KAPCB_HUMAN - dbPTM
KAPCB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAPCB_HUMAN
UniProt AC P22694
Protein Name cAMP-dependent protein kinase catalytic subunit beta
Gene Name PRKACB
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Cytoplasm . Cell membrane . Membrane
Lipid-anchor . Nucleus. Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm..
Protein Description Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. [PubMed: 12420224]
Protein Sequence MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPTQNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCAKEFGEF
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
2Myristoylation------MGNAATAKK
------CCCCCCCCC		32.2725255805
3Deamidated asparagine-----MGNAATAKKG
-----CCCCCCCCCC		25.71-
3Deamidation-----MGNAATAKKG
-----CCCCCCCCCC		25.71-
4 (in isoform 2)Phosphorylation-10.6426552605
4 (in isoform 4)Ubiquitination-10.64-
4 (in isoform 9)Phosphorylation-10.6424719451
6Phosphorylation--MGNAATAKKGSEV
--CCCCCCCCCCCCC		36.28-
6 (in isoform 10)Phosphorylation-36.2829083192
6 (in isoform 5)Phosphorylation-36.2829083192
7 (in isoform 10)Phosphorylation-13.5629083192
7 (in isoform 5)Phosphorylation-13.5629083192
7 (in isoform 7)Phosphorylation-13.5629083192
8 (in isoform 7)Phosphorylation-54.0029083192
10 (in isoform 10)Phosphorylation-28.4729083192
10 (in isoform 5)Phosphorylation-28.4729083192
11PhosphorylationAATAKKGSEVESVKE
CCCCCCCCCCHHHHH		47.5523312004
11 (in isoform 4)Ubiquitination-47.5521890473
11 (in isoform 7)Phosphorylation-47.5529083192
12 (in isoform 2)Phosphorylation-60.0026552605
12 (in isoform 3)Ubiquitination-60.0021906983
13 (in isoform 10)Phosphorylation-7.7129083192
13 (in isoform 2)Phosphorylation-7.7126552605
13 (in isoform 5)Phosphorylation-7.7129083192
14 (in isoform 10)Phosphorylation-45.8429083192
14 (in isoform 5)Phosphorylation-45.8429083192
14 (in isoform 7)Phosphorylation-45.8422210691
15PhosphorylationKKGSEVESVKEFLAK
CCCCCCHHHHHHHHH		43.6023312004
15 (in isoform 10)Phosphorylation-43.6029083192
15 (in isoform 2)Phosphorylation-43.6026552605
15 (in isoform 5)Phosphorylation-43.6029083192
15 (in isoform 7)Phosphorylation-43.6022210691
16 (in isoform 2)Phosphorylation-4.3326552605
16 (in isoform 7)Phosphorylation-4.3329083192
17UbiquitinationGSEVESVKEFLAKAK
CCCCHHHHHHHHHHH		52.61-
17 (in isoform 2)Phosphorylation-52.6126552605
17 (in isoform 4)Ubiquitination-52.6121890473
18 (in isoform 10)Phosphorylation-43.6829083192
18 (in isoform 3)Ubiquitination-43.6821906983
18 (in isoform 5)Phosphorylation-43.6829083192
19 (in isoform 7)Phosphorylation-7.1422210691
21 (in isoform 9)Phosphorylation-18.3224719451
24UbiquitinationKEFLAKAKEDFLKKW
HHHHHHHHHHHHHHC		58.05-
24 (in isoform 1)Ubiquitination-58.0521906983
24 (in isoform 8)Ubiquitination-58.0521906983
27 (in isoform 2)Phosphorylation-12.9726552605
27 (in isoform 5)Ubiquitination-12.9721906983
28 (in isoform 7)Ubiquitination-9.6121906983
30UbiquitinationAKEDFLKKWENPTQN
HHHHHHHHCCCCCCC		62.9821906983
30 (in isoform 1)Ubiquitination-62.9821906983
30 (in isoform 6)Ubiquitination-62.9821906983
30 (in isoform 8)Ubiquitination-62.9821906983
33 (in isoform 5)Ubiquitination-43.7521906983
34 (in isoform 2)Phosphorylation-24.6827251275
34 (in isoform 7)Ubiquitination-24.6821906983
36 (in isoform 6)Ubiquitination-42.3021906983
47AcetylationGLEDFERKKTLGTGS
CCHHHHHHHCCCCCC		42.8019816749
48UbiquitinationLEDFERKKTLGTGSF
CHHHHHHHCCCCCCC		56.02-
49PhosphorylationEDFERKKTLGTGSFG
HHHHHHHCCCCCCCC		33.1928857561
52PhosphorylationERKKTLGTGSFGRVM
HHHHCCCCCCCCEEE		32.5328857561
54PhosphorylationKKTLGTGSFGRVMLV
HHCCCCCCCCEEEEE		25.1029116813
60 (in isoform 4)Ubiquitination-4.2021890473
61 (in isoform 3)Ubiquitination-3.0921906983
64UbiquitinationRVMLVKHKATEQYYA
EEEEEECCCCCHHHH		51.81-
69PhosphorylationKHKATEQYYAMKILD
ECCCCCHHHHHHHHC		6.2225884760
70PhosphorylationHKATEQYYAMKILDK
CCCCCHHHHHHHHCH		10.4220736484
71 (in isoform 2)Ubiquitination-6.4521906983
71 (in isoform 4)Ubiquitination-6.4521890473
72SulfoxidationATEQYYAMKILDKQK
CCCHHHHHHHHCHHH		1.2830846556
72 (in isoform 3)Ubiquitination-1.2821906983
73UbiquitinationTEQYYAMKILDKQKV
CCHHHHHHHHCHHHC		31.7621906983
73 (in isoform 1)Ubiquitination-31.7621906983
73 (in isoform 8)Ubiquitination-31.7621906983
76 (in isoform 5)Ubiquitination-55.6121906983
77UbiquitinationYAMKILDKQKVVKLK
HHHHHHCHHHCEEHH		48.88-
77 (in isoform 2)Ubiquitination-48.8821906983
77 (in isoform 7)Ubiquitination-48.8821906983
79 (in isoform 6)Ubiquitination-55.5321906983
80 (in isoform 4)Ubiquitination-4.2021890473
81 (in isoform 3)Ubiquitination-8.5021906983
84UbiquitinationKQKVVKLKQIEHTLN
HHHCEEHHHHEHHCC		43.44-
84 (in isoform 1)Ubiquitination-43.4421906983
84 (in isoform 8)Ubiquitination-43.4421906983
87 (in isoform 5)Ubiquitination-28.4621906983
88 (in isoform 7)Ubiquitination-36.9721906983
89PhosphorylationKLKQIEHTLNEKRIL
EHHHHEHHCCHHHHH		20.6325159151
90 (in isoform 6)Ubiquitination-9.3321906983
93UbiquitinationIEHTLNEKRILQAVN
HEHHCCHHHHHHHHC		43.6021906983
93 (in isoform 1)Ubiquitination-43.6021906983
93 (in isoform 8)Ubiquitination-43.6021906983
96 (in isoform 5)Ubiquitination-2.8821906983
97 (in isoform 7)Ubiquitination-40.6721906983
99 (in isoform 6)Ubiquitination-4.9721906983
120 (in isoform 2)Ubiquitination-1.3421906983
131 (in isoform 2)Ubiquitination-21.9421906983
140PhosphorylationLRRIGRFSEPHARFY
HHHHCCCCCHHHHHH		49.1926437602
140 (in isoform 2)Ubiquitination-49.1921906983
157PhosphorylationQIVLTFEYLHSLDLI
HHHHHHHHHHHHHHH		12.9121214269
165PhosphorylationLHSLDLIYRDLKPEN
HHHHHHHCCCCCHHH		12.8421214269
180PhosphorylationLLIDHQGYIQVTDFG
EEECCCCEEEEECCC		5.0021214269
184PhosphorylationHQGYIQVTDFGFAKR
CCCEEEEECCCCEEE		14.8321214269
196PhosphorylationAKRVKGRTWTLCGTP
EEECCCCEEEECCCH		31.3222322096
198PhosphorylationRVKGRTWTLCGTPEY
ECCCCEEEECCCHHH		16.1422322096
202PhosphorylationRTWTLCGTPEYLAPE
CEEEECCCHHHHCCH		16.3822167270
205PhosphorylationTLCGTPEYLAPEIIL
EECCCHHHHCCHHHH		14.9027461979
213PhosphorylationLAPEIILSKGYNKAV
HCCHHHHCCCCHHHH		17.3923403867
214UbiquitinationAPEIILSKGYNKAVD
CCHHHHCCCCHHHHH		63.07-
237AcetylationYEMAAGYPPFFADQP
HHHHCCCCCCCCCCC		20.5019608861
237UbiquitinationYEMAAGYPPFFADQP
HHHHCCCCCCCCCCC		20.5019608861
237 (in isoform 2)Ubiquitination-20.50-
253O-linked_GlycosylationQIYEKIVSGKVRFPS
EEHHHHHCCCCCCCC		36.0526840030
254 (in isoform 4)Ubiquitination-22.9121890473
255AcetylationYEKIVSGKVRFPSHF
HHHHHCCCCCCCCCC		23.8019608861
255UbiquitinationYEKIVSGKVRFPSHF
HHHHHCCCCCCCCCC		23.8019608861
255 (in isoform 3)Ubiquitination-23.8021906983
260PhosphorylationSGKVRFPSHFSSDLK
CCCCCCCCCCCHHHH		34.1626657352
263PhosphorylationVRFPSHFSSDLKDLL
CCCCCCCCHHHHHHH		19.9522673903
264PhosphorylationRFPSHFSSDLKDLLR
CCCCCCCHHHHHHHH		46.1226437602
267AcetylationSHFSSDLKDLLRNLL
CCCCHHHHHHHHHHH		51.8522637175
267UbiquitinationSHFSSDLKDLLRNLL
CCCCHHHHHHHHHHH		51.8519608861
267 (in isoform 1)Ubiquitination-51.8521906983
267 (in isoform 4)Ubiquitination-51.8521890473
268 (in isoform 3)Ubiquitination-59.2321906983
270 (in isoform 5)Ubiquitination-4.9721906983
271AcetylationSDLKDLLRNLLQVDL
HHHHHHHHHHHHHHH		38.7619608861
271UbiquitinationSDLKDLLRNLLQVDL
HHHHHHHHHHHHHHH		38.7619608861
271 (in isoform 7)Ubiquitination-38.7621906983
273AcetylationLKDLLRNLLQVDLTK
HHHHHHHHHHHHHHH		2.6019608861
273UbiquitinationLKDLLRNLLQVDLTK
HHHHHHHHHHHHHHH		2.6019608861
273 (in isoform 4)Ubiquitination-2.6021890473
273 (in isoform 6)Ubiquitination-2.6021906983
274AcetylationKDLLRNLLQVDLTKR
HHHHHHHHHHHHHHH		5.5019608861
274 (in isoform 3)Ubiquitination-5.5021906983
280AcetylationLLQVDLTKRFGNLKN
HHHHHHHHHHCCCCC		53.6930591355
280UbiquitinationLLQVDLTKRFGNLKN
HHHHHHHHHHCCCCC		53.6921906983
280 (in isoform 1)Ubiquitination-53.6921906983
283 (in isoform 5)Ubiquitination-42.4621906983
284 (in isoform 7)Ubiquitination-45.1721906983
286UbiquitinationTKRFGNLKNGVSDIK
HHHHCCCCCCCCCCC		56.512190698
286 (in isoform 1)Ubiquitination-56.5121906983
286 (in isoform 6)Ubiquitination-56.5121906983
289 (in isoform 5)Ubiquitination-6.9421906983
290 (in isoform 7)Ubiquitination-34.7121906983
292 (in isoform 6)Ubiquitination-4.2821906983
293UbiquitinationKNGVSDIKTHKWFAT
CCCCCCCCCCCEEEE		49.95-
310UbiquitinationWIAIYQRKVEAPFIP
EEEEEEHHCCCCCCC		28.97-
314AcetylationYQRKVEAPFIPKFRG
EEHHCCCCCCCCCCC		17.7519608861
314UbiquitinationYQRKVEAPFIPKFRG
EEHHCCCCCCCCCCC		17.7519608861
314 (in isoform 2)Ubiquitination-17.7521906983
318UbiquitinationVEAPFIPKFRGSGDT
CCCCCCCCCCCCCCC		42.76-
322PhosphorylationFIPKFRGSGDTSNFD
CCCCCCCCCCCCCCC		29.2826657352
325PhosphorylationKFRGSGDTSNFDDYE
CCCCCCCCCCCCCCC		29.1530108239
326PhosphorylationFRGSGDTSNFDDYEE
CCCCCCCCCCCCCCH		39.9926657352
327 (in isoform 2)Ubiquitination-46.5921906983
331PhosphorylationDTSNFDDYEEEDIRV
CCCCCCCCCHHHCCH		27.3826657352
333 (in isoform 2)Ubiquitination-55.5321906983
339PhosphorylationEEEDIRVSITEKCAK
CHHHCCHHHHHHHHH		17.5930266825
341PhosphorylationEDIRVSITEKCAKEF
HHCCHHHHHHHHHHH		23.1430266825
343UbiquitinationIRVSITEKCAKEFGE
CCHHHHHHHHHHHCC		30.73-
357 (in isoform 2)Ubiquitination--
365 (in isoform 2)Ubiquitination--
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
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:31189917
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAPCB_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 KAPCB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TNR16_HUMANNGFRphysical
12682012
RYR2_HUMANRYR2physical
10830164
STP1_HUMANTNP1physical
9837753
STP2_HUMANTNP2physical
9837753
RS6_HUMANRPS6physical
21988832
RL27A_HUMANRPL27Aphysical
21988832
KBP_HUMANKIAA1279physical
22863883
VAPB_HUMANVAPBphysical
23455922
HS90A_HUMANHSP90AA1physical
23455922
HS90B_HUMANHSP90AB1physical
23455922
KAP0_HUMANPRKAR1Aphysical
23455922
KAP2_HUMANPRKAR2Aphysical
23455922
KAPCA_HUMANPRKACAphysical
23455922
AKAP5_HUMANAKAP5physical
23455922
KAP1_HUMANPRKAR1Bphysical
23455922
KAP3_HUMANPRKAR2Bphysical
23455922
DCAF7_HUMANDCAF7physical
23455922
DYL1_HUMANDYNLL1physical
23455922
TRAP1_HUMANTRAP1physical
23455922
DYR1A_HUMANDYRK1Aphysical
23455922
MARE1_HUMANMAPRE1physical
23455922
MYOME_HUMANPDE4DIPphysical
23455922
AKAP1_HUMANAKAP1physical
23455922
CK5P2_HUMANCDK5RAP2physical
23455922
AKAP9_HUMANAKAP9physical
23455922
VAPA_HUMANVAPAphysical
23455922
AKA7A_HUMANAKAP7physical
23455922
AKA7G_HUMANAKAP7physical
23455922
AKA11_HUMANAKAP11physical
23455922
APBP2_HUMANAPPBP2physical
25416956
RPE_HUMANRPEphysical
26344197
KAP3_HUMANPRKAR2Bphysical
28514442
KAP0_HUMANPRKAR1Aphysical
28514442
MYOME_HUMANPDE4DIPphysical
28514442
GP161_HUMANGPR161physical
28514442
AKA7A_HUMANAKAP7physical
28514442
AKA7G_HUMANAKAP7physical
28514442
AKAP9_HUMANAKAP9physical
28514442
AKA11_HUMANAKAP11physical
28514442
AKAP5_HUMANAKAP5physical
28514442
KAP1_HUMANPRKAR1Bphysical
28514442
KAPCG_HUMANPRKACGphysical
28514442
AKAP1_HUMANAKAP1physical
28514442
CK5P2_HUMANCDK5RAP2physical
28514442
KAPCA_HUMANPRKACAphysical
28514442
FKBP5_HUMANFKBP5physical
28514442
DYR1A_HUMANDYRK1Aphysical
28514442
KAP2_HUMANPRKAR2Aphysical
28514442
ETFB_HUMANETFBphysical
28514442
MAVS_HUMANMAVSphysical
28934360
TRAF6_HUMANTRAF6physical
28934360
TRAF3_HUMANTRAF3physical
28934360
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 KAPCB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND MASS SPECTROMETRY.

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