Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00684
Entry Name
UniProt Accession
Theoretical PI
6.42
Molecular Weight
34655.91
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Serine/threonine-protein kinase 16
Protein Synonyms/Alias
2.7.11.1; Myristoylated and palmitoylated serine/threonine-protein kinase; MPSK; Protein kinase PKL12; TGF-beta-stimulated factor 1; TSF-1; Tyrosine-protein kinase STK16; 2.7.10.2; hPSK;
Gene Name
STK16
Gene Synonyms/Alias
MPSK1; PKL12; TSF1;
Created Date
21-FEB-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGHALCVCS
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Berson AE, Young C, Morrison SL, Fujii GH, Sheung J, Wu B, Bolen JB, BurkhardtAL. Identification and characterization of a myristylated and palmitylatedserine/threonine protein kinase. Biochem Biophys Res Commun. 1999 Jun16;259(3):533-8.[PMID:10364453]
Functional Description
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.
Sequence Annotation
Domain: 20 293 Protein kinase.
Nucleotide-binding: 26 34 ATP.
Region: 166 202 Activation loop.
Active site: 148 148 Proton acceptor.
Binding site: 49 49 ATP.
Modified residue: 185 185 Phosphothreonine; by autocatalysis.
Modified residue: 197 197 Phosphoserine; by autocatalysis.
Modified residue: 198 198 Phosphotyrosine; by autocatalysis.
Protein Length
305 AA.
Protein Sequence
(Canonical)
MGHALCVCSR GTVIIDNKRY LFIQKLGEGG FSYVDLVEGL HDGHFYALKR ILCHEQQDRE  60
EAQREADMHR LFNHPNILRL VAYCLRERGA KHEAWLLLPF FKRGTLWNEI ERLKDKGNFL  120
TEDQILWLLL GICRGLEAIH AKGYAHRDLK PTNILLGDEG QPVLMDLGSM NQACIHVEGS  180
RQALTLQDWA AQRCTISYRA PELFSVQSHC VIDERTDVWS LGCVLYAMMF GEGPYDMVFQ  240
KGDSVALAVQ NQLSIPQSPR HSSALRQLLN SMMTVDPHQR PHIPLLLSQL EALQPPAPGQ  300
HTTQI                                                              305
FASTA
(Canonical)
>LipidDB-9606-00684|O75716
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDRE
EAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFL
TEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGS
RQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQ
KGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQ
HTTQI
Gene Ontology
GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW
GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IEA:Ensembl
GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl
GO:0046777; P:protein autophosphorylation; IDA:UniProtKB
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00069; Pkinase;
SMART
PROSITE
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS