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O94804 (STK10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase 10

EC=2.7.11.1
Alternative name(s):
Lymphocyte-oriented kinase
Gene names
Name:STK10
Synonyms:LOK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length968 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. Ref.7 Ref.8 Ref.16

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.22

Enzyme regulation

Inhibited by the pyrrole-indolinone inhibitor SU11274 (K00593): intercalates between the ATP-binding Lys-65 and alpha-C glutamate (Glu-81), resulting in a partial disordering of the lysine side chain. Also specifically inhibited by erlotinib. Slightly inhibited by gefitinib. Ref.20 Ref.22

Subunit structure

Homodimer; homodimerization is required for activation segment autophosphorylation. Ref.22

Subcellular location

Cell membrane; Peripheral membrane protein Ref.16.

Tissue specificity

Highly expressed in rapidly proliferating tissues (spleen, placenta, and peripheral blood leukocytes). Also expressed in brain, heart, skeletal muscle, colon, thymus, kidney, liver, small intestine and lung. Ref.8

Post-translational modification

Autophosphorylates following homodimerization, leading to activation of the protein.

Involvement in disease

Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.23

Miscellaneous

Inhibition by erlotinib, an orally administered EGFR tyrosine kinase inhibitor used for treatment, enhances STK10-dependent lymphocytic responses, possibly leading to the aggravation of skin inflammation observed upon treatment by erlotinib (Ref.20).

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 BAG51143.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

lymphocyte aggregation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay Ref.8Ref.22. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 9278426. Source: ProtInc

regulation of lymphocyte migration

Inferred from mutant phenotype Ref.16. Source: UniProtKB

signal transduction by phosphorylation

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.22. Source: IntAct

polo kinase kinase activity

Traceable author statement Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.16. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.22. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.22Ref.16. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-3951541,EBI-3951541

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 968968Serine/threonine-protein kinase 10
PRO_0000086697

Regions

Domain36 – 294259Protein kinase
Nucleotide binding42 – 509ATP By similarity
Region175 – 22450Activation segment
Coiled coil573 – 947375 Potential
Compositional bias750 – 884135Gln-rich

Sites

Active site1571Proton acceptor By similarity
Binding site651ATP Probable
Binding site1111Inhibitor
Binding site1131Inhibitor
Binding site1171Inhibitor; via amide nitrogen
Binding site1751Inhibitor

Amino acid modifications

Modified residue131Phosphoserine Ref.13
Modified residue1911Phosphoserine Ref.12 Ref.13 Ref.15
Modified residue4381Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.18 Ref.21
Modified residue4441Phosphoserine Ref.15
Modified residue4541Phosphoserine Ref.13
Modified residue5491Phosphoserine Ref.15
Modified residue9521Phosphothreonine Ref.13

Natural variations

Natural variant2681R → C. Ref.24
Corresponds to variant rs35826078 [ dbSNP | Ensembl ].
VAR_041131
Natural variant2771K → E in TGCT; somatic mutation. Ref.23 Ref.24
VAR_023827
Natural variant3221R → W. Ref.24
Corresponds to variant rs56214442 [ dbSNP | Ensembl ].
VAR_041132
Natural variant3361T → I. Ref.24
Corresponds to variant rs55972616 [ dbSNP | Ensembl ].
VAR_041133
Natural variant4671N → S. Ref.24
Corresponds to variant rs56063773 [ dbSNP | Ensembl ].
VAR_041134
Natural variant4801P → L.
Corresponds to variant rs34505340 [ dbSNP | Ensembl ].
VAR_051671
Natural variant5201P → L.
Corresponds to variant rs17074311 [ dbSNP | Ensembl ].
VAR_051672
Natural variant7101M → T. Ref.24
Corresponds to variant rs34936670 [ dbSNP | Ensembl ].
VAR_041135
Natural variant8531S → L. Ref.24
Corresponds to variant rs56066852 [ dbSNP | Ensembl ].
VAR_041136
Natural variant9051S → T. Ref.24
Corresponds to variant rs55791916 [ dbSNP | Ensembl ].
VAR_041137
Natural variant9421S → N.
Corresponds to variant rs1128204 [ dbSNP | Ensembl ].
VAR_051673
Natural variant9471C → Y. Ref.24
Corresponds to variant rs56355550 [ dbSNP | Ensembl ].
VAR_041138

Experimental info

Mutagenesis651K → I: Loss of kinase activity. Ref.8
Sequence conflict621A → V in AAH70077. Ref.5
Sequence conflict1361V → E in AAH70077. Ref.5
Sequence conflict3171E → G in AAH70077. Ref.5

Secondary structure

.................................................... 968
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O94804 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 15E245193ECC553D

FASTA968112,135
        10         20         30         40         50         60 
MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV YKAKNKETGA 

        70         80         90        100        110        120 
LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY YHDGKLWIMI EFCPGGAVDA 

       130        140        150        160        170        180 
IMLELDRGLT EPQIQVVCRQ MLEALNFLHS KRIIHRDLKA GNVLMTLEGD IRLADFGVSA 

       190        200        210        220        230        240 
KNLKTLQKRD SFIGTPYWMA PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL 

       250        260        270        280        290        300 
NPMRVLLKIA KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLE HPFVSSITSN 

       310        320        330        340        350        360 
KALRELVAEA KAEVMEEIED GRDEGEEEDA VDAASTLENH TQNSSEVSPP SLNADKPLEE 

       370        380        390        400        410        420 
SPSTPLAPSQ SQDSVNEPCS QPSGDRSLQT TSPPVVAPGN ENGLAVPVPL RKSRPVSMDA 

       430        440        450        460        470        480 
RIQVAQEKQV AEQGGDLSPA ANRSQKASQS RPNSSALETL GGEKLANGSL EPPAQAAPGP 

       490        500        510        520        530        540 
SKRDSDCSSL CTSESMDYGT NLSTDLSLNK EMGSLSIKDP KLYKKTLKRT RKFVVDGVEV 

       550        560        570        580        590        600 
SITTSKIISE DEKKDEEMRF LRRQELRELR LLQKEEHRNQ TQLSNKHELQ LEQMHKRFEQ 

       610        620        630        640        650        660 
EINAKKKFFD TELENLERQQ KQQVEKMEQD HAVRRREEAR RIRLEQDRDY TRFQEQLKLM 

       670        680        690        700        710        720 
KKEVKNEVEK LPRQQRKESM KQKMEEHTQK KQLLDRDFVA KQKEDLELAM KRLTTDNRRE 

       730        740        750        760        770        780 
ICDKERECLM KKQELLRDRE AALWEMEEHQ LQERHQLVKQ QLKDQYFLQR HELLRKHEKE 

       790        800        810        820        830        840 
REQMQRYNQR MIEQLKVRQQ QEKARLPKIQ RSEGKTRMAM YKKSLHINGG GSAAEQREKI 

       850        860        870        880        890        900 
KQFSQQEEKR QKSERLQQQQ KHENQMRDML AQCESNMSEL QQLQNEKCHL LVEHETQKLK 

       910        920        930        940        950        960 
ALDESHNQNL KEWRDKLRPR KKALEEDLNQ KKREQEMFFK LSEEAECPNP STPSKAAKFF 


PYSSADAS 

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References

« Hide 'large scale' references
[1]"Molecular cloning of the human gene STK10 encoding lymphocyte-oriented kinase, and comparative chromosomal mapping of the human, mouse, and rat homologues."
Kuramochi S., Matsuda Y., Okamoto M., Kitamura F., Yonekawa H., Karasuyama H.
Immunogenetics 49:369-375(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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: Teratocarcinoma and Testis.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Testis.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-968.
Tissue: Testis.
[7]"Opposing roles of serine/threonine kinases MEKK1 and LOK in regulating the CD28 responsive element in T-cells."
Tao L., Wadsworth S., Mercer J., Mueller C., Lynn K., Siekierka J., August A.
Biochem. J. 363:175-182(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue."
Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J.
J. Biol. Chem. 278:18221-18228(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-65.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-13; SER-191; SER-454 AND THR-952, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-438; SER-444 AND SER-549, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation."
Belkina N.V., Liu Y., Hao J.J., Karasuyama H., Shaw S.
Proc. Natl. Acad. Sci. U.S.A. 106:4707-4712(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]"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.
[18]"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-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"Off-target serine/threonine kinase 10 inhibition by erlotinib enhances lymphocytic activity leading to severe skin disorders."
Yamamoto N., Honma M., Suzuki H.
Mol. Pharmacol. 80:466-475(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[21]"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-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites."
Pike A.C., Rellos P., Niesen F.H., Turnbull A., Oliver A.W., Parker S.A., Turk B.E., Pearl L.H., Knapp S.
EMBO J. 27:704-714(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-317 IN COMPLEX WITH PYRROLE-INDOLINONE INHIBITOR, ENZYME REGULATION, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, SUBUNIT.
[23]"Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents and adults."
Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J. expand/collapse author list , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., Wooster R., Stratton M.R.
Genes Chromosomes Cancer 45:42-46(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TGCT GLU-277.
[24]"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] CYS-268; GLU-277; TRP-322; ILE-336; SER-467; THR-710; LEU-853; THR-905 AND TYR-947.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015718 mRNA. Translation: BAA35073.1.
AK022960 mRNA. Translation: BAG51143.1. Different initiation.
AK313350 mRNA. Translation: BAG36152.1.
AC024561 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61439.1.
BC070077 mRNA. Translation: AAH70077.1.
AL133081 mRNA. Translation: CAB61400.1.
CCDSCCDS34290.1.
PIRT42687.
RefSeqNP_005981.3. NM_005990.3.
UniGeneHs.744005.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J7TX-ray2.00A18-317[»]
4AOTX-ray2.33A/B18-317[»]
4BC6X-ray2.20A24-316[»]
4EQUX-ray2.00A/B18-317[»]
ProteinModelPortalO94804.
SMRO94804. Positions 24-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112669. 2 interactions.

Chemistry

BindingDBO94804.
ChEMBLCHEMBL3981.
GuidetoPHARMACOLOGY2211.

PTM databases

PhosphoSiteO94804.

Proteomic databases

MaxQBO94804.
PaxDbO94804.
PRIDEO94804.

Protocols and materials databases

DNASU6793.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000176763; ENSP00000176763; ENSG00000072786.
GeneID6793.
KEGGhsa:6793.
UCSCuc003mbo.1. human.

Organism-specific databases

CTD6793.
GeneCardsGC05M171403.
HGNCHGNC:11388. STK10.
HPACAB020840.
HPA015083.
MIM273300. phenotype.
603919. gene.
neXtProtNX_O94804.
PharmGKBPA36197.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000236268.
HOVERGENHBG052712.
InParanoidO94804.
KOK08837.
OMASEEAECP.
OrthoDBEOG7CNZF6.
PhylomeDBO94804.
TreeFamTF351445.

Enzyme and pathway databases

SignaLinkO94804.

Gene expression databases

BgeeO94804.
CleanExHS_STK10.
GenevestigatorO94804.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR022165. PKK.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[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.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTK10. human.
EvolutionaryTraceO94804.
GeneWikiSTK10.
GenomeRNAi6793.
NextBio26535.
PROO94804.
SOURCESearch...

Entry information

Entry nameSTK10_HUMAN
AccessionPrimary (citable) accession number: O94804
Secondary accession number(s): A6ND35 expand/collapse secondary AC list , B2R8F5, B3KMY1, Q6NSK0, Q9UIW4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 141 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 5

Human chromosome 5: entries, gene names and cross-references to MIM