Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase 17B

Gene

STK17B

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

Functioni

Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621ATP
Active sitei158 – 1581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 479ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • protein kinase activity 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 fibroblast apoptotic process Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation 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.
SignaLinkiO94768.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 17B (EC:2.7.11.1)
Alternative name(s):
DAP kinase-related apoptosis-inducing protein kinase 2
Gene namesi
Name:STK17B
Synonyms:DRAK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11396. STK17B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621K → A: Loss of activity and of apoptotic function. 1 Publication

Organism-specific databases

PharmGKBiPA36204.

Chemistry

ChEMBLiCHEMBL3980.
GuidetoPHARMACOLOGYi2215.

Polymorphism and mutation databases

BioMutaiSTK17B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Serine/threonine-protein kinase 17BPRO_0000086706Add
BLAST

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO94768.
PaxDbiO94768.
PRIDEiO94768.

PTM databases

iPTMnetiO94768.
PhosphoSiteiO94768.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiO94768.
CleanExiHS_STK17B.
ExpressionAtlasiO94768. baseline and differential.
GenevisibleiO94768. HS.

Organism-specific databases

HPAiHPA034858.

Interactioni

Subunit structurei

Interacts with CHP1; the interaction induces CHP1 to translocate from the Golgi to the nucleus.By similarity

Protein-protein interaction databases

BioGridi114684. 23 interactions.
IntActiO94768. 14 interactions.
STRINGi9606.ENSP00000263955.

Chemistry

BindingDBiO94768.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 317Combined sources
Beta strandi32 – 4211Combined sources
Beta strandi45 – 528Combined sources
Turni53 – 553Combined sources
Beta strandi58 – 6811Combined sources
Helixi74 – 8613Combined sources
Turni87 – 893Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi103 – 1119Combined sources
Helixi118 – 1225Combined sources
Helixi124 – 1263Combined sources
Helixi132 – 15120Combined sources
Helixi161 – 1633Combined sources
Beta strandi164 – 1674Combined sources
Turni169 – 1724Combined sources
Beta strandi175 – 1773Combined sources
Helixi180 – 1823Combined sources
Helixi199 – 2013Combined sources
Helixi204 – 2074Combined sources
Helixi215 – 23016Combined sources
Helixi240 – 24910Combined sources
Turni256 – 2616Combined sources
Helixi264 – 27310Combined sources
Helixi278 – 2803Combined sources
Helixi284 – 2874Combined sources
Helixi291 – 2933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LM0X-ray2.35A25-329[»]
3LM5X-ray2.29A25-329[»]
ProteinModelPortaliO94768.
SMRiO94768. Positions 25-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 293261Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 3114Poly-Ser

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
HOGENOMiHOG000233016.
HOVERGENiHBG106718.
InParanoidiO94768.
KOiK08804.
OMAiCPHVINL.
OrthoDBiEOG7QZGBH.
PhylomeDBiO94768.
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.

O94768-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRRFDCRS ISGLLTTTPQ IPIKMENFNN FYILTSKELG RGKFAVVRQC
60 70 80 90 100
ISKSTGQEYA AKFLKKRRRG QDCRAEILHE IAVLELAKSC PRVINLHEVY
110 120 130 140 150
ENTSEIILIL EYAAGGEIFS LCLPELAEMV SENDVIRLIK QILEGVYYLH
160 170 180 190 200
QNNIVHLDLK PQNILLSSIY PLGDIKIVDF GMSRKIGHAC ELREIMGTPE
210 220 230 240 250
YLAPEILNYD PITTATDMWN IGIIAYMLLT HTSPFVGEDN QETYLNISQV
260 270 280 290 300
NVDYSEETFS SVSQLATDFI QSLLVKNPEK RPTAEICLSH SWLQQWDFEN
310 320 330 340 350
LFHPEETSSS SQTQDHSVRS SEDKTSKSSC NGTCGDREDK ENIPEDSSMV
360 370
SKRFRFDDSL PNPHELVSDL LC
Length:372
Mass (Da):42,344
Last modified:May 1, 1999 - v1
Checksum:i7E69FFAED6DC1FF3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201S → F.1 Publication
Corresponds to variant rs34740616 [ dbSNP | Ensembl ].
VAR_041147

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011421 mRNA. Translation: BAA34127.1.
BC016040 mRNA. Translation: AAH16040.1.
CCDSiCCDS2315.1.
RefSeqiNP_004217.1. NM_004226.3.
XP_011510470.1. XM_011512168.1.
XP_011510471.1. XM_011512169.1.
XP_011510472.1. XM_011512170.1.
UniGeneiHs.88297.

Genome annotation databases

EnsembliENST00000263955; ENSP00000263955; ENSG00000081320.
ENST00000409228; ENSP00000386853; ENSG00000081320.
GeneIDi9262.
KEGGihsa:9262.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB011421 mRNA. Translation: BAA34127.1.
BC016040 mRNA. Translation: AAH16040.1.
CCDSiCCDS2315.1.
RefSeqiNP_004217.1. NM_004226.3.
XP_011510470.1. XM_011512168.1.
XP_011510471.1. XM_011512169.1.
XP_011510472.1. XM_011512170.1.
UniGeneiHs.88297.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LM0X-ray2.35A25-329[»]
3LM5X-ray2.29A25-329[»]
ProteinModelPortaliO94768.
SMRiO94768. Positions 25-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114684. 23 interactions.
IntActiO94768. 14 interactions.
STRINGi9606.ENSP00000263955.

Chemistry

BindingDBiO94768.
ChEMBLiCHEMBL3980.
GuidetoPHARMACOLOGYi2215.

PTM databases

iPTMnetiO94768.
PhosphoSiteiO94768.

Polymorphism and mutation databases

BioMutaiSTK17B.

Proteomic databases

EPDiO94768.
PaxDbiO94768.
PRIDEiO94768.

Protocols and materials databases

DNASUi9262.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263955; ENSP00000263955; ENSG00000081320.
ENST00000409228; ENSP00000386853; ENSG00000081320.
GeneIDi9262.
KEGGihsa:9262.

Organism-specific databases

CTDi9262.
GeneCardsiSTK17B.
HGNCiHGNC:11396. STK17B.
HPAiHPA034858.
MIMi604727. gene.
neXtProtiNX_O94768.
PharmGKBiPA36204.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0032. Eukaryota.
ENOG410XRMJ. LUCA.
HOGENOMiHOG000233016.
HOVERGENiHBG106718.
InParanoidiO94768.
KOiK08804.
OMAiCPHVINL.
OrthoDBiEOG7QZGBH.
PhylomeDBiO94768.
TreeFamiTF314166.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
SignaLinkiO94768.

Miscellaneous databases

ChiTaRSiSTK17B. human.
EvolutionaryTraceiO94768.
GenomeRNAii9262.
PROiO94768.
SOURCEiSearch...

Gene expression databases

BgeeiO94768.
CleanExiHS_STK17B.
ExpressionAtlasiO94768. baseline and differential.
GenevisibleiO94768. 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, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-62.
    Tissue: Liver and Placenta.
  2. "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: B-cell.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "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.
  5. "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: VARIANT [LARGE SCALE ANALYSIS] PHE-320.

Entry informationi

Entry nameiST17B_HUMAN
AccessioniPrimary (citable) accession number: O94768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 151 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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.