KAP0_HUMAN - dbPTM
KAP0_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAP0_HUMAN
UniProt AC P10644
Protein Name cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene Name PRKAR1A
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Cell membrane .
Protein Description Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells..
Protein Sequence MESGSTAASEEARSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFERLEKEEAKQIQNLQKAGTRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFSVSFIAGETVIQQGDEGDNFYVIDQGETDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
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
1Sulfoxidation-------MESGSTAA
-------CCCCCCHH		9.2628465586
1Acetylation-------MESGSTAA
-------CCCCCCHH		9.2619413330
3Phosphorylation-----MESGSTAASE
-----CCCCCCHHHH		36.4223186163
5Phosphorylation---MESGSTAASEEA
---CCCCCCHHHHHH		24.9325159151
6Phosphorylation--MESGSTAASEEAR
--CCCCCCHHHHHHH		29.7523186163
9PhosphorylationESGSTAASEEARSLR
CCCCCHHHHHHHHHH		33.2420860994
14PhosphorylationAASEEARSLRECELY
HHHHHHHHHHHHHHH		38.5327251275
24UbiquitinationECELYVQKHNIQALL
HHHHHHHHHCHHHHH		28.6821890473
59UbiquitinationEYFERLEKEEAKQIQ
HHHHHHHHHHHHHHH		66.50-
63UbiquitinationRLEKEEAKQIQNLQK
HHHHHHHHHHHHHHH		51.7321906983
70UbiquitinationKQIQNLQKAGTRTDS
HHHHHHHHHCCCCCC		52.5321890473
73PhosphorylationQNLQKAGTRTDSRED
HHHHHHCCCCCCCCC		34.9425867546
75PhosphorylationLQKAGTRTDSREDEI
HHHHCCCCCCCCCCC		37.8622167270
77PhosphorylationKAGTRTDSREDEISP
HHCCCCCCCCCCCCC		36.6422167270
83PhosphorylationDSREDEISPPPPNPV
CCCCCCCCCCCCCCC		29.3419664994
92UbiquitinationPPPNPVVKGRRRRGA
CCCCCCCCCCCCCCC		47.1121906983
101PhosphorylationRRRRGAISAEVYTEE
CCCCCCCEEEEECHH		20.1721082442
106PhosphorylationAISAEVYTEEDAASY
CCEEEEECHHHHHHH		37.7728674419
112PhosphorylationYTEEDAASYVRKVIP
ECHHHHHHHHHHHCC		26.3629759185
122PhosphorylationRKVIPKDYKTMAALA
HHHCCCCHHHHHHHH		17.93-
123MalonylationKVIPKDYKTMAALAK
HHCCCCHHHHHHHHH		41.7926320211
123AcetylationKVIPKDYKTMAALAK
HHCCCCHHHHHHHHH		41.7925953088
123UbiquitinationKVIPKDYKTMAALAK
HHCCCCHHHHHHHHH		41.7921906983
124O-linked_GlycosylationVIPKDYKTMAALAKA
HCCCCHHHHHHHHHH		13.0530379171
130UbiquitinationKTMAALAKAIEKNVL
HHHHHHHHHHHHCCC		51.23-
130AcetylationKTMAALAKAIEKNVL
HHHHHHHHHHHHCCC		51.237665109
134UbiquitinationALAKAIEKNVLFSHL
HHHHHHHHCCCCCCC		46.3621906983
1342-HydroxyisobutyrylationALAKAIEKNVLFSHL
HHHHHHHHCCCCCCC		46.36-
207PhosphorylationFGELALIYGTPRAAT
HHHEEEEECCCCCEE		18.79-
209PhosphorylationELALIYGTPRAATVK
HEEEEECCCCCEEEE		7.8216582606
222UbiquitinationVKAKTNVKLWGIDRD
EEECCCCEEEECCHH		40.3621906983
236SulfoxidationDSYRRILMGSTLRKR
HHHHHHHCCCHHHHH		3.5621406390
238PhosphorylationYRRILMGSTLRKRKM
HHHHHCCCHHHHHHH		15.4230108239
239PhosphorylationRRILMGSTLRKRKMY
HHHHCCCHHHHHHHH		25.5023403867
244UbiquitinationGSTLRKRKMYEEFLS
CCHHHHHHHHHHHHH		49.2021906983
244UbiquitinationGSTLRKRKMYEEFLS
CCHHHHHHHHHHHHH		49.2021906983
246PhosphorylationTLRKRKMYEEFLSKV
HHHHHHHHHHHHHHH		18.4923828894
251PhosphorylationKMYEEFLSKVSILES
HHHHHHHHHHHHHHC		36.0125850435
252UbiquitinationMYEEFLSKVSILESL
HHHHHHHHHHHHHCC		41.9921890473
254PhosphorylationEEFLSKVSILESLDK
HHHHHHHHHHHCCCH		25.7823828894
258PhosphorylationSKVSILESLDKWERL
HHHHHHHCCCHHCCC		38.12-
261AcetylationSILESLDKWERLTVA
HHHHCCCHHCCCCHH		57.1421339330
261UbiquitinationSILESLDKWERLTVA
HHHHCCCHHCCCCHH		57.1421890473
307PhosphorylationAAVLQRRSENEEFVE
HHHHHCCCCCCCCEE		47.1426437602
323PhosphorylationGRLGPSDYFGEIALL
CCCCCCCCHHHHHHH		20.16-
338PhosphorylationMNRPRAATVVARGPL
HCCCCCEEEEECCCE		17.9623312004
342MethylationRAATVVARGPLKCVK
CCEEEEECCCEEEEE		35.34-
346UbiquitinationVVARGPLKCVKLDRP
EEECCCEEEEECCCH		39.86-
349AcetylationRGPLKCVKLDRPRFE
CCCEEEEECCCHHHH		54.8925953088
349UbiquitinationRGPLKCVKLDRPRFE
CCCEEEEECCCHHHH		54.8921906983
363PhosphorylationERVLGPCSDILKRNI
HHHHCHHHHHHHHHH		30.7124719451
367UbiquitinationGPCSDILKRNIQQYN
CHHHHHHHHHHHHHH		43.67-
367AcetylationGPCSDILKRNIQQYN
CHHHHHHHHHHHHHH		43.6725953088
373PhosphorylationLKRNIQQYNSFVSLS
HHHHHHHHHCCEEEC		9.0825159151
375PhosphorylationRNIQQYNSFVSLSV-
HHHHHHHCCEEECC-		23.3022322096
378PhosphorylationQQYNSFVSLSV----
HHHHCCEEECC----		16.9629888752
380PhosphorylationYNSFVSLSV------
HHCCEEECC------		20.4829888752
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
83SPhosphorylationKinaseCDK16Q00536
PSP
83SPhosphorylationKinaseCDK2P24941
PSP
101SPhosphorylationKinasePRKG1Q13976
GPS
-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 KAP0_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 KAP0_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAP1_HUMANPRKAR1Bphysical
12634056
AKAP1_HUMANAKAP1physical
12634056
AKA10_HUMANAKAP10physical
9326583
SMAKA_HUMANC2orf88physical
16189514
PKHF2_HUMANPLEKHF2physical
16189514
ASC_HUMANPYCARDphysical
16189514
AKA10_HUMANAKAP10physical
16189514
UBC12_HUMANUBE2Mphysical
17353931
KAPCA_HUMANPRKACAphysical
17353931
KAP0_HUMANPRKAR1Aphysical
12634056
BIG2_HUMANARFGEF2physical
12571360
BIG1_HUMANARFGEF1physical
12571360
KAP1_HUMANPRKAR1Bphysical
8407966
PJA2_HUMANPJA2physical
21423175
CBS_HUMANCBSphysical
21900206
NELL2_HUMANNELL2physical
21900206
WDCP_HUMANC2orf44physical
21900206
BAHD1_HUMANBAHD1physical
21900206
ZBED1_HUMANZBED1physical
21900206
PATZ1_HUMANPATZ1physical
20026299
PRP31_HUMANPRPF31physical
22939629
SAFB1_HUMANSAFBphysical
22939629
MEN1_HUMANMEN1physical
22939629
S38A5_HUMANSLC38A5physical
22939629
CCNE1_HUMANCCNE1physical
16582606
CDK2_HUMANCDK2physical
16582606
PP1A_HUMANPPP1CAphysical
16582606
SETD7_HUMANSETD7physical
21988832
SET_HUMANSETphysical
20195357
TAU_HUMANMAPTphysical
19014373
MTOR_HUMANMTORphysical
16963469
KAP1_HUMANPRKAR1Bphysical
26186194
AKA11_HUMANAKAP11physical
26186194
STML2_HUMANSTOML2physical
26186194
KAPCA_HUMANPRKACAphysical
26186194
KAPCG_HUMANPRKACGphysical
26186194
KAPCB_HUMANPRKACBphysical
26186194
AKAP3_HUMANAKAP3physical
26186194
GP161_HUMANGPR161physical
26186194
ANR26_HUMANANKRD26physical
26186194
ZBED1_HUMANZBED1physical
26186194
AKAP3_HUMANAKAP3physical
28514442
GP161_HUMANGPR161physical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
ANR26_HUMANANKRD26physical
28514442
AKA11_HUMANAKAP11physical
28514442
KAPCA_HUMANPRKACAphysical
28514442
STML2_HUMANSTOML2physical
28514442
ZBED1_HUMANZBED1physical
28514442
IQCB1_HUMANIQCB1physical
27173435
1433Z_HUMANYWHAZphysical
16376338
Drug and Disease Associations
Kegg Disease
H00260 Pigmented micronodular adrenocortical disease (PPNAD)
H01102 Pituitary adenomas, including: Multiple endocrine neoplasia type 1 (MEN1); MEN1-like syndrome (MEN4)
OMIM Disease
160980Carney complex 1 (CNC1)
255960Intracardiac myxoma (INTMYX)
610489Primary pigmented nodular adrenocortical disease 1 (PPNAD1)
101800Acrodysostosis 1, with or without hormone resistance (ACRDYS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAP0_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-13, AND ACETYLATION AT MET-1.
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-83, AND MASSSPECTROMETRY.
"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-83, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY.
"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-83, 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-83, AND MASSSPECTROMETRY.
"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-83, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, 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 SER-83, 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-83, 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 SER-83, 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-83, AND MASSSPECTROMETRY.

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