GLO2_HUMAN - dbPTM
GLO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLO2_HUMAN
UniProt AC Q16775
Protein Name Hydroxyacylglutathione hydrolase, mitochondrial {ECO:0000303|PubMed:15117945}
Gene Name HAGH
Organism Homo sapiens (Human).
Sequence Length 308
Subcellular Localization Isoform 1: Mitochondrion matrix .
Isoform 2: Cytoplasm .
Protein Description Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid..
Protein Sequence MVVGRGLLGRRSLAALGAACARRGLGPALLGVFCHTDLRKNLTVDEGTMKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
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
35UbiquitinationALLGVFCHTDLRKNL
HHHHHEECCCHHCCC		15.7929967540
61PhosphorylationLPALTDNYMYLVIDD
ECCCCCCEEEEEECC		7.0222817900
63PhosphorylationALTDNYMYLVIDDET
CCCCCEEEEEECCCC		6.3530257219
65UbiquitinationTDNYMYLVIDDETKE
CCCEEEEEECCCCCE		2.1932015554
68UbiquitinationYMYLVIDDETKEAAI
EEEEEECCCCCEEEE		55.1029967540
83UbiquitinationVDPVQPQKVVDAARK
ECCCCHHHHHHHHHH		51.4129967540
96PhosphorylationRKHGVKLTTVLTTHH
HHHCCEEEEEEECCC		14.7822468782
100PhosphorylationVKLTTVLTTHHHWDH
CEEEEEEECCCCCCC		21.5322468782
101PhosphorylationKLTTVLTTHHHWDHA
EEEEEEECCCCCCCC		18.3022468782
113AcetylationDHAGGNEKLVKLESG
CCCCCCCEEEEECCC		63.6825038526
113UbiquitinationDHAGGNEKLVKLESG
CCCCCCCEEEEECCC		63.6832015554
116AcetylationGGNEKLVKLESGLKV
CCCCEEEEECCCCEE		57.9025953088
116MalonylationGGNEKLVKLESGLKV
CCCCEEEEECCCCEE		57.9026320211
116UbiquitinationGGNEKLVKLESGLKV
CCCCEEEEECCCCEE		57.9029967540
124PhosphorylationLESGLKVYGGDDRIG
ECCCCEEECCCCHHH		17.5029496907
129MethylationKVYGGDDRIGALTHK
EEECCCCHHHHHHHH		33.70-
141PhosphorylationTHKITHLSTLQVGSL
HHHECCCCCCCCCCC		21.3328348404
142PhosphorylationHKITHLSTLQVGSLN
HHECCCCCCCCCCCC		27.8026437602
147PhosphorylationLSTLQVGSLNVKCLA
CCCCCCCCCCEEEEE		20.2220068231
154UbiquitinationSLNVKCLATPCHTSG
CCCEEEEEECCCCCC		20.9732015554
181AcetylationEPPAVFTGDTLFVAG
CCCCEEECCEEEEEC		17.9119608861
181UbiquitinationEPPAVFTGDTLFVAG
CCCCEEECCEEEEEC		17.9132015554
193PhosphorylationVAGCGKFYEGTADEM
EECCCCCCCCCHHHH		19.5527642862
196UbiquitinationCGKFYEGTADEMCKA
CCCCCCCCHHHHHHH		20.9929967540
201UbiquitinationEGTADEMCKALLEVL
CCCHHHHHHHHHHHH		1.8832015554
202AcetylationGTADEMCKALLEVLG
CCHHHHHHHHHHHHC		40.5325038526
202UbiquitinationGTADEMCKALLEVLG
CCHHHHHHHHHHHHC		40.5332015554
218PhosphorylationLPPDTRVYCGHEYTI
CCCCCEEECCCEEEE		6.8829496907
223PhosphorylationRVYCGHEYTINNLKF
EEECCCEEEECCEEE		13.7729496907
224PhosphorylationVYCGHEYTINNLKFA
EECCCEEEECCEEEE		17.7829496907
229SuccinylationEYTINNLKFARHVEP
EEEECCEEEEECCCC		38.82-
229UbiquitinationEYTINNLKFARHVEP
EEEECCEEEEECCCC		38.8232015554
229SuccinylationEYTINNLKFARHVEP
EEEECCEEEEECCCC		38.82-
229AcetylationEYTINNLKFARHVEP
EEEECCEEEEECCCC		38.8219608861
230UbiquitinationYTINNLKFARHVEPG
EEECCEEEEECCCCC		9.0024816145
244UbiquitinationGNAAIREKLAWAKEK
CCHHHHHHHHHHHHH		33.3929967540
249UbiquitinationREKLAWAKEKYSIGE
HHHHHHHHHHCCCCC		44.0032015554
251AcetylationKLAWAKEKYSIGEPT
HHHHHHHHCCCCCCC		43.5225038526
252PhosphorylationLAWAKEKYSIGEPTV
HHHHHHHCCCCCCCC		13.4524275569
252UbiquitinationLAWAKEKYSIGEPTV
HHHHHHHCCCCCCCC		13.4524816145
256UbiquitinationKEKYSIGEPTVPSTL
HHHCCCCCCCCCCCH		35.8129967540
278UbiquitinationPFMRVREKTVQQHAG
CCHHEEHHHHHHHCC		43.3524816145
278AcetylationPFMRVREKTVQQHAG
CCHHEEHHHHHHHCC		43.3525953088
279PhosphorylationFMRVREKTVQQHAGE
CHHEEHHHHHHHCCC		20.8520068231
287PhosphorylationVQQHAGETDPVTTMR
HHHHCCCCCCHHHHH		44.6920068231
291PhosphorylationAGETDPVTTMRAVRR
CCCCCCHHHHHHHHH		21.9120068231
291O-linked_GlycosylationAGETDPVTTMRAVRR
CCCCCCHHHHHHHHH		21.91OGP
292PhosphorylationGETDPVTTMRAVRRE
CCCCCHHHHHHHHHH		12.6120068231
292O-linked_GlycosylationGETDPVTTMRAVRRE
CCCCCHHHHHHHHHH		12.61OGP
293SulfoxidationETDPVTTMRAVRREK
CCCCHHHHHHHHHHH		1.5730846556
300UbiquitinationMRAVRREKDQFKMPR
HHHHHHHHHHCCCCC		55.8324816145
304UbiquitinationRREKDQFKMPRD---
HHHHHHCCCCCC---		42.2229967540
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 GLO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLO2_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 GLO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CH10_HUMANHSPE1physical
26344197
LACB2_HUMANLACTB2physical
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
DB00143Glutathione
Regulatory Network of GLO2_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-229, AND MASS SPECTROMETRY.

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