GNPI1_HUMAN - dbPTM
GNPI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNPI1_HUMAN
UniProt AC P46926
Protein Name Glucosamine-6-phosphate isomerase 1
Gene Name GNPDA1
Organism Homo sapiens (Human).
Sequence Length 289
Subcellular Localization Cytoplasm.
Protein Description Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity)..
Protein Sequence MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLPTGSTPLGCYKKLIEYYKNGDLSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDAFEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGELTKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCDEDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKSQSSKKPYSD
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
10PhosphorylationLIILEHYSQASEWAA
EEEEEECHHHHHHHH		22.6029116813
13PhosphorylationLEHYSQASEWAAKYI
EEECHHHHHHHHHHH		26.4929116813
36PhosphorylationPGPEKYFTLGLPTGS
CCCHHEEEECCCCCC		19.4725072903
41PhosphorylationYFTLGLPTGSTPLGC
EEEECCCCCCCCCHH		49.1325072903
43PhosphorylationTLGLPTGSTPLGCYK
EECCCCCCCCCHHHH		29.3625072903
44PhosphorylationLGLPTGSTPLGCYKK
ECCCCCCCCCHHHHH		24.7125072903
49PhosphorylationGSTPLGCYKKLIEYY
CCCCCHHHHHHHHHH		14.9025072903
50UbiquitinationSTPLGCYKKLIEYYK
CCCCHHHHHHHHHHH		45.22-
50UbiquitinationSTPLGCYKKLIEYYK
CCCCHHHHHHHHHHH		45.2221890473
50AcetylationSTPLGCYKKLIEYYK
CCCCHHHHHHHHHHH		45.2223954790
51AcetylationTPLGCYKKLIEYYKN
CCCHHHHHHHHHHHC		28.3769911
51UbiquitinationTPLGCYKKLIEYYKN
CCCHHHHHHHHHHHC		28.3730230243
51UbiquitinationTPLGCYKKLIEYYKN
CCCHHHHHHHHHHHC		28.37-
57UbiquitinationKKLIEYYKNGDLSFK
HHHHHHHHCCCCEEE		54.26-
57UbiquitinationKKLIEYYKNGDLSFK
HHHHHHHHCCCCEEE		54.26-
62PhosphorylationYYKNGDLSFKYVKTF
HHHCCCCEEEEEEEE		25.1624719451
64AcetylationKNGDLSFKYVKTFNM
HCCCCEEEEEEEECH		45.8419608861
64UbiquitinationKNGDLSFKYVKTFNM
HCCCCEEEEEEEECH		45.8423000965
64MalonylationKNGDLSFKYVKTFNM
HCCCCEEEEEEEECH		45.8426320211
64AcetylationKNGDLSFKYVKTFNM
HCCCCEEEEEEEECH		45.84-
67UbiquitinationDLSFKYVKTFNMDEY
CCEEEEEEEECHHHC		44.2923000965
68PhosphorylationLSFKYVKTFNMDEYV
CEEEEEEEECHHHCC		15.36-
71SulfoxidationKYVKTFNMDEYVGLP
EEEEEECHHHCCCCC		3.4631801345
74PhosphorylationKTFNMDEYVGLPRDH
EEECHHHCCCCCCCC		8.78-
79UbiquitinationDEYVGLPRDHPESYH
HHCCCCCCCCHHHHH		60.9721890473
83UbiquitinationGLPRDHPESYHSFMW
CCCCCCHHHHHHHHH		61.58-
93UbiquitinationHSFMWNNFFKHIDIH
HHHHHHHHHCCCCCC		8.5723000965
96UbiquitinationMWNNFFKHIDIHPEN
HHHHHHCCCCCCCCC		20.1421890473
118GlutathionylationAVDLQAECDAFEEKI
EEEEHHHHHHHHHHH		5.2522555962
124UbiquitinationECDAFEEKIKAAGGI
HHHHHHHHHHHCCCE		42.1629967540
124AcetylationECDAFEEKIKAAGGI
HHHHHHHHHHHCCCE		42.1626051181
126UbiquitinationDAFEEKIKAAGGIEL
HHHHHHHHHCCCEEE		43.16-
151PhosphorylationIAFNEPGSSLVSRTR
EEECCCCCCHHCHHH		31.0828111955
152PhosphorylationAFNEPGSSLVSRTRV
EECCCCCCHHCHHHH		38.4128111955
155PhosphorylationEPGSSLVSRTRVKTL
CCCCCHHCHHHHHHH		32.9728111955
157PhosphorylationGSSLVSRTRVKTLAM
CCCHHCHHHHHHHHH		32.1018452278
160UbiquitinationLVSRTRVKTLAMDTI
HHCHHHHHHHHHHHH		34.2323000965
161PhosphorylationVSRTRVKTLAMDTIL
HCHHHHHHHHHHHHH		19.5225159151
164SulfoxidationTRVKTLAMDTILANA
HHHHHHHHHHHHHCC		5.4121406390
166PhosphorylationVKTLAMDTILANARF
HHHHHHHHHHHCCCC		12.5728857561
176UbiquitinationANARFFDGELTKVPT
HCCCCCCCCCCCCCE		27.02-
179UbiquitinationRFFDGELTKVPTMAL
CCCCCCCCCCCEEEE		26.2021890473
183PhosphorylationGELTKVPTMALTVGV
CCCCCCCEEEEEECC		20.3322210691
187UbiquitinationKVPTMALTVGVGTVM
CCCEEEEEECCCCEE		12.9921890473
187PhosphorylationKVPTMALTVGVGTVM
CCCEEEEEECCCCEE		12.9920068231
189UbiquitinationPTMALTVGVGTVMDA
CEEEEEECCCCEECH		13.6023000965
192PhosphorylationALTVGVGTVMDAREV
EEEECCCCEECHHHH		15.3922210691
196UbiquitinationGVGTVMDAREVMILI
CCCCEECHHHHEEEE		7.4621890473
239GlutathionylationHPRTVFVCDEDATLE
CCCEEEEECCCCCEE		3.0122555962
250UbiquitinationATLELKVKTVKYFKG
CCEEEEEEEEHHCCC		46.1123000965
253UbiquitinationELKVKTVKYFKGLML
EEEEEEEHHCCCEEE		50.6423000965
254PhosphorylationLKVKTVKYFKGLMLV
EEEEEEHHCCCEEEE		13.2429514088
256UbiquitinationVKTVKYFKGLMLVHN
EEEEHHCCCEEEECC		48.3123000965
259SulfoxidationVKYFKGLMLVHNKLV
EHHCCCEEEECCCCC		5.1130846556
264UbiquitinationGLMLVHNKLVDPLYS
CEEEECCCCCCCCHH		34.7021906983
264AcetylationGLMLVHNKLVDPLYS
CEEEECCCCCCCCHH		34.7026051181
270PhosphorylationNKLVDPLYSIKEKET
CCCCCCCHHCCHHHC		17.4621945579
271PhosphorylationKLVDPLYSIKEKETE
CCCCCCHHCCHHHCC		34.5621945579
273UbiquitinationVDPLYSIKEKETEKS
CCCCHHCCHHHCCCC		57.7121906983
275UbiquitinationPLYSIKEKETEKSQS
CCHHCCHHHCCCCCC		66.0022817900
277PhosphorylationYSIKEKETEKSQSSK
HHCCHHHCCCCCCCC		60.83-
279UbiquitinationIKEKETEKSQSSKKP
CCHHHCCCCCCCCCC		62.3023000965
282PhosphorylationKETEKSQSSKKPYSD
HHCCCCCCCCCCCCC		51.74-
282UbiquitinationKETEKSQSSKKPYSD
HHCCCCCCCCCCCCC		51.7423000965
285UbiquitinationEKSQSSKKPYSD---
CCCCCCCCCCCC---		51.6521890473
287PhosphorylationSQSSKKPYSD-----
CCCCCCCCCC-----		34.06-
293UbiquitinationPYSD-----------
CCCC-----------		21890473
302Ubiquitination--------------------
--------------------		22817900
304Ubiquitination----------------------
----------------------		22817900
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 GNPI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNPI1_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 GNPI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2R1_HUMANCDC34physical
22863883
EZRI_HUMANEZRphysical
22863883
GNPI2_HUMANGNPDA2physical
22863883
NUBP2_HUMANNUBP2physical
22863883
OGFD1_HUMANOGFOD1physical
22863883
PABP1_HUMANPABPC1physical
22863883
PSMD9_HUMANPSMD9physical
22863883
RD23A_HUMANRAD23Aphysical
22863883
TBCE_HUMANTBCEphysical
22863883
UBA6_HUMANUBA6physical
22863883
UB2R2_HUMANUBE2R2physical
22863883
PRDC1_HUMANPRTFDC1physical
25416956
GNPI2_HUMANGNPDA2physical
26186194
NAGA_HUMANAMDHD2physical
26186194
ASSY_HUMANASS1physical
26344197
TNG2_HUMANTANGO2physical
26344197
GNPI2_HUMANGNPDA2physical
28514442
NAGA_HUMANAMDHD2physical
28514442
1A1L1_HUMANACCSphysical
28514442
SC31A_HUMANSEC31Aphysical
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 GNPI1_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-64, AND MASS SPECTROMETRY.

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