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Protein

Serine/threonine-protein kinase 16

Gene

Stk16

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins.By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei148 – 1481Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl

GO - Biological processi

  1. cellular response to transforming growth factor beta stimulus Source: Ensembl
  2. protein autophosphorylation Source: UniProtKB
  3. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase 16 (EC:2.7.11.1)
Alternative name(s):
Embryo-derived protein kinase
Short name:
Edpk
Myristoylated and palmitoylated serine/threonine-protein kinase
Short name:
MPSK
Protein kinase Krct
Protein kinase PKL12
TGF-beta-stimulated factor 1
Short name:
TSF-1
Tyrosine-protein kinase STK16 (EC:2.7.10.2)
Gene namesi
Name:Stk16
Synonyms:Edpk, Krct, Mpsk1, Pkl12, Tsf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1313271. Stk16.

Subcellular locationi

Cytoplasmperinuclear region 1 Publication. Membrane By similarity; Lipid-anchor By similarity
Note: Associates with Golgi and Golgi-derived vesicles.

GO - Cellular componenti

  1. Golgi-associated vesicle Source: UniProtKB
  2. membrane Source: UniProtKB-SubCell
  3. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 305304Serine/threonine-protein kinase 16PRO_0000086702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Lipidationi6 – 61S-palmitoyl cysteineBy similarity
Lipidationi8 – 81S-palmitoyl cysteineBy similarity
Modified residuei197 – 1971Phosphoserine; by autocatalysisBy similarity
Modified residuei198 – 1981Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198 (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO88697.
PaxDbiO88697.
PRIDEiO88697.

PTM databases

PhosphoSiteiO88697.

Expressioni

Tissue specificityi

Ubiquitously expressed at low levels. Relatively higher levels in testis, kidney and liver.2 Publications

Developmental stagei

Expressed at all stages of developing embryo.1 Publication

Gene expression databases

BgeeiO88697.
CleanExiMM_STK16.
ExpressionAtlasiO88697. baseline and differential.
GenevestigatoriO88697.

Interactioni

Subunit structurei

Monomer. Interacts with DRG1 (via its N-terminal); the interaction phosphorylates DRG1.By similarity

Protein-protein interaction databases

MINTiMINT-224631.
STRINGi10090.ENSMUSP00000027401.

Structurei

3D structure databases

ProteinModelPortaliO88697.
SMRiO88697. Positions 13-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 293274Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 20237Activation loopBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000075037.
HOGENOMiHOG000157694.
HOVERGENiHBG054359.
InParanoidiO88697.
KOiK08856.
OMAiTEDQILW.
OrthoDBiEOG7Z3F55.
PhylomeDBiO88697.
TreeFamiTF350433.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88697-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGHALCVCSR GTVIIDNKRY LFVQKLGEGG FSYVDLVEGL HDGHFYALKR
60 70 80 90 100
ILCHEQQDQE EAQREAEMHR LFQHPNILRL MAYSLKERGA KHEAWLLLPF
110 120 130 140 150
FKKGTLWNEI ERLKDQGSFL TEDQILPLLL GISRGLEAIH AKGYAHRDLK
160 170 180 190 200
PTNILLGDEG QPVLMDLGSM NQACIQVEGS RQALALQDWA AQRCTISYRA
210 220 230 240 250
PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ KGDSVALAVQ
260 270 280 290 300
NELSIPQSPR HSSALRQLLS SMMTVDPQQR PHIPVLLSQL EALQPPAPGQ

HTTQI
Length:305
Mass (Da):34,382
Last modified:January 23, 2007 - v3
Checksum:iEB4725D26B210537
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 284KLGE → EIGG in BAA89662. (PubMed:10947953)Curated
Sequence conflicti25 – 284KLGE → EIGG in BAA89499. (PubMed:16141072)Curated
Sequence conflicti195 – 1951T → A in BAA89499. (PubMed:16141072)Curated
Sequence conflicti267 – 2682QL → HV in AAD02811. (PubMed:10364453)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005790 mRNA. Translation: CAA06699.1.
AB017197 mRNA. Translation: BAA74457.1.
AF089869 mRNA. Translation: AAC98502.1.
AF062076 mRNA. Translation: AAD02811.1.
AB022285 Genomic DNA. Translation: BAA89662.1.
AB022179 mRNA. Translation: BAA89499.1.
AK149539 mRNA. Translation: BAE28946.1.
CH466548 Genomic DNA. Translation: EDL00383.1.
CH466548 Genomic DNA. Translation: EDL00384.1.
CH466548 Genomic DNA. Translation: EDL00386.1.
BC028999 mRNA. Translation: AAH28999.1.
CCDSiCCDS15067.1.
RefSeqiNP_001264921.1. NM_001277992.1.
NP_035624.3. NM_011494.5.
XP_006496524.1. XM_006496461.1.
UniGeneiMm.1155.
Mm.17461.

Genome annotation databases

EnsembliENSMUST00000027401; ENSMUSP00000027401; ENSMUSG00000026201.
GeneIDi20872.
KEGGimmu:20872.
UCSCiuc007boh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005790 mRNA. Translation: CAA06699.1.
AB017197 mRNA. Translation: BAA74457.1.
AF089869 mRNA. Translation: AAC98502.1.
AF062076 mRNA. Translation: AAD02811.1.
AB022285 Genomic DNA. Translation: BAA89662.1.
AB022179 mRNA. Translation: BAA89499.1.
AK149539 mRNA. Translation: BAE28946.1.
CH466548 Genomic DNA. Translation: EDL00383.1.
CH466548 Genomic DNA. Translation: EDL00384.1.
CH466548 Genomic DNA. Translation: EDL00386.1.
BC028999 mRNA. Translation: AAH28999.1.
CCDSiCCDS15067.1.
RefSeqiNP_001264921.1. NM_001277992.1.
NP_035624.3. NM_011494.5.
XP_006496524.1. XM_006496461.1.
UniGeneiMm.1155.
Mm.17461.

3D structure databases

ProteinModelPortaliO88697.
SMRiO88697. Positions 13-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-224631.
STRINGi10090.ENSMUSP00000027401.

PTM databases

PhosphoSiteiO88697.

Proteomic databases

MaxQBiO88697.
PaxDbiO88697.
PRIDEiO88697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027401; ENSMUSP00000027401; ENSMUSG00000026201.
GeneIDi20872.
KEGGimmu:20872.
UCSCiuc007boh.2. mouse.

Organism-specific databases

CTDi8576.
MGIiMGI:1313271. Stk16.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000075037.
HOGENOMiHOG000157694.
HOVERGENiHBG054359.
InParanoidiO88697.
KOiK08856.
OMAiTEDQILW.
OrthoDBiEOG7Z3F55.
PhylomeDBiO88697.
TreeFamiTF350433.

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.

Miscellaneous databases

NextBioi299715.
PROiO88697.
SOURCEiSearch...

Gene expression databases

BgeeiO88697.
CleanExiMM_STK16.
ExpressionAtlasiO88697. baseline and differential.
GenevestigatoriO88697.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression analysis, and functional characterization of PKL12, a member of a new subfamily of ser/thr kinases."
    Ligos J.M., Gerwin N., Fernandez P., Gutierrez-Ramos J.-C., Bernad A.
    Biochem. Biophys. Res. Commun. 249:380-384(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  2. "Molecular cloning and characterization of a novel protein serine/threonine kinase highly expressed in mouse embryo."
    Kurioka K., Nakagawa K., Denda K., Miyazawa K., Kitamura N.
    Biochim. Biophys. Acta 1443:275-284(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
    Tissue: Liver.
  3. "Cloning and characterization of Krct, a member of a novel subfamily of serine/threonine kinases."
    Stairs D.B., Perry Gardner H., Ha S.I., Copeland N.G., Gilbert D.J., Jenkins N.A., Chodosh L.A.
    Hum. Mol. Genet. 7:2157-2166(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB.
    Tissue: Mammary gland.
  4. "Identification and characterization of a myristylated and palmitylated serine/threonine protein kinase."
    Berson A.E., Young C., Morrison S.L., Fujii G.H., Sheung J., Wu B., Bolen J.B., Burkhardt A.L.
    Biochem. Biophys. Res. Commun. 259:533-538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "A novel transcriptional factor with Ser/Thr kinase activity involved in the transforming growth factor (TGF)-beta signalling pathway."
    Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.
    Biochem. J. 350:395-404(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvJ.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.

Entry informationi

Entry nameiSTK16_MOUSE
AccessioniPrimary (citable) accession number: O88697
Secondary accession number(s): Q3UEG5
, Q9JMJ0, Q9JMJ1, Q9QX00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.