KAP1_HUMAN - dbPTM
KAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAP1_HUMAN
UniProt AC P31321
Protein Name cAMP-dependent protein kinase type I-beta regulatory subunit
Gene Name PRKAR1B
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 MASPPACPSEEDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQILARQKSNSQSDSHDEEVSPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRYNSFISLTV
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
3Phosphorylation-----MASPPACPSE
-----CCCCCCCCCC		30.0729255136
9PhosphorylationASPPACPSEEDESLK
CCCCCCCCCCCCCCC		54.2020044836
14PhosphorylationCPSEEDESLKGCELY
CCCCCCCCCCCCCEE		47.9425159151
21Nitrated tyrosineSLKGCELYVQLHGIQ
CCCCCCEEHHHCCHH		2.38-
21NitrationSLKGCELYVQLHGIQ
CCCCCCEEHHHCCHH		2.3816777052
21NitrationSLKGCELYVQLHGIQ
CCCCCCEEHHHCCHH		2.3816777052
37UbiquitinationVLKDCIVHLCISKPE
HHHHHHHHHHCCCCC		8.6221963094
71PhosphorylationQILARQKSNSQSDSH
HHHHHHHCCCCCCCC		33.1225159151
73PhosphorylationLARQKSNSQSDSHDE
HHHHHCCCCCCCCCC		37.8523401153
75PhosphorylationRQKSNSQSDSHDEEV
HHHCCCCCCCCCCCC		40.6829255136
77PhosphorylationKSNSQSDSHDEEVSP
HCCCCCCCCCCCCCC		37.7829255136
83PhosphorylationDSHDEEVSPTPPNPV
CCCCCCCCCCCCCHH		26.7429255136
85PhosphorylationHDEEVSPTPPNPVVK
CCCCCCCCCCCHHHH		43.8229255136
90UbiquitinationSPTPPNPVVKARRRR
CCCCCCHHHHHHHHC		9.7922817900
92UbiquitinationTPPNPVVKARRRRGG
CCCCHHHHHHHHCCC		36.0927667366
97MethylationVVKARRRRGGVSAEV
HHHHHHHCCCCCEEE		44.39-
100UbiquitinationARRRRGGVSAEVYTE
HHHHCCCCCEEEECH		5.6622817900
109UbiquitinationAEVYTEEDAVSYVRK
EEEECHHHHHHHHHH		46.1421890473
112UbiquitinationYTEEDAVSYVRKVIP
ECHHHHHHHHHHHCC		21.4522817900
114UbiquitinationEEDAVSYVRKVIPKD
HHHHHHHHHHHCCCC		3.5821890473
122UbiquitinationRKVIPKDYKTMTALA
HHHCCCCHHHHHHHH		17.9322817900
131UbiquitinationTMTALAKAISKNVLF
HHHHHHHHHHHCCEE		12.9921890473
187UbiquitinationGEVDVYVNGEWVTNI
CEEEEEECCEEEEEE		25.6122817900
189UbiquitinationVDVYVNGEWVTNISE
EEEEECCEEEEEECC		33.3021890473
194UbiquitinationNGEWVTNISEGGSFG
CCEEEEEECCCCCHH		2.6423000965
197UbiquitinationWVTNISEGGSFGELA
EEEEECCCCCHHHEE		30.1923000965
206UbiquitinationSFGELALIYGTPRAA
CHHHEEEEECCCCCC		2.1921890473
207PhosphorylationFGELALIYGTPRAAT
HHHEEEEECCCCCCE		18.79-
209PhosphorylationELALIYGTPRAATVK
HEEEEECCCCCCEEE		7.8216582606
215UbiquitinationGTPRAATVKAKTDLK
CCCCCCEEEECCCCE		4.9424816145
216UbiquitinationTPRAATVKAKTDLKL
CCCCCEEEECCCCEE		39.5523000965
219UbiquitinationAATVKAKTDLKLWGI
CCEEEECCCCEECCC		51.9623000965
222UbiquitinationVKAKTDLKLWGIDRD
EEECCCCEECCCCHH		45.0333845483
237UbiquitinationSYRRILMGSTLRKRK
HHHHHHCCHHHHHHH		17.6524816145
238PhosphorylationYRRILMGSTLRKRKM
HHHHHCCHHHHHHHH		15.4230108239
239PhosphorylationRRILMGSTLRKRKMY
HHHHCCHHHHHHHHH		25.5023403867
242UbiquitinationLMGSTLRKRKMYEEF
HCCHHHHHHHHHHHH		60.5322817900
244UbiquitinationGSTLRKRKMYEEFLS
CHHHHHHHHHHHHHH		49.2021906983
246PhosphorylationTLRKRKMYEEFLSKV
HHHHHHHHHHHHHHH		18.49-
251PhosphorylationKMYEEFLSKVSILES
HHHHHHHHHHHHHHH		36.0125850435
252UbiquitinationMYEEFLSKVSILESL
HHHHHHHHHHHHHHH		41.9922817900
254PhosphorylationEEFLSKVSILESLEK
HHHHHHHHHHHHHHH		25.7820068231
258PhosphorylationSKVSILESLEKWERL
HHHHHHHHHHHHHCC		38.0820068231
261UbiquitinationSILESLEKWERLTVA
HHHHHHHHHHCCCHH		60.7021963094
291UbiquitinationVQGEPGDDFYIITEG
ECCCCCCCEEEEEEC		44.1323000965
294UbiquitinationEPGDDFYIITEGTAS
CCCCCEEEEEECCHH		2.9523000965
307PhosphorylationASVLQRRSPNEEYVE
HHHHCCCCCCCCCEE		33.9827642862
312UbiquitinationRRSPNEEYVEVGRLG
CCCCCCCCEEECCCC		8.8424816145
312PhosphorylationRRSPNEEYVEVGRLG
CCCCCCCCEEECCCC		8.8424927040
323PhosphorylationGRLGPSDYFGEIALL
CCCCCCCCHHHHHHH		20.16-
338PhosphorylationLNRPRAATVVARGPL
HCCCCCEEEEECCCE		17.9623312004
342MethylationRAATVVARGPLKCVK
CCEEEEECCCEEEEE		35.34-
346UbiquitinationVVARGPLKCVKLDRP
EEECCCEEEEECCCH		39.8623000965
349UbiquitinationRGPLKCVKLDRPRFE
CCCEEEEECCCHHHH		54.8923000965
367UbiquitinationGPCSEILKRNIQRYN
HHHHHHHHHHHHHHH		49.4024816145
373PhosphorylationLKRNIQRYNSFISLT
HHHHHHHHHCCEEEE		9.9730257219
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 ligasePJA2O43164
PMID:21423175
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAP1_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 KAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKAP1_HUMANAKAP1physical
12634056
KAP1_HUMANPRKAR1Bphysical
12634056
KAP0_HUMANPRKAR1Aphysical
12634056
THG1_HUMANTHG1Lphysical
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 KAP1_HUMAN

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-21, AND MASS SPECTROMETRY.
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.
"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-77 AND 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-3 AND SER-83, AND MASSSPECTROMETRY.

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