Reviewed, UniProtKB/Swiss-Prot O75716 (STK16_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase 16
    EC=2.7.11.1
Alternative name(s):
    Protein kinase PKL12
    Myristoylated and palmitoylated serine/threonine-protein kinase
      Short name=MPSK
    TGF-beta-stimulated factor 1
      Short name=TSF-1
    hPSK

Gene names

Name:	STK16
Synonyms:	MPSK1, PKL12, TSF1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that act on both serine and threonine residues.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Membrane; Lipid-anchor Probable.
Tissue specificity	Ubiquitously expressed at very low levels.
Post-translational modification	Autophosphorylated on serine and threonine residues. It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8.
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.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Ref.1 Traceable author statement. Source: ProtInc protein complex assembly Ref.1 Traceable author statement. Source: ProtInc
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAMTSL4	Q6UY14	2	EBI-749295,EBI-742002
CNTF	P26441	1	EBI-749295,EBI-1050897
EXT2	Q93063	1	EBI-749295,EBI-1047761
GK006	Q6P2I7	1	EBI-749295,EBI-1047027
HNF4A	P41235	1	EBI-749295,EBI-1049011
ICA1	Q05084	1	EBI-749295,EBI-1046751
MKKS	Q9HB66	1	EBI-749295,EBI-1054754
PASK	Q96RG2	1	EBI-749295,EBI-1042651
ROCK2	O75116	1	EBI-749295,EBI-366288
SNRK	Q9NRH2	1	EBI-749295,EBI-1053132
SNRPN	P63162	1	EBI-749295,EBI-712493
TGIF1	Q15583	1	EBI-749295,EBI-714215
VHL	P40337	1	EBI-749295,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 305

304

Serine/threonine-protein kinase 16

PRO_0000086701

Regions

Domain

20 – 293

274

Protein kinase

Nucleotide binding

26 – 34

9

ATP By similarity

Sites

Active site

148

1

Proton acceptor By similarity

Binding site

49

1

ATP By similarity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Ref.2

Lipidation

6

1

S-palmitoyl cysteine Probable

Lipidation

8

1

S-palmitoyl cysteine Probable

Natural variations

Natural variant

41

1

H → R: dbSNP rs34799131. Ref.10

VAR_041140

Natural variant

55

1

E → K: dbSNP rs35947471. Ref.10

VAR_041141

Natural variant

77

1

I → V: dbSNP rs34282267. Ref.10

VAR_041142

Natural variant

266

1

R → W: dbSNP rs17849638. Ref.10 Ref.8 Ref.9

VAR_041143

Natural variant

277

1

P → L: dbSNP rs35454203. Ref.10

VAR_041144

Experimental info

Mutagenesis

2

1

G → A: Loss of myristoylation.

Mutagenesis

6

1

C → S: Loss of palmitoylation.

Mutagenesis

8

1

C → S: Loss of palmitoylation.

Sequence conflict

59

1

R → L in AAV38392. Ref.6

Sequence conflict

180

1

S → P in BAF85383. Ref.7

Sequence conflict

213

1

D → G in CAA06700. Ref.1

Sequence conflict

213

1

D → G in CAA09387. Ref.4

Sequence conflict

221

1

L → F in AAC28337. Ref.2

Sequence conflict

222

1

G → S in CAA09387. Ref.4

Secondary structure

1

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305

Helix Strand Turn

Details...

Beta strand

13 – 15

3

Beta strand

18 – 27

10

Beta strand

32 – 39

8

Turn

40 – 42

3

Beta strand

45 – 55

11

Helix

56 – 70

15

Beta strand

82 – 88

7

Beta strand

91 – 99

9

Helix

106 – 114

9

Turn

115 – 117

3

Helix

122 – 141

20

Helix

151 – 153

3

Beta strand

154 – 156

3

Beta strand

162 – 164

3

Beta strand

171 – 173

3

Beta strand

175 – 179

5

Helix

180 – 193

14

Helix

196 – 198

3

Helix

201 – 203

3

Beta strand

208 – 212

5

Helix

215 – 230

16

Helix

236 – 240

5

Helix

245 – 250

6

Helix

263 – 272

10

Helix

277 – 279

3

Helix

283 – 292

10

Sequences

	Sequence		Length	Mass (Da)
	O75716-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 593B2AEB8505009C	FASTA	305	34,656
	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

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: 9712705] [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: 10364453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-6 AND CYS-8.
[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: 10947953] [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. , 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: 14702039] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-266. Tissue: Colon and Lymph.
[10]	"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: 17344846] [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.

IPI

IPI00306833.

RefSeq

NP_001008910.1.

UniGene

Hs.153003

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BUJ	X-ray	2.60	A/B	13-304	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29598N.

IntAct

O75716. 21 interactions.

STRING

O75716.

PTM databases

PhosphoSite

O75716.

Proteomic databases

PRIDE

O75716.

Genome annotation databases

Ensembl

ENST00000396738; ENSP00000379964; ENSG00000115661; Homo sapiens. [Genome view]
ENST00000409638; ENSP00000386928; ENSG00000115661; Homo sapiens. [Genome view]

GeneID

8576.

KEGG

hsa:8576.

UCSC

uc002vko.1. human.

Organism-specific databases

CTD

8576.

GeneCards

GC02P219818.

H-InvDB

HIX0002856.

HGNC

HGNC:11394. STK16.

MIM

604719. gene.

PharmGKB

PA36202.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18801.

HOVERGEN

O75716.

OrthoDB

EOG9SN47R.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Gene expression databases

ArrayExpress

O75716.

Bgee

O75716.

CleanEx

HS_STK16.

Genevestigator

O75716.

GermOnline

ENSG00000115661. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32169.

SOURCE

Search...

Entry information

Entry name

STK16_HUMAN

Accession

Primary (citable) accession number: O75716
Secondary accession number(s): A8K9H9 , Q5U0F8, Q96KI2, Q9BUH4, Q9UEN3, Q9UP78

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 103 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.