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Q15208

- STK38_HUMAN

UniProt

Q15208 - STK38_HUMAN

Protein

Serine/threonine-protein kinase 38

Gene

STK38

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by binding of S100B which releases autoinhibitory N-lobe interactions, enabling ATP to bind and the autophosphorylation of Ser-281. Thr-444 then undergoes calcium-dependent phosphorylation by STK24/MST3. Interactions between phosphorylated Thr-444 and the N-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of MOB1/MOBKL1A and MOB2/HCCA2 to the N-terminal of STK38.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei118 – 1181ATP2 PublicationsPROSITE-ProRule annotation
    Active sitei212 – 2121Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 1039ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. intracellular signal transduction Source: UniProtKB
    3. negative regulation of MAP kinase activity Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ15208.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 38 (EC:2.7.11.1)
    Alternative name(s):
    NDR1 protein kinase
    Nuclear Dbf2-related kinase 1
    Gene namesi
    Name:STK38Imported
    Synonyms:NDR11 Publication
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17847. STK38.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. MLL5-L complex Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741T → A: Decreases autophosphorylation and kinase activity. Reduced binding of S100B. 1 Publication
    Mutagenesisi118 – 1181K → A: Loss of autophosphorylation and kinase activity. 2 Publications
    Mutagenesisi281 – 2811S → A: Loss of autophosphorylation and kinase activity. 1 Publication
    Mutagenesisi444 – 4441T → A: Decreases autophosphorylation and kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 465464Serine/threonine-protein kinase 38PRO_0000086718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei74 – 741Phosphothreonine2 Publications
    Modified residuei264 – 2641Phosphoserine2 Publications
    Modified residuei281 – 2811Phosphoserine; by autocatalysis2 Publications
    Modified residuei444 – 4441Phosphothreonine; by STK24/MST32 Publications

    Post-translational modificationi

    ISGylated.1 Publication
    Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15208.
    PaxDbiQ15208.
    PRIDEiQ15208.

    PTM databases

    PhosphoSiteiQ15208.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels observed in peripheral blood leukocytes.2 Publications

    Gene expression databases

    BgeeiQ15208.
    CleanExiHS_STK38.
    GenevestigatoriQ15208.

    Organism-specific databases

    HPAiCAB004673.

    Interactioni

    Subunit structurei

    Interacts with MICAL1; leading to inhibit the protein kinase activity by antagonizing activation by MST1/STK4 By similarity. Homodimeric S100B binds two molecules of STK38. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with MOB1 and MOB2. Interacts with MAP3K1 and MAP3K2 (via the kinase catalytic domain). Forms a tripartite complex with MOBKL1B and STK3/MST2.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494073EBI-458376,EBI-743313
    ARRB2P321213EBI-458376,EBI-714559
    HSP90AB1P082382EBI-458376,EBI-352572
    MOB1AQ9H8S92EBI-458376,EBI-748229
    S100BP026383EBI-458376,EBI-458452From a different organism.

    Protein-protein interaction databases

    BioGridi116457. 38 interactions.
    IntActiQ15208. 12 interactions.
    MINTiMINT-1217042.
    STRINGi9606.ENSP00000229812.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi74 – 8512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PSBNMR-C/D62-87[»]
    ProteinModelPortaliQ15208.
    SMRiQ15208. Positions 23-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15208.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini89 – 382294Protein kinaseImportedPROSITE-ProRule annotationAdd
    BLAST
    Domaini383 – 45573AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni62 – 8726Interaction with S100BAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG104247.
    InParanoidiQ15208.
    KOiK08790.
    OMAiFCCEEEH.
    OrthoDBiEOG7BZVS1.
    PhylomeDBiQ15208.
    TreeFamiTF105337.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q15208-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK    50
    VMEEEGLKDE EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF 100
    GEVRLVQKKD TGHVYAMKIL RKADMLEKEQ VGHIRAERDI LVEADSLWVV 150
    KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK KDTLTEEETQ FYIAETVLAI 200
    DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA HRTEFYRNLN 250
    HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN 300
    KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS 350
    EKAKDLILRF CCEWEHRIGA PGVEEIKSNS FFEGVDWEHI RERPAAISIE 400
    IKSIDDTSNF DEFPESDILK PTVATSNHPE TDYKNKDWVF INYTYKRFEG 450
    LTARGAIPSY MKAAK 465
    Length:465
    Mass (Da):54,190
    Last modified:November 1, 1996 - v1
    Checksum:i7262221DBFFAF83C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041196
    Natural varianti145 – 1451D → N.1 Publication
    Corresponds to variant rs56005153 [ dbSNP | Ensembl ].
    VAR_041197
    Natural varianti267 – 2671K → R.1 Publication
    Corresponds to variant rs56105564 [ dbSNP | Ensembl ].
    VAR_041198

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35102 mRNA. Translation: CAA84485.1.
    Z85986 Genomic DNA. Translation: CAB39180.1.
    BC012085 mRNA. Translation: AAH12085.1.
    BC095413 mRNA. Translation: AAH95413.1.
    CCDSiCCDS4822.1.
    PIRiI38133.
    RefSeqiNP_009202.1. NM_007271.2.
    XP_005248896.1. XM_005248839.1.
    XP_006715051.1. XM_006714988.1.
    XP_006715052.1. XM_006714989.1.
    UniGeneiHs.409578.

    Genome annotation databases

    EnsembliENST00000229812; ENSP00000229812; ENSG00000112079.
    GeneIDi11329.
    KEGGihsa:11329.
    UCSCiuc003omg.3. human.

    Polymorphism databases

    DMDMi56749457.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35102 mRNA. Translation: CAA84485.1 .
    Z85986 Genomic DNA. Translation: CAB39180.1 .
    BC012085 mRNA. Translation: AAH12085.1 .
    BC095413 mRNA. Translation: AAH95413.1 .
    CCDSi CCDS4822.1.
    PIRi I38133.
    RefSeqi NP_009202.1. NM_007271.2.
    XP_005248896.1. XM_005248839.1.
    XP_006715051.1. XM_006714988.1.
    XP_006715052.1. XM_006714989.1.
    UniGenei Hs.409578.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PSB NMR - C/D 62-87 [» ]
    ProteinModelPortali Q15208.
    SMRi Q15208. Positions 23-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116457. 38 interactions.
    IntActi Q15208. 12 interactions.
    MINTi MINT-1217042.
    STRINGi 9606.ENSP00000229812.

    Chemistry

    BindingDBi Q15208.
    ChEMBLi CHEMBL1075155.
    GuidetoPHARMACOLOGYi 1517.

    PTM databases

    PhosphoSitei Q15208.

    Polymorphism databases

    DMDMi 56749457.

    Proteomic databases

    MaxQBi Q15208.
    PaxDbi Q15208.
    PRIDEi Q15208.

    Protocols and materials databases

    DNASUi 11329.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229812 ; ENSP00000229812 ; ENSG00000112079 .
    GeneIDi 11329.
    KEGGi hsa:11329.
    UCSCi uc003omg.3. human.

    Organism-specific databases

    CTDi 11329.
    GeneCardsi GC06M036461.
    HGNCi HGNC:17847. STK38.
    HPAi CAB004673.
    MIMi 606964. gene.
    neXtProti NX_Q15208.
    PharmGKBi PA38251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG104247.
    InParanoidi Q15208.
    KOi K08790.
    OMAi FCCEEEH.
    OrthoDBi EOG7BZVS1.
    PhylomeDBi Q15208.
    TreeFami TF105337.

    Enzyme and pathway databases

    SignaLinki Q15208.

    Miscellaneous databases

    ChiTaRSi STK38. human.
    EvolutionaryTracei Q15208.
    GeneWikii STK38.
    GenomeRNAii 11329.
    NextBioi 43035.
    PROi Q15208.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15208.
    CleanExi HS_STK38.
    Genevestigatori Q15208.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a conserved nuclear serine/threonine protein kinase."
      Millward T.A., Cron P., Hemmings B.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-118.
      Tissue: Fetal brainImported.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Placenta and UterusImported.
    4. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 25-44; 51-63; 72-78; 82-97; 110-118; 122-159; 182-239; 248-266; 277-301; 334-391; 394-402 AND 437-454, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    5. "Mechanism of Ca2+-mediated regulation of NDR protein kinase through autophosphorylation and phosphorylation by an upstream kinase."
      Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.
      J. Biol. Chem. 278:6710-6718(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-74; SER-281 AND THR-444, MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444.
    6. "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases."
      Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.
      J. Biol. Chem. 279:24444-24451(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
    7. "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."
      Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.
      J. Biol. Chem. 279:35228-35235(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, INTERACTION WITH MOB1 AND MOB2.
    8. "Identification and Herc5-mediated ISGylation of novel target proteins."
      Takeuchi T., Inoue S., Yokosawa H.
      Biochem. Biophys. Res. Commun. 348:473-477(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.
    9. "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."
      Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M., Kawata A., Ohno K., Hata Y.
      Oncogene 27:4281-4292(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STK3/MST2 AND MOBKL1B, SUBCELLULAR LOCATION, PHOSPHORYLATION BY STK3/MST2.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
    12. "Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)."
      Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N., Hosoi Y., Miyagawa K.
      Oncogene 27:1930-1938(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K1 AND MAP3K2.
    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: 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-264, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase."
      Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.
      Biochemistry 42:14416-14426(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 62-84, ENZYME REGULATION, INTERACTION WITH S100B.
    18. "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] LYS-18; ASN-145 AND ARG-267.

    Entry informationi

    Entry nameiSTK38_HUMAN
    AccessioniPrimary (citable) accession number: Q15208
    Secondary accession number(s): Q503A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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