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Protein

Serine/threonine-protein kinase 17A

Gene

STK17A

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

Functioni

Acts as a positive regulator of apoptosis. Also acts as a regulator of cellular reactive oxygen species.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by thiazolidinedione-type compounds: inhibited by furan- and pyridone- thiazolidinediones.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901ATP
Active sitei186 – 1861Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 759ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • intracellular signal transduction Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of fibroblast apoptotic process Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of reactive oxygen species metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiQ9UEE5.
SIGNORiQ9UEE5.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 17A (EC:2.7.11.1)
Alternative name(s):
DAP kinase-related apoptosis-inducing protein kinase 1
Gene namesi
Name:STK17A
Synonyms:DRAK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:11395. STK17A.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901K → A: Loss of activity and of apoptotic function. 1 Publication

Organism-specific databases

PharmGKBiPA36203.

Chemistry

ChEMBLiCHEMBL4525.
GuidetoPHARMACOLOGYi2214.

Polymorphism and mutation databases

BioMutaiSTK17A.
DMDMi317373279.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Serine/threonine-protein kinase 17APRO_0000086704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei28 – 281PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UEE5.
MaxQBiQ9UEE5.
PaxDbiQ9UEE5.
PeptideAtlasiQ9UEE5.
PRIDEiQ9UEE5.

PTM databases

iPTMnetiQ9UEE5.
PhosphoSiteiQ9UEE5.

Expressioni

Tissue specificityi

Highly expressed in placenta. Lower levels in heart, lung, skeletal muscle, kidney and pancreas.1 Publication

Inductioni

Directly regulated by p53/TP53: induced following cisplatin treatment in a p53/TP53-dependent manner. p53/TP53 activates expression by directly binding to its regulatory regions.2 Publications

Gene expression databases

BgeeiQ9UEE5.
CleanExiHS_STK17A.
GenevisibleiQ9UEE5. HS.

Organism-specific databases

HPAiHPA037979.

Interactioni

Protein-protein interaction databases

BioGridi114685. 1 interaction.
IntActiQ9UEE5. 4 interactions.
STRINGi9606.ENSP00000319192.

Chemistry

BindingDBiQ9UEE5.

Structurei

3D structure databases

ProteinModelPortaliQ9UEE5.
SMRiQ9UEE5. Positions 14-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 321261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 375Poly-Pro

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG106718.
InParanoidiQ9UEE5.
KOiK08804.
OMAiTEQKAIS.
OrthoDBiEOG7QZGBH.
PhylomeDBiQ9UEE5.
TreeFamiTF314166.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[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.

Q9UEE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPLEKPGSG GSSPGATSGS GRAGRGLSGP CRPPPPPQAR GLLTEIRAVV
60 70 80 90 100
RTEPFQDGYS LCPGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD
110 120 130 140 150
CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC
160 170 180 190 200
VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL
210 220 230 240 250
GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG
260 270 280 290 300
VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT
310 320 330 340 350
LLVKKPEDRA TAEECLKHPW LTQSSIQEPS FRMEKALEEA NALQEGHSVP
360 370 380 390 400
EINSDTDKSE TKESIVTEEL IVVTSYTLGQ CRQSEKEKME QKAISKRFKF
410
EEPLLQEIPG EFIY
Length:414
Mass (Da):46,558
Last modified:January 11, 2011 - v2
Checksum:iE2140290492C2A10
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261E → D.1 Publication
Corresponds to variant rs56286238 [ dbSNP | Ensembl ].
VAR_041145
Natural varianti167 – 1671M → T.1 Publication
Corresponds to variant rs35940029 [ dbSNP | Ensembl ].
VAR_041146
Natural varianti286 – 2861E → Q.1 Publication
Corresponds to variant rs3779062 [ dbSNP | Ensembl ].
VAR_032823
Natural varianti362 – 3621K → E.5 Publications
Corresponds to variant rs1044141 [ dbSNP | Ensembl ].
VAR_019991

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011420 mRNA. Translation: BAA34126.1.
CH236951 Genomic DNA. Translation: EAL24008.1.
AC005189 Genomic DNA. No translation available.
AC011738 Genomic DNA. No translation available.
AC093645 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW94162.1.
BC023508 mRNA. Translation: AAH23508.2.
BC047696 mRNA. Translation: AAH47696.1.
CCDSiCCDS5470.1.
RefSeqiNP_004751.2. NM_004760.2.
UniGeneiHs.709489.

Genome annotation databases

EnsembliENST00000319357; ENSP00000319192; ENSG00000164543.
GeneIDi9263.
KEGGihsa:9263.
UCSCiuc003tih.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011420 mRNA. Translation: BAA34126.1.
CH236951 Genomic DNA. Translation: EAL24008.1.
AC005189 Genomic DNA. No translation available.
AC011738 Genomic DNA. No translation available.
AC093645 Genomic DNA. No translation available.
CH471073 Genomic DNA. Translation: EAW94162.1.
BC023508 mRNA. Translation: AAH23508.2.
BC047696 mRNA. Translation: AAH47696.1.
CCDSiCCDS5470.1.
RefSeqiNP_004751.2. NM_004760.2.
UniGeneiHs.709489.

3D structure databases

ProteinModelPortaliQ9UEE5.
SMRiQ9UEE5. Positions 14-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114685. 1 interaction.
IntActiQ9UEE5. 4 interactions.
STRINGi9606.ENSP00000319192.

Chemistry

BindingDBiQ9UEE5.
ChEMBLiCHEMBL4525.
GuidetoPHARMACOLOGYi2214.

PTM databases

iPTMnetiQ9UEE5.
PhosphoSiteiQ9UEE5.

Polymorphism and mutation databases

BioMutaiSTK17A.
DMDMi317373279.

Proteomic databases

EPDiQ9UEE5.
MaxQBiQ9UEE5.
PaxDbiQ9UEE5.
PeptideAtlasiQ9UEE5.
PRIDEiQ9UEE5.

Protocols and materials databases

DNASUi9263.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319357; ENSP00000319192; ENSG00000164543.
GeneIDi9263.
KEGGihsa:9263.
UCSCiuc003tih.4. human.

Organism-specific databases

CTDi9263.
GeneCardsiSTK17A.
H-InvDBHIX0019195.
HIX0025491.
HGNCiHGNC:11395. STK17A.
HPAiHPA037979.
MIMi604726. gene.
neXtProtiNX_Q9UEE5.
PharmGKBiPA36203.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
GeneTreeiENSGT00760000118877.
HOGENOMiHOG000233016.
HOVERGENiHBG106718.
InParanoidiQ9UEE5.
KOiK08804.
OMAiTEQKAIS.
OrthoDBiEOG7QZGBH.
PhylomeDBiQ9UEE5.
TreeFamiTF314166.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiQ9UEE5.
SIGNORiQ9UEE5.

Miscellaneous databases

ChiTaRSiSTK17A. human.
GenomeRNAii9263.
PROiQ9UEE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UEE5.
CleanExiHS_STK17A.
GenevisibleiQ9UEE5. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DRAKs, novel serine/threonine kinases related to death-associated protein kinase that trigger apoptosis."
    Sanjo H., Kawai T., Akira S.
    J. Biol. Chem. 273:29066-29071(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-90, VARIANT GLU-362.
    Tissue: Liver and Placenta.
  2. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-362.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-362.
  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], VARIANT GLU-362.
    Tissue: Colon and Placenta.
  6. "A p53-dominant transcriptional response to cisplatin in testicular germ cell tumor-derived human embryonal carcinoma."
    Kerley-Hamilton J.S., Pike A.M., Li N., DiRenzo J., Spinella M.J.
    Oncogene 24:6090-6100(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "High-throughput kinase profiling: a more efficient approach toward the discovery of new kinase inhibitors."
    Miduturu C.V., Deng X., Kwiatkowski N., Yang W., Brault L., Filippakopoulos P., Chung E., Yang Q., Schwaller J., Knapp S., King R.W., Lee J.D., Herrgard S., Zarrinkar P., Gray N.S.
    Chem. Biol. 18:868-879(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "Serine/threonine kinase 17A is a novel p53 target gene and modulator of cisplatin toxicity and reactive oxygen species in testicular cancer cells."
    Mao P., Hever M.P., Niemaszyk L.M., Haghkerdar J.M., Yanco E.G., Desai D., Beyrouthy M.J., Kerley-Hamilton J.S., Freemantle S.J., Spinella M.J.
    J. Biol. Chem. 286:19381-19391(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-28, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. "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] ASP-126; THR-167; GLN-286 AND GLU-362.

Entry informationi

Entry nameiST17A_HUMAN
AccessioniPrimary (citable) accession number: Q9UEE5
Secondary accession number(s): A4D1V6, Q8IVC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 11, 2011
Last modified: July 6, 2016
This is version 148 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.