PCKGM_HUMAN - dbPTM
PCKGM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCKGM_HUMAN
UniProt AC Q16822
Protein Name Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
Gene Name PCK2
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Mitochondrion.
Protein Description Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle..
Protein Sequence MAALYRPGLRLNWHGLSPLGWPSCRSIQTLRVLSGDLGQLPTGIRDFVEHSARLCQPEGIHICDGTEAENTATLTLLEQQGLIRKLPKYNNCWLARTDPKDVARVESKTVIVTPSQRDTVPLPPGGARGQLGNWMSPADFQRAVDERFPGCMQGRTMYVLPFSMGPVGSPLSRIGVQLTDSAYVVASMRIMTRLGTPVLQALGDGDFVKCLHSVGQPLTGQGEPVSQWPCNPEKTLIGHVPDQREIISFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITSPAGKKRYVAAAFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGRLRAINPENGFFGVAPGTSATTNPNAMATIQSNTIFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHPNSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFNWRHGVFVGSAMRSESTAAAEHKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGAQLPRIFHVNWFRRDEAGHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGALDLSGLRAIDTTQLFSLPKDFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM
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
34PhosphorylationIQTLRVLSGDLGQLP
HHHHHHHHCCCCCCC		27.6624114839
42PhosphorylationGDLGQLPTGIRDFVE
CCCCCCCCCHHHHHH		54.5628857561
45MethylationGQLPTGIRDFVEHSA
CCCCCCHHHHHHHHH		32.43115486641
88AcetylationGLIRKLPKYNNCWLA
CHHHHCCCCCCEEEE		71.67-
97PhosphorylationNNCWLARTDPKDVAR
CCEEEECCCHHHHCC		51.5520393185
100SuccinylationWLARTDPKDVARVES
EEECCCHHHHCCCCC		68.5923954790
107PhosphorylationKDVARVESKTVIVTP
HHHCCCCCCEEEECC		30.6720068231
108MalonylationDVARVESKTVIVTPS
HHCCCCCCEEEECCC		33.0526320211
108UbiquitinationDVARVESKTVIVTPS
HHCCCCCCEEEECCC		33.052190698
109PhosphorylationVARVESKTVIVTPSQ
HCCCCCCEEEECCCC		25.4120068231
113PhosphorylationESKTVIVTPSQRDTV
CCCEEEECCCCCCCC		13.1920068231
115PhosphorylationKTVIVTPSQRDTVPL
CEEEECCCCCCCCCC		28.6020068231
127UbiquitinationVPLPPGGARGQLGNW
CCCCCCCCCCCCCCC		20.53-
128UbiquitinationPLPPGGARGQLGNWM
CCCCCCCCCCCCCCC		36.34-
156PhosphorylationPGCMQGRTMYVLPFS
CCCCCCCEEEEEECC		21.4821406692
158PhosphorylationCMQGRTMYVLPFSMG
CCCCCEEEEEECCCC		9.7521406692
160UbiquitinationQGRTMYVLPFSMGPV
CCCEEEEEECCCCCC		1.63-
163PhosphorylationTMYVLPFSMGPVGSP
EEEEEECCCCCCCCC		22.3821406692
169PhosphorylationFSMGPVGSPLSRIGV
CCCCCCCCCHHHCEE		23.9321406692
172PhosphorylationGPVGSPLSRIGVQLT
CCCCCCHHHCEEEEC		25.8221406692
179PhosphorylationSRIGVQLTDSAYVVA
HHCEEEECCCCHHHH		15.7122210691
183PhosphorylationVQLTDSAYVVASMRI
EEECCCCHHHHCHHH		10.2122210691
196PhosphorylationRIMTRLGTPVLQALG
HHHHHHCCHHHHHHC		18.1528348404
234UbiquitinationQWPCNPEKTLIGHVP
CCCCCHHCEEECCCC		50.30-
235PhosphorylationWPCNPEKTLIGHVPD
CCCCHHCEEECCCCC		23.1925332170
251PhosphorylationREIISFGSGYGGNSL
CEEEECCCCCCCCHH		27.1627080861
253PhosphorylationIISFGSGYGGNSLLG
EEECCCCCCCCHHHH		24.4528152594
257PhosphorylationGSGYGGNSLLGKKCF
CCCCCCCHHHHHHHH		28.3927080861
261MalonylationGGNSLLGKKCFALRI
CCCHHHHHHHHHHHH		46.4626320211
261UbiquitinationGGNSLLGKKCFALRI
CCCHHHHHHHHHHHH		46.4621906983
270PhosphorylationCFALRIASRLARDEG
HHHHHHHHHHHHCCC		26.0020068231
289PhosphorylationHMLILGITSPAGKKR
EEEEEEECCCCCCCH		27.1924719451
290PhosphorylationMLILGITSPAGKKRY
EEEEEECCCCCCCHH		15.7227080861
294UbiquitinationGITSPAGKKRYVAAA
EECCCCCCCHHHEEE		35.86-
297PhosphorylationSPAGKKRYVAAAFPS
CCCCCCHHHEEECCC		11.8820068231
304PhosphorylationYVAAAFPSACGKTNL
HHEEECCCCCCCCCH		29.7225159151
309PhosphorylationFPSACGKTNLAMMRP
CCCCCCCCCHHHCCC		22.2820068231
337PhosphorylationIAWMRFDSEGRLRAI
EEEEEECCCCCEEEE		38.9620068231
410 (in isoform 2)Ubiquitination-47.88-
422PhosphorylationEPCAHPNSRFCAPAR
CCCCCCCCCCCCCHH		31.05-
444UbiquitinationAWEAPEGVPIDAIIF
CCCCCCCCCCCEEEE		3.42-
457SuccinylationIFGGRRPKGVPLVYE
EECCCCCCCCCCEEE		71.39-
457SuccinylationIFGGRRPKGVPLVYE
EECCCCCCCCCCEEE		71.39-
466UbiquitinationVPLVYEAFNWRHGVF
CCCEEEECCCCCCEE		6.35-
479MethylationVFVGSAMRSESTAAA
EEHHHHHCCCCCCHH		36.67115486635
482PhosphorylationGSAMRSESTAAAEHK
HHHHCCCCCCHHHHC		25.2928348404
483PhosphorylationSAMRSESTAAAEHKG
HHHCCCCCCHHHHCC		19.1028348404
491MalonylationAAAEHKGKIIMHDPF
CHHHHCCEEEECCCC		33.5926320211
491AcetylationAAAEHKGKIIMHDPF
CHHHHCCEEEECCCC		33.59-
578UbiquitinationTPIGLVPKEGALDLS
CCCCEECCCCCCCCC		62.39-
585PhosphorylationKEGALDLSGLRAIDT
CCCCCCCCCCEECCC		35.1321815630
592PhosphorylationSGLRAIDTTQLFSLP
CCCEECCCHHHCCCC		15.4428857561
593PhosphorylationGLRAIDTTQLFSLPK
CCEECCCHHHCCCCH		21.3717525332
597PhosphorylationIDTTQLFSLPKDFWE
CCCHHHCCCCHHHHH		52.9724719451
600UbiquitinationTQLFSLPKDFWEQEV
HHHCCCCHHHHHHHH		71.50-
624AcetylationQVNQDLPKEVLAELE
HHCCCCCHHHHHHHH		68.6920167786
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 PCKGM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCKGM_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 PCKGM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SMAD3_HUMANSMAD3physical
21988832
CH10_HUMANHSPE1physical
26344197
PPIA_HUMANPPIAphysical
26344197
UB2L3_HUMANUBE2L3physical
26344197
CH60_HUMANHSPD1physical
26496610
PRCC_HUMANPRCCphysical
26496610
TS101_HUMANTSG101physical
26496610
PLPHP_HUMANPROSCphysical
26496610
CWC15_HUMANCWC15physical
26496610
MUC13_HUMANMUC13physical
26496610
PCKGC_HUMANPCK1physical
28514442
MUC5B_HUMANMUC5Bphysical
28514442
BPIB1_HUMANBPIFB1physical
28514442
DMBT1_HUMANDMBT1physical
28514442
BPIA1_HUMANBPIFA1physical
28514442
ZMYM2_HUMANZMYM2physical
28514442
PIGR_HUMANPIGRphysical
28514442
AHNK2_HUMANAHNAK2physical
28514442
ZMYM4_HUMANZMYM4physical
28514442
ZG16B_HUMANZG16Bphysical
28514442
PHAG1_HUMANPAG1physical
28514442
SUFU_HUMANSUFUphysical
28514442
HEM1_HUMANALAS1physical
28514442
AHNK_HUMANAHNAKphysical
28514442
LACRT_HUMANLACRTphysical
28514442
ZMYM3_HUMANZMYM3physical
28514442
RCOR3_HUMANRCOR3physical
28514442
NEUM_HUMANGAP43physical
28514442
BBS2_HUMANBBS2physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261650Mitochondrial phosphoenolpyruvate carboxykinase deficiency (M-PEPCKD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCKGM_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-593, AND MASSSPECTROMETRY.

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