DHSO_HUMAN - dbPTM
DHSO_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHSO_HUMAN
UniProt AC Q00796
Protein Name Sorbitol dehydrogenase
Gene Name SORD
Organism Homo sapiens (Human).
Sequence Length 357
Subcellular Localization Mitochondrion membrane
Peripheral membrane protein . Cell projection, cilium, flagellum . Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted b
Protein Description Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm..
Protein Sequence MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
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------MAAAAKPNN
------CCCCCCCCC		13.0525944712
6Acetylation--MAAAAKPNNLSLV
--CCCCCCCCCEEEE		43.4821339330
6Ubiquitination--MAAAAKPNNLSLV
--CCCCCCCCCEEEE		43.48-
6Ubiquitination--MAAAAKPNNLSLV
--CCCCCCCCCEEEE		43.48-
11PhosphorylationAAKPNNLSLVVHGPG
CCCCCCEEEEEECCC		22.6528857561
25PhosphorylationGDLRLENYPIPEPGP
CCCEEECCCCCCCCC		7.99-
51PhosphorylationICGSDVHYWEYGRIG
ECCCCCCCCCCCCCC		10.3627642862
54PhosphorylationSDVHYWEYGRIGNFI
CCCCCCCCCCCCEEE		9.5027642862
63UbiquitinationRIGNFIVKKPMVLGH
CCCEEEECCCEECCC		46.4722817900
63SuccinylationRIGNFIVKKPMVLGH
CCCEEEECCCEECCC		46.4723954790
64AcetylationIGNFIVKKPMVLGHE
CCEEEECCCEECCCC		27.7026051181
64UbiquitinationIGNFIVKKPMVLGHE
CCEEEECCCEECCCC		27.7021906983
64UbiquitinationIGNFIVKKPMVLGHE
CCEEEECCCEECCCC		27.7021906983
66SulfoxidationNFIVKKPMVLGHEAS
EEEECCCEECCCCCC		5.5130846556
73PhosphorylationMVLGHEASGTVEKVG
EECCCCCCCCEEECC		31.8226074081
75PhosphorylationLGHEASGTVEKVGSS
CCCCCCCCEEECCCC		24.0126074081
78AcetylationEASGTVEKVGSSVKH
CCCCCEEECCCCCCC		47.7825953088
78UbiquitinationEASGTVEKVGSSVKH
CCCCCEEECCCCCCC		47.78-
78UbiquitinationEASGTVEKVGSSVKH
CCCCCEEECCCCCCC		47.78-
84UbiquitinationEKVGSSVKHLKPGDR
EECCCCCCCCCCCCE		45.2129967540
107UbiquitinationRENDEFCKMGRYNLS
CCCCHHHCCCCCCCC		50.1121963094
114PhosphorylationKMGRYNLSPSIFFCA
CCCCCCCCCCEEEEC		16.9828348404
116PhosphorylationGRYNLSPSIFFCATP
CCCCCCCCEEEECCC		28.7528348404
122PhosphorylationPSIFFCATPPDDGNL
CCEEEECCCCCCCCC		36.2127251275
134AcetylationGNLCRFYKHNAAFCY
CCCCHHEECCEEEEE		27.8925953088
134UbiquitinationGNLCRFYKHNAAFCY
CCCCHHEECCEEEEE		27.89-
167MethylationVGIHACRRGGVTLGH
CCHHHHHCCCCCCCC		46.21115917541
195SulfoxidationTLLVAKAMGAAQVVV
HHHHHHHHCCCEEEE		3.5521406390
203PhosphorylationGAAQVVVTDLSATRL
CCCEEEEECCCCCCH		21.4420068231
206PhosphorylationQVVVTDLSATRLSKA
EEEEECCCCCCHHHH		30.3325850435
208PhosphorylationVVTDLSATRLSKAKE
EEECCCCCCHHHHHH		28.8525850435
211PhosphorylationDLSATRLSKAKEIGA
CCCCCCHHHHHHHCC		27.5528857561
225PhosphorylationADLVLQISKESPQEI
CCEEEEECCCCHHHH		19.877782086
226UbiquitinationDLVLQISKESPQEIA
CEEEEECCCCHHHHH		64.9322817900
228PhosphorylationVLQISKESPQEIARK
EEEECCCCHHHHHHH		35.30-
295UbiquitinationAIREVDIKGVFRYCN
HHHHCCCCHHHHHCC		44.5524816145
2952-HydroxyisobutyrylationAIREVDIKGVFRYCN
HHHHCCCCHHHHHCC		44.55-
300PhosphorylationDIKGVFRYCNTWPVA
CCCHHHHHCCHHHHH		4.4121406692
303PhosphorylationGVFRYCNTWPVAISM
HHHHHCCHHHHHHHH		27.8220068231
309PhosphorylationNTWPVAISMLASKSV
CHHHHHHHHHHCCCC		9.6721406692
313PhosphorylationVAISMLASKSVNVKP
HHHHHHHCCCCCCCC		22.8521406692
314UbiquitinationAISMLASKSVNVKPL
HHHHHHCCCCCCCCC		53.4622817900
319UbiquitinationASKSVNVKPLVTHRF
HCCCCCCCCCEECCC		27.6821906983
3392-HydroxyisobutyrylationLEAFETFKKGLGLKI
HHHHHHHHHCCCCEE		54.04-
339AcetylationLEAFETFKKGLGLKI
HHHHHHHHHCCCCEE		54.0425953088
339UbiquitinationLEAFETFKKGLGLKI
HHHHHHHHHCCCCEE		54.0427667366
340UbiquitinationEAFETFKKGLGLKIM
HHHHHHHHCCCCEEE		56.0022817900
349UbiquitinationLGLKIMLKCDPSDQN
CCCEEEEECCCCCCC		21.1521963094
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 DHSO_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHSO_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 DHSO_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DHSO_HUMANSORDphysical
16189514
PFD4_HUMANPFDN4physical
22939629
NUDC2_HUMANNUDCD2physical
22939629
RAGP1_HUMANRANGAP1physical
22939629
GSH0_HUMANGCLMphysical
22939629
RD23A_HUMANRAD23Aphysical
22939629
TIPRL_HUMANTIPRLphysical
22939629
TPM1_HUMANTPM1physical
22939629
ETFA_HUMANETFAphysical
22939629
PIEZ1_HUMANPIEZO1physical
22939629
FAD1_HUMANFLAD1physical
22939629
BCCIP_HUMANBCCIPphysical
22863883
DX39A_HUMANDDX39Aphysical
22863883
FPPS_HUMANFDPSphysical
22863883
GUAD_HUMANGDAphysical
22863883
NDKA_HUMANNME1physical
22863883
6PGD_HUMANPGDphysical
22863883
PLST_HUMANPLS3physical
22863883
TALDO_HUMANTALDO1physical
22863883
DHSO_HUMANSORDphysical
25416956
ALDR_HUMANAKR1B1physical
26344197
CATA_HUMANCATphysical
26344197
FAHD1_HUMANFAHD1physical
26344197
FAH2A_HUMANFAHD2Aphysical
26344197
G6PI_HUMANGPIphysical
26344197
NIT2_HUMANNIT2physical
26344197
PGM1_HUMANPGM1physical
26344197
TALDO_HUMANTALDO1physical
26344197
TKFC_HUMANDAKphysical
26344197
TPIS_HUMANTPI1physical
26344197
DHSO_HUMANSORDphysical
21516116
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 DHSO_HUMAN

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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.
"The human sorbitol dehydrogenase gene: cDNA cloning, sequencedetermination, and mapping by fluorescence in situ hybridization.";
Lee F.K., Cheung M.C., Chung S.;
Genomics 21:354-358(1994).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-269.

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