KAP3_HUMAN - dbPTM
KAP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAP3_HUMAN
UniProt AC P31323
Protein Name cAMP-dependent protein kinase type II-beta regulatory subunit
Gene Name PRKAR2B
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Cytoplasm . Cell membrane . Colocalizes with PJA2 in the cytoplasm and at 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 MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFGHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA
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------MSIEIPAGL
------CCCCCCCCH
29.0024043423
10PhosphorylationIEIPAGLTELLQGFT
CCCCCCHHHHHCCCC
24.5424043423
17PhosphorylationTELLQGFTVEVLRHQ
HHHHCCCCEEHHHCC
23.6824043423
69PhosphorylationGAAAGGGTPSKGVNF
CHHCCCCCCCCCCCC
27.8819664994
71PhosphorylationAAGGGTPSKGVNFAE
HCCCCCCCCCCCCCC
41.7130266825
83PhosphorylationFAEEPMQSDSEDGEE
CCCCCCCCCCCCCCC
36.5330266825
85PhosphorylationEEPMQSDSEDGEEEE
CCCCCCCCCCCCCHH
42.7230266825
110PhosphorylationAPVINRFTRRASVCA
HHHHHHHHHHHHHHH
18.9326074081
114PhosphorylationNRFTRRASVCAEAYN
HHHHHHHHHHHHHHC
18.8729255136
120PhosphorylationASVCAEAYNPDEEED
HHHHHHHHCCCCCCC
20.8022617229
131PhosphorylationEEEDDAESRIIHPKT
CCCCCHHHCCCCCCC
30.4223403867
137UbiquitinationESRIIHPKTDDQRNR
HHCCCCCCCHHHHHH
50.88-
149GlutathionylationRNRLQEACKDILLFK
HHHHHHHHHHHHHHC
3.9122555962
150UbiquitinationNRLQEACKDILLFKN
HHHHHHHHHHHHHCC
55.65-
202PhosphorylationDRGTFDIYVKCDGVG
ECCEEEEEEEECCCC
8.8328064214
220PhosphorylationGNYDNRGSFGELALM
CCCCCCCCHHHHHHH
27.1727499020
227SulfoxidationSFGELALMYNTPRAA
CHHHHHHHCCCCCCE
1.7030846556
228PhosphorylationFGELALMYNTPRAAT
HHHHHHHCCCCCCEE
19.4120068231
230PhosphorylationELALMYNTPRAATIT
HHHHHCCCCCCEEEE
9.1821082442
357PhosphorylationFGELALVTNKPRAAS
EEEEEEECCCCCCCH
38.07-
359UbiquitinationELALVTNKPRAASAH
EEEEECCCCCCCHHH
26.8921890473
364PhosphorylationTNKPRAASAHAIGTV
CCCCCCCHHHHHHHH
21.4328348404
372UbiquitinationAHAIGTVKCLAMDVQ
HHHHHHHHHHHCCHH
24.30-
417PhosphorylationNMDIVEPTA------
CCCCCCCCC------
31.34-

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
114SPhosphorylationKinasePRKACAP17612
GPS
114SPhosphorylationKinaseAKT-FAMILY-GPS
114SPhosphorylationKinasePKA-FAMILY-GPS
114SPhosphorylationKinasePKA_GROUP-PhosphoELM
114SPhosphorylationKinasePKB_GROUP-PhosphoELM
-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 KAP3_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 KAP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNAI3_HUMANGNAI3physical
22186894
TAF12_HUMANTAF12physical
25416956
AKA7A_HUMANAKAP7physical
25416956
AKA7G_HUMANAKAP7physical
25416956
AKAP1_HUMANAKAP1physical
26186194
AKA11_HUMANAKAP11physical
26186194
KAP2_HUMANPRKAR2Aphysical
26186194
AKAP9_HUMANAKAP9physical
26186194
AKP13_HUMANAKAP13physical
26186194
MYOME_HUMANPDE4DIPphysical
26186194
CK5P2_HUMANCDK5RAP2physical
26186194
KAPCA_HUMANPRKACAphysical
26186194
KAPCG_HUMANPRKACGphysical
26186194
KAPCB_HUMANPRKACBphysical
26186194
AKAP2_HUMANAKAP2physical
26186194
MTAP2_HUMANMAP2physical
26186194
AKA7A_HUMANAKAP7physical
26186194
AKA7G_HUMANAKAP7physical
26186194
ZG16B_HUMANZG16Bphysical
26186194
AKAP5_HUMANAKAP5physical
26186194
PRKX_HUMANPRKXphysical
26186194
CRBG3_HUMANCRYBG3physical
26186194
KAP1_HUMANPRKAR1Bphysical
26186194
NAA25_HUMANNAA25physical
26186194
VAPB_HUMANVAPBphysical
26186194
KC1D_HUMANCSNK1Dphysical
26496610
DC1I2_HUMANDYNC1I2physical
26496610
PCM1_HUMANPCM1physical
26496610
KAPCB_HUMANPRKACBphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
SURF4_HUMANSURF4physical
26496610
VAV2_HUMANVAV2physical
26496610
OFD1_HUMANOFD1physical
26496610
MYOME_HUMANPDE4DIPphysical
26496610
CE170_HUMANCEP170physical
26496610
SC16A_HUMANSEC16Aphysical
26496610
AKAP9_HUMANAKAP9physical
26496610
CP131_HUMANCEP131physical
26496610
CEP68_HUMANCEP68physical
26496610
HBP1_HUMANHBP1physical
26496610
BABA1_HUMANBABAM1physical
26496610
CSN7A_HUMANCOPS7Aphysical
26496610
CEP72_HUMANCEP72physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610
MIB1_HUMANMIB1physical
26496610
CCD77_HUMANCCDC77physical
26496610
KAPCA_HUMANPRKACAphysical
26496610
KAPCA_HUMANPRKACAphysical
21795691
AKP13_HUMANAKAP13physical
28514442
PRKX_HUMANPRKXphysical
28514442
CRBG3_HUMANCRYBG3physical
28514442
AKAP1_HUMANAKAP1physical
28514442
MYOME_HUMANPDE4DIPphysical
28514442
AKA7A_HUMANAKAP7physical
28514442
AKA7G_HUMANAKAP7physical
28514442
AKAP9_HUMANAKAP9physical
28514442
AKAP5_HUMANAKAP5physical
28514442
AKAP2_HUMANAKAP2physical
28514442
MTAP2_HUMANMAP2physical
28514442
AKA11_HUMANAKAP11physical
28514442
KAPCA_HUMANPRKACAphysical
28514442
KAP2_HUMANPRKAR2Aphysical
28514442
CK5P2_HUMANCDK5RAP2physical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
ZG16B_HUMANZG16Bphysical
28514442
NAA25_HUMANNAA25physical
28514442
KAP0_HUMANPRKAR1Aphysical
28514442

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 KAP3_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-83; SER-85 AND SER-114,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 SER-83 AND SER-85, 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-114, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex.";
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.;
J. Proteome Res. 4:306-315(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.

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