O94804 (STK10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase 10
EC=2.7.11.1

Alternative name(s):
Lymphocyte-oriented kinase

Gene names

Name:	STK10
Synonyms:	LOK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	968 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.21
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.19 Ref.21
Subunit structure	Homodimer; homodimerization is required for activation segment autophosphorylation. Ref.21
Subcellular location	Cell membrane; Peripheral membrane protein Ref.15.
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.22
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.19).
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 process	Cell cycle
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW lymphocyte aggregation Inferred from sequence or structural similarity PubMed 10692593. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.8Ref.21. Source: UniProtKB regulation of lymphocyte migration Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	plasma membrane Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW polo kinase kinase activity Traceable author statement Ref.8. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.21. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 968

968

Serine/threonine-protein kinase 10

PRO_0000086697

Regions

Domain

36 – 294

259

Protein kinase

Nucleotide binding

42 – 50

9

ATP By similarity

Region

175 – 224

50

Activation segment

Coiled coil

573 – 947

375

Potential

Compositional bias

750 – 884

135

Gln-rich

Sites

Active site

157

1

Proton acceptor By similarity

Binding site

65

1

ATP Probable

Binding site

111

1

Inhibitor

Binding site

113

1

Inhibitor

Binding site

117

1

Inhibitor; via amide nitrogen

Binding site

175

1

Inhibitor

Amino acid modifications

Modified residue

13

1

Phosphoserine Ref.13

Modified residue

185

1

Phosphothreonine Ref.12 Ref.14

Modified residue

191

1

Phosphoserine Ref.12 Ref.13 Ref.14

Modified residue

438

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.20

Modified residue

444

1

Phosphoserine Ref.14

Modified residue

454

1

Phosphoserine Ref.13

Modified residue

549

1

Phosphoserine Ref.14

Modified residue

952

1

Phosphothreonine Ref.13

Natural variations

Natural variant

268

1

R → C. Ref.23
Corresponds to variant rs35826078 [ dbSNP | Ensembl ].

VAR_041131

Natural variant

277

1

K → E in TGCT; somatic mutation. Ref.22 Ref.23

VAR_023827

Natural variant

322

1

R → W. Ref.23
Corresponds to variant rs56214442 [ dbSNP | Ensembl ].

VAR_041132

Natural variant

336

1

T → I. Ref.23
Corresponds to variant rs55972616 [ dbSNP | Ensembl ].

VAR_041133

Natural variant

467

1

N → S. Ref.23
Corresponds to variant rs56063773 [ dbSNP | Ensembl ].

VAR_041134

Natural variant

480

1

P → L.
Corresponds to variant rs34505340 [ dbSNP | Ensembl ].

VAR_051671

Natural variant

520

1

P → L.
Corresponds to variant rs17074311 [ dbSNP | Ensembl ].

VAR_051672

Natural variant

710

1

M → T. Ref.23
Corresponds to variant rs34936670 [ dbSNP | Ensembl ].

VAR_041135

Natural variant

853

1

S → L. Ref.23
Corresponds to variant rs56066852 [ dbSNP | Ensembl ].

VAR_041136

Natural variant

905

1

S → T. Ref.23
Corresponds to variant rs55791916 [ dbSNP | Ensembl ].

VAR_041137

Natural variant

942

1

S → N.
Corresponds to variant rs1128204 [ dbSNP | Ensembl ].

VAR_051673

Natural variant

947

1

C → Y. Ref.23
Corresponds to variant rs56355550 [ dbSNP | Ensembl ].

VAR_041138

Experimental info

Mutagenesis

65

1

K → I: Loss of kinase activity. Ref.8

Sequence conflict

62

1

A → V in AAH70077. Ref.5

Sequence conflict

136

1

V → E in AAH70077. Ref.5

Sequence conflict

317

1

E → G in AAH70077. Ref.5

Secondary structure

1

.

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968

Helix Strand Turn

Details...

Beta strand

27 – 30

4

Helix

32 – 34

3

Beta strand

36 – 43

8

Beta strand

50 – 55

6

Turn

56 – 58

3

Beta strand

61 – 67

7

Helix

75 – 87

13

Beta strand

96 – 101

6

Beta strand

106 – 111

6

Helix

118 – 125

8

Helix

131 – 150

20

Helix

160 – 162

3

Beta strand

163 – 165

3

Beta strand

171 – 173

3

Helix

177 – 187

11

Helix

196 – 198

3

Helix

201 – 208

8

Turn

212 – 216

5

Helix

217 – 232

16

Turn

236 – 239

4

Helix

242 – 251

10

Helix

260 – 262

3

Helix

265 – 274

10

Turn

279 – 281

3

Helix

285 – 288

4

Turn

292 – 296

5

Helix

301 – 314

14

Sequences

	Sequence		Length	Mass (Da)
	O94804 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 15E245193ECC553D	FASTA	968	112,135
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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 THR-185; SER-191 AND SER-438, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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 THR-185; SER-191; SER-438; SER-444 AND SER-549, MASS SPECTROMETRY.
[15]	"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.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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.
[20]	"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, MASS SPECTROMETRY.
[21]	"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.
[22]	"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. , 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.
[23]	"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] 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.

IPI

IPI00304742.

PIR

T42687.

RefSeq

NP_005981.3. NM_005990.3.

UniGene

Hs.519756.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J7T	X-ray	2.00	A	18-317	[»]
4AOT	X-ray	2.33	A/B	18-317	[»]
4BC6	X-ray	2.20	A	24-316	[»]
4EQU	X-ray	2.00	A/B	18-317	[»]

ProteinModelPortal

O94804.

ModBase

Search...

PTM databases

PhosphoSite

O94804.

Proteomic databases

PaxDb

O94804.

PRIDE

O94804.

Protocols and materials databases

DNASU

6793.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000176763; ENSP00000176763; ENSG00000072786.
ENST00000545839; ENSP00000442209; ENSG00000072786.

GeneID

6793.

KEGG

hsa:6793.

UCSC

uc003mbo.1. human.

Organism-specific databases

CTD

6793.

GeneCards

GC05M171403.

HGNC

HGNC:11388. STK10.

HPA

CAB020840.
HPA015083.

MIM

273300. phenotype.
603919. gene.

neXtProt

NX_O94804.

PharmGKB

PA36197.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000236268.

HOVERGEN

HBG052712.

InParanoid

O94804.

KO

K08837.

OMA

SESMDYG.

OrthoDB

EOG4DR9BT.

Gene expression databases

Bgee

O94804.

CleanEx

HS_STK10.

Genevestigator

O94804.

GermOnline

ENSG00000072786. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR022165. PKK.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O94804.

ChEMBL

CHEMBL3981.

ChiTaRS

STK10. human.

EvolutionaryTrace

O94804.

GenomeRNAi

6793.

NextBio

26535.

SOURCE

Search...

Entry information

Entry name

STK10_HUMAN

Accession

Primary (citable) accession number: O94804
Secondary accession number(s): A6ND35 , B2R8F5, B3KMY1, Q6NSK0, Q9UIW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.