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O75716 (STK16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Myristoylated and palmitoylated serine/threonine-protein kinase
Short name=MPSK
Protein kinase PKL12
TGF-beta-stimulated factor 1
Short name=TSF-1
Tyrosine-protein kinase STK16
EC=2.7.10.2
hPSK
Gene names
Name:STK16
Synonyms:MPSK1, PKL12, TSF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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. Interacts with DRG1 (via its N-terminal); the interaction phosphorylates DRG1. Ref.10

Subcellular location

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

Tissue specificity

Ubiquitously expressed at very low levels. Ref.2

Post-translational modification

Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198. Ref.2 Ref.10

It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8. Ref.2

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence caution

The sequence AAV38392.1 differs from that shown. Reason: Frameshift at position 305.

The sequence CAA06700.1 differs from that shown. Reason: Frameshift at position 305.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADAMTSL4Q6UY143EBI-749295,EBI-742002

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 305304Serine/threonine-protein kinase 16
PRO_0000086701

Regions

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

Sites

Active site1481Proton acceptor By similarity
Binding site491ATP By similarity

Amino acid modifications

Modified residue1851Phosphothreonine; by autocatalysis Ref.10
Modified residue1971Phosphoserine; by autocatalysis Ref.10
Modified residue1981Phosphotyrosine; by autocatalysis Ref.10
Lipidation21N-myristoyl glycine Ref.2
Lipidation61S-palmitoyl cysteine Probable
Lipidation81S-palmitoyl cysteine Probable

Natural variations

Natural variant411H → R. Ref.11
Corresponds to variant rs34799131 [ dbSNP | Ensembl ].
VAR_041140
Natural variant551E → K. Ref.11
Corresponds to variant rs35947471 [ dbSNP | Ensembl ].
VAR_041141
Natural variant771I → V. Ref.11
Corresponds to variant rs34282267 [ dbSNP | Ensembl ].
VAR_041142
Natural variant2661R → W. Ref.8 Ref.9 Ref.11
Corresponds to variant rs17849638 [ dbSNP | Ensembl ].
VAR_041143
Natural variant2771P → L. Ref.11
Corresponds to variant rs35454203 [ dbSNP | Ensembl ].
VAR_041144

Experimental info

Mutagenesis21G → A: Loss of myristoylation. Ref.2
Mutagenesis61C → S: Loss of palmitoylation. Ref.2
Mutagenesis81C → S: Loss of palmitoylation. Ref.2
Sequence conflict591R → L in AAV38392. Ref.6
Sequence conflict1801S → P in BAF85383. Ref.7
Sequence conflict2131D → G in CAA06700. Ref.1
Sequence conflict2131D → G in CAA09387. Ref.4
Sequence conflict2211L → F in AAC28337. Ref.2
Sequence conflict2221G → S in CAA09387. Ref.4

Secondary structure

................................................ 305
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75716 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 593B2AEB8505009C

FASTA30534,656
        10         20         30         40         50         60 
MGHALCVCSR GTVIIDNKRY LFIQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDRE 

        70         80         90        100        110        120 
EAQREADMHR LFNHPNILRL VAYCLRERGA KHEAWLLLPF FKRGTLWNEI ERLKDKGNFL 

       130        140        150        160        170        180 
TEDQILWLLL GICRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIHVEGS 

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

       250        260        270        280        290        300 
KGDSVALAVQ NQLSIPQSPR HSSALRQLLN SMMTVDPHQR PHIPLLLSQL 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].
[2]"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], TISSUE SPECIFICITY, FUNCTION, AUTOPHOSPHORYLATION, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-6 AND CYS-8, MUTAGENESIS OF GLY-2; CYS-6 AND CYS-8.
Tissue: Dendritic cell.
[3]"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 [MRNA].
[4]"Characterization of a ubiquitous expressed human serine/threonine kinase."
Wabakken T.K., Aasheim H.-C.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[5]Stairs D.B., Ha S.I., Chodosh L.A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-266.
[9]"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 TRP-266.
Tissue: Colon and Lymph.
[10]"Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture."
Eswaran J., Bernad A., Ligos J.M., Guinea B., Debreczeni J.E., Sobott F., Parker S.A., Najmanovich R., Turk B.E., Knapp S.
Structure 16:115-124(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 13-304 OF WILD TYPE AND IN COMPLEX WITH STAUROSPORINE, SUBUNIT, INTERACTION WITH DRG1, AUTOPHOSPHORYLATION AT THR-185; SER-197 AND TYR-198, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"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. expand/collapse author list , 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] ARG-41; LYS-55; VAL-77; TRP-266 AND LEU-277.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005791 mRNA. Translation: CAA06700.1. Frameshift.
AF060798 mRNA. Translation: AAC28337.1.
AB020739 mRNA. Translation: BAB16311.1.
AJ010872 mRNA. Translation: CAA09387.1.
AF203910 mRNA. Translation: AAG23728.1.
BT019585 mRNA. Translation: AAV38392.1. Frameshift.
AK292694 mRNA. Translation: BAF85383.1.
CR407675 mRNA. Translation: CAG28603.1.
BC002618 mRNA. Translation: AAH02618.1.
BC053998 mRNA. Translation: AAH53998.1.
CCDSCCDS42822.1.
RefSeqNP_001008910.1. NM_001008910.2.
UniGeneHs.153003.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BUJX-ray2.60A/B13-305[»]
ProteinModelPortalO75716.
SMRO75716. Positions 13-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114144. 23 interactions.
DIPDIP-29598N.
IntActO75716. 5 interactions.
MINTMINT-3001680.
STRING9606.ENSP00000379964.

Chemistry

BindingDBO75716.
ChEMBLCHEMBL3938.
GuidetoPHARMACOLOGY2213.

PTM databases

PhosphoSiteO75716.

Proteomic databases

PaxDbO75716.
PRIDEO75716.

Protocols and materials databases

DNASU8576.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396738; ENSP00000379964; ENSG00000115661.
ENST00000409638; ENSP00000386928; ENSG00000115661.
GeneID8576.
KEGGhsa:8576.
UCSCuc002vko.2. human.

Organism-specific databases

CTD8576.
GeneCardsGC02P220110.
HGNCHGNC:11394. STK16.
HPAHPA029450.
MIM604719. gene.
neXtProtNX_O75716.
PharmGKBPA36202.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG054359.
KOK08856.
OrthoDBEOG7Z3F55.
PhylomeDBO75716.
TreeFamTF350433.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkO75716.

Gene expression databases

ArrayExpressO75716.
BgeeO75716.
CleanExHS_STK16.
GenevestigatorO75716.

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

ChiTaRSSTK16. human.
EvolutionaryTraceO75716.
GeneWikiSTK16.
GenomeRNAi8576.
NextBio32169.
PROO75716.
SOURCESearch...

Entry information

Entry nameSTK16_HUMAN
AccessionPrimary (citable) accession number: O75716
Secondary accession number(s): A8K9H9 expand/collapse secondary AC list , Q5U0F8, Q96KI2, Q9BUH4, Q9UEN3, Q9UP78
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM