Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00677
Entry Name
UniProt Accession
Theoretical PI
5.49
Molecular Weight
49307.97
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Serine/threonine-protein kinase 24 12 kDa subunit
Protein Synonyms/Alias
2.7.11.1; Mammalian STE20-like protein kinase 3; MST-3; STE20-like kinase MST3; Mammalian STE20-like protein kinase 3 N-terminal; MST3/N; Mammalian STE20-like protein kinase 3 C-terminal; MST3/C;
Gene Name
STK24
Gene Synonyms/Alias
MST3; STK3;
Created Date
21-FEB-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
326
Canonical
DSDAETDGQASGGSD
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Martin DD, Vilas GL, Prescher JA, Rajaiah G, Falck JR, Bertozzi CR, BerthiaumeLG. Rapid detection, discovery, and identification of post-translationallymyristoylated proteins during apoptosis using a bio-orthogonal azidomyristateanalog. FASEB J. 2008 Mar;22(3):797-806. Epub 2007 Oct 10.[PMID:17932026]
Functional Description
Serine/threonine-protein kinase that acts on both serine and threonine residues and promotes apoptosis in response to stress stimuli and caspase activation. Mediates oxidative-stress- induced cell death by modulating phosphorylation of JNK1-JNK2 (MAPK8 and MAPK9), p38 (MAPK11, MAPK12, MAPK13 and MAPK14) during oxidative stress. Plays a role in a staurosporine-induced caspase- independent apoptotic pathway by regulating the nuclear translocation of AIFM1 and ENDOG and the DNase activity associated with ENDOG. Phosphorylates STK38L on 'Thr-442' and stimulates its kinase activity. Regulates cellular migration with alteration of PTPN12 activity and PXN phosphorylation: phosphorylates PTPN12 and inhibits its activity and may regulate PXN phosphorylation through PTPN12. May act as a key regulator of axon regeneration in the optic nerve and radial nerve.
Sequence Annotation
Domain: 36 286 Protein kinase.
Nucleotide-binding: 42 50 ATP.
Nucleotide-binding: 112 114 ATP.
Region: 335 386 Nuclear export signal (NES).
Motif: 278 292 Bipartite nuclear localization signal.
Active site: 156 156 Proton acceptor.
Metal binding site: 161 161 Magnesium.
Metal binding site: 174 174 Magnesium.
Binding site: 65 65 ATP.
Functional site: 325 326 Cleavage; by caspase-3, caspase-7 andcaspase-8.
Modified residue: 18 18 Phosphothreonine; by PKA.
Modified residue: 190 190 Phosphothreonine; by autocatalysis.
Modified residue: 320 320 Phosphoserine.
Protein Length
443 AA.
Protein Sequence
(Canonical)
MDSRAQLWGL ALNKRRATLP HPGGSTNLKA DPEELFTKLE KIGKGSFGEV FKGIDNRTQK  60
VVAIKIIDLE EAEDEIEDIQ QEITVLSQCD SPYVTKYYGS YLKDTKLWII MEYLGGGSAL  120
DLLEPGPLDE TQIATILREI LKGLDYLHSE KKIHRDIKAA NVLLSEHGEV KLADFGVAGQ  180
LTDTQIKRNT FVGTPFWMAP EVIKQSAYDS KADIWSLGIT AIELARGEPP HSELHPMKVL  240
FLIPKNNPPT LEGNYSKPLK EFVEACLNKE PSFRPTAKEL LKHKFILRNA KKTSYLTELI  300
DRYKRWKAEQ SHDDSSSEDS DAETDGQASG GSDSGDWIFT IREKDPKNLE NGALQPSDLD  360
RNKMKDIPKR PFSQCLSTII SPLFAELKEK SQACGGNLGS IEELRGAIYL AEEACPGISD  420
TMVAQLVQRL QRYSLSGGGT SSH                                          443
FASTA
(Canonical)
>LipidDB-9606-00677|Q9Y6E0
MDSRAQLWGLALNKRRATLPHPGGSTNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQK
VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSAL
DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQ
LTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVL
FLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELI
DRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLD
RNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISD
TMVAQLVQRLQRYSLSGGGTSSH
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005730; C:nucleolus; IDA:HPA
GO:0005654; C:nucleoplasm; TAS:Reactome
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004672; F:protein kinase activity; TAS:ProtInc
GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB
GO:0006915; P:apoptotic process; TAS:Reactome
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome
GO:0097194; P:execution phase of apoptosis; IMP:UniProtKB
GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:UniProtKB
GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB
GO:0046777; P:protein autophosphorylation; IDA:UniProtKB
GO:0006468; P:protein phosphorylation; IDA:UniProtKB
GO:0048679; P:regulation of axon regeneration; IMP:UniProtKB
GO:0007165; P:signal transduction; TAS:ProtInc
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
Pfam
Pfam; PF00069; Pkinase;
SMART
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PRINTS