OXSR1_HUMAN - dbPTM
OXSR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OXSR1_HUMAN
UniProt AC O95747
Protein Name Serine/threonine-protein kinase OSR1
Gene Name OXSR1 {ECO:0000312|HGNC:HGNC:8508}
Organism Homo sapiens (Human).
Sequence Length 527
Subcellular Localization Cytoplasm .
Protein Description Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton..
Protein Sequence MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKTLQRAPTISERAKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSPRVKESISNSELFPTTDPVGTLLQVPEQISAHLPQPAGQIATQPTQVSLPPTAEPAKTAQALSSGSGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS
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------MSEDSSALP
------CCCCCCCCC		50.5420873877
2Acetylation------MSEDSSALP
------CCCCCCCCC		50.5422223895
5Phosphorylation---MSEDSSALPWSI
---CCCCCCCCCCCC		17.2920873877
6Phosphorylation--MSEDSSALPWSIN
--CCCCCCCCCCCCC		46.2620873877
42AcetylationYCAPKKEKVAIKRIN
HHCCCCCCEEEEECC		45.9388637
46AcetylationKKEKVAIKRINLEKC
CCCCEEEEECCHHHH		37.1788635
52UbiquitinationIKRINLEKCQTSMDE
EEECCHHHHCCCHHH		34.5130230243
55PhosphorylationINLEKCQTSMDELLK
CCHHHHCCCHHHHHH		35.1723917254
56PhosphorylationNLEKCQTSMDELLKE
CHHHHCCCHHHHHHH		9.8123917254
81UbiquitinationNIVSYYTSFVVKDEL
CHHHHEEEEEECHHH		10.4222817900
105UbiquitinationGSVLDIIKHIVAKGE
CCHHHHHHHHHHCCC		27.8429967540
110UbiquitinationIIKHIVAKGEHKSGV
HHHHHHHCCCCCCCC		54.6729967540
114UbiquitinationIVAKGEHKSGVLDES
HHHCCCCCCCCCCHH		44.6029967540
139AcetylationEGLEYLHKNGQIHRD
HHHHHHHHCCCCCCC		61.2425953088
139UbiquitinationEGLEYLHKNGQIHRD
HHHHHHHHCCCCCCC		61.2429967540
148UbiquitinationGQIHRDVKAGNILLG
CCCCCCCCCCCEEEC		55.6622817900
178PhosphorylationLATGGDITRNKVRKT
EEECCCCCCCCCCCC		32.69-
184UbiquitinationITRNKVRKTFVGTPC
CCCCCCCCCCCCCCC		49.6730230243
185PhosphorylationTRNKVRKTFVGTPCW
CCCCCCCCCCCCCCC		17.0022322096
189PhosphorylationVRKTFVGTPCWMAPE
CCCCCCCCCCCCCHH		15.2423403867
201UbiquitinationAPEVMEQVRGYDFKA
CHHHHHHHCCCCCCH		3.0622817900
227PhosphorylationLATGAAPYHKYPPMK
HHHCCCCCCCCCCCE		13.2520044836
230PhosphorylationGAAPYHKYPPMKVLM
CCCCCCCCCCCEEEE		10.1520044836
253UbiquitinationSLETGVQDKEMLKKY
CCCCCCCCHHHHHHH		46.6124816145
254UbiquitinationLETGVQDKEMLKKYG
CCCCCCCHHHHHHHH		28.1229967540
260PhosphorylationDKEMLKKYGKSFRKM
CHHHHHHHHHHHHHH		28.3526074081
263PhosphorylationMLKKYGKSFRKMISL
HHHHHHHHHHHHHHH		26.3926074081
266MalonylationKYGKSFRKMISLCLQ
HHHHHHHHHHHHHHC		38.2826320211
269PhosphorylationKSFRKMISLCLQKDP
HHHHHHHHHHHCCCH		14.9926074081
278AcetylationCLQKDPEKRPTAAEL
HHCCCHHHCCCHHHH		69.9025953088
278UbiquitinationCLQKDPEKRPTAAEL
HHCCCHHHCCCHHHH		69.9029967540
287MethylationPTAAELLRHKFFQKA
CCHHHHHHHHHHHHH		43.50115486091
289AcetylationAAELLRHKFFQKAKN
HHHHHHHHHHHHHCC		41.2526051181
297MethylationFFQKAKNKEFLQEKT
HHHHHCCHHHHHHHH		49.49115974491
303UbiquitinationNKEFLQEKTLQRAPT
CHHHHHHHHHHCCCC		41.3932015554
304PhosphorylationKEFLQEKTLQRAPTI
HHHHHHHHHHCCCCH		27.6323882029
310PhosphorylationKTLQRAPTISERAKK
HHHHCCCCHHHHHHH		35.8323911959
312PhosphorylationLQRAPTISERAKKVR
HHCCCCHHHHHHHHH		24.4129514088
324PhosphorylationKVRRVPGSSGRLHKT
HHHCCCCCCCCCEEC		24.4525159151
325PhosphorylationVRRVPGSSGRLHKTE
HHCCCCCCCCCEECC		33.5725159151
331PhosphorylationSSGRLHKTEDGGWEW
CCCCCEECCCCCCCC		28.6722167270
339PhosphorylationEDGGWEWSDDEFDEE
CCCCCCCCCCCCCCC		24.5419664994
347PhosphorylationDDEFDEESEEGKAAI
CCCCCCCCHHHHHHH		38.6122167270
355PhosphorylationEEGKAAISQLRSPRV
HHHHHHHHHHCCHHH		20.5925159151
359PhosphorylationAAISQLRSPRVKESI
HHHHHHCCHHHHHCC		26.1729255136
365PhosphorylationRSPRVKESISNSELF
CCHHHHHCCCCCCCC		26.1221406692
367PhosphorylationPRVKESISNSELFPT
HHHHHCCCCCCCCCC		43.5121406692
369PhosphorylationVKESISNSELFPTTD
HHHCCCCCCCCCCCC		28.9629496963
374PhosphorylationSNSELFPTTDPVGTL
CCCCCCCCCCCCCCH		36.1721406692
375PhosphorylationNSELFPTTDPVGTLL
CCCCCCCCCCCCCHH		38.2521406692
378UbiquitinationLFPTTDPVGTLLQVP
CCCCCCCCCCHHCCC		11.5724816145
417PhosphorylationPTAEPAKTAQALSSG
CCCCCCHHHHHHHCC		26.5523403867
417O-linked_GlycosylationPTAEPAKTAQALSSG
CCCCCCHHHHHHHCC		26.55OGP
422PhosphorylationAKTAQALSSGSGSQE
CHHHHHHHCCCCCCC		35.3528176443
423PhosphorylationKTAQALSSGSGSQET
HHHHHHHCCCCCCCC		37.5228176443
425PhosphorylationAQALSSGSGSQETKI
HHHHHCCCCCCCCCC		36.9025159151
427PhosphorylationALSSGSGSQETKIPI
HHHCCCCCCCCCCCH		26.9225159151
430PhosphorylationSGSGSQETKIPISLV
CCCCCCCCCCCHHHE		27.0025159151
435PhosphorylationQETKIPISLVLRLRN
CCCCCCHHHEEHHCC		13.6830108239
443PhosphorylationLVLRLRNSKKELNDI
HEEHHCCCCCHHCCC		38.3824719451
444MethylationVLRLRNSKKELNDIR
EEHHCCCCCHHCCCE		54.54116251977
445UbiquitinationLRLRNSKKELNDIRF
EHHCCCCCHHCCCEE		68.2224816145
451MethylationKKELNDIRFEFTPGR
CCHHCCCEEEECCCC		28.10-
486UbiquitinationLVIVAANLQKIVEEP
EEEEEECHHHHHCCC		4.7424816145
495O-linked_GlycosylationKIVEEPQSNRSVTFK
HHHCCCCCCCCEEEE		44.9530620550
498UbiquitinationEEPQSNRSVTFKLAS
CCCCCCCCEEEEECC		29.7424816145
510PhosphorylationLASGVEGSDIPDDGK
ECCCCCCCCCCCCCC		20.8925159151
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
185TPhosphorylationKinaseWNK1Q9H4A3
PSP
325SPhosphorylationKinaseWNK1Q9H4A3
PSP
339SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OXSR1_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 OXSR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_HUMANTGFBR1physical
15761153
TGFR2_HUMANTGFBR2physical
15761153
A4_HUMANAPPphysical
21832049
RNH2C_HUMANRNASEH2Cphysical
22939629
SLFN5_HUMANSLFN5physical
22939629
AN32A_HUMANANP32Aphysical
22863883
RL17_HUMANRPL17physical
22863883
UBP5_HUMANUSP5physical
22863883
AIFM1_HUMANAIFM1physical
23455922
MD2L1_HUMANMAD2L1physical
23455922
RELL2_HUMANRELL2physical
25416956
THUM1_HUMANTHUMPD1physical
26344197
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 OXSR1_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-339 AND SER-347, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-427, ANDMASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, 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-339 AND SER-427, ANDMASS 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-427, 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-339, AND MASSSPECTROMETRY.

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