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O95747 (OXSR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase OSR1

EC=2.7.11.1
Alternative name(s):
Oxidative stress-responsive 1 protein
Gene names
Name:OXSR1
Synonyms:KIAA1101, OSR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton. Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.6

Cofactor

Magnesium. Ref.6

Enzyme regulation

By autophosphorylation on threonine. Ref.6

Subunit structure

Binds to and phosphorylates PAK1. Interacts with chloride channel proteins SLC12A6 isoform 2 SLC12A1 and SLC12A2 but not with SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules that initiate the cellular response to environmental stress. Binds to and phosphorylates RELL1, RELL2 AND RELT. Ref.6 Ref.7 UniProtKB Q6P9R2

Subcellular location

Cytoplasm Ref.17.

Tissue specificity

Ubiquitously expressed in all tissue examined. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAP97192.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA83053.2 differs from that shown. Reason: Frameshift at position 63.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 527526Serine/threonine-protein kinase OSR1
PRO_0000086456

Regions

Domain17 – 291275Protein kinase
Nucleotide binding23 – 319ATP By similarity UniProtKB Q9Z1W9

Sites

Active site1461Proton acceptor By similarity UniProtKB Q9Z1W9
Binding site461ATP Ref.6

Amino acid modifications

Modified residue21N-acetylserine
Modified residue3391Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16
Modified residue3471Phosphoserine Ref.13
Modified residue4271Phosphoserine Ref.9 Ref.10 Ref.14

Natural variations

Natural variant3041T → I. Ref.1 Ref.3 Ref.19
Corresponds to variant rs6599079 [ dbSNP | Ensembl ].
VAR_023232
Natural variant4251S → T. Ref.3
Corresponds to variant rs35295772 [ dbSNP | Ensembl ].
VAR_025181
Natural variant4331P → S in a metastatic melanoma sample; somatic mutation. Ref.19
VAR_040969

Experimental info

Mutagenesis461K → A: Loss of autophosphorylation and kinase activity. Ref.6 Ref.7
Mutagenesis461K → M: Loss of RELT, RELL1 and RELL2 phosphorylation. Retention of some autophosphorylation activity may be due to complex formation with other endogenous kinases in the assay. Ref.6 Ref.7
Sequence conflict3161K → R in AAP97192. Ref.5
Sequence conflict3251S → G in AAP97192. Ref.5
Sequence conflict3631K → R in AAP97192. Ref.5

Secondary structure

.......................................................................... 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95747 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: B46EC934E95A3A1F

FASTA52758,022
        10         20         30         40         50         60 
MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK EKVAIKRINL EKCQTSMDEL 

        70         80         90        100        110        120 
LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIVAK GEHKSGVLDE 

       130        140        150        160        170        180 
STIATILREV LEGLEYLHKN GQIHRDVKAG NILLGEDGSV QIADFGVSAF LATGGDITRN 

       190        200        210        220        230        240 
KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL 

       250        260        270        280        290        300 
QNDPPSLETG VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL 

       310        320        330        340        350        360 
QEKTLQRAPT ISERAKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG KAAISQLRSP 

       370        380        390        400        410        420 
RVKESISNSE LFPTTDPVGT LLQVPEQISA HLPQPAGQIA TQPTQVSLPP TAEPAKTAQA 

       430        440        450        460        470        480 
LSSGSGSQET KIPISLVLRL RNSKKELNDI RFEFTPGRDT AEGVSQELIS AGLVDGRDLV 

       490        500        510        520 
IVAANLQKIV EEPQSNRSVT FKLASGVEGS DIPDDGKLIG FAQLSIS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a novel serine threonine kinase gene on chromosome 3p22-21.3."
Tamari M., Daigo Y., Nakamura Y.
J. Hum. Genet. 44:116-120(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT ILE-304.
Tissue: Skeletal muscle.
[2]"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."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]NIEHS SNPs program
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-304 AND THR-425.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Cloning and characterization of a novel human cDNA homologous to human DCHT mRNA."
Ding J.B., Yu L., Gong R.M., Mao N.H., Han X.F., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-527.
[6]"Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily."
Chen W., Yazicioglu M., Cobb M.H.
J. Biol. Chem. 279:11129-11136(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, AUTOPHOSPHORYLATION, ENZYME REGULATION, INTERACTION WITH PAK1, MUTAGENESIS OF LYS-46.
[7]"Identification of RELT homologues that associate with RELT and are phosphorylated by OSR1."
Cusick J.K., Xu L.-G., Bin L.-H., Han K.-J., Shu H.-B.
Biochem. Biophys. Res. Commun. 340:535-543(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RELL1; RELL2 AND RELT, MUTAGENESIS OF LYS-46.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Systematic validation of antibody binding and protein subcellular localization using siRNA and confocal microscopy."
Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M., Lundberg E.
J. Proteomics 75:2236-2251(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , 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 D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-304 AND SER-433.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017642 mRNA. Translation: BAA75674.1.
AB029024 mRNA. Translation: BAA83053.2. Frameshift.
DQ201638 Genomic DNA. Translation: ABA27097.1.
BC008726 mRNA. Translation: AAH08726.1.
AF087893 mRNA. Translation: AAP97192.1. Different initiation.
RefSeqNP_005100.1. NM_005109.2.
UniGeneHs.475970.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V3SX-ray1.70A/B433-527[»]
2VWIX-ray2.15A/B/C/D1-303[»]
3DAKX-ray2.25A/B/C/D6-295[»]
ProteinModelPortalO95747.
SMRO95747. Positions 7-358, 433-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115269. 145 interactions.
IntActO95747. 10 interactions.
MINTMINT-5207465.
STRING9606.ENSP00000311713.

Chemistry

BindingDBO95747.
ChEMBLCHEMBL1163104.
GuidetoPHARMACOLOGY2132.

PTM databases

PhosphoSiteO95747.

Proteomic databases

PaxDbO95747.
PeptideAtlasO95747.
PRIDEO95747.

Protocols and materials databases

DNASU9943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311806; ENSP00000311713; ENSG00000172939.
GeneID9943.
KEGGhsa:9943.
UCSCuc003chy.3. human.

Organism-specific databases

CTD9943.
GeneCardsGC03P038183.
HGNCHGNC:8508. OXSR1.
HPACAB017181.
HPA008237.
MIM604046. gene.
neXtProtNX_O95747.
PharmGKBPA134973207.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000234204.
HOVERGENHBG108518.
InParanoidO95747.
KOK08835.
OMAEPQANRS.
PhylomeDBO95747.
TreeFamTF105339.

Enzyme and pathway databases

SignaLinkO95747.

Gene expression databases

ArrayExpressO95747.
BgeeO95747.
CleanExHS_OSR1.
HS_OXSR1.
GenevestigatorO95747.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR024678. Kinase_OSR1/WNK_CCT.
IPR028749. Oxsr1.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PANTHERPTHR24361:SF202. PTHR24361:SF202. 1 hit.
PfamPF12202. OSR1_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOXSR1. human.
EvolutionaryTraceO95747.
GeneWikiOXSR1.
GenomeRNAi9943.
NextBio37516.
PROO95747.
SOURCESearch...

Entry information

Entry nameOXSR1_HUMAN
AccessionPrimary (citable) accession number: O95747
Secondary accession number(s): Q3LR53, Q7Z501, Q9UPQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: May 1, 1999
Last modified: March 19, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM