PGK2_HUMAN - dbPTM
PGK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGK2_HUMAN
UniProt AC P07205
Protein Name Phosphoglycerate kinase 2
Gene Name PGK2
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Cytoplasm.
Protein Description Essential for sperm motility and male fertility. [PubMed: 26677959 Not required for the completion of spermatogenesis (By similarity]
Protein Sequence MSLSKKLTLDKLDVRGKRVIMRVDFNVPMKKNQITNNQRIKASIPSIKYCLDNGAKAVVLMSHLGRPDGVPMPDKYSLAPVAVELKSLLGKDVLFLKDCVGAEVEKACANPAPGSVILLENLRFHVEEEGKGQDPSGKKIKAEPDKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPHKASGFLMKKELDYFAKALENPVRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAYTFLKVLNNMEIGASLFDEEGAKIVKDIMAKAQKNGVRITFPVDFVTGDKFDENAQVGKATVASGISPGWMGLDCGPESNKNHAQVVAQARLIVWNGPLGVFEWDAFAKGTKALMDEIVKATSKGCITVIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKILPGVEALSNM
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------MSLSKKLTL
------CCCCCCCCC		41.1529083192
2Acetylation------MSLSKKLTL
------CCCCCCCCC		41.15-
4Phosphorylation----MSLSKKLTLDK
----CCCCCCCCCCC		22.0429083192
6Succinylation--MSLSKKLTLDKLD
--CCCCCCCCCCCCC		43.24-
8PhosphorylationMSLSKKLTLDKLDVR
CCCCCCCCCCCCCCC		41.6229083192
11AcetylationSKKLTLDKLDVRGKR
CCCCCCCCCCCCCCE		50.1025038526
31AcetylationDFNVPMKKNQITNNQ
EECCCCCCCCCCCCH		48.0820167786
35PhosphorylationPMKKNQITNNQRIKA
CCCCCCCCCCHHHHC		20.5324719451
43PhosphorylationNNQRIKASIPSIKYC
CCHHHHCCCCCHHHH		29.9924719451
46PhosphorylationRIKASIPSIKYCLDN
HHHCCCCCHHHHHHC		30.0024719451
48SuccinylationKASIPSIKYCLDNGA
HCCCCCHHHHHHCCC		33.96-
48AcetylationKASIPSIKYCLDNGA
HCCCCCHHHHHHCCC		33.9625038526
62PhosphorylationAKAVVLMSHLGRPDG
CEEEEEHHHCCCCCC		16.05-
75AcetylationDGVPMPDKYSLAPVA
CCCCCCCCCCCHHHH		30.7625038526
76PhosphorylationGVPMPDKYSLAPVAV
CCCCCCCCCCHHHHH		19.12-
77PhosphorylationVPMPDKYSLAPVAVE
CCCCCCCCCHHHHHH		24.64-
86AcetylationAPVAVELKSLLGKDV
HHHHHHHHHHCCCCE		26.08-
87PhosphorylationPVAVELKSLLGKDVL
HHHHHHHHHCCCCEE		41.2622617229
91AcetylationELKSLLGKDVLFLKD
HHHHHCCCCEEEEHH		44.6322637785
91UbiquitinationELKSLLGKDVLFLKD
HHHHHCCCCEEEEHH		44.6321890473
97AcetylationGKDVLFLKDCVGAEV
CCCEEEEHHHHCHHH		41.57-
115PhosphorylationCANPAPGSVILLENL
HCCCCCCCEEEEECE		12.6230622161
131AcetylationFHVEEEGKGQDPSGK
EEEEECCCCCCCCCC		57.59-
136PhosphorylationEGKGQDPSGKKIKAE
CCCCCCCCCCCCCCC		72.1027542207
138AcetylationKGQDPSGKKIKAEPD
CCCCCCCCCCCCCHH		56.5130591241
146AcetylationKIKAEPDKIEAFRAS
CCCCCHHHHHHHHHH		53.84-
153PhosphorylationKIEAFRASLSKLGDV
HHHHHHHHHHHHCCE		28.9925159151
155PhosphorylationEAFRASLSKLGDVYV
HHHHHHHHHHCCEEE		24.2829523821
156UbiquitinationAFRASLSKLGDVYVN
HHHHHHHHHCCEEEC		62.8821890473
156AcetylationAFRASLSKLGDVYVN
HHHHHHHHHCCEEEC		62.8822637779
161PhosphorylationLSKLGDVYVNDAFGT
HHHHCCEEECCCCCC		9.7728796482
168PhosphorylationYVNDAFGTAHRAHSS
EECCCCCCCCCCCCC		16.9128857561
174PhosphorylationGTAHRAHSSMVGVNL
CCCCCCCCCCCCCCC		21.1024275569
175PhosphorylationTAHRAHSSMVGVNLP
CCCCCCCCCCCCCCC		13.9720068231
186PhosphorylationVNLPHKASGFLMKKE
CCCCCCCCCEECHHH		34.5820068231
191SuccinylationKASGFLMKKELDYFA
CCCCEECHHHHHHHH		45.29-
196PhosphorylationLMKKELDYFAKALEN
ECHHHHHHHHHHHCC		20.3321552520
199AcetylationKELDYFAKALENPVR
HHHHHHHHHHCCCHH		43.54-
220AcetylationGGAKVADKIQLIKNM
CCCHHHHHHHHHHHH		23.7125038526
230AcetylationLIKNMLDKVNEMIIG
HHHHHHHHHHHHHCC		42.8925038526
242PhosphorylationIIGGGMAYTFLKVLN
HCCCHHHHHHHHHHH		6.80-
256PhosphorylationNNMEIGASLFDEEGA
HCCCCCHHHCCHHHH		25.1025693802
267UbiquitinationEEGAKIVKDIMAKAQ
HHHHHHHHHHHHHHH		45.0419608861
267AcetylationEEGAKIVKDIMAKAQ
HHHHHHHHHHHHHHH		45.0419608861
291AcetylationVDFVTGDKFDENAQV
ECCCCCCCCCCCCCC		56.94-
302PhosphorylationNAQVGKATVASGISP
CCCCCCEEECCCCCC		21.7930622161
305PhosphorylationVGKATVASGISPGWM
CCCEEECCCCCCCCC		32.1230622161
308PhosphorylationATVASGISPGWMGLD
EEECCCCCCCCCCCC		22.3830622161
322AcetylationDCGPESNKNHAQVVA
CCCCCCCCCHHHHHH		60.4325038526
361AcetylationALMDEIVKATSKGCI
HHHHHHHHHHCCCCE		52.16-
363PhosphorylationMDEIVKATSKGCITV
HHHHHHHHCCCCEEE		25.8328857561
364PhosphorylationDEIVKATSKGCITVI
HHHHHHHCCCCEEEE		31.7328857561
365AcetylationEIVKATSKGCITVIG
HHHHHHCCCCEEEEC		54.1419807321
369PhosphorylationATSKGCITVIGGGDT
HHCCCCEEEECCCCC		15.3328857561
378PhosphorylationIGGGDTATCCAKWNT
ECCCCCEEEECCCCC		15.3722798277
385PhosphorylationTCCAKWNTEDKVSHV
EEECCCCCCCCEEEE		44.4322798277
388AcetylationAKWNTEDKVSHVSTG
CCCCCCCCEEEEECC		39.13-
388UbiquitinationAKWNTEDKVSHVSTG
CCCCCCCCEEEEECC		39.13-
390PhosphorylationWNTEDKVSHVSTGGG
CCCCCCEEEEECCCC		24.7420068231
393PhosphorylationEDKVSHVSTGGGASL
CCCEEEEECCCCHHH		18.8620068231
394PhosphorylationDKVSHVSTGGGASLE
CCEEEEECCCCHHHH		38.4625693802
399PhosphorylationVSTGGGASLELLEGK
EECCCCHHHHHHCCC		26.1725849741
415PhosphorylationLPGVEALSNM-----
CCCHHHHHCC-----		37.5830622161
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 PGK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGK2_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 PGK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AK1A1_HUMANAKR1A1physical
26344197
ALDR_HUMANAKR1B1physical
26344197
ALDOC_HUMANALDOCphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOB_HUMANENO3physical
26344197
PGK1_HUMANPGK1physical
28514442
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 PGK2_HUMAN

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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-91; LYS-156 AND LYS-267, ANDMASS SPECTROMETRY.

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