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O88697 (STK16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Stk16
Synonyms:Edpk, Krct, Mpsk1, Pkl12, Tsf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

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

Subcellular location

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

Tissue specificity

Ubiquitously expressed at low levels. Relatively higher levels in testis, kidney and liver. Ref.1 Ref.2

Developmental stage

Expressed at all stages of developing embryo. Ref.1

Post-translational modification

Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198 By similarity. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 305304Serine/threonine-protein kinase 16
PRO_0000086702

Regions

Domain20 – 293274Protein kinase
Nucleotide binding26 – 349ATP By similarity
Region166 – 20237Activation loop By similarity

Sites

Active site1481Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1971Phosphoserine; by autocatalysis By similarity
Modified residue1981Phosphotyrosine; by autocatalysis By similarity
Lipidation21N-myristoyl glycine By similarity
Lipidation61S-palmitoyl cysteine By similarity
Lipidation81S-palmitoyl cysteine By similarity

Experimental info

Sequence conflict25 – 284KLGE → EIGG in BAA89662. Ref.5
Sequence conflict25 – 284KLGE → EIGG in BAA89499. Ref.6
Sequence conflict1951T → A in BAA89499. Ref.6
Sequence conflict267 – 2682QL → HV in AAD02811. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O88697 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EB4725D26B210537

FASTA30534,382
        10         20         30         40         50         60 
MGHALCVCSR GTVIIDNKRY LFVQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDQE 

        70         80         90        100        110        120 
EAQREAEMHR LFQHPNILRL MAYSLKERGA KHEAWLLLPF FKKGTLWNEI ERLKDQGSFL 

       130        140        150        160        170        180 
TEDQILPLLL GISRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIQVEGS 

       190        200        210        220        230        240 
RQALALQDWA AQRCTISYRA PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ 

       250        260        270        280        290        300 
KGDSVALAVQ NELSIPQSPR HSSALRQLLS SMMTVDPQQR PHIPVLLSQL EALQPPAPGQ 


HTTQI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001264921.1. NM_001277992.1.
NP_035624.3. NM_011494.5.
XP_006496524.1. XM_006496461.1.
UniGeneMm.1155.
Mm.17461.

3D structure databases

ProteinModelPortalO88697.
SMRO88697. Positions 13-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-224631.
STRING10090.ENSMUSP00000027401.

PTM databases

PhosphoSiteO88697.

Proteomic databases

PaxDbO88697.
PRIDEO88697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027401; ENSMUSP00000027401; ENSMUSG00000026201.
GeneID20872.
KEGGmmu:20872.
UCSCuc007boh.2. mouse.

Organism-specific databases

CTD8576.
MGIMGI:1313271. Stk16.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000075037.
HOGENOMHOG000157694.
HOVERGENHBG054359.
InParanoidQ3UEG5.
KOK08856.
OMACIIDERT.
OrthoDBEOG7Z3F55.
PhylomeDBO88697.
TreeFamTF350433.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressO88697.
BgeeO88697.
CleanExMM_STK16.
GenevestigatorO88697.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299715.
PROO88697.
SOURCESearch...

Entry information

Entry nameSTK16_MOUSE
AccessionPrimary (citable) accession number: O88697
Secondary accession number(s): Q3UEG5 expand/collapse secondary AC list , Q9JMJ0, Q9JMJ1, Q9QX00
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot