KPBB_HUMAN - dbPTM
KPBB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPBB_HUMAN
UniProt AC Q93100
Protein Name Phosphorylase b kinase regulatory subunit beta
Gene Name PHKB
Organism Homo sapiens (Human).
Sequence Length 1093
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation..
Protein Sequence MAGAAGLTAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDHYYRIVKSTLLLYQSPTTGLFPTKTCGGDQKAKIQDSLYCAAGAWALALAYRRIDDDKGRTHELEHSAIKCMRGILYCYMRQADKVQQFKQDPRPTTCLHSVFNVHTGDELLSYEEYGHLQINAVSLYLLYLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCISYPAFALDDEVLFSQTLDKVVRKLKGKYGFKRFLRDGYRTSLEDPNRCYYKPAEIKLFDGIECEFPIFFLYMMIDGVFRGNPKQVQEYQDLLTPVLHHTTEGYPVVPKYYYVPADFVEYEKNNPGSQKRFPSNCGRDGKLFLWGQALYIIAKLLADELISPKDIDPVQRYVPLKDQRNVSMRFSNQGPLENDLVVHVALIAESQRLQVFLNTYGIQTQTPQQVEPIQIWPQQELVKAYLQLGINEKLGLSGRPDRPIGCLGTSKIYRILGKTVVCYPIIFDLSDFYMSQDVFLLIDDIKNALQFIKQYWKMHGRPLFLVLIREDNIRGSRFNPILDMLAALKKGIIGGVKVHVDRLQTLISGAVVEQLDFLRISDTEELPEFKSFEELEPPKHSKVKRQSSTPSAPELGQQPDVNISEWKDKPTHEILQKLNDCSCLASQAILLGILLKREGPNFITKEGTVSDHIERVYRRAGSQKLWLAVRYGAAFTQKFSSSIAPHITTFLVHGKQVTLGAFGHEEEVISNPLSPRVIQNIIYYKCNTHDEREAVIQQELVIHIGWIISNNPELFSGMLKIRIGWIIHAMEYELQIRGGDKPALDLYQLSPSEVKQLLLDILQPQQNGRCWLNRRQIDGSLNRTPTGFYDRVWQILERTPNGIIVAGKHLPQQPTLSDMTMYEMNFSLLVEDTLGNIDQPQYRQIVVELLMVVSIVLERNPELEFQDKVDLDRLVKEAFNEFQKDQSRLKEIEKQDDMTSFYNTPPLGKRGTCSYLTKAVMNLLLEGEVKPNNDDPCLIS
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
2Acetylation------MAGAAGLTA
------CCCCCCCHH		27.86-
2 (in isoform 4)Acetylation-27.8620068231
2 (in isoform 2)Acetylation-27.8620068231
4 (in isoform 4)Phosphorylation-12.8625159151
4 (in isoform 2)Phosphorylation-12.8625159151
8PhosphorylationMAGAAGLTAEVSWKV
CCCCCCCHHHHHHHH		21.6120068231
10 (in isoform 4)Phosphorylation-31.6725159151
10 (in isoform 2)Phosphorylation-31.6725159151
12PhosphorylationAGLTAEVSWKVLERR
CCCHHHHHHHHHHHH		16.8220068231
12 (in isoform 4)Phosphorylation-16.8223663014
12 (in isoform 2)Phosphorylation-16.8223663014
13 (in isoform 4)Phosphorylation-10.4323663014
13 (in isoform 2)Phosphorylation-10.4323663014
18 (in isoform 4)Phosphorylation-33.1424275569
18 (in isoform 2)Phosphorylation-33.1424275569
20 (in isoform 4)Phosphorylation-29.7125849741
20 (in isoform 2)Phosphorylation-29.7125849741
22 (in isoform 4)Phosphorylation-29.8018691976
22 (in isoform 2)Phosphorylation-29.8018691976
25PhosphorylationRRARTKRSGSVYEPL
HHHCCCCCCCCCCCH		36.6621945579
26UbiquitinationRARTKRSGSVYEPLK
HHCCCCCCCCCCCHH		25.7629967540
27PhosphorylationARTKRSGSVYEPLKS
HCCCCCCCCCCCHHH		23.8323927012
27 (in isoform 4)Phosphorylation-23.8325159151
27 (in isoform 2)Phosphorylation-23.8325159151
29PhosphorylationTKRSGSVYEPLKSIN
CCCCCCCCCCHHHCC		17.3321945579
33UbiquitinationGSVYEPLKSINLPRP
CCCCCCHHHCCCCCC		61.07-
34PhosphorylationSVYEPLKSINLPRPD
CCCCCHHHCCCCCCC		25.1325159151
67UbiquitinationLLLYQSPTTGLFPTK
EEEEECCCCCCCCCC		38.4529967540
74UbiquitinationTTGLFPTKTCGGDQK
CCCCCCCCCCCCCCC		41.8929967540
226UbiquitinationGVWERGSKYNNGSTE
CCCCCCCCCCCCCCE		55.62-
227PhosphorylationVWERGSKYNNGSTEL
CCCCCCCCCCCCCEE		18.6326437602
231PhosphorylationGSKYNNGSTELHSSS
CCCCCCCCCEECCCH		22.3426437602
314PhosphorylationLDDEVLFSQTLDKVV
CCCHHHHHHHHHHHH		20.35-
316PhosphorylationDEVLFSQTLDKVVRK
CHHHHHHHHHHHHHH		35.41-
338PhosphorylationKRFLRDGYRTSLEDP
HHHHHCCCCCCCCCC		18.2730576142
340PhosphorylationFLRDGYRTSLEDPNR
HHHCCCCCCCCCCCC		29.2230576142
341PhosphorylationLRDGYRTSLEDPNRC
HHCCCCCCCCCCCCC		22.2930576142
344UbiquitinationGYRTSLEDPNRCYYK
CCCCCCCCCCCCCCC		51.5829967540
351UbiquitinationDPNRCYYKPAEIKLF
CCCCCCCCCEEEEEC		15.9829967540
388PhosphorylationNPKQVQEYQDLLTPV
CHHHHHHHHHHHHHH		7.1027251275
393PhosphorylationQEYQDLLTPVLHHTT
HHHHHHHHHHHCCCC		20.7427251275
399PhosphorylationLTPVLHHTTEGYPVV
HHHHHCCCCCCCCCC		18.7827542207
400PhosphorylationTPVLHHTTEGYPVVP
HHHHCCCCCCCCCCC		24.0527542207
401UbiquitinationPVLHHTTEGYPVVPK
HHHCCCCCCCCCCCC		58.8629967540
403PhosphorylationLHHTTEGYPVVPKYY
HCCCCCCCCCCCCEE		6.1427542207
408UbiquitinationEGYPVVPKYYYVPAD
CCCCCCCCEEEEEHH		33.9829967540
414UbiquitinationPKYYYVPADFVEYEK
CCEEEEEHHHEEECC		16.9029967540
421UbiquitinationADFVEYEKNNPGSQK
HHHEEECCCCCCCCC		62.2129967540
455UbiquitinationYIIAKLLADELISPK
HHHHHHHHCCCCCCC		20.7629967540
460PhosphorylationLLADELISPKDIDPV
HHHCCCCCCCCCCCC		38.22-
462UbiquitinationADELISPKDIDPVQR
HCCCCCCCCCCCCHH		61.6029967540
474UbiquitinationVQRYVPLKDQRNVSM
CHHHCCCCCCCCEEE		45.83-
684PhosphorylationEELPEFKSFEELEPP
CCCCCCCCHHHCCCC		43.1228192239
693PhosphorylationEELEPPKHSKVKRQS
HHCCCCCCCCCCCCC		38.3332142685
694PhosphorylationELEPPKHSKVKRQSS
HCCCCCCCCCCCCCC		45.3218691976
695PhosphorylationLEPPKHSKVKRQSST
CCCCCCCCCCCCCCC		52.0433259812
700PhosphorylationHSKVKRQSSTPSAPE
CCCCCCCCCCCCCHH		39.9722167270
701PhosphorylationSKVKRQSSTPSAPEL
CCCCCCCCCCCCHHH		35.6822167270
702PhosphorylationKVKRQSSTPSAPELG
CCCCCCCCCCCHHHC		26.8922167270
704PhosphorylationKRQSSTPSAPELGQQ
CCCCCCCCCHHHCCC		57.4522167270
717PhosphorylationQQPDVNISEWKDKPT
CCCCCCHHHHCCCCH		32.0023927012
735PhosphorylationLQKLNDCSCLASQAI
HHHHHHCHHHHHHHH		18.2826503514
739PhosphorylationNDCSCLASQAILLGI
HHCHHHHHHHHHHHH		13.7526503514
751UbiquitinationLGILLKREGPNFITK
HHHHHHCCCCCCCCC		76.9229967540
758UbiquitinationEGPNFITKEGTVSDH
CCCCCCCCCCCHHHH		49.7029967540
944MethylationTPTGFYDRVWQILER
CCCCHHHHHHHHHHH		21.86115487483
1030UbiquitinationDLDRLVKEAFNEFQK
CHHHHHHHHHHHHHH		51.5229967540
1036UbiquitinationKEAFNEFQKDQSRLK
HHHHHHHHHHHHHHH		42.0933845483
1037UbiquitinationEAFNEFQKDQSRLKE
HHHHHHHHHHHHHHH		64.1629967540
1040UbiquitinationNEFQKDQSRLKEIEK
HHHHHHHHHHHHHHH		50.1133845483
1043AcetylationQKDQSRLKEIEKQDD
HHHHHHHHHHHHHCC		56.387265701
1043UbiquitinationQKDQSRLKEIEKQDD
HHHHHHHHHHHHHCC		56.3833845483
1047UbiquitinationSRLKEIEKQDDMTSF
HHHHHHHHHCCCHHH		65.7629901268
1055PhosphorylationQDDMTSFYNTPPLGK
HCCCHHHCCCCCCCC		20.2122817900
1068PhosphorylationGKRGTCSYLTKAVMN
CCCCCHHHHHHHHHH		22.1222817900
1090FarnesylationKPNNDDPCLIS----
CCCCCCCCCCC----		7.29-
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

Oops, there are no upstream regulatory protein records of KPBB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
701SPhosphorylation

-
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 KPBB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CT027_HUMANC20orf27physical
16189514
RAVR1_HUMANRAVER1physical
22939629
COR1B_HUMANCORO1Bphysical
26344197
COR1C_HUMANCORO1Cphysical
26344197
Drug and Disease Associations
Kegg Disease
H00069 Glycogen storage diseases (GSD), including: von Gierke disease (GSD type Ia); Pompe disease (GSD typ
OMIM Disease
261750Glycogen storage disease 9B (GSD9B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPBB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-25; SER-27; SER-700 ANDSER-701, 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 SER-27, 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 TYR-29, AND MASSSPECTROMETRY.

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