BDH_HUMAN - dbPTM
BDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BDH_HUMAN
UniProt AC Q02338
Protein Name D-beta-hydroxybutyrate dehydrogenase, mitochondrial {ECO:0000305}
Gene Name BDH1 {ECO:0000312|HGNC:HGNC:1027}
Organism Homo sapiens (Human).
Sequence Length 343
Subcellular Localization Mitochondrion inner membrane . Mitochondrion matrix .
Protein Description
Protein Sequence MLATRLSRPLSRLPGKTLSACDRENGARRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGNFIAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTDTSPVIDAVTHALTATTPYTRYHPMDYYWWLRMQIMTHLPGAISDMIYIR
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
4Phosphorylation----MLATRLSRPLS
----CCCHHCCCCHH		28.3430622161
7Phosphorylation-MLATRLSRPLSRLP
-CCCHHCCCCHHHCC		28.6730622161
11PhosphorylationTRLSRPLSRLPGKTL
HHCCCCHHHCCCCCC		34.1624043423
73AcetylationGFGFSLAKHLHSKGF
CCCHHHHHHHHHCCE		52.58-
97AcetylationDKGHDGVKELDSLNS
CCCCCCCHHHHHCCC		59.08-
97UbiquitinationDKGHDGVKELDSLNS
CCCCCCCHHHHHCCC		59.08-
116PhosphorylationTVQLNVCSSEEVEKV
EEEEEECCHHHHHHH		36.1824275569
132AcetylationEIVRSSLKDPEKGMW
HHHHHHCCCHHCCCE		73.51-
177AcetylationWGTVRMTKSFLPLIR
HHHHHCCHHHHHHHH		29.84-
208PhosphorylationANPARSPYCITKFGV
CCCCCCCCEEEHHHH		9.57-
212AcetylationRSPYCITKFGVEAFS
CCCCEEEHHHHHHHH		21.87-
219O-linked_GlycosylationKFGVEAFSDCLRYEM
HHHHHHHHHHHHHCC		34.17UniProtKB CARBOHYD
219PhosphorylationKFGVEAFSDCLRYEM
HHHHHHHHHHHHHCC		34.1725850435
227PhosphorylationDCLRYEMYPLGVKVS
HHHHHCCEECCCEEE		5.37-
246PhosphorylationGNFIAATSLYSPESI
CCEEEEECCCCHHHH		22.1524275569
248PhosphorylationFIAATSLYSPESIQA
EEEEECCCCHHHHHH		23.1925147952
258AcetylationESIQAIAKKMWEELP
HHHHHHHHHHHHHCH		36.73-
259SuccinylationSIQAIAKKMWEELPE
HHHHHHHHHHHHCHH		39.98-
259AcetylationSIQAIAKKMWEELPE
HHHHHHHHHHHHCHH		39.98-
259SuccinylationSIQAIAKKMWEELPE
HHHHHHHHHHHHCHH		39.98-
280AcetylationGKKYFDEKIAKMETY
CHHHHHHHHHCCCHH		50.2127178108
283AcetylationYFDEKIAKMETYCSS
HHHHHHHCCCHHCCC		40.5261103
286PhosphorylationEKIAKMETYCSSGST
HHHHCCCHHCCCCCC		26.7424043423
287PhosphorylationKIAKMETYCSSGSTD
HHHCCCHHCCCCCCC		4.1424043423
289PhosphorylationAKMETYCSSGSTDTS
HCCCHHCCCCCCCCH		27.5924043423
290PhosphorylationKMETYCSSGSTDTSP
CCCHHCCCCCCCCHH		32.9524043423
292PhosphorylationETYCSSGSTDTSPVI
CHHCCCCCCCCHHHH		25.6724043423
293PhosphorylationTYCSSGSTDTSPVID
HHCCCCCCCCHHHHH		46.9924043423
295PhosphorylationCSSGSTDTSPVIDAV
CCCCCCCCHHHHHHH		34.7124043423
296PhosphorylationSSGSTDTSPVIDAVT
CCCCCCCHHHHHHHH		21.7124043423
303PhosphorylationSPVIDAVTHALTATT
HHHHHHHHHHHHCCC		11.8024043423
307PhosphorylationDAVTHALTATTPYTR
HHHHHHHHCCCCCCC		23.8124043423
309PhosphorylationVTHALTATTPYTRYH
HHHHHHCCCCCCCCC		24.0624043423
310PhosphorylationTHALTATTPYTRYHP
HHHHHCCCCCCCCCC		16.3124043423
312PhosphorylationALTATTPYTRYHPMD
HHHCCCCCCCCCCCC		11.1924043423
313PhosphorylationLTATTPYTRYHPMDY
HHCCCCCCCCCCCCH		26.4224043423
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 BDH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BDH_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 BDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AGM1_HUMANPGM3physical
27173435
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 BDH_HUMAN

loading...

Related Literatures of Post-Translational Modification

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