Serine/threonine-protein kinase OSR1

Details

Name

Serine/threonine-protein kinase OSR1

Synonyms

• 2.7.11.1
• KIAA1101
• OSR1
• Oxidative stress-responsive 1 protein

Gene Name

OXSR1

Organism

Humans

Amino acid sequence

>lcl|BSEQ0051886|Serine/threonine-protein kinase OSR1
MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDEL
LKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDE
STIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRN
KVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTL
QNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFL
QEKTLQRAPTISERAKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSP
RVKESISNSELFPTTDPVGTLLQVPEQISAHLPQPAGQIATQPTQVSLPPTAEPAKTAQA
LSSGSGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLV
IVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS

Number of residues

527

Molecular Weight

58021.7

Theoretical pI

Not Available

GO Classification

Functions

ATP binding / identical protein binding / magnesium ion binding / protein serine/threonine kinase activity / signal transducer, downstream of receptor, with serine/threonine kinase activity

Processes

activation of protein kinase activity / cellular hypotonic response / intracellular signal transduction / negative regulation of potassium ion transmembrane transporter activity / peptidyl-threonine phosphorylation / protein phosphorylation / regulation of apoptotic process / regulation of mitotic cell cycle / response to oxidative stress / signal transduction by protein phosphorylation / stress-activated protein kinase signaling cascade

Components

cytoplasm / cytosol / extracellular exosome

General Function

Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton.

Specific Function

Atp binding

Pfam Domain Function

• Pkinase (PF00069)
• OSR1_C (PF12202)

Transmembrane Regions

Not Available

Cellular Location

Cytoplasm

Gene sequence

>lcl|BSEQ0051887|Serine/threonine-protein kinase OSR1 (OXSR1)
ATGTCCGAGGACTCGAGCGCCCTGCCCTGGTCCATCAACAGGGACGATTACGAGCTGCAG
GAGGTGATCGGGAGTGGAGCAACTGCTGTAGTCCAAGCAGCTTATTGTGCCCCTAAAAAG
GAGAAAGTGGCAATCAAACGGATAAACCTTGAGAAATGTCAAACTAGCATGGATGAACTC
CTGAAAGAAATTCAAGCCATGAGTCAATGCCATCATCCTAATATTGTATCTTACTACACA
TCTTTTGTGGTAAAAGATGAGCTGTGGCTTGTCATGAAGCTGCTAAGTGGAGGTTCTGTT
CTGGATATTATTAAGCACATTGTGGCAAAAGGGGAACACAAAAGTGGAGTCCTAGATGAA
TCTACCATTGCTACGATACTCCGAGAAGTACTGGAAGGGCTGGAATATCTGCATAAAAAT
GGACAGATCCACAGAGATGTGAAAGCTGGAAACATTCTTCTTGGAGAAGATGGCTCAGTA
CAGATTGCAGACTTTGGGGTTAGTGCTTTTTTAGCAACTGGTGGTGATATTACCCGAAAT
AAAGTGAGAAAGACCTTTGTTGGCACCCCTTGTTGGATGGCACCTGAAGTTATGGAACAG
GTCCGTGGTTATGATTTCAAAGCTGATATTTGGAGTTTTGGAATTACAGCAATTGAATTG
GCTACAGGGGCGGCTCCTTATCATAAATATCCACCAATGAAGGTTTTAATGCTGACACTG
CAGAACGATCCTCCTTCTTTGGAAACTGGTGTTCAAGATAAAGAAATGCTGAAAAAATAT
GGAAAATCATTTAGAAAAATGATTTCATTGTGCCTTCAAAAAGATCCAGAAAAAAGACCA
ACAGCAGCAGAACTATTAAGGCACAAATTTTTCCAGAAAGCAAAGAATAAAGAATTTCTT
CAAGAAAAAACATTGCAGAGAGCACCAACCATTTCTGAAAGAGCAAAAAAGGTTCGGAGA
GTACCAGGTTCCAGTGGGCGTCTTCATAAGACAGAGGATGGAGGCTGGGAGTGGAGTGAT
GATGAATTTGATGAAGAAAGTGAGGAAGGGAAAGCAGCAATTTCACAACTCAGGTCTCCC
CGAGTGAAAGAATCAATATCAAATTCTGAGCTCTTTCCAACAACTGATCCTGTGGGTACT
TTGCTCCAAGTTCCAGAACAGATCTCTGCTCATCTACCTCAGCCAGCTGGGCAGATTGCT
ACACAGCCAACTCAAGTCTCTCTCCCACCCACCGCAGAGCCAGCAAAAACAGCTCAGGCT
TTGTCTTCAGGATCAGGTTCACAAGAAACCAAGATCCCAATCAGTCTAGTACTAAGATTA
AGGAATTCCAAAAAAGAACTAAATGATATTCGATTTGAATTTACTCCTGGGAGAGATACA
GCAGAGGGTGTCTCTCAGGAACTCATTTCTGCTGGCCTGGTCGACGGAAGGGATTTAGTA
ATAGTGGCAGCTAATTTGCAGAAAATTGTGGAAGAACCTCAGTCAAATCGATCTGTCACT
TTCAAACTGGCATCTGGTGTCGAAGGCTCAGATATTCCTGATGATGGTAAACTGATAGGA
TTTGCCCAGCTCAGCATCAGCTAA

Chromosome Location

3

Locus

3p22.2

External Identifiers

Resource	Link
UniProtKB ID	O95747
UniProtKB Entry Name	OXSR1_HUMAN
HGNC ID	HGNC:8508

General References

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2. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [Article]
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4. Chen W, Yazicioglu M, Cobb MH: Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily. J Biol Chem. 2004 Mar 19;279(12):11129-36. Epub 2004 Jan 5. [Article]
5. Cusick JK, Xu LG, Bin LH, Han KJ, Shu HB: Identification of RELT homologues that associate with RELT and are phosphorylated by OSR1. Biochem Biophys Res Commun. 2006 Feb 10;340(2):535-43. Epub 2005 Dec 19. [Article]
6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
7. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [Article]
8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
9. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. doi: 10.1002/pmic.200700884. [Article]
10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
12. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
13. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
14. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
15. Stadler C, Hjelmare M, Neumann B, Jonasson K, Pepperkok R, Uhlen M, Lundberg E: Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy. J Proteomics. 2012 Apr 3;75(7):2236-51. doi: 10.1016/j.jprot.2012.01.030. Epub 2012 Feb 15. [Article]
16. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [Article]
17. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
18. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
19. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB12010	Fostamatinib	approved, investigational	unknown	inhibitor	Details