L2HDH_HUMAN - dbPTM
L2HDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID L2HDH_HUMAN
UniProt AC Q9H9P8
Protein Name L-2-hydroxyglutarate dehydrogenase, mitochondrial
Gene Name L2HGDH
Organism Homo sapiens (Human).
Sequence Length 463
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MVPALRYLVGACGRARGLFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL
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
64UbiquitinationGIVGLASARALILRH
CHHHHHHHHHHHHHC		8.6524816145
102PhosphorylationGVIHSGIYYKPESLK
CCCCCCEEECCHHHH		14.68-
103PhosphorylationVIHSGIYYKPESLKA
CCCCCEEECCHHHHH		20.39-
104AcetylationIHSGIYYKPESLKAK
CCCCEEECCHHHHHH		25.9023954790
104SuccinylationIHSGIYYKPESLKAK
CCCCEEECCHHHHHH		25.9023954790
104MalonylationIHSGIYYKPESLKAK
CCCCEEECCHHHHHH		25.9026320211
109AcetylationYYKPESLKAKLCVQG
EECCHHHHHHHHHHH		53.4025038526
155AcetylationRLQALYEKGLQNGVP
HHHHHHHHHHHCCCC		51.9019608861
155UbiquitinationRLQALYEKGLQNGVP
HHHHHHHHHHHCCCC		51.9019608861
155SuccinylationRLQALYEKGLQNGVP
HHHHHHHHHHHCCCC		51.9027452117
165MethylationQNGVPGLRLIQQEDI
HCCCCCCCEEEHHHH		35.34115481519
173AcetylationLIQQEDIKKKEPYCR
EEEHHHHCCCCCCCC		70.8425953088
173UbiquitinationLIQQEDIKKKEPYCR
EEEHHHHCCCCCCCC		70.8429967540
173SuccinylationLIQQEDIKKKEPYCR
EEEHHHHCCCCCCCC		70.8423954790
201UbiquitinationDYRQVALSFAQDFQE
CHHHHHHHHHHHHHH		14.5924816145
209UbiquitinationFAQDFQEAGGSVLTN
HHHHHHHCCCCEEEE		19.5024816145
226AcetylationVKGIEMAKESPSRSI
EECEEECCCCCCCCC		58.3727452117
226UbiquitinationVKGIEMAKESPSRSI
EECEEECCCCCCCCC		58.37-
230PhosphorylationEMAKESPSRSIDGMQ
EECCCCCCCCCCCCC		48.1925627689
232PhosphorylationAKESPSRSIDGMQYP
CCCCCCCCCCCCCCC		29.3925159151
243UbiquitinationMQYPIVIKNTKGEEI
CCCCEEEECCCCCEE		47.90-
246UbiquitinationPIVIKNTKGEEIRCQ
CEEEECCCCCEEEEE		73.9624816145
270PhosphorylationSDRISELSGCTPDPR
HHHHHHHHCCCCCCC		27.98-
285PhosphorylationIVPFRGDYLLLKPEK
EECCCCCEEEECCCE		11.32-
289AcetylationRGDYLLLKPEKCYLV
CCCEEEECCCEEEEE		51.6125953088
297AcetylationPEKCYLVKGNIYPVP
CCEEEEEECCEEECC		43.5826051181
297UbiquitinationPEKCYLVKGNIYPVP
CCEEEEEECCEEECC		43.58-
322PhosphorylationFTPRMDGSIWLGPNA
EECCCCCCEEECCCE		13.3132142685
334AcetylationPNAVLAFKREGYRPF
CCEEEEEECCCCCCC		43.892380205
346PhosphorylationRPFDFSATDVMDIII
CCCCCCHHHHHHHHH		28.1124275748
362PhosphorylationSGLIKLASQNFSYGV
CCHHHHHHCCCCCCH		35.7728509920
440PhosphorylationLHVRNAPSPAATSSI
EEEECCCCCCCCCHH		25.4327251275
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 L2HDH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of L2HDH_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 L2HDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGM1_HUMANTGM1physical
26186194
NGAL_HUMANLCN2physical
26186194
SAP3_HUMANGM2Aphysical
26186194
CATL2_HUMANCTSVphysical
26186194
INVO_HUMANIVLphysical
26186194
KLK10_HUMANKLK10physical
26186194
NGAL_HUMANLCN2physical
28514442
INVO_HUMANIVLphysical
28514442
KLK10_HUMANKLK10physical
28514442
CATL2_HUMANCTSVphysical
28514442
PPAP_HUMANACPPphysical
28514442
TGM1_HUMANTGM1physical
28514442
SPB4_HUMANSERPINB4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
236792L-2-hydroxyglutaric aciduria (L2HGA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of L2HDH_HUMAN

loading...

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-155, AND MASS SPECTROMETRY.

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