCCCCC		40.1523927012
251PhosphorylationFLPSARSSPASSPEL
CCCCCCCCCCCCCCC		20.9423927012
254PhosphorylationSARSSPASSPELPWR
CCCCCCCCCCCCCCC		50.2223927012
255PhosphorylationARSSPASSPELPWRP
CCCCCCCCCCCCCCC		25.2123927012
263PhosphorylationPELPWRPRGLRNLPR
CCCCCCCCCHHCCCC		48.4832645325
271PhosphorylationGLRNLPRSRSQPCDL
CHHCCCCCCCCCCCC		34.0523927012
273PhosphorylationRNLPRSRSQPCDLDA
HCCCCCCCCCCCCCH		39.4625159151
283PhosphorylationCDLDARKTGVKRRHE
CCCCHHHHCCCCHHC		41.4728555341
289PhosphorylationKTGVKRRHEEDPRRL
HHCCCCHHCCCCCCC		46.9932142685
299PhosphorylationDPRRLRPSLDFDKMN
CCCCCCCCCCHHHCC		33.8523401153
310PhosphorylationDKMNQKPYSGGLCLQ
HHCCCCCCCCCCCCH		27.3028464451
311PhosphorylationKMNQKPYSGGLCLQE
HCCCCCCCCCCCCHH		34.6125159151
327PhosphorylationAREGSSISPPWFMAC
HCCCCCCCCCCEEEE		27.1926074081
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 FA53C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FA53C_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 FA53C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLK1_HUMANPLK1physical
26186194
DYR1B_HUMANDYRK1Bphysical
26186194
DYR1A_HUMANDYRK1Aphysical
26186194
FNTB_HUMANFNTBphysical
26186194
TRAF3_HUMANTRAF3physical
26186194
DYR1B_HUMANDYRK1Bphysical
28514442
DYR1A_HUMANDYRK1Aphysical
28514442
FNTB_HUMANFNTBphysical
28514442
PLK1_HUMANPLK1physical
28514442
1433Z_HUMANYWHAZphysical
28514442
1433G_HUMANYWHAGphysical
28514442
LRFN1_HUMANLRFN1physical
27173435
SRS12_HUMANSRSF12physical
27173435
UBP21_HUMANUSP21physical
27173435
F110A_HUMANFAM110Aphysical
27173435
F110B_HUMANFAM110Bphysical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
LIMA1_HUMANLIMA1physical
27173435
DCLK1_HUMANDCLK1physical
27173435
TBC25_HUMANTBC1D25physical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
SRGP2_HUMANSRGAP2physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
KCTD3_HUMANKCTD3physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
NADK_HUMANNADKphysical
27173435
AFAD_HUMANMLLT4physical
27173435
SH3B4_HUMANSH3BP4physical
27173435
MELK_HUMANMELKphysical
27173435
DEP1B_HUMANDEPDC1Bphysical
27173435
NGAP_HUMANRASAL2physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
KIF1C_HUMANKIF1Cphysical
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 FA53C_HUMAN

loading...

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-122 AND SER-234, ANDMASS SPECTROMETRY.
"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-232 AND SER-234, ANDMASS SPECTROMETRY.
"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-122; SER-232; SER-234;SER-251; SER-254 AND SER-255, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND THR-13, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory