O88697 (STK16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Stk16
Synonyms:	Edpk, Krct, Mpsk1, Pkl12, Tsf1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › perinuclear 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.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	Golgi-associated vesicle Inferred from direct assay Ref.1. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from electronic annotation. Source: Compara non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 305	305	Serine/threonine-protein kinase 16		PRO_0000086702
Regions
	Domain	20 – 293	274	Protein kinase
	Nucleotide binding	26 – 34	9	ATP By similarity
	Region	166 – 202	37	Activation loop By similarity
Sites
	Active site	148	1	Proton acceptor By similarity
	Binding site	49	1	ATP By similarity
Amino acid modifications
	Modified residue	197	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	198	1	Phosphotyrosine; by autocatalysis By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity
	Lipidation	6	1	S-palmitoyl cysteine By similarity
	Lipidation	8	1	S-palmitoyl cysteine By similarity
Experimental info
	Sequence conflict	25 – 28	4	KLGE → EIGG in BAA89662. Ref.5
	Sequence conflict	25 – 28	4	KLGE → EIGG in BAA89499. Ref.6
	Sequence conflict	195	1	T → A in BAA89499. Ref.6
	Sequence conflict	267 – 268	2	QL → HV in AAD02811. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O88697 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EB4725D26B210537	FASTA	305	34,382
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00310280.
RefSeq	NP_035624.3. NM_011494.5.
UniGene	Mm.1155. Mm.17461.
3D structure databases
ProteinModelPortal	O88697.
SMR	O88697. Positions 13-299.
ModBase	Search...
PTM databases
PhosphoSite	O88697.
Proteomic databases
PaxDb	O88697.
PRIDE	O88697.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027401; ENSMUSP00000027401; ENSMUSG00000026201.
GeneID	20872.
KEGG	mmu:20872.
Organism-specific databases
CTD	8576.
MGI	MGI:1313271. Stk16.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000075037.
HOGENOM	HOG000157694.
HOVERGEN	HBG054359.
InParanoid	Q3UEG5.
KO	K08856.
OMA	VESHCII.
OrthoDB	EOG402WSS.
Enzyme and pathway databases
BRENDA	2.7.11.1. 3474.
Gene expression databases
ArrayExpress	O88697.
Bgee	O88697.
CleanEx	MM_STK16.
Genevestigator	O88697.
GermOnline	ENSMUSG00000026201. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	299715.
SOURCE	Search...

Entry information

Entry name

STK16_MOUSE

Accession

Primary (citable) accession number: O88697
Secondary accession number(s): Q3UEG5 , Q9JMJ0, Q9JMJ1, Q9QX00

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program