KAP2_HUMAN - dbPTM
KAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAP2_HUMAN
UniProt AC P13861
Protein Name cAMP-dependent protein kinase type II-alpha regulatory subunit
Gene Name PRKAR2A
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Cytoplasm . Cell membrane . Colocalizes with PJA2 in the cytoplasm and the cell membrane.
Protein Description Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase..
Protein Sequence MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSRTKSNKDGGNQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSVDLGNLGQ
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------MSHIQIPPG
------CCCCCCCCC		29.3326270265
2Acetylation------MSHIQIPPG
------CCCCCCCCC		29.3322223895
11PhosphorylationIQIPPGLTELLQGYT
CCCCCCHHHHHCCCE		30.4226270265
17PhosphorylationLTELLQGYTVEVLRQ
HHHHHCCCEEEHHHH		8.4726270265
18PhosphorylationTELLQGYTVEVLRQQ
HHHHCCCEEEHHHHC		19.6026270265
48PhosphorylationREARAPASVLPAATP
HHCCCCCCCCCCCCC		24.1129255136
54PhosphorylationASVLPAATPRQSLGH
CCCCCCCCCCHHCCC		22.5530266825
58PhosphorylationPAATPRQSLGHPPPE
CCCCCCHHCCCCCCC		37.2823927012
78PhosphorylationVADAKGDSESEEDED
CCCCCCCCCCCCCCC		52.2529255136
80PhosphorylationDAKGDSESEEDEDLE
CCCCCCCCCCCCCCC		50.6829255136
92PhosphorylationDLEVPVPSRFNRRVS
CCCCCCCCCCCCEEE		50.1423927012
99PhosphorylationSRFNRRVSVCAETYN
CCCCCEEEEEEEECC		15.0720201521
104PhosphorylationRVSVCAETYNPDEEE
EEEEEEEECCCCCCC		15.2922167270
105PhosphorylationVSVCAETYNPDEEEE
EEEEEEECCCCCCCC		19.0629209046
114PhosphorylationPDEEEEDTDPRVIHP
CCCCCCCCCCCCCCC		51.7023927012
122UbiquitinationDPRVIHPKTDEQRCR
CCCCCCCCCHHHHHH		55.21-
134GlutathionylationRCRLQEACKDILLFK
HHHHHHHHHHHHHHC		3.9122555962
135AcetylationCRLQEACKDILLFKN
HHHHHHHHHHHHHCC		55.6526051181
135UbiquitinationCRLQEACKDILLFKN
HHHHHHHHHHHHHCC		55.65-
149PhosphorylationNLDQEQLSQVLDAMF
CCCHHHHHHHHHHHH		20.2425693802
161UbiquitinationAMFERIVKADEHVID
HHHHHHHHCCCCEEC		47.9921890473
161UbiquitinationAMFERIVKADEHVID
HHHHHHHHCCCCEEC		47.9921906983
177PhosphorylationGDDGDNFYVIERGTY
CCCCCCEEEEECCEE		13.53-
183PhosphorylationFYVIERGTYDILVTK
EEEEECCEEEEEEEC		25.0028152594
184PhosphorylationYVIERGTYDILVTKD
EEEECCEEEEEEECC		12.1028152594
190UbiquitinationTYDILVTKDNQTRSV
EEEEEEECCCCCCCE		47.4021906983
190UbiquitinationTYDILVTKDNQTRSV
EEEEEEECCCCCCCE		47.4021890473
190AcetylationTYDILVTKDNQTRSV
EEEEEEECCCCCCCE		47.4026051181
196PhosphorylationTKDNQTRSVGQYDNR
ECCCCCCCEEEECCC		33.7129978859
200PhosphorylationQTRSVGQYDNRGSFG
CCCCEEEECCCCCHH		14.8429978859
205PhosphorylationGQYDNRGSFGELALM
EEECCCCCHHHHHHH		27.1720068231
213PhosphorylationFGELALMYNTPRAAT
HHHHHHHCCCCCEEE		19.4120068231
215PhosphorylationELALMYNTPRAATIV
HHHHHCCCCCEEEEE		9.1821082442
254PhosphorylationKKRKMFESFIESVPL
HHHHHHHHHHHHHHH		21.9128857561
258PhosphorylationMFESFIESVPLLKSL
HHHHHHHHHHHHHHC		24.9928348404
263UbiquitinationIESVPLLKSLEVSER
HHHHHHHHHCCHHHH		61.76-
264PhosphorylationESVPLLKSLEVSERM
HHHHHHHHCCHHHHC		29.7226437602
268PhosphorylationLLKSLEVSERMKIVD
HHHHCCHHHHCCEEE		15.3120860994
272UbiquitinationLEVSERMKIVDVIGE
CCHHHHCCEEEECCC		45.88-
272MalonylationLEVSERMKIVDVIGE
CCHHHHCCEEEECCC		45.8830639696
272AcetylationLEVSERMKIVDVIGE
CCHHHHCCEEEECCC		45.8826051181
280UbiquitinationIVDVIGEKIYKDGER
EEEECCCEEEECCCE		46.2321906983
280UbiquitinationIVDVIGEKIYKDGER
EEEECCCEEEECCCE		46.2321890473
2802-HydroxyisobutyrylationIVDVIGEKIYKDGER
EEEECCCEEEECCCE		46.23-
290PhosphorylationKDGERIITQGEKADS
ECCCEEEECCCCCCE		28.3121406692
290 (in isoform 2)Phosphorylation-28.3121406692
292 (in isoform 2)Phosphorylation-29.7121406692
299PhosphorylationGEKADSFYIIESGEV
CCCCCEEEEEECCEE		12.6322468782
303PhosphorylationDSFYIIESGEVSILI
CEEEEEECCEEEEEE		29.8228787133
307PhosphorylationIIESGEVSILIRSRT
EEECCEEEEEEEECC		13.8422468782
314PhosphorylationSILIRSRTKSNKDGG
EEEEEECCCCCCCCC		39.8229083192
315MethylationILIRSRTKSNKDGGN
EEEEECCCCCCCCCC		51.42116252117
316PhosphorylationLIRSRTKSNKDGGNQ
EEEECCCCCCCCCCC		48.8029083192
318UbiquitinationRSRTKSNKDGGNQEV
EECCCCCCCCCCCEE		65.91-
318MalonylationRSRTKSNKDGGNQEV
EECCCCCCCCCCCEE		65.9126320211
318AcetylationRSRTKSNKDGGNQEV
EECCCCCCCCCCCEE		65.9111793943
323UbiquitinationSNKDGGNQEVEIARC
CCCCCCCCEEEEEEE		60.4321890473
332UbiquitinationVEIARCHKGQYFGEL
EEEEEEECCCEEEEE		51.87-
332AcetylationVEIARCHKGQYFGEL
EEEEEEECCCEEEEE		51.8726051181
343PhosphorylationFGELALVTNKPRAAS
EEEEEEEECCCCCCC		38.07-
345UbiquitinationELALVTNKPRAASAY
EEEEEECCCCCCCCE		26.8921890473
345AcetylationELALVTNKPRAASAY
EEEEEECCCCCCCCE		26.8926051181
350PhosphorylationTNKPRAASAYAVGDV
ECCCCCCCCEECCCE		22.3430206219
352PhosphorylationKPRAASAYAVGDVKC
CCCCCCCEECCCEEE		10.1820068231
379AcetylationGPCMDIMKRNISHYE
HHHHHHHHHHHHHHH		42.5025038526
3792-HydroxyisobutyrylationGPCMDIMKRNISHYE
HHHHHHHHHHHHHHH		42.50-
383PhosphorylationDIMKRNISHYEEQLV
HHHHHHHHHHHHHHH		24.4628634298
385PhosphorylationMKRNISHYEEQLVKM
HHHHHHHHHHHHHHH		17.8628796482
395PhosphorylationQLVKMFGSSVDLGNL
HHHHHHCCCCCCCCC		18.8725159151
396PhosphorylationLVKMFGSSVDLGNLG
HHHHHCCCCCCCCCC		21.7425159151
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
99SPhosphorylationKinasePKA-FAMILY-GPS
99SPhosphorylationKinasePKA-Uniprot
99SPhosphorylationKinasePKA_GROUP-PhosphoELM
215TPhosphorylationKinasePDPK1O15530
Uniprot
-KUbiquitinationE3 ubiquitin ligasePJA2O43164
PMID:21423175
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAP2_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 KAP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKP13_HUMANAKAP13physical
12672969
AKA7A_HUMANAKAP7physical
12672969
AKA7G_HUMANAKAP7physical
12672969
AKAP5_HUMANAKAP5physical
12672969
AKAP6_HUMANAKAP6physical
12672969
AKAP2_HUMANAKAP2physical
12672969
AKA11_HUMANAKAP11physical
12672969
AKAP9_HUMANAKAP9physical
12672969
RAB32_HUMANRAB32physical
12672969
AKA11_HUMANAKAP11physical
12147701
GSK3B_HUMANGSK3Bphysical
12147701
AKAP8_HUMANAKAP8physical
9473338
MTG8_HUMANRUNX1T1physical
11593431
RAB32_HUMANRAB32physical
12186851
PDE4A_HUMANPDE4Aphysical
11296225
AKAP8_HUMANAKAP8physical
10601332
AKP13_HUMANAKAP13physical
1618839
PJA2_HUMANPJA2physical
21423175
KAPCB_HUMANPRKACBphysical
22939629
IMDH2_HUMANIMPDH2physical
22863883
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 KAP2_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-78; SER-80 AND SER-99,AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, 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-78 AND SER-80, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99,AND MASS 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 THR-54; SER-58; SER-78;SER-80 AND SER-99, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78 ANDSER-80, AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99,AND MASS SPECTROMETRY.
"Phosphoproteome analysis of capacitated human sperm. Evidence oftyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation.";
Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F.,Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F.,Visconti P.E.;
J. Biol. Chem. 278:11579-11589(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND MASSSPECTROMETRY.

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