DPOA2_HUMAN - dbPTM
DPOA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOA2_HUMAN
UniProt AC Q14181
Protein Name DNA polymerase alpha subunit B
Gene Name POLA2
Organism Homo sapiens (Human).
Sequence Length 598
Subcellular Localization Nucleus.
Protein Description May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery..
Protein Sequence MSASAQQLAEELQIFGLDCEEALIEKLVELCVQYGQNEEGMVGELIAFCTSTHKVGLTSEILNSFEHEFLSKRLSKARHSTCKDSGHAGARDIVSIQELIEVEEEEEILLNSYTTPSKGSQKRAISTPETPLTKRSVSTRSPHQLLSPSSFSPSATPSQKYNSRSNRGEVVTSFGLAQGVSWSGRGGAGNISLKVLGCPEALTGSYKSMFQKLPDIREVLTCKIEELGSELKEHYKIEAFTPLLAPAQEPVTLLGQIGCDSNGKLNNKSVILEGDREHSSGAQIPVDLSELKEYSLFPGQVVIMEGINTTGRKLVATKLYEGVPLPFYQPTEEDADFEQSMVLVACGPYTTSDSITYDPLLDLIAVINHDRPDVCILFGPFLDAKHEQVENCLLTSPFEDIFKQCLRTIIEGTRSSGSHLVFVPSLRDVHHEPVYPQPPFSYSDLSREDKKQVQFVSEPCSLSINGVIFGLTSTDLLFHLGAEEISSSSGTSDRFSRILKHILTQRSYYPLYPPQEDMAIDYESFYVYAQLPVTPDVLIIPSELRYFVKDVLGCVCVNPGRLTKGQVGGTFARLYLRRPAADGAERQSPCIAVQVVRI
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
2Phosphorylation------MSASAQQLA
------CCHHHHHHH		30.8229759185
15UbiquitinationLAEELQIFGLDCEEA
HHHHHHHHCCCHHHH		5.25-
24UbiquitinationLDCEEALIEKLVELC
CCHHHHHHHHHHHHH		5.90-
56UbiquitinationCTSTHKVGLTSEILN
HHHCCCCCCCHHHHH		28.21-
60UbiquitinationHKVGLTSEILNSFEH
CCCCCCHHHHHHHHH		46.38-
72UbiquitinationFEHEFLSKRLSKARH
HHHHHHHHHHHHHCC		60.5521906983
76UbiquitinationFLSKRLSKARHSTCK
HHHHHHHHHCCCCCC		54.7722817900
83UbiquitinationKARHSTCKDSGHAGA
HHCCCCCCCCCCCCH		55.8329967540
112PhosphorylationEEEILLNSYTTPSKG
HHHHHHHCCCCCCCC		24.6727732954
113PhosphorylationEEILLNSYTTPSKGS
HHHHHHCCCCCCCCC		17.3527732954
114PhosphorylationEILLNSYTTPSKGSQ
HHHHHCCCCCCCCCC		31.8625159151
115PhosphorylationILLNSYTTPSKGSQK
HHHHCCCCCCCCCCC		19.8226074081
117PhosphorylationLNSYTTPSKGSQKRA
HHCCCCCCCCCCCCC		47.7826074081
118UbiquitinationNSYTTPSKGSQKRAI
HCCCCCCCCCCCCCC		64.8829967540
120PhosphorylationYTTPSKGSQKRAIST
CCCCCCCCCCCCCCC		35.9426074081
126PhosphorylationGSQKRAISTPETPLT
CCCCCCCCCCCCCCC		36.6029255136
127PhosphorylationSQKRAISTPETPLTK
CCCCCCCCCCCCCCC		21.0219664994
130PhosphorylationRAISTPETPLTKRSV
CCCCCCCCCCCCCCC		25.4629255136
133PhosphorylationSTPETPLTKRSVSTR
CCCCCCCCCCCCCCC		26.1430266825
134AcetylationTPETPLTKRSVSTRS
CCCCCCCCCCCCCCC		50.8125953088
134UbiquitinationTPETPLTKRSVSTRS
CCCCCCCCCCCCCCC		50.8127667366
136PhosphorylationETPLTKRSVSTRSPH
CCCCCCCCCCCCCCC		23.2125159151
138PhosphorylationPLTKRSVSTRSPHQL
CCCCCCCCCCCCCCC		21.2523927012
139PhosphorylationLTKRSVSTRSPHQLL
CCCCCCCCCCCCCCC		32.7723927012
141PhosphorylationKRSVSTRSPHQLLSP
CCCCCCCCCCCCCCC		27.1622167270
147PhosphorylationRSPHQLLSPSSFSPS
CCCCCCCCCCCCCCC		31.1823927012
149PhosphorylationPHQLLSPSSFSPSAT
CCCCCCCCCCCCCCC		40.4125159151
150PhosphorylationHQLLSPSSFSPSATP
CCCCCCCCCCCCCCC		32.8830266825
152PhosphorylationLLSPSSFSPSATPSQ
CCCCCCCCCCCCCCC		21.6423927012
154PhosphorylationSPSSFSPSATPSQKY
CCCCCCCCCCCCCCC		43.5123927012
156PhosphorylationSSFSPSATPSQKYNS
CCCCCCCCCCCCCCC		28.0125159151
158PhosphorylationFSPSATPSQKYNSRS
CCCCCCCCCCCCCCC		34.6423927012
160UbiquitinationPSATPSQKYNSRSNR
CCCCCCCCCCCCCCC		51.2221906983
160AcetylationPSATPSQKYNSRSNR
CCCCCCCCCCCCCCC		51.2223954790
161PhosphorylationSATPSQKYNSRSNRG
CCCCCCCCCCCCCCC		15.6723312004
163PhosphorylationTPSQKYNSRSNRGEV
CCCCCCCCCCCCCCE		33.7123312004
165PhosphorylationSQKYNSRSNRGEVVT
CCCCCCCCCCCCEEE		30.6025278378
172PhosphorylationSNRGEVVTSFGLAQG
CCCCCEEEEEEEEEC		24.4225278378
173PhosphorylationNRGEVVTSFGLAQGV
CCCCEEEEEEEEECC		13.0025278378
181PhosphorylationFGLAQGVSWSGRGGA
EEEEECCCCCCCCCC		23.5025278378
183PhosphorylationLAQGVSWSGRGGAGN
EEECCCCCCCCCCCC		15.8825278378
192PhosphorylationRGGAGNISLKVLGCP
CCCCCCEEEEEECCH		26.5720044836
194UbiquitinationGAGNISLKVLGCPEA
CCCCEEEEEECCHHH		28.7322505724
195UbiquitinationAGNISLKVLGCPEAL
CCCEEEEEECCHHHH		7.24-
198S-nitrosocysteineISLKVLGCPEALTGS
EEEEEECCHHHHCCH		2.11-
198S-nitrosylationISLKVLGCPEALTGS
EEEEEECCHHHHCCH		2.1119483679
207UbiquitinationEALTGSYKSMFQKLP
HHHCCHHHHHHHHCC		36.8222817900
212UbiquitinationSYKSMFQKLPDIREV
HHHHHHHHCCCHHHH		51.2022817900
223UbiquitinationIREVLTCKIEELGSE
HHHHHHHCHHHHHHH		48.1732015554
229PhosphorylationCKIEELGSELKEHYK
HCHHHHHHHHHHHHC		52.9920068231
232UbiquitinationEELGSELKEHYKIEA
HHHHHHHHHHHCEEE		38.0932015554
264UbiquitinationIGCDSNGKLNNKSVI
ECCCCCCCCCCEEEE		52.9022817900
268UbiquitinationSNGKLNNKSVILEGD
CCCCCCCEEEEEECC		45.0521906983
269PhosphorylationNGKLNNKSVILEGDR
CCCCCCEEEEEECCC		19.2621815630
292UbiquitinationPVDLSELKEYSLFPG
CCCHHHHHHHCCCCC		51.0229967540
292UbiquitinationPVDLSELKEYSLFPG
CCCHHHHHHHCCCCC		51.0221890473
318SumoylationGRKLVATKLYEGVPL
CCHHHEEECCCCCCC		39.06-
396PhosphorylationVENCLLTSPFEDIFK
HHHHCCCCCHHHHHH		27.7923898821
403UbiquitinationSPFEDIFKQCLRTII
CCHHHHHHHHHHHHH		40.2021963094
418PhosphorylationEGTRSSGSHLVFVPS
HCCCCCCCEEEEECC		18.65-
425PhosphorylationSHLVFVPSLRDVHHE
CEEEEECCCCCCCCC		30.6324719451
500UbiquitinationDRFSRILKHILTQRS
HHHHHHHHHHHHCCC		26.6522817900
549UbiquitinationSELRYFVKDVLGCVC
HHHHHHHHHHCCCEE		32.02-
564UbiquitinationVNPGRLTKGQVGGTF
ECCCCCCCCCCCCCC		52.5221906983
575PhosphorylationGGTFARLYLRRPAAD
CCCCHHHEEECCCCC		7.8118452278
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 DPOA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOA2_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 DPOA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SETB1_HUMANSETDB1physical
16169070
DPOLA_HUMANPOLA1physical
8223465
PARP1_HUMANPARP1physical
9518481
A4_HUMANAPPphysical
21832049
DPOLA_HUMANPOLA1physical
22939629
PRI1_HUMANPRIM1physical
22939629
PRI2_HUMANPRIM2physical
22939629
E41L1_HUMANEPB41L1physical
22863883
HEXI1_HUMANHEXIM1physical
22863883
DPOLA_HUMANPOLA1physical
22863883
POP7_HUMANPOP7physical
22863883
REPI1_HUMANREPIN1physical
22863883
DPOLA_HUMANPOLA1physical
26344197
PRI1_HUMANPRIM1physical
26344197
SCYL1_HUMANSCYL1physical
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
DB00851Dacarbazine
Regulatory Network of DPOA2_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-141 AND SER-152, 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-126; THR-127; THR-130;SER-141; SER-147 AND SER-149, AND MASS SPECTROMETRY.
"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 THR-127; SER-141 ANDSER-152, AND MASS 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 THR-127 AND THR-130, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-127 AND THR-130, ANDMASS SPECTROMETRY.

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