KPYR_HUMAN - dbPTM
KPYR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPYR_HUMAN
UniProt AC P30613
Protein Name Pyruvate kinase PKLR
Gene Name PKLR
Organism Homo sapiens (Human).
Sequence Length 574
Subcellular Localization
Protein Description Plays a key role in glycolysis..
Protein Sequence MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
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------MSIQENISS
------CCHHHHHHH		32.7423186163
8PhosphorylationMSIQENISSLQLRSW
CCHHHHHHHHHHHHH		36.2625693802
9PhosphorylationSIQENISSLQLRSWV
CHHHHHHHHHHHHHH		19.1523186163
14PhosphorylationISSLQLRSWVSKSQR
HHHHHHHHHHCHHHH		40.1820068231
17PhosphorylationLQLRSWVSKSQRDLA
HHHHHHHCHHHHHHH		21.9726434776
19PhosphorylationLRSWVSKSQRDLAKS
HHHHHCHHHHHHHHH		23.9626434776
26PhosphorylationSQRDLAKSILIGAPG
HHHHHHHHHHHCCCC		19.6120068231
38PhosphorylationAPGGPAGYLRRASVA
CCCCHHHHHHHHHHH		10.1120068231
43PhosphorylationAGYLRRASVAQLTQE
HHHHHHHHHHHHHHH		19.0428258704
48PhosphorylationRASVAQLTQELGTAF
HHHHHHHHHHHHHHH		14.1228258704
68PhosphorylationLPAAMADTFLEHLCL
HCHHHHHHHHHHHHC		22.1528258704
105AcetylationSRSVERLKEMIKAGM
CHHHHHHHHHHHHCC		52.00-
109SuccinylationERLKEMIKAGMNIAR
HHHHHHHHHCCCEEE		37.26-
140PhosphorylationNVREAVESFAGSPLS
HHHHHHHHHCCCCCC		17.50-
144PhosphorylationAVESFAGSPLSYRPV
HHHHHCCCCCCCCCE		21.1623186163
148PhosphorylationFAGSPLSYRPVAIAL
HCCCCCCCCCEEEEE		26.98-
158UbiquitinationVAIALDTKGPEIRTG
EEEEECCCCCCCCCC		72.62-
181PhosphorylationEVELVKGSQVLVTVD
HEEEEECCEEEEEEC		16.0520860994
218PhosphorylationVPVGGRIYIDDGLIS
EEECCEEEECCCHHE		9.27-
245UbiquitinationTQVENGGVLGSRKGV
EEEECCCCCCCCCCC		6.0822817900
249UbiquitinationNGGVLGSRKGVNLPG
CCCCCCCCCCCCCCC		37.6422817900
278UbiquitinationDLRFGVEHGVDIVFA
HHHHCHHCCCCEEEH		38.8922817900
282UbiquitinationGVEHGVDIVFASFVR
CHHCCCCEEEHHHCC		2.2622817900
284UbiquitinationEHGVDIVFASFVRKA
HCCCCEEEHHHCCHH		4.8823000965
290MethylationVFASFVRKASDVAAV
EEHHHCCHHHHHHHH		47.11-
290UbiquitinationVFASFVRKASDVAAV
EEHHHCCHHHHHHHH		47.1123000965
292PhosphorylationASFVRKASDVAAVRA
HHHCCHHHHHHHHHH		35.3421794208
309UbiquitinationGPEGHGIKIISKIEN
CCCCCCEEEEEEECC		38.2822817900
313UbiquitinationHGIKIISKIENHEGV
CCEEEEEEECCCCCC		43.5622817900
313AcetylationHGIKIISKIENHEGV
CCEEEEEEECCCCCC		43.56-
317UbiquitinationIISKIENHEGVKRFD
EEEEECCCCCCCCHH		22.0123000965
317NeddylationIISKIENHEGVKRFD
EEEEECCCCCCCCHH		22.0132015554
323UbiquitinationNHEGVKRFDEILEVS
CCCCCCCHHHHEEEC		9.0623000965
348AcetylationGIEIPAEKVFLAQKM
CCCCCHHHHHHHHHH		40.1570489
348UbiquitinationGIEIPAEKVFLAQKM
CCCCCHHHHHHHHHH		40.1523000965
348NeddylationGIEIPAEKVFLAQKM
CCCCCHHHHHHHHHH		40.1532015554
348 (in isoform 1)Ubiquitination-40.1521890473
354UbiquitinationEKVFLAQKMMIGRCN
HHHHHHHHHHHCCCC		25.4823000965
354 (in isoform 1)Ubiquitination-25.4821890473
365AcetylationGRCNLAGKPVVCATQ
CCCCCCCCCEEEEHH		29.09-
365SuccinylationGRCNLAGKPVVCATQ
CCCCCCCCCEEEEHH		29.09-
373 (in isoform 2)Ubiquitination-3.7821890473
379PhosphorylationQMLESMITKPRPTRA
HHHHHHHCCCCCCCC		26.7626503514
379 (in isoform 2)Ubiquitination-26.7621890473
388PhosphorylationPRPTRAETSDVANAV
CCCCCCCHHHHHHHH		29.28-
405PhosphorylationGADCIMLSGETAKGN
CCCEEEECCCCCCCC		19.7322210691
408PhosphorylationCIMLSGETAKGNFPV
EEEECCCCCCCCCCH		36.8822210691
448PhosphorylationLRRAAPLSRDPTEVT
HHHHCCCCCCCCCHH		33.3122673903
452PhosphorylationAPLSRDPTEVTAIGA
CCCCCCCCCHHHHHH		47.5822673903
455PhosphorylationSRDPTEVTAIGAVEA
CCCCCCHHHHHHHHH		13.3122673903
475PhosphorylationAAAIIVLTTTGRSAQ
HHHHHHHCCCCHHHH		16.0630624053
476PhosphorylationAAIIVLTTTGRSAQL
HHHHHHCCCCHHHHH		24.0830624053
477PhosphorylationAIIVLTTTGRSAQLL
HHHHHCCCCHHHHHH		25.9330624053
541SuccinylationQFGIESGKLRGFLRV
HEECCCCCCCEEEEE		44.27-
556PhosphorylationGDLVIVVTGWRPGSG
CCEEEEEECCCCCCC		21.8217081983
562PhosphorylationVTGWRPGSGYTNIMR
EECCCCCCCCCCCEE		31.17-
564PhosphorylationGWRPGSGYTNIMRVL
CCCCCCCCCCCEEEE		9.7921253578
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 KPYR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPYR_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 KPYR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF23_HUMANKIF23physical
8524282
ARHG6_HUMANARHGEF6physical
12006652
PAXI_HUMANPXNphysical
12006652
PAK1_HUMANPAK1physical
12006652
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
102900Pyruvate kinase hyperactivity (PKHYP)
266200Pyruvate kinase deficiency of red cells (PKRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00119Pyruvic acid
Regulatory Network of KPYR_HUMAN

loading...

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-348, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-556, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory