SQOR_HUMAN - dbPTM
SQOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SQOR_HUMAN
UniProt AC Q9Y6N5
Protein Name Sulfide:quinone oxidoreductase, mitochondrial {ECO:0000305}
Gene Name SQOR {ECO:0000312|HGNC:HGNC:20390}
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Mitochondrion .
Protein Description Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro)..
Protein Sequence MVPLVAVVSGPRAQLFACLLRLGTQQVGPLQLHTGASHAARNHYEVLVLGGGSGGITMAARMKRKVGAENVAIVEPSERHFYQPIWTLVGAGAKQLSSSGRPTASVIPSGVEWIKARVTELNPDKNCIHTDDDEKISYRYLIIALGIQLDYEKIKGLPEGFAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRSKANIIFNTSLGAIFGVKKYADALQEIIQERNLTVNYKKNLIEVRADKQEAVFENLDKPGETQVISYEMLHVTPPMSPPDVLKTSPVADAAGWVDVDKETLQHRRYPNVFGIGDCTNLPTSKTAAAVAAQSGILDRTISVIMKNQTPTKKYDGYTSCPLVTGYNRVILAEFDYKAEPLETFPFDQSKERLSMYLMKADLMPFLYWNMMLRGYWGGPAFLRKLFHLGMS
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
9PhosphorylationVPLVAVVSGPRAQLF
CCEEEEECCHHHHHH
22210691
97PhosphorylationGAGAKQLSSSGRPTA
HHCHHHCCCCCCCCC
27080861
98PhosphorylationAGAKQLSSSGRPTAS
HCHHHCCCCCCCCCE
27080861
99PhosphorylationGAKQLSSSGRPTASV
CHHHCCCCCCCCCEE
27080861
103PhosphorylationLSSSGRPTASVIPSG
CCCCCCCCCEECCCC
27080861
105PhosphorylationSSGRPTASVIPSGVE
CCCCCCCEECCCCCH
27080861
115AcetylationPSGVEWIKARVTELN
CCCCHHHHHHHCCCC
7706167
1152-HydroxyisobutyrylationPSGVEWIKARVTELN
CCCCHHHHHHHCCCC
-
115UbiquitinationPSGVEWIKARVTELN
CCCCHHHHHHHCCCC
-
125UbiquitinationVTELNPDKNCIHTDD
HCCCCCCCCCCCCCC
-
125SuccinylationVTELNPDKNCIHTDD
HCCCCCCCCCCCCCC
27452117
125AcetylationVTELNPDKNCIHTDD
HCCCCCCCCCCCCCC
25953088
1252-HydroxyisobutyrylationVTELNPDKNCIHTDD
HCCCCCCCCCCCCCC
-
125MalonylationVTELNPDKNCIHTDD
HCCCCCCCCCCCCCC
26320211
1352-HydroxyisobutyrylationIHTDDDEKISYRYLI
CCCCCCCHHHHHHHH
-
135MalonylationIHTDDDEKISYRYLI
CCCCCCCHHHHHHHH
26320211
135AcetylationIHTDDDEKISYRYLI
CCCCCCCHHHHHHHH
23954790
135SuccinylationIHTDDDEKISYRYLI
CCCCCCCHHHHHHHH
27452117
137PhosphorylationTDDDEKISYRYLIIA
CCCCCHHHHHHHHHH
21712546
151PhosphorylationALGIQLDYEKIKGLP
HHCCCCCHHHHCCCC
21712546
155MalonylationQLDYEKIKGLPEGFA
CCCHHHHCCCCCCCC
26320211
155UbiquitinationQLDYEKIKGLPEGFA
CCCHHHHCCCCCCCC
-
165UbiquitinationPEGFAHPKIGSNYSV
CCCCCCCCCCCCCEE
-
168PhosphorylationFAHPKIGSNYSVKTV
CCCCCCCCCCEEEHH
29759185
170PhosphorylationHPKIGSNYSVKTVEK
CCCCCCCCEEEHHHH
29759185
171PhosphorylationPKIGSNYSVKTVEKT
CCCCCCCEEEHHHHH
29759185
173MalonylationIGSNYSVKTVEKTWK
CCCCCEEEHHHHHHH
26320211
173UbiquitinationIGSNYSVKTVEKTWK
CCCCCEEEHHHHHHH
19608861
173AcetylationIGSNYSVKTVEKTWK
CCCCCEEEHHHHHHH
19608861
173SuccinylationIGSNYSVKTVEKTWK
CCCCCEEEHHHHHHH
27452117
174PhosphorylationGSNYSVKTVEKTWKA
CCCCEEEHHHHHHHH
29759185
177UbiquitinationYSVKTVEKTWKALQD
CEEEHHHHHHHHHHH
-
177MalonylationYSVKTVEKTWKALQD
CEEEHHHHHHHHHHH
26320211
1772-HydroxyisobutyrylationYSVKTVEKTWKALQD
CEEEHHHHHHHHHHH
-
180SuccinylationKTVEKTWKALQDFKE
EHHHHHHHHHHHHHC
23954790
180MalonylationKTVEKTWKALQDFKE
EHHHHHHHHHHHHHC
26320211
180AcetylationKTVEKTWKALQDFKE
EHHHHHHHHHHHHHC
19608861
186UbiquitinationWKALQDFKEGNAIFT
HHHHHHHHCCCEEEE
-
186AcetylationWKALQDFKEGNAIFT
HHHHHHHHCCCEEEE
25953088
186SuccinylationWKALQDFKEGNAIFT
HHHHHHHHCCCEEEE
23954790
193PhosphorylationKEGNAIFTFPNTPVK
HCCCEEEECCCCCCC
27050516
197PhosphorylationAIFTFPNTPVKCAGA
EEEECCCCCCCCCCC
28450419
2412-HydroxyisobutyrylationGAIFGVKKYADALQE
HHHHCHHHHHHHHHH
-
259PhosphorylationERNLTVNYKKNLIEV
HCCCCCCCCCCEEEE
-
260SuccinylationRNLTVNYKKNLIEVR
CCCCCCCCCCEEEEE
23954790
260AcetylationRNLTVNYKKNLIEVR
CCCCCCCCCCEEEEE
25953088
2602-HydroxyisobutyrylationRNLTVNYKKNLIEVR
CCCCCCCCCCEEEEE
-
261MalonylationNLTVNYKKNLIEVRA
CCCCCCCCCEEEEEC
26320211
261UbiquitinationNLTVNYKKNLIEVRA
CCCCCCCCCEEEEEC
-
320AcetylationAGWVDVDKETLQHRR
CCCEECCHHHHHCCC
23954790
322PhosphorylationWVDVDKETLQHRRYP
CEECCHHHHHCCCCC
27080861
328PhosphorylationETLQHRRYPNVFGIG
HHHHCCCCCCCCCCC
28152594
338PhosphorylationVFGIGDCTNLPTSKT
CCCCCCCCCCCCHHH
23403867
342PhosphorylationGDCTNLPTSKTAAAV
CCCCCCCCHHHHHHH
29691806
343PhosphorylationDCTNLPTSKTAAAVA
CCCCCCCHHHHHHHH
23401153
345PhosphorylationTNLPTSKTAAAVAAQ
CCCCCHHHHHHHHHH
28857561
359PhosphorylationQSGILDRTISVIMKN
HCCCHHHHHHHHCCC
27080861
361PhosphorylationGILDRTISVIMKNQT
CCHHHHHHHHCCCCC
23312004
365MalonylationRTISVIMKNQTPTKK
HHHHHHCCCCCCCCC
26320211
365SuccinylationRTISVIMKNQTPTKK
HHHHHHCCCCCCCCC
27452117
3712-HydroxyisobutyrylationMKNQTPTKKYDGYTS
CCCCCCCCCCCCCCC
-
372AcetylationKNQTPTKKYDGYTSC
CCCCCCCCCCCCCCC
27452117
3722-HydroxyisobutyrylationKNQTPTKKYDGYTSC
CCCCCCCCCCCCCCC
-
373PhosphorylationNQTPTKKYDGYTSCP
CCCCCCCCCCCCCCC
26552605
376PhosphorylationPTKKYDGYTSCPLVT
CCCCCCCCCCCCCCC
26552605
377PhosphorylationTKKYDGYTSCPLVTG
CCCCCCCCCCCCCCC
26552605
378PhosphorylationKKYDGYTSCPLVTGY
CCCCCCCCCCCCCCC
26552605
383PhosphorylationYTSCPLVTGYNRVIL
CCCCCCCCCCCEEEE
26552605
385PhosphorylationSCPLVTGYNRVILAE
CCCCCCCCCEEEEEE
26552605
395PhosphorylationVILAEFDYKAEPLET
EEEEECCCCCCCCCC
-
408PhosphorylationETFPFDQSKERLSMY
CCCCCCCCHHHHHHH
24719451
409UbiquitinationTFPFDQSKERLSMYL
CCCCCCCHHHHHHHH
-
4092-HydroxyisobutyrylationTFPFDQSKERLSMYL
CCCCCCCHHHHHHHH
-
413PhosphorylationDQSKERLSMYLMKAD
CCCHHHHHHHHHHHC
20068231
415PhosphorylationSKERLSMYLMKADLM
CHHHHHHHHHHHCHH
20068231
426PhosphorylationADLMPFLYWNMMLRG
HCHHHHHHHHHHHCC
20068231
443MalonylationGGPAFLRKLFHLGMS
CHHHHHHHHHHCCCC
26320211
4432-HydroxyisobutyrylationGGPAFLRKLFHLGMS
CHHHHHHHHHHCCCC
-
443AcetylationGGPAFLRKLFHLGMS
CHHHHHHHHHHCCCC
25825284
450PhosphorylationKLFHLGMS-------
HHHHCCCC-------
23312004

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 SQOR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SQOR_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 SQOR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SQOR_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SQOR_HUMAN

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Related Literatures of Post-Translational Modification

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