KPB2_HUMAN - dbPTM
KPB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPB2_HUMAN
UniProt AC P46019
Protein Name Phosphorylase b kinase regulatory subunit alpha, liver isoform
Gene Name PHKA2
Organism Homo sapiens (Human).
Sequence Length 1235
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 alpha chain may bind calmodulin..
Protein Sequence MRSRSNSGVRLDGYARLVQQTILCYQNPVTGLLSASHEQKDAWVRDNIYSILAVWGLGMAYRKNADRDEDKAKAYELEQNVVKLMRGLLQCMMRQVAKVEKFKHTQSTKDSLHAKYNTATCGTVVGDDQWGHLQVDATSLFLLFLAQMTASGLRIIFTLDEVAFIQNLVFYIEAAYKVADYGMWERGDKTNQGIPELNASSVGMAKAALEAIDELDLFGAHGGRKSVIHVLPDEVEHCQSILFSMLPRASTSKEIDAGLLSIISFPAFAVEDVNLVNVTKNEIISKLQGRYGCCRFLRDGYKTPREDPNRLHYDPAELKLFENIECEWPVFWTYFIIDGVFSGDAVQVQEYREALEGILIRGKNGIRLVPELYAVPPNKVDEEYKNPHTVDRVPMGKVPHLWGQSLYILSSLLAEGFLAAGEIDPLNRRFSTSVKPDVVVQVTVLAENNHIKDLLRKHGVNVQSIADIHPIQVQPGRILSHIYAKLGRNKNMNLSGRPYRHIGVLGTSKLYVIRNQIFTFTPQFTDQHHFYLALDNEMIVEMLRIELAYLCTCWRMTGRPTLTFPISRTMLTNDGSDIHSAVLSTIRKLEDGYFGGARVKLGNLSEFLTTSFYTYLTFLDPDCDEKLFDNASEGTFSPDSDSDLVGYLEDTCNQESQDELDHYINHLLQSTSLRSYLPPLCKNTEDRHVFSAIHSTRDILSVMAKAKGLEVPFVPMTLPTKVLSAHRKSLNLVDSPQPLLEKVPESDFQWPRDDHGDVDCEKLVEQLKDCSNLQDQADILYILYVIKGPSWDTNLSGQHGVTVQNLLGELYGKAGLNQEWGLIRYISGLLRKKVEVLAEACTDLLSHQKQLTVGLPPEPREKIISAPLPPEELTKLIYEASGQDISIAVLTQEIVVYLAMYVRAQPSLFVEMLRLRIGLIIQVMATELARSLNCSGEEASESLMNLSPFDMKNLLHHILSGKEFGVERSVRPIHSSTSSPTISIHEVGHTGVTKTERSGINRLRSEMKQMTRRFSADEQFFSVGQAASSSAHSSKSARSSTPSSPTGTSSSDSGGHHIGWGERQGQWLRRRRLDGAINRVPVGFYQRVWKILQKCHGLSIDGYVLPSSTTREMTPHEIKFAVHVESVLNRVPQPEYRQLLVEAIMVLTLLSDTEMTSIGGIIHVDQIVQMASQLFLQDQVSIGAMDTLEKDQATGICHFFYDSAPSGAYGTMTYLTRAVASYLQELLPNSGCQMQ
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-----MRSRSNSGVR
-----CCCCCCCCCC		52.5026074081
5Phosphorylation---MRSRSNSGVRLD
---CCCCCCCCCCCC		36.2723927012
7Phosphorylation-MRSRSNSGVRLDGY
-CCCCCCCCCCCCHH		39.6523401153
14PhosphorylationSGVRLDGYARLVQQT
CCCCCCHHHHHHHHH		6.5523403867
49PhosphorylationAWVRDNIYSILAVWG
HHHHHHHHHHHHHHH		8.9123401153
50PhosphorylationWVRDNIYSILAVWGL
HHHHHHHHHHHHHHH		13.8223401153
61PhosphorylationVWGLGMAYRKNADRD
HHHHHHHHHCCCCCC		17.1523401153
286UbiquitinationTKNEIISKLQGRYGC
CHHHHHHHHCCCCCC		34.1329967540
291PhosphorylationISKLQGRYGCCRFLR
HHHHCCCCCCHHHHC		22.7224719451
303PhosphorylationFLRDGYKTPREDPNR
HHCCCCCCCCCCCCC		21.0624719451
313PhosphorylationEDPNRLHYDPAELKL
CCCCCCCCCHHHHHH		28.3727642862
379UbiquitinationLYAVPPNKVDEEYKN
EEECCCCCCCCHHCC		57.7629967540
457UbiquitinationHIKDLLRKHGVNVQS
CHHHHHHHHCCCHHH		44.6829967540
485UbiquitinationILSHIYAKLGRNKNM
HHHHHHHHHCCCCCC		34.2129967540
508PhosphorylationHIGVLGTSKLYVIRN
EEEEECCCEEEEEEC		20.90-
613PhosphorylationEFLTTSFYTYLTFLD
HHHHHHHHHHHHHCC		8.34-
615PhosphorylationLTTSFYTYLTFLDPD
HHHHHHHHHHHCCCC		7.74-
617PhosphorylationTSFYTYLTFLDPDCD
HHHHHHHHHCCCCCC		16.25-
682UbiquitinationSYLPPLCKNTEDRHV
HHCCCCCCCCCCHHH		74.6833845483
691PhosphorylationTEDRHVFSAIHSTRD
CCCHHHHHHHHCHHH		25.8122322096
695PhosphorylationHVFSAIHSTRDILSV
HHHHHHHCHHHHHHH		21.0124275569
696PhosphorylationVFSAIHSTRDILSVM
HHHHHHCHHHHHHHH		20.4228857561
701PhosphorylationHSTRDILSVMAKAKG
HCHHHHHHHHHHHCC		15.3528857561
705UbiquitinationDILSVMAKAKGLEVP
HHHHHHHHHCCCCCC		32.3232015554
707UbiquitinationLSVMAKAKGLEVPFV
HHHHHHHCCCCCCCC		64.4232015554
717PhosphorylationEVPFVPMTLPTKVLS
CCCCCCCCCCHHHHH		24.42-
724PhosphorylationTLPTKVLSAHRKSLN
CCCHHHHHHHHHHHC		25.6424719451
728UbiquitinationKVLSAHRKSLNLVDS
HHHHHHHHHHCCCCC		49.8029967540
729PhosphorylationVLSAHRKSLNLVDSP
HHHHHHHHHCCCCCC		23.5829255136
735PhosphorylationKSLNLVDSPQPLLEK
HHHCCCCCCHHHHHC		20.2530266825
742UbiquitinationSPQPLLEKVPESDFQ
CCHHHHHCCCHHHCC		64.1632015554
762AcetylationHGDVDCEKLVEQLKD
CCCCCHHHHHHHHHH		65.2525038526
762UbiquitinationHGDVDCEKLVEQLKD
CCCCCHHHHHHHHHH		65.2529967540
771PhosphorylationVEQLKDCSNLQDQAD
HHHHHHCCCCCHHHH		51.19-
796PhosphorylationPSWDTNLSGQHGVTV
CCCCCCCCCCCCCCH		38.18-
802PhosphorylationLSGQHGVTVQNLLGE
CCCCCCCCHHHHHHH		22.44-
811PhosphorylationQNLLGELYGKAGLNQ
HHHHHHHHCCCCCCC		16.57-
960PhosphorylationNLLHHILSGKEFGVE
HHHHHHHHCCCCCCC		47.4124719451
962UbiquitinationLHHILSGKEFGVERS
HHHHHHCCCCCCCCC		46.6332015554
969PhosphorylationKEFGVERSVRPIHSS
CCCCCCCCEECCCCC		14.6923927012
975PhosphorylationRSVRPIHSSTSSPTI
CCEECCCCCCCCCEE		35.7123927012
976PhosphorylationSVRPIHSSTSSPTIS
CEECCCCCCCCCEEE		20.3923927012
977PhosphorylationVRPIHSSTSSPTISI
EECCCCCCCCCEEEE		35.9223927012
978PhosphorylationRPIHSSTSSPTISIH
ECCCCCCCCCEEEEE		35.9523927012
979PhosphorylationPIHSSTSSPTISIHE
CCCCCCCCCEEEEEE		26.5923927012
981PhosphorylationHSSTSSPTISIHEVG
CCCCCCCEEEEEECC		29.3323927012
983PhosphorylationSTSSPTISIHEVGHT
CCCCCEEEEEECCCC		21.9923927012
990PhosphorylationSIHEVGHTGVTKTER
EEEECCCCCCCHHHH		27.6730108239
993PhosphorylationEVGHTGVTKTERSGI
ECCCCCCCHHHHHHH		33.3330108239
995PhosphorylationGHTGVTKTERSGINR
CCCCCCHHHHHHHHH		27.5426437602
998PhosphorylationGVTKTERSGINRLRS
CCCHHHHHHHHHHHH		37.4826437602
1011PhosphorylationRSEMKQMTRRFSADE
HHHHHHHHHHCCCCH		19.05-
1015PhosphorylationKQMTRRFSADEQFFS
HHHHHHCCCCHHHHC		32.7622322096
1022PhosphorylationSADEQFFSVGQAASS
CCCHHHHCHHHHHCC		26.9922322096
1028PhosphorylationFSVGQAASSSAHSSK
HCHHHHHCCCCCCCC		28.0423403867
1029PhosphorylationSVGQAASSSAHSSKS
CHHHHHCCCCCCCCC		27.1523403867
1034PhosphorylationASSSAHSSKSARSST
HCCCCCCCCCCCCCC		22.2923403867
1036PhosphorylationSSAHSSKSARSSTPS
CCCCCCCCCCCCCCC		30.7523312004
1039PhosphorylationHSSKSARSSTPSSPT
CCCCCCCCCCCCCCC		37.9823927012
1040PhosphorylationSSKSARSSTPSSPTG
CCCCCCCCCCCCCCC		38.4923927012
1041PhosphorylationSKSARSSTPSSPTGT
CCCCCCCCCCCCCCC		28.5623401153
1043PhosphorylationSARSSTPSSPTGTSS
CCCCCCCCCCCCCCC		49.3823927012
1044PhosphorylationARSSTPSSPTGTSSS
CCCCCCCCCCCCCCC		27.9023401153
1046PhosphorylationSSTPSSPTGTSSSDS
CCCCCCCCCCCCCCC		55.8523927012
1048PhosphorylationTPSSPTGTSSSDSGG
CCCCCCCCCCCCCCC		28.1023927012
1049PhosphorylationPSSPTGTSSSDSGGH
CCCCCCCCCCCCCCC		29.2323927012
1050PhosphorylationSSPTGTSSSDSGGHH
CCCCCCCCCCCCCCC		37.6923927012
1051PhosphorylationSPTGTSSSDSGGHHI
CCCCCCCCCCCCCCC		35.2523927012
1053PhosphorylationTGTSSSDSGGHHIGW
CCCCCCCCCCCCCCC		48.9323663014
1232FarnesylationELLPNSGCQMQ----
HHCCCCCCCCC----		2.82-
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 KPB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPB2_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 KPB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MMS19_HUMANMMS19physical
22939629
WASC5_HUMANKIAA0196physical
22939629
UBE3C_HUMANUBE3Cphysical
22939629
Drug and Disease Associations
Kegg Disease
H00069 Glycogen storage diseases (GSD), including: von Gierke disease (GSD type Ia); Pompe disease (GSD typ
OMIM Disease
306000Glycogen storage disease 9A (GSD9A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KPB2_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-729 AND SER-1015, ANDMASS SPECTROMETRY.
"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-729, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, 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-1015, 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-729; SER-735 ANDSER-1015, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, AND MASSSPECTROMETRY.

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