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O94804

- STK10_HUMAN

UniProt

O94804 - STK10_HUMAN

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Protein

Serine/threonine-protein kinase 10

Gene
STK10, LOK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651ATP Inferred
Binding sitei111 – 1111Inhibitor
Binding sitei113 – 1131Inhibitor
Binding sitei117 – 1171Inhibitor; via amide nitrogen
Active sitei157 – 1571Proton acceptor By similarity
Binding sitei175 – 1751Inhibitor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 509ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. polo kinase kinase activity Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: UniProtKB
  7. receptor signaling protein serine/threonine kinase activity Source: RefGenome

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. lymphocyte aggregation Source: Ensembl
  3. protein autophosphorylation Source: UniProtKB
  4. protein phosphorylation Source: ProtInc
  5. regulation of lymphocyte migration Source: UniProtKB
  6. signal transduction by phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiO94804.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 10 (EC:2.7.11.1)
Alternative name(s):
Lymphocyte-oriented kinase
Gene namesi
Name:STK10
Synonyms:LOK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:11388. STK10.

Subcellular locationi

Cell membrane; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. extracellular vesicular exosome Source: UniProt
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771K → E in TGCT; somatic mutation. 2 Publications
VAR_023827

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi65 – 651K → I: Loss of kinase activity. 1 Publication

Organism-specific databases

MIMi273300. phenotype.
PharmGKBiPA36197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Serine/threonine-protein kinase 10PRO_0000086697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei191 – 1911Phosphoserine3 Publications
Modified residuei438 – 4381Phosphoserine7 Publications
Modified residuei444 – 4441Phosphoserine1 Publication
Modified residuei454 – 4541Phosphoserine1 Publication
Modified residuei549 – 5491Phosphoserine1 Publication
Modified residuei952 – 9521Phosphothreonine1 Publication

Post-translational modificationi

Autophosphorylates following homodimerization, leading to activation of the protein.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94804.
PaxDbiO94804.
PRIDEiO94804.

PTM databases

PhosphoSiteiO94804.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO94804.
CleanExiHS_STK10.
GenevestigatoriO94804.

Organism-specific databases

HPAiCAB020840.
HPA015083.

Interactioni

Subunit structurei

Homodimer; homodimerization is required for activation segment autophosphorylation.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-3951541,EBI-3951541

Protein-protein interaction databases

BioGridi112669. 2 interactions.

Structurei

Secondary structure

1
968
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 304
Helixi32 – 343
Beta strandi36 – 438
Beta strandi50 – 556
Turni56 – 583
Beta strandi61 – 677
Helixi75 – 8713
Beta strandi96 – 1016
Beta strandi106 – 1116
Helixi118 – 1258
Helixi131 – 15020
Helixi160 – 1623
Beta strandi163 – 1653
Beta strandi171 – 1733
Helixi177 – 18711
Helixi196 – 1983
Helixi201 – 2088
Turni212 – 2165
Helixi217 – 23216
Turni236 – 2394
Helixi242 – 25110
Helixi260 – 2623
Helixi265 – 27410
Turni279 – 2813
Helixi285 – 2884
Turni292 – 2965
Helixi301 – 31414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J7TX-ray2.00A18-317[»]
4AOTX-ray2.33A/B18-317[»]
4BC6X-ray2.20A24-316[»]
4EQUX-ray2.00A/B18-317[»]
ProteinModelPortaliO94804.
SMRiO94804. Positions 24-316.

Miscellaneous databases

EvolutionaryTraceiO94804.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 294259Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 22450Activation segmentAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili573 – 947375 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi750 – 884135Gln-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000236268.
HOVERGENiHBG052712.
InParanoidiO94804.
KOiK08837.
OMAiSEEAECP.
OrthoDBiEOG7CNZF6.
PhylomeDBiO94804.
TreeFamiTF351445.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94804-1 [UniParc]FASTAAdd to Basket

« Hide

MAFANFRRIL RLSTFEKRKS REYEHVRRDL DPNEVWEIVG ELGDGAFGKV    50
YKAKNKETGA LAAAKVIETK SEEELEDYIV EIEILATCDH PYIVKLLGAY 100
YHDGKLWIMI EFCPGGAVDA IMLELDRGLT EPQIQVVCRQ MLEALNFLHS 150
KRIIHRDLKA GNVLMTLEGD IRLADFGVSA KNLKTLQKRD SFIGTPYWMA 200
PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL NPMRVLLKIA 250
KSDPPTLLTP SKWSVEFRDF LKIALDKNPE TRPSAAQLLE HPFVSSITSN 300
KALRELVAEA KAEVMEEIED GRDEGEEEDA VDAASTLENH TQNSSEVSPP 350
SLNADKPLEE SPSTPLAPSQ SQDSVNEPCS QPSGDRSLQT TSPPVVAPGN 400
ENGLAVPVPL RKSRPVSMDA RIQVAQEKQV AEQGGDLSPA ANRSQKASQS 450
RPNSSALETL GGEKLANGSL EPPAQAAPGP SKRDSDCSSL CTSESMDYGT 500
NLSTDLSLNK EMGSLSIKDP KLYKKTLKRT RKFVVDGVEV SITTSKIISE 550
DEKKDEEMRF LRRQELRELR LLQKEEHRNQ TQLSNKHELQ LEQMHKRFEQ 600
EINAKKKFFD TELENLERQQ KQQVEKMEQD HAVRRREEAR RIRLEQDRDY 650
TRFQEQLKLM KKEVKNEVEK LPRQQRKESM KQKMEEHTQK KQLLDRDFVA 700
KQKEDLELAM KRLTTDNRRE ICDKERECLM KKQELLRDRE AALWEMEEHQ 750
LQERHQLVKQ QLKDQYFLQR HELLRKHEKE REQMQRYNQR MIEQLKVRQQ 800
QEKARLPKIQ RSEGKTRMAM YKKSLHINGG GSAAEQREKI KQFSQQEEKR 850
QKSERLQQQQ KHENQMRDML AQCESNMSEL QQLQNEKCHL LVEHETQKLK 900
ALDESHNQNL KEWRDKLRPR KKALEEDLNQ KKREQEMFFK LSEEAECPNP 950
STPSKAAKFF PYSSADAS 968
Length:968
Mass (Da):112,135
Last modified:May 1, 1999 - v1
Checksum:i15E245193ECC553D
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti268 – 2681R → C.1 Publication
Corresponds to variant rs35826078 [ dbSNP | Ensembl ].
VAR_041131
Natural varianti277 – 2771K → E in TGCT; somatic mutation. 2 Publications
VAR_023827
Natural varianti322 – 3221R → W.1 Publication
Corresponds to variant rs56214442 [ dbSNP | Ensembl ].
VAR_041132
Natural varianti336 – 3361T → I.1 Publication
Corresponds to variant rs55972616 [ dbSNP | Ensembl ].
VAR_041133
Natural varianti467 – 4671N → S.1 Publication
Corresponds to variant rs56063773 [ dbSNP | Ensembl ].
VAR_041134
Natural varianti480 – 4801P → L.
Corresponds to variant rs34505340 [ dbSNP | Ensembl ].
VAR_051671
Natural varianti520 – 5201P → L.
Corresponds to variant rs17074311 [ dbSNP | Ensembl ].
VAR_051672
Natural varianti710 – 7101M → T.1 Publication
Corresponds to variant rs34936670 [ dbSNP | Ensembl ].
VAR_041135
Natural varianti853 – 8531S → L.1 Publication
Corresponds to variant rs56066852 [ dbSNP | Ensembl ].
VAR_041136
Natural varianti905 – 9051S → T.1 Publication
Corresponds to variant rs55791916 [ dbSNP | Ensembl ].
VAR_041137
Natural varianti942 – 9421S → N.
Corresponds to variant rs1128204 [ dbSNP | Ensembl ].
VAR_051673
Natural varianti947 – 9471C → Y.1 Publication
Corresponds to variant rs56355550 [ dbSNP | Ensembl ].
VAR_041138

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621A → V in AAH70077. 1 Publication
Sequence conflicti136 – 1361V → E in AAH70077. 1 Publication
Sequence conflicti317 – 3171E → G in AAH70077. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34290.1.
PIRiT42687.
RefSeqiNP_005981.3. NM_005990.3.
UniGeneiHs.744005.

Genome annotation databases

EnsembliENST00000176763; ENSP00000176763; ENSG00000072786.
GeneIDi6793.
KEGGihsa:6793.
UCSCiuc003mbo.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34290.1.
PIRi T42687.
RefSeqi NP_005981.3. NM_005990.3.
UniGenei Hs.744005.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O94804.
SMRi O94804. Positions 24-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112669. 2 interactions.

Chemistry

BindingDBi O94804.
ChEMBLi CHEMBL3981.
GuidetoPHARMACOLOGYi 2211.

PTM databases

PhosphoSitei O94804.

Proteomic databases

MaxQBi O94804.
PaxDbi O94804.
PRIDEi O94804.

Protocols and materials databases

DNASUi 6793.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000176763 ; ENSP00000176763 ; ENSG00000072786 .
GeneIDi 6793.
KEGGi hsa:6793.
UCSCi uc003mbo.1. human.

Organism-specific databases

CTDi 6793.
GeneCardsi GC05M171403.
HGNCi HGNC:11388. STK10.
HPAi CAB020840.
HPA015083.
MIMi 273300. phenotype.
603919. gene.
neXtProti NX_O94804.
PharmGKBi PA36197.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000236268.
HOVERGENi HBG052712.
InParanoidi O94804.
KOi K08837.
OMAi SEEAECP.
OrthoDBi EOG7CNZF6.
PhylomeDBi O94804.
TreeFami TF351445.

Enzyme and pathway databases

SignaLinki O94804.

Miscellaneous databases

ChiTaRSi STK10. human.
EvolutionaryTracei O94804.
GeneWikii STK10.
GenomeRNAii 6793.
NextBioi 26535.
PROi O94804.
SOURCEi Search...

Gene expression databases

Bgeei O94804.
CleanExi HS_STK10.
Genevestigatori O94804.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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. 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.
    , 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.
    , 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.

Entry informationi

Entry nameiSTK10_HUMAN
AccessioniPrimary (citable) accession number: O94804
Secondary accession number(s): A6ND35
, B2R8F5, B3KMY1, Q6NSK0, Q9UIW4
Entry historyi
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 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

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 (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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