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O95747

- OXSR1_HUMAN

UniProt

O95747 - OXSR1_HUMAN

Protein

Serine/threonine-protein kinase OSR1

Gene

OXSR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Regulates downstream kinases in response to environmental stress. May also have a function in regulating the actin cytoskeleton.1 Publication1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    By autophosphorylation on threonine.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATP1 PublicationPROSITE-ProRule annotation
    Active sitei146 – 1461Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 319ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. receptor signaling protein serine/threonine kinase activity Source: InterPro

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. peptidyl-threonine phosphorylation Source: BHF-UCL
    3. protein phosphorylation Source: UniProtKB
    4. response to oxidative stress Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiO95747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase OSR1 (EC:2.7.11.1)
    Alternative name(s):
    Oxidative stress-responsive 1 protein
    Gene namesi
    Name:OXSR1Imported
    Synonyms:KIAA1101Imported, OSR1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8508. OXSR1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461K → A: Loss of autophosphorylation and kinase activity. 2 Publications
    Mutagenesisi46 – 461K → 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. 2 Publications

    Organism-specific databases

    PharmGKBiPA134973207.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 527526Serine/threonine-protein kinase OSR1PRO_0000086456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei339 – 3391Phosphoserine6 Publications
    Modified residuei347 – 3471Phosphoserine1 Publication
    Modified residuei427 – 4271Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95747.
    PaxDbiO95747.
    PeptideAtlasiO95747.
    PRIDEiO95747.

    PTM databases

    PhosphoSiteiO95747.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissue examined.1 Publication

    Gene expression databases

    ArrayExpressiO95747.
    BgeeiO95747.
    CleanExiHS_OSR1.
    HS_OXSR1.
    GenevestigatoriO95747.

    Organism-specific databases

    HPAiCAB017181.
    HPA008237.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAB39Q9Y3763EBI-620853,EBI-306905
    SLC12A2P550112EBI-620853,EBI-2801449
    WNK1Q9H4A32EBI-620853,EBI-457907
    WNK4Q96J9211EBI-620853,EBI-766352

    Protein-protein interaction databases

    BioGridi115269. 19 interactions.
    IntActiO95747. 10 interactions.
    MINTiMINT-5207465.
    STRINGi9606.ENSP00000311713.

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 163
    Beta strandi18 – 247
    Beta strandi31 – 355
    Helixi37 – 393
    Beta strandi42 – 465
    Turni50 – 545
    Helixi57 – 6913
    Beta strandi78 – 869
    Beta strandi88 – 936
    Helixi100 – 10910
    Turni110 – 1156
    Helixi120 – 13920
    Helixi149 – 1513
    Beta strandi152 – 1543
    Beta strandi160 – 1623
    Helixi166 – 1705
    Helixi195 – 2028
    Helixi207 – 22216
    Turni226 – 2294
    Helixi232 – 2343
    Helixi235 – 2406
    Turni247 – 2504
    Helixi254 – 2574
    Helixi262 – 27110
    Helixi276 – 2783
    Helixi282 – 2865
    Helixi289 – 2935
    Beta strandi434 – 4418
    Beta strandi447 – 4548
    Turni456 – 4583
    Helixi461 – 47010
    Helixi476 – 4783
    Helixi479 – 49113
    Turni493 – 4953
    Beta strandi497 – 5026
    Helixi504 – 5063
    Beta strandi507 – 5115
    Helixi515 – 5173
    Beta strandi519 – 5268

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V3SX-ray1.70A/B433-527[»]
    2VWIX-ray2.15A/B/C/D1-303[»]
    3DAKX-ray2.25A/B/C/D6-295[»]
    ProteinModelPortaliO95747.
    SMRiO95747. Positions 7-358, 433-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95747.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 291275Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234204.
    HOVERGENiHBG108518.
    InParanoidiO95747.
    KOiK08835.
    OMAiYCIPKKE.
    PhylomeDBiO95747.
    TreeFamiTF105339.

    Family and domain databases

    InterProiIPR011009. 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]
    PANTHERiPTHR24361:SF202. PTHR24361:SF202. 1 hit.
    PfamiPF12202. OSR1_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O95747-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK EKVAIKRINL    50
    EKCQTSMDEL LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV 100
    LDIIKHIVAK GEHKSGVLDE STIATILREV LEGLEYLHKN GQIHRDVKAG 150
    NILLGEDGSV QIADFGVSAF LATGGDITRN KVRKTFVGTP CWMAPEVMEQ 200
    VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL QNDPPSLETG 250
    VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL 300
    QEKTLQRAPT ISERAKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG 350
    KAAISQLRSP RVKESISNSE LFPTTDPVGT LLQVPEQISA HLPQPAGQIA 400
    TQPTQVSLPP TAEPAKTAQA LSSGSGSQET KIPISLVLRL RNSKKELNDI 450
    RFEFTPGRDT AEGVSQELIS AGLVDGRDLV IVAANLQKIV EEPQSNRSVT 500
    FKLASGVEGS DIPDDGKLIG FAQLSIS 527
    Length:527
    Mass (Da):58,022
    Last modified:May 1, 1999 - v1
    Checksum:iB46EC934E95A3A1F
    GO

    Sequence cautioni

    The sequence BAA83053.2 differs from that shown. Reason: Frameshift at position 63.
    The sequence AAP97192.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3161K → R in AAP97192. 1 PublicationCurated
    Sequence conflicti325 – 3251S → G in AAP97192. 1 PublicationCurated
    Sequence conflicti363 – 3631K → R in AAP97192. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti304 – 3041T → I.3 Publications
    Corresponds to variant rs6599079 [ dbSNP | Ensembl ].
    VAR_023232
    Natural varianti425 – 4251S → T.1 Publication
    Corresponds to variant rs35295772 [ dbSNP | Ensembl ].
    VAR_025181
    Natural varianti433 – 4331P → S in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040969

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2675.1.
    RefSeqiNP_005100.1. NM_005109.2.
    UniGeneiHs.475970.

    Genome annotation databases

    EnsembliENST00000311806; ENSP00000311713; ENSG00000172939.
    GeneIDi9943.
    KEGGihsa:9943.
    UCSCiuc003chy.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS2675.1.
    RefSeqi NP_005100.1. NM_005109.2.
    UniGenei Hs.475970.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V3S X-ray 1.70 A/B 433-527 [» ]
    2VWI X-ray 2.15 A/B/C/D 1-303 [» ]
    3DAK X-ray 2.25 A/B/C/D 6-295 [» ]
    ProteinModelPortali O95747.
    SMRi O95747. Positions 7-358, 433-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115269. 19 interactions.
    IntActi O95747. 10 interactions.
    MINTi MINT-5207465.
    STRINGi 9606.ENSP00000311713.

    Chemistry

    BindingDBi O95747.
    ChEMBLi CHEMBL1163104.
    GuidetoPHARMACOLOGYi 2132.

    PTM databases

    PhosphoSitei O95747.

    Proteomic databases

    MaxQBi O95747.
    PaxDbi O95747.
    PeptideAtlasi O95747.
    PRIDEi O95747.

    Protocols and materials databases

    DNASUi 9943.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311806 ; ENSP00000311713 ; ENSG00000172939 .
    GeneIDi 9943.
    KEGGi hsa:9943.
    UCSCi uc003chy.3. human.

    Organism-specific databases

    CTDi 9943.
    GeneCardsi GC03P038183.
    HGNCi HGNC:8508. OXSR1.
    HPAi CAB017181.
    HPA008237.
    MIMi 604046. gene.
    neXtProti NX_O95747.
    PharmGKBi PA134973207.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234204.
    HOVERGENi HBG108518.
    InParanoidi O95747.
    KOi K08835.
    OMAi YCIPKKE.
    PhylomeDBi O95747.
    TreeFami TF105339.

    Enzyme and pathway databases

    SignaLinki O95747.

    Miscellaneous databases

    ChiTaRSi OXSR1. human.
    EvolutionaryTracei O95747.
    GeneWikii OXSR1.
    GenomeRNAii 9943.
    NextBioi 37516.
    PROi O95747.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95747.
    Bgeei O95747.
    CleanExi HS_OSR1.
    HS_OXSR1.
    Genevestigatori O95747.

    Family and domain databases

    InterProi IPR011009. 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 ]
    PANTHERi PTHR24361:SF202. PTHR24361:SF202. 1 hit.
    Pfami PF12202. OSR1_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 muscleImported.
    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: BrainImported.
    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: BrainImported.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. 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. 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.
      , 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.

    Entry informationi

    Entry nameiOXSR1_HUMAN
    AccessioniPrimary (citable) accession number: O95747
    Secondary accession number(s): Q3LR53, Q7Z501, Q9UPQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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