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O95747

- OXSR1_HUMAN

UniProt

O95747 - OXSR1_HUMAN

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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

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

Mg2+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 serine/threonine kinase activity Source: UniProtKB
  4. receptor signaling protein serine/threonine kinase activity Source: InterPro

GO - Biological processi

  1. cellular hypotonic response Source: Ensembl
  2. intracellular signal transduction Source: UniProtKB
  3. negative regulation of potassium ion transmembrane transport Source: Ensembl
  4. negative regulation of potassium ion transmembrane transporter activity Source: Ensembl
  5. negative regulation of rubidium ion transmembrane transporter activity Source: Ensembl
  6. negative regulation of rubidium ion transport Source: Ensembl
  7. peptidyl-threonine phosphorylation Source: BHF-UCL
  8. protein phosphorylation Source: UniProtKB
  9. response to oxidative stress Source: ProtInc
Complete GO annotation...

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-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

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

BgeeiO95747.
CleanExiHS_OSR1.
HS_OXSR1.
ExpressionAtlasiO95747. baseline and differential.
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. 20 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 – 163Combined sources
Beta strandi18 – 247Combined sources
Beta strandi31 – 355Combined sources
Helixi37 – 393Combined sources
Beta strandi42 – 465Combined sources
Turni50 – 545Combined sources
Helixi57 – 6913Combined sources
Beta strandi78 – 869Combined sources
Beta strandi88 – 936Combined sources
Helixi100 – 10910Combined sources
Turni110 – 1156Combined sources
Helixi120 – 13920Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi160 – 1623Combined sources
Helixi166 – 1705Combined sources
Helixi195 – 2028Combined sources
Helixi207 – 22216Combined sources
Turni226 – 2294Combined sources
Helixi232 – 2343Combined sources
Helixi235 – 2406Combined sources
Turni247 – 2504Combined sources
Helixi254 – 2574Combined sources
Helixi262 – 27110Combined sources
Helixi276 – 2783Combined sources
Helixi282 – 2865Combined sources
Helixi289 – 2935Combined sources
Beta strandi434 – 4418Combined sources
Beta strandi447 – 4548Combined sources
Turni456 – 4583Combined sources
Helixi461 – 47010Combined sources
Helixi476 – 4783Combined sources
Helixi479 – 49113Combined sources
Turni493 – 4953Combined sources
Beta strandi497 – 5026Combined sources
Helixi504 – 5063Combined sources
Beta strandi507 – 5115Combined sources
Helixi515 – 5173Combined sources
Beta strandi519 – 5268Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00680000099731.
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.
[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

        10         20         30         40         50
MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK EKVAIKRINL
60 70 80 90 100
EKCQTSMDEL LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV
110 120 130 140 150
LDIIKHIVAK GEHKSGVLDE STIATILREV LEGLEYLHKN GQIHRDVKAG
160 170 180 190 200
NILLGEDGSV QIADFGVSAF LATGGDITRN KVRKTFVGTP CWMAPEVMEQ
210 220 230 240 250
VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL QNDPPSLETG
260 270 280 290 300
VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL
310 320 330 340 350
QEKTLQRAPT ISERAKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG
360 370 380 390 400
KAAISQLRSP RVKESISNSE LFPTTDPVGT LLQVPEQISA HLPQPAGQIA
410 420 430 440 450
TQPTQVSLPP TAEPAKTAQA LSSGSGSQET KIPISLVLRL RNSKKELNDI
460 470 480 490 500
RFEFTPGRDT AEGVSQELIS AGLVDGRDLV IVAANLQKIV EEPQSNRSVT
510 520
FKLASGVEGS DIPDDGKLIG FAQLSIS
Length:527
Mass (Da):58,022
Last modified:May 1, 1999 - v1
Checksum:iB46EC934E95A3A1F
GO

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 20 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.
GeneTreei ENSGT00680000099731.
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

Bgeei O95747.
CleanExi HS_OSR1.
HS_OXSR1.
ExpressionAtlasi O95747. baseline and differential.
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.
[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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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

Dasty 3