GLOD4_HUMAN - dbPTM
GLOD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLOD4_HUMAN
UniProt AC Q9HC38
Protein Name Glyoxalase domain-containing protein 4
Gene Name GLOD4
Organism Homo sapiens (Human).
Sequence Length 313
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAARRALHFVFKVGNRFQTARFYRDVLGMKVESCSVARLECSGAISAHCSDYTRITEDSFSKPYDGKWSKTMVGFGPEDDHFVAELTYNYGVGDYKLGNDFMGITLASSQAVSNARKLEWPLTEVAEGVFETEAPGGYKFYLQNRSLPQSDPVLKVTLAVSDLQKSLNYWCNLLGMKIYEKDEEKQRALLGYADNQCKLELQGVKGGVDHAAAFGRIAFSCPQKELPDLEDLMKRENQKILTPLVSLDTPGKATVQVVILADPDGHEICFVGDEAFRELSKMDPEGSKLLDDAMAADKSDEWFAKHNKPKASG
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
2Acetylation------MAARRALHF
------CCHHHHHHH		15.07-
19PhosphorylationKVGNRFQTARFYRDV
ECCCCHHHHHHHHHH		19.65-
23PhosphorylationRFQTARFYRDVLGMK
CHHHHHHHHHHHCCE		10.59-
30UbiquitinationYRDVLGMKVESCSVA
HHHHHCCEEEECCEE		40.8423000965
30 (in isoform 3)Ubiquitination-40.8421890473
30 (in isoform 2)Ubiquitination-40.8421890473
33MethylationVLGMKVESCSVARLE
HHCCEEEECCEEEEE		18.06-
42UbiquitinationSVARLECSGAISAHC
CEEEEECCCCEEECC		23.1432015554
46UbiquitinationLECSGAISAHCSDYT
EECCCCEEECCCCCC		16.0732015554
50PhosphorylationGAISAHCSDYTRITE
CCEEECCCCCCCCCC		24.6430576142
55UbiquitinationHCSDYTRITEDSFSK
CCCCCCCCCCCCCCC		3.6932015554
59PhosphorylationYTRITEDSFSKPYDG
CCCCCCCCCCCCCCC		25.7824719451
68UbiquitinationSKPYDGKWSKTMVGF
CCCCCCCCCCCEEEC		15.5832015554
69PhosphorylationKPYDGKWSKTMVGFG
CCCCCCCCCCEEECC		23.0230576142
70UbiquitinationPYDGKWSKTMVGFGP
CCCCCCCCCEEECCC		39.2532015554
102UbiquitinationYKLGNDFMGITLASS
CEECCCCCCEEECCC		4.1829967540
102SulfoxidationYKLGNDFMGITLASS
CEECCCCCCEEECCC		4.1828183972
115UbiquitinationSSQAVSNARKLEWPL
CCHHHHCCHHCCCCH		11.5032015554
124UbiquitinationKLEWPLTEVAEGVFE
HCCCCHHHHEECEEE		47.6232015554
127UbiquitinationWPLTEVAEGVFETEA
CCHHHHEECEEECCC		62.1532015554
127NeddylationWPLTEVAEGVFETEA
CCHHHHEECEEECCC		62.1532015554
131PhosphorylationEVAEGVFETEAPGGY
HHEECEEECCCCCCE		43.2527251275
134UbiquitinationEGVFETEAPGGYKFY
ECEEECCCCCCEEEE		18.5623000965
139UbiquitinationTEAPGGYKFYLQNRS
CCCCCCEEEEEECCC		30.7032015554
146PhosphorylationKFYLQNRSLPQSDPV
EEEEECCCCCCCCCC		52.5328348404
153UbiquitinationSLPQSDPVLKVTLAV
CCCCCCCCEEEEEEH		10.9632015554
163UbiquitinationVTLAVSDLQKSLNYW
EEEEHHHHHHHHHHH		5.5624816145
168UbiquitinationSDLQKSLNYWCNLLG
HHHHHHHHHHHHHHC		35.0421890473
174NeddylationLNYWCNLLGMKIYEK
HHHHHHHHCCCCEEC		3.8132015554
174UbiquitinationLNYWCNLLGMKIYEK
HHHHHHHHCCCCEEC		3.8132015554
181AcetylationLGMKIYEKDEEKQRA
HCCCCEECCHHHHHH		54.1723749302
181UbiquitinationLGMKIYEKDEEKQRA
HCCCCEECCHHHHHH		54.1723000965
183UbiquitinationMKIYEKDEEKQRALL
CCCEECCHHHHHHHH		77.4932015554
183 (in isoform 2)Ubiquitination-77.49-
183NeddylationMKIYEKDEEKQRALL
CCCEECCHHHHHHHH		77.4932015554
190UbiquitinationEEKQRALLGYADNQC
HHHHHHHHHHCCCCC		4.8723000965
190 (in isoform 2)Ubiquitination-4.87-
192PhosphorylationKQRALLGYADNQCKL
HHHHHHHHCCCCCEE		15.6828152594
197S-nitrosylationLGYADNQCKLELQGV
HHHCCCCCEEEECCC		7.3324105792
198UbiquitinationGYADNQCKLELQGVK
HHCCCCCEEEECCCC		34.9232015554
198NeddylationGYADNQCKLELQGVK
HHCCCCCEEEECCCC		34.9232015554
200UbiquitinationADNQCKLELQGVKGG
CCCCCEEEECCCCCC		25.2532015554
205UbiquitinationKLELQGVKGGVDHAA
EEEECCCCCCHHHHH		57.6932015554
209UbiquitinationQGVKGGVDHAAAFGR
CCCCCCHHHHHHHHH		29.0532015554
210UbiquitinationGVKGGVDHAAAFGRI
CCCCCHHHHHHHHHH		18.1824816145
215UbiquitinationVDHAAAFGRIAFSCP
HHHHHHHHHHHHCCC		18.5021890473
219UbiquitinationAAFGRIAFSCPQKEL
HHHHHHHHCCCCHHC		7.8032015554
219 (in isoform 2)Ubiquitination-7.80-
221S-nitrosocysteineFGRIAFSCPQKELPD
HHHHHHCCCCHHCCC		3.15-
221S-nitrosylationFGRIAFSCPQKELPD
HHHHHHCCCCHHCCC		3.1519483679
224UbiquitinationIAFSCPQKELPDLED
HHHCCCCHHCCCHHH		46.4921890473
224 (in isoform 2)Ubiquitination-46.4921890473
227UbiquitinationSCPQKELPDLEDLMK
CCCCHHCCCHHHHHH		45.2732015554
233SulfoxidationLPDLEDLMKRENQKI
CCCHHHHHHHHHCCC		6.2621406390
2342-HydroxyisobutyrylationPDLEDLMKRENQKIL
CCHHHHHHHHHCCCE		64.95-
234AcetylationPDLEDLMKRENQKIL
CCHHHHHHHHHCCCE		64.9525953088
234UbiquitinationPDLEDLMKRENQKIL
CCHHHHHHHHHCCCE		64.9532015554
239UbiquitinationLMKRENQKILTPLVS
HHHHHHCCCEEEEEE		51.79-
239AcetylationLMKRENQKILTPLVS
HHHHHHCCCEEEEEE		51.7925953088
239 (in isoform 1)Ubiquitination-51.7921890473
242PhosphorylationRENQKILTPLVSLDT
HHHCCCEEEEEECCC		20.32-
246PhosphorylationKILTPLVSLDTPGKA
CCEEEEEECCCCCCE		28.36-
249PhosphorylationTPLVSLDTPGKATVQ
EEEEECCCCCCEEEE		38.95-
274UbiquitinationEICFVGDEAFRELSK
EEEEECHHHHHHHHC		43.7232015554
280PhosphorylationDEAFRELSKMDPEGS
HHHHHHHHCCCCCCC		22.60-
283 (in isoform 2)Ubiquitination-41.66-
283UbiquitinationFRELSKMDPEGSKLL
HHHHHCCCCCCCHHH		41.6632015554
287PhosphorylationSKMDPEGSKLLDDAM
HCCCCCCCHHHHHHH		20.6123403867
288SuccinylationKMDPEGSKLLDDAMA
CCCCCCCHHHHHHHH		65.02-
288SuccinylationKMDPEGSKLLDDAMA
CCCCCCCHHHHHHHH		65.02-
290UbiquitinationDPEGSKLLDDAMAAD
CCCCCHHHHHHHHCC		6.8629967540
290AcetylationDPEGSKLLDDAMAAD
CCCCCHHHHHHHHCC		6.8619608861
293AcetylationGSKLLDDAMAADKSD
CCHHHHHHHHCCCCC		6.8119608861
294SulfoxidationSKLLDDAMAADKSDE
CHHHHHHHHCCCCCH		3.9821406390
298AcetylationDDAMAADKSDEWFAK
HHHHHCCCCCHHHHH		55.8925953088
298UbiquitinationDDAMAADKSDEWFAK
HHHHHCCCCCHHHHH		55.8932015554
305AcetylationKSDEWFAKHNKPKAS
CCCHHHHHHCCCCCC		37.9319608861
308AcetylationEWFAKHNKPKASG--
HHHHHHCCCCCCC--		47.8419608861
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 GLOD4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLOD4_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 GLOD4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ALDOC_HUMANALDOCphysical
26344197
FKB1B_HUMANFKBP1Bphysical
26344197
FKBP2_HUMANFKBP2physical
26344197
GMPPB_HUMANGMPPBphysical
26344197
SIAS_HUMANNANSphysical
26344197
PCBP1_HUMANPCBP1physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PPIL3_HUMANPPIL3physical
26344197
PRDX2_HUMANPRDX2physical
26344197
SDHA_HUMANSDHAphysical
26344197
SPB5_HUMANSERPINB5physical
26344197
SNX3_HUMANSNX3physical
26344197
TALDO_HUMANTALDO1physical
26344197
TKT_HUMANTKTphysical
26344197
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 GLOD4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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