OXR1_HUMAN - dbPTM
OXR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OXR1_HUMAN
UniProt AC Q8N573
Protein Name Oxidation resistance protein 1
Gene Name OXR1
Organism Homo sapiens (Human).
Sequence Length 874
Subcellular Localization Mitochondrion .
Protein Description May be involved in protection from oxidative damage..
Protein Sequence MTKDKNSPGLKKKSQSVDINAPGFNPLAGAGKQTPQASKPPAPKTPIIEEEQNNAANTQKHPSRRSELKRFYTIDTGQKKTLDKKDGRRMSFQKPKGTIEYTVESRDSLNSIALKFDTTPNELVQLNKLFSRAVVTGQVLYVPDPEYVSSVESSPSLSPVSPLSPTSSEAEFDKTTNPDVHPTEATPSSTFTGIRPARVVSSTSEEEEAFTEKFLKINCKYITSGKGTVSGVLLVTPNNIMFDPHKNDPLVQENGCEEYGIMCPMEEVMSAAMYKEILDSKIKESLPIDIDQLSGRDFCHSKKMTGSNTEEIDSRIRDAGNDSASTAPRSTEESLSEDVFTESELSPIREELVSSDELRQDKSSGASSESVQTVNQAEVESLTVKSESTGTPGHLRSDTEHSTNEVGTLCHKTDLNNLEMAIKEDQIADNFQGISGPKEDSTSIKGNSDQDSFLHENSLHQEESQKENMPCGETAEFKQKQSVNKGKQGKEQNQDSQTEAEELRKLWKTHTMQQTKQQRENIQQVSQKEAKHKITSADGHIESSALLKEKQRHRLHKFLCLRVGKPMRKTFVSQASATMQQYAQRDKKHEYWFAVPQERTDHLYAFFIQWSPEIYAEDTGEYTREPGFIVVKKIEESETIEDSSNQAAAREWEVVSVAEYHRRIDALNTEELRTLCRRLQITTREDINSKQVATVKADLESESFRPNLSDPSELLLPDQIEKLTKHLPPRTIGYPWTLVYGTGKHGTSLKTLYRTMTGLDTPVLMVIKDSDGQVFGALASEPLKVSDGFYGTGETFVFTFCPEFEVFKWTGDNMFFIKGDMDSLAFGGGGGEFALWLDGDLYHGRSHSCKTFGNRTLSKKEDFFIQDIEIWAFE
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
2Phosphorylation------MTKDKNSPG
------CCCCCCCCC
48.2029759185
2 (in isoform 5)Phosphorylation-48.2027251275
2 (in isoform 8)Phosphorylation-48.2027251275
3 (in isoform 2)Phosphorylation-66.4627642862
3 (in isoform 4)Methylation-66.46-
6 (in isoform 4)Phosphorylation-64.6727762562
6 (in isoform 7)Phosphorylation-64.6727762562
7Phosphorylation-MTKDKNSPGLKKKS
-CCCCCCCCCCCCCC
26.5324719451
13 (in isoform 5)Phosphorylation-52.7429507054
13 (in isoform 8)Phosphorylation-52.7429507054
14PhosphorylationSPGLKKKSQSVDINA
CCCCCCCCCCCCCCC
36.2528857561
15 (in isoform 5)Phosphorylation-57.2529507054
15 (in isoform 8)Phosphorylation-57.2529507054
16PhosphorylationGLKKKSQSVDINAPG
CCCCCCCCCCCCCCC
28.9328857561
16 (in isoform 2)Methylation-28.93-
19UbiquitinationKKSQSVDINAPGFNP
CCCCCCCCCCCCCCC
4.4329967540
20 (in isoform 7)Phosphorylation-35.3027642862
34PhosphorylationLAGAGKQTPQASKPP
CCCCCCCCCCCCCCC
22.3629083192
38PhosphorylationGKQTPQASKPPAPKT
CCCCCCCCCCCCCCC
40.2129083192
52 (in isoform 2)Phosphorylation-52.3223663014
61 (in isoform 2)Phosphorylation-18.7525849741
62 (in isoform 2)Phosphorylation-36.2423663014
68 (in isoform 2)Phosphorylation-5.2023663014
72PhosphorylationRSELKRFYTIDTGQK
HHHHHEEEECCCCCC
13.5628060719
73PhosphorylationSELKRFYTIDTGQKK
HHHHEEEECCCCCCC
15.0628060719
76PhosphorylationKRFYTIDTGQKKTLD
HEEEECCCCCCCEEC
37.3528270605
81PhosphorylationIDTGQKKTLDKKDGR
CCCCCCCEECCCCCC
47.4228270605
83 (in isoform 2)Phosphorylation-62.28-
91PhosphorylationKKDGRRMSFQKPKGT
CCCCCCCEEECCCCE
23.7823401153
92UbiquitinationKDGRRMSFQKPKGTI
CCCCCCEEECCCCEE
8.7129967540
102PhosphorylationPKGTIEYTVESRDSL
CCCEEEEEECCHHHC
12.6627251275
105PhosphorylationTIEYTVESRDSLNSI
EEEEEECCHHHCCEE
36.7327251275
108PhosphorylationYTVESRDSLNSIALK
EEECCHHHCCEEEEE
28.4827251275
111PhosphorylationESRDSLNSIALKFDT
CCHHHCCEEEEEECC
17.9627251275
112PhosphorylationSRDSLNSIALKFDTT
CHHHCCEEEEEECCC
5.1818669648
113PhosphorylationRDSLNSIALKFDTTP
HHHCCEEEEEECCCH
12.4318669648
114PhosphorylationDSLNSIALKFDTTPN
HHCCEEEEEECCCHH
5.6018669648
115PhosphorylationSLNSIALKFDTTPNE
HCCEEEEEECCCHHH
31.9718669648
118PhosphorylationSIALKFDTTPNELVQ
EEEEEECCCHHHHHH
47.4927251275
119PhosphorylationIALKFDTTPNELVQL
EEEEECCCHHHHHHH
26.4321815630
119UbiquitinationIALKFDTTPNELVQL
EEEEECCCHHHHHHH
26.4329967540
149PhosphorylationVPDPEYVSSVESSPS
ECCHHHHCCCCCCCC
27.9727251275
150PhosphorylationPDPEYVSSVESSPSL
CCHHHHCCCCCCCCC
21.6227251275
153PhosphorylationEYVSSVESSPSLSPV
HHHCCCCCCCCCCCC
45.4527251275
154PhosphorylationYVSSVESSPSLSPVS
HHCCCCCCCCCCCCC
12.6627251275
156PhosphorylationSSVESSPSLSPVSPL
CCCCCCCCCCCCCCC
43.3527251275
158PhosphorylationVESSPSLSPVSPLSP
CCCCCCCCCCCCCCC
27.8227251275
161PhosphorylationSPSLSPVSPLSPTSS
CCCCCCCCCCCCCCC
24.4127251275
164PhosphorylationLSPVSPLSPTSSEAE
CCCCCCCCCCCCHHH
29.5227251275
166PhosphorylationPVSPLSPTSSEAEFD
CCCCCCCCCCHHHCC
41.3228348404
167PhosphorylationVSPLSPTSSEAEFDK
CCCCCCCCCHHHCCC
29.5728348404
168PhosphorylationSPLSPTSSEAEFDKT
CCCCCCCCHHHCCCC
43.2228348404
176PhosphorylationEAEFDKTTNPDVHPT
HHHCCCCCCCCCCCC
50.96-
183PhosphorylationTNPDVHPTEATPSST
CCCCCCCCCCCCCCC
24.3128348404
186PhosphorylationDVHPTEATPSSTFTG
CCCCCCCCCCCCCCC
19.9225159151
190PhosphorylationTEATPSSTFTGIRPA
CCCCCCCCCCCCEEE
29.56-
192PhosphorylationATPSSTFTGIRPARV
CCCCCCCCCCEEEEE
31.61-
193 (in isoform 2)Phosphorylation-15.09-
194PhosphorylationPSSTFTGIRPARVVS
CCCCCCCCEEEEEEC
4.3033259812
194 (in isoform 2)Phosphorylation-4.30-
195 (in isoform 2)Phosphorylation-21.85-
196PhosphorylationSTFTGIRPARVVSST
CCCCCCEEEEEECCC
23.6132645325
196 (in isoform 2)Phosphorylation-23.61-
201PhosphorylationIRPARVVSSTSEEEE
CEEEEEECCCCHHHH
25.6629255136
202PhosphorylationRPARVVSSTSEEEEA
EEEEEECCCCHHHHH
25.0929255136
203PhosphorylationPARVVSSTSEEEEAF
EEEEECCCCHHHHHH
32.4329255136
204PhosphorylationARVVSSTSEEEEAFT
EEEECCCCHHHHHHH
44.9829255136
205UbiquitinationRVVSSTSEEEEAFTE
EEECCCCHHHHHHHH
70.3029967540
211PhosphorylationSEEEEAFTEKFLKIN
CHHHHHHHHHHHEEE
45.3623927012
212UbiquitinationEEEEAFTEKFLKINC
HHHHHHHHHHHEEEC
35.0429967540
213UbiquitinationEEEAFTEKFLKINCK
HHHHHHHHHHEEECE
53.6029967540
285PhosphorylationLDSKIKESLPIDIDQ
HCHHHHHCCCCCHHH
34.1523312004
294PhosphorylationPIDIDQLSGRDFCHS
CCCHHHCCCCCCCCC
26.5823312004
301PhosphorylationSGRDFCHSKKMTGSN
CCCCCCCCCCCCCCC
34.8423312004
305PhosphorylationFCHSKKMTGSNTEEI
CCCCCCCCCCCHHHH
46.4628450419
307PhosphorylationHSKKMTGSNTEEIDS
CCCCCCCCCHHHHHH
31.2625159151
309PhosphorylationKKMTGSNTEEIDSRI
CCCCCCCHHHHHHHH
36.3728450419
314PhosphorylationSNTEEIDSRIRDAGN
CCHHHHHHHHHHCCC
34.9623090842
323PhosphorylationIRDAGNDSASTAPRS
HHHCCCCCCCCCCCC
28.2829496963
330PhosphorylationSASTAPRSTEESLSE
CCCCCCCCCCHHHCC
38.8328102081
331PhosphorylationASTAPRSTEESLSED
CCCCCCCCCHHHCCC
45.0828102081
334PhosphorylationAPRSTEESLSEDVFT
CCCCCCHHHCCCCCC
30.8526055452
336PhosphorylationRSTEESLSEDVFTES
CCCCHHHCCCCCCHH
40.8228348404
341PhosphorylationSLSEDVFTESELSPI
HHCCCCCCHHHCHHH
38.1528102081
343PhosphorylationSEDVFTESELSPIRE
CCCCCCHHHCHHHHH
40.5626657352
346PhosphorylationVFTESELSPIREELV
CCCHHHCHHHHHHHC
17.7718510355
346 (in isoform 2)Phosphorylation-17.77-
354PhosphorylationPIREELVSSDELRQD
HHHHHHCCCHHHHCC
44.7018510355
355PhosphorylationIREELVSSDELRQDK
HHHHHCCCHHHHCCC
27.8529255136
363PhosphorylationDELRQDKSSGASSES
HHHHCCCCCCCCCHH
42.1524076635
364PhosphorylationELRQDKSSGASSESV
HHHCCCCCCCCCHHC
44.0824076635
367PhosphorylationQDKSSGASSESVQTV
CCCCCCCCCHHCEEC
37.8628348404
368PhosphorylationDKSSGASSESVQTVN
CCCCCCCCHHCEECC
33.1028348404
370PhosphorylationSSGASSESVQTVNQA
CCCCCCHHCEECCHH
22.8225307156
373PhosphorylationASSESVQTVNQAEVE
CCCHHCEECCHHHEE
21.1924076635
381PhosphorylationVNQAEVESLTVKSES
CCHHHEEEEEEEECC
34.2227251275
386PhosphorylationVESLTVKSESTGTPG
EEEEEEEECCCCCCC
32.2327251275
388PhosphorylationSLTVKSESTGTPGHL
EEEEEECCCCCCCCC
38.9525159151
389PhosphorylationLTVKSESTGTPGHLR
EEEEECCCCCCCCCC
40.8125849741
391PhosphorylationVKSESTGTPGHLRSD
EEECCCCCCCCCCCC
26.6225159151
397PhosphorylationGTPGHLRSDTEHSTN
CCCCCCCCCCCCCCC
56.0723312004
399PhosphorylationPGHLRSDTEHSTNEV
CCCCCCCCCCCCCCH
36.5228348404
402PhosphorylationLRSDTEHSTNEVGTL
CCCCCCCCCCCHHHH
27.0528348404
403PhosphorylationRSDTEHSTNEVGTLC
CCCCCCCCCCHHHHC
36.9928348404
435PhosphorylationADNFQGISGPKEDST
HHCCCCCCCCCCCCC
56.7323898821
437PhosphorylationNFQGISGPKEDSTSI
CCCCCCCCCCCCCCC
30.0317525332
440 (in isoform 2)Phosphorylation-64.44-
441PhosphorylationISGPKEDSTSIKGNS
CCCCCCCCCCCCCCC
25.7522496350
442PhosphorylationSGPKEDSTSIKGNSD
CCCCCCCCCCCCCCC
46.9526657352
443PhosphorylationGPKEDSTSIKGNSDQ
CCCCCCCCCCCCCCH
26.6723917254
448PhosphorylationSTSIKGNSDQDSFLH
CCCCCCCCCHHHHHC
45.3720068231
450 (in isoform 2)Phosphorylation-48.33-
452PhosphorylationKGNSDQDSFLHENSL
CCCCCHHHHHCCCCC
24.8725849741
458PhosphorylationDSFLHENSLHQEESQ
HHHHCCCCCCHHHHH
25.0125849741
464PhosphorylationNSLHQEESQKENMPC
CCCCHHHHHHHCCCC
45.8820068231
474PhosphorylationENMPCGETAEFKQKQ
HCCCCCCHHHHHHHH
19.4430631047
482PhosphorylationAEFKQKQSVNKGKQG
HHHHHHHHHCCCCCC
34.39-
496PhosphorylationGKEQNQDSQTEAEEL
CCCCCCCHHHHHHHH
29.2728348404
498PhosphorylationEQNQDSQTEAEELRK
CCCCCHHHHHHHHHH
40.9123312004
518 (in isoform 2)Phosphorylation-57.10-
523UbiquitinationKQQRENIQQVSQKEA
HHHHHHHHHHHHHHH
49.5630230243
526PhosphorylationRENIQQVSQKEAKHK
HHHHHHHHHHHHHHH
31.0625262027
530UbiquitinationQQVSQKEAKHKITSA
HHHHHHHHHHHCCCC
26.7030230243
531UbiquitinationQVSQKEAKHKITSAD
HHHHHHHHHHCCCCC
46.6630230243
535PhosphorylationKEAKHKITSADGHIE
HHHHHHCCCCCCCHH
23.7523312004
536PhosphorylationEAKHKITSADGHIES
HHHHHCCCCCCCHHH
28.0323312004
544PhosphorylationADGHIESSALLKEKQ
CCCCHHHHHHHHHHH
15.3328555341
573PhosphorylationPMRKTFVSQASATMQ
CCHHHHHHHHHHHHH
18.8128555341
576PhosphorylationKTFVSQASATMQQYA
HHHHHHHHHHHHHHH
19.3528857561
622PhosphorylationYAEDTGEYTREPGFI
EECCCCCCCCCCCEE
16.6720736484
669PhosphorylationRRIDALNTEELRTLC
HHHHCCCHHHHHHHH
31.52-
690UbiquitinationTREDINSKQVATVKA
CHHHCCCCEEEEEEE
44.28-
715UbiquitinationLSDPSELLLPDQIEK
CCCHHHHCCHHHHHH
5.9929967540
722UbiquitinationLLPDQIEKLTKHLPP
CCHHHHHHHHCCCCC
64.1929967540
749UbiquitinationTGKHGTSLKTLYRTM
CCCCCCCHHHHHHHH
5.0229967540
750UbiquitinationGKHGTSLKTLYRTMT
CCCCCCHHHHHHHHC
35.9329967540
751PhosphorylationKHGTSLKTLYRTMTG
CCCCCHHHHHHHHCC
34.0225599653
753PhosphorylationGTSLKTLYRTMTGLD
CCCHHHHHHHHCCCC
14.8525599653
755PhosphorylationSLKTLYRTMTGLDTP
CHHHHHHHHCCCCCC
12.9122210691
757PhosphorylationKTLYRTMTGLDTPVL
HHHHHHHCCCCCCEE
33.7025599653
761PhosphorylationRTMTGLDTPVLMVIK
HHHCCCCCCEEEEEE
21.9722210691
851PhosphorylationGRSHSCKTFGNRTLS
CCCCCCCCCCCCCCC
40.8921406692
856PhosphorylationCKTFGNRTLSKKEDF
CCCCCCCCCCCCCCE
39.1121406692
858PhosphorylationTFGNRTLSKKEDFFI
CCCCCCCCCCCCEEE
40.8621406692

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 OXR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OXR1_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 OXR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS35_HUMANVPS35physical
22863883

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 OXR1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-202 ANDSER-204, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-202, ANDMASS SPECTROMETRY.

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