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O75716

- STK16_HUMAN

UniProt

O75716 - STK16_HUMAN

Protein

Serine/threonine-protein kinase 16

Gene

STK16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei148 – 1481Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB-KW
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl

    GO - Biological processi

    1. cellular response to transforming growth factor beta stimulus Source: Ensembl
    2. protein autophosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiO75716.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase 16 (EC:2.7.11.1)
    Alternative name(s):
    Myristoylated and palmitoylated serine/threonine-protein kinase
    Short name:
    MPSK
    Protein kinase PKL12
    TGF-beta-stimulated factor 1
    Short name:
    TSF-1
    Tyrosine-protein kinase STK16 (EC:2.7.10.2)
    hPSK
    Gene namesi
    Name:STK16
    Synonyms:MPSK1, PKL12, TSF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11394. STK16.

    Subcellular locationi

    Cytoplasmperinuclear region. Membrane By similarity; Lipid-anchor By similarity
    Note: Associates with Golgi and Golgi-derived vesicles.By similarity

    GO - Cellular componenti

    1. Golgi-associated vesicle Source: Ensembl
    2. membrane Source: UniProtKB-SubCell
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Loss of myristoylation. 1 Publication
    Mutagenesisi6 – 61C → S: Loss of palmitoylation. 1 Publication
    Mutagenesisi8 – 81C → S: Loss of palmitoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA36202.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 305304Serine/threonine-protein kinase 16PRO_0000086701Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi6 – 61S-palmitoyl cysteine1 Publication
    Lipidationi8 – 81S-palmitoyl cysteine1 Publication
    Modified residuei185 – 1851Phosphothreonine; by autocatalysis1 Publication
    Modified residuei197 – 1971Phosphoserine; by autocatalysis1 Publication
    Modified residuei198 – 1981Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198.1 Publication
    It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiO75716.
    PRIDEiO75716.

    PTM databases

    PhosphoSiteiO75716.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed at very low levels.1 Publication

    Gene expression databases

    ArrayExpressiO75716.
    BgeeiO75716.
    CleanExiHS_STK16.
    GenevestigatoriO75716.

    Organism-specific databases

    HPAiHPA029450.

    Interactioni

    Subunit structurei

    Monomer. Interacts with DRG1 (via its N-terminal); the interaction phosphorylates DRG1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAMTSL4Q6UY143EBI-749295,EBI-742002

    Protein-protein interaction databases

    BioGridi114144. 23 interactions.
    DIPiDIP-29598N.
    IntActiO75716. 5 interactions.
    MINTiMINT-3001680.
    STRINGi9606.ENSP00000379964.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 153
    Beta strandi18 – 2710
    Beta strandi32 – 398
    Turni40 – 423
    Beta strandi45 – 5511
    Helixi56 – 7015
    Beta strandi82 – 887
    Beta strandi91 – 999
    Helixi106 – 1149
    Turni115 – 1173
    Helixi122 – 14120
    Helixi151 – 1533
    Beta strandi154 – 1563
    Beta strandi162 – 1643
    Beta strandi171 – 1733
    Beta strandi175 – 1795
    Helixi180 – 19314
    Helixi196 – 1983
    Helixi201 – 2033
    Beta strandi208 – 2125
    Helixi215 – 23016
    Helixi236 – 2405
    Helixi245 – 2506
    Helixi263 – 27210
    Helixi277 – 2793
    Helixi283 – 29210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BUJX-ray2.60A/B13-305[»]
    ProteinModelPortaliO75716.
    SMRiO75716. Positions 13-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75716.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 293274Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 20237Activation loopAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG054359.
    KOiK08856.
    OrthoDBiEOG7Z3F55.
    PhylomeDBiO75716.
    TreeFamiTF350433.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. 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.

    O75716-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGHALCVCSR GTVIIDNKRY LFIQKLGEGG FSYVDLVEGL HDGHFYALKR    50
    ILCHEQQDRE EAQREADMHR LFNHPNILRL VAYCLRERGA KHEAWLLLPF 100
    FKRGTLWNEI ERLKDKGNFL TEDQILWLLL GICRGLEAIH AKGYAHRDLK 150
    PTNILLGDEG QPVLMDLGSM NQACIHVEGS RQALTLQDWA AQRCTISYRA 200
    PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ KGDSVALAVQ 250
    NQLSIPQSPR HSSALRQLLN SMMTVDPHQR PHIPLLLSQL EALQPPAPGQ 300
    HTTQI 305
    Length:305
    Mass (Da):34,656
    Last modified:January 23, 2007 - v4
    Checksum:i593B2AEB8505009C
    GO

    Sequence cautioni

    The sequence AAV38392.1 differs from that shown. Reason: Frameshift at position 305.
    The sequence CAA06700.1 differs from that shown. Reason: Frameshift at position 305.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 591R → L in AAV38392. 1 PublicationCurated
    Sequence conflicti180 – 1801S → P in BAF85383. (PubMed:14702039)Curated
    Sequence conflicti213 – 2131D → G in CAA06700. (PubMed:9712705)Curated
    Sequence conflicti213 – 2131D → G in CAA09387. 1 PublicationCurated
    Sequence conflicti221 – 2211L → F in AAC28337. (PubMed:10364453)Curated
    Sequence conflicti222 – 2221G → S in CAA09387. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411H → R.1 Publication
    Corresponds to variant rs34799131 [ dbSNP | Ensembl ].
    VAR_041140
    Natural varianti55 – 551E → K.1 Publication
    Corresponds to variant rs35947471 [ dbSNP | Ensembl ].
    VAR_041141
    Natural varianti77 – 771I → V.1 Publication
    Corresponds to variant rs34282267 [ dbSNP | Ensembl ].
    VAR_041142
    Natural varianti266 – 2661R → W.3 Publications
    Corresponds to variant rs17849638 [ dbSNP | Ensembl ].
    VAR_041143
    Natural varianti277 – 2771P → L.1 Publication
    Corresponds to variant rs35454203 [ dbSNP | Ensembl ].
    VAR_041144

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005791 mRNA. Translation: CAA06700.1. Frameshift.
    AF060798 mRNA. Translation: AAC28337.1.
    AB020739 mRNA. Translation: BAB16311.1.
    AJ010872 mRNA. Translation: CAA09387.1.
    AF203910 mRNA. Translation: AAG23728.1.
    BT019585 mRNA. Translation: AAV38392.1. Frameshift.
    AK292694 mRNA. Translation: BAF85383.1.
    CR407675 mRNA. Translation: CAG28603.1.
    BC002618 mRNA. Translation: AAH02618.1.
    BC053998 mRNA. Translation: AAH53998.1.
    CCDSiCCDS42822.1.
    RefSeqiNP_001008910.1. NM_001008910.2.
    UniGeneiHs.153003.

    Genome annotation databases

    EnsembliENST00000396738; ENSP00000379964; ENSG00000115661.
    ENST00000409638; ENSP00000386928; ENSG00000115661.
    GeneIDi8576.
    KEGGihsa:8576.
    UCSCiuc002vko.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005791 mRNA. Translation: CAA06700.1 . Frameshift.
    AF060798 mRNA. Translation: AAC28337.1 .
    AB020739 mRNA. Translation: BAB16311.1 .
    AJ010872 mRNA. Translation: CAA09387.1 .
    AF203910 mRNA. Translation: AAG23728.1 .
    BT019585 mRNA. Translation: AAV38392.1 . Frameshift.
    AK292694 mRNA. Translation: BAF85383.1 .
    CR407675 mRNA. Translation: CAG28603.1 .
    BC002618 mRNA. Translation: AAH02618.1 .
    BC053998 mRNA. Translation: AAH53998.1 .
    CCDSi CCDS42822.1.
    RefSeqi NP_001008910.1. NM_001008910.2.
    UniGenei Hs.153003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BUJ X-ray 2.60 A/B 13-305 [» ]
    ProteinModelPortali O75716.
    SMRi O75716. Positions 13-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114144. 23 interactions.
    DIPi DIP-29598N.
    IntActi O75716. 5 interactions.
    MINTi MINT-3001680.
    STRINGi 9606.ENSP00000379964.

    Chemistry

    BindingDBi O75716.
    ChEMBLi CHEMBL3938.
    GuidetoPHARMACOLOGYi 2213.

    PTM databases

    PhosphoSitei O75716.

    Proteomic databases

    PaxDbi O75716.
    PRIDEi O75716.

    Protocols and materials databases

    DNASUi 8576.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000396738 ; ENSP00000379964 ; ENSG00000115661 .
    ENST00000409638 ; ENSP00000386928 ; ENSG00000115661 .
    GeneIDi 8576.
    KEGGi hsa:8576.
    UCSCi uc002vko.2. human.

    Organism-specific databases

    CTDi 8576.
    GeneCardsi GC02P220110.
    HGNCi HGNC:11394. STK16.
    HPAi HPA029450.
    MIMi 604719. gene.
    neXtProti NX_O75716.
    PharmGKBi PA36202.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG054359.
    KOi K08856.
    OrthoDBi EOG7Z3F55.
    PhylomeDBi O75716.
    TreeFami TF350433.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki O75716.

    Miscellaneous databases

    ChiTaRSi STK16. human.
    EvolutionaryTracei O75716.
    GeneWikii STK16.
    GenomeRNAii 8576.
    NextBioi 32169.
    PROi O75716.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75716.
    Bgeei O75716.
    CleanExi HS_STK16.
    Genevestigatori O75716.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression analysis, and functional characterization of PKL12, a member of a new subfamily of ser/thr kinases."
      Ligos J.M., Gerwin N., Fernandez P., Gutierrez-Ramos J.-C., Bernad A.
      Biochem. Biophys. Res. Commun. 249:380-384(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification and characterization of a myristylated and palmitylated serine/threonine protein kinase."
      Berson A.E., Young C., Morrison S.L., Fujii G.H., Sheung J., Wu B., Bolen J.B., Burkhardt A.L.
      Biochem. Biophys. Res. Commun. 259:533-538(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AUTOPHOSPHORYLATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-6 AND CYS-8, MUTAGENESIS OF GLY-2; CYS-6 AND CYS-8.
      Tissue: Dendritic cell.
    3. "A novel transcriptional factor with Ser/Thr kinase activity involved in the transforming growth factor (TGF)-beta signalling pathway."
      Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.
      Biochem. J. 350:395-404(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Characterization of a ubiquitous expressed human serine/threonine kinase."
      Wabakken T.K., Aasheim H.-C.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Blood.
    5. Stairs D.B., Ha S.I., Chodosh L.A.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thymus.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-266.
    9. "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], VARIANT TRP-266.
      Tissue: Colon and Lymph.
    10. "Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture."
      Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E., Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.
      Structure 16:115-124(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 13-304 OF WILD TYPE AND IN COMPLEX WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1, PHOSPHORYLATION AT THR-185; SER-197 AND TYR-198, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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] ARG-41; LYS-55; VAL-77; TRP-266 AND LEU-277.

    Entry informationi

    Entry nameiSTK16_HUMAN
    AccessioniPrimary (citable) accession number: O75716
    Secondary accession number(s): A8K9H9
    , Q5U0F8, Q96KI2, Q9BUH4, Q9UEN3, Q9UP78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 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 2
      Human chromosome 2: 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