Full text data of STK38
STK38
(NDR1)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein kinase 38; 2.7.11.1 (NDR1 protein kinase; Nuclear Dbf2-related kinase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein kinase 38; 2.7.11.1 (NDR1 protein kinase; Nuclear Dbf2-related kinase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15208
ID STK38_HUMAN Reviewed; 465 AA.
AC Q15208; Q503A1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Serine/threonine-protein kinase 38;
DE EC=2.7.11.1;
DE AltName: Full=NDR1 protein kinase;
DE AltName: Full=Nuclear Dbf2-related kinase 1;
GN Name=STK38; Synonyms=NDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-118.
RC TISSUE=Fetal brain;
RX PubMed=7761441; DOI=10.1073/pnas.92.11.5022;
RA Millward T.A., Cron P., Hemmings B.A.;
RT "Molecular cloning and characterization of a conserved nuclear
RT serine/threonine protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-17; 25-44; 51-63; 72-78; 82-97; 110-118;
RP 122-159; 182-239; 248-266; 277-301; 334-391; 394-402 AND 437-454,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-74; SER-281 AND
RP THR-444, AND MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444.
RX PubMed=12493777; DOI=10.1074/jbc.M210590200;
RA Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.;
RT "Mechanism of Ca2+-mediated regulation of NDR protein kinase through
RT autophosphorylation and phosphorylation by an upstream kinase.";
RL J. Biol. Chem. 278:6710-6718(2003).
RN [6]
RP ENZYME REGULATION, AND INTERACTION WITH MOB1 AND MOB2.
RX PubMed=15067004; DOI=10.1074/jbc.M401999200;
RA Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.;
RT "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine
RT kinases.";
RL J. Biol. Chem. 279:24444-24451(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION,
RP AND INTERACTION WITH MOB1 AND MOB2.
RX PubMed=15197186; DOI=10.1074/jbc.M404542200;
RA Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.;
RT "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase
RT by the hMOB1 protein.";
RL J. Biol. Chem. 279:35228-35235(2004).
RN [8]
RP ISGYLATION.
RX PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076;
RA Takeuchi T., Inoue S., Yokosawa H.;
RT "Identification and Herc5-mediated ISGylation of novel target
RT proteins.";
RL Biochem. Biophys. Res. Commun. 348:473-477(2006).
RN [9]
RP INTERACTION WITH STK3/MST2 AND MOBKL1B, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION BY STK3/MST2.
RX PubMed=18362890; DOI=10.1038/onc.2008.66;
RA Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M.,
RA Kawata A., Ohno K., Hata Y.;
RT "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2
RT to form the scaffold to activate nuclear Dbf2-related kinase 1.";
RL Oncogene 27:4281-4292(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION IN THE MLL5-L COMPLEX.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP3K1 AND
RP MAP3K2.
RX PubMed=17906693; DOI=10.1038/sj.onc.1210828;
RA Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N.,
RA Hosoi Y., Miyagawa K.;
RT "Negative regulation of MEKK1/2 signaling by serine-threonine kinase
RT 38 (STK38).";
RL Oncogene 27:1930-1938(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP STRUCTURE BY NMR OF 62-84, ENZYME REGULATION, AND INTERACTION WITH
RP S100B.
RX PubMed=14661952; DOI=10.1021/bi035089a;
RA Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.;
RT "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into
RT S100 target specificity and activation of the kinase.";
RL Biochemistry 42:14416-14426(2003).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-18; ASN-145 AND ARG-267.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts
CC MAP3K2 from its phosphorylated form to its non-phosphorylated form
CC and inhibits autophosphorylation of MAP3K2.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by binding of S100B which releases
CC autoinhibitory N-lobe interactions, enabling ATP to bind and the
CC autophosphorylation of Ser-281. Thr-444 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-444 and the N-lobe promote additional
CC structural changes that complete the activation of the kinase.
CC Autoinhibition is also released by the binding of MOB1/MOBKL1A and
CC MOB2/HCCA2 to the N-terminal of STK38.
CC -!- SUBUNIT: Interacts with MICAL1; leading to inhibit the protein
CC kinase activity by antagonizing activation by MST1/STK4 (By
CC similarity). Homodimeric S100B binds two molecules of STK38.
CC Component of the MLL5-L complex, at least composed of KMT2E/MLL5,
CC STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with
CC MOB1 and MOB2. Interacts with MAP3K1 and MAP3K2 (via the kinase
CC catalytic domain). Forms a tripartite complex with MOBKL1B and
CC STK3/MST2.
CC -!- INTERACTION:
CC P49407:ARRB1; NbExp=3; IntAct=EBI-458376, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-458376, EBI-714559;
CC P08238:HSP90AB1; NbExp=2; IntAct=EBI-458376, EBI-352572;
CC Q9H8S9:MOB1A; NbExp=2; IntAct=EBI-458376, EBI-748229;
CC P02638:S100B (xeno); NbExp=3; IntAct=EBI-458376, EBI-458452;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC observed in peripheral blood leukocytes.
CC -!- PTM: ISGylated (Probable).
CC -!- PTM: Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; Z35102; CAA84485.1; -; mRNA.
DR EMBL; Z85986; CAB39180.1; -; Genomic_DNA.
DR EMBL; BC012085; AAH12085.1; -; mRNA.
DR EMBL; BC095413; AAH95413.1; -; mRNA.
DR PIR; I38133; I38133.
DR RefSeq; NP_009202.1; NM_007271.2.
DR RefSeq; XP_005248896.1; XM_005248839.1.
DR UniGene; Hs.409578; -.
DR PDB; 1PSB; NMR; -; C/D=62-87.
DR PDBsum; 1PSB; -.
DR ProteinModelPortal; Q15208; -.
DR SMR; Q15208; 23-452.
DR IntAct; Q15208; 13.
DR MINT; MINT-1217042; -.
DR STRING; 9606.ENSP00000229812; -.
DR BindingDB; Q15208; -.
DR ChEMBL; CHEMBL1075155; -.
DR GuidetoPHARMACOLOGY; 1517; -.
DR PhosphoSite; Q15208; -.
DR DMDM; 56749457; -.
DR PaxDb; Q15208; -.
DR PRIDE; Q15208; -.
DR DNASU; 11329; -.
DR Ensembl; ENST00000229812; ENSP00000229812; ENSG00000112079.
DR GeneID; 11329; -.
DR KEGG; hsa:11329; -.
DR UCSC; uc003omg.3; human.
DR CTD; 11329; -.
DR GeneCards; GC06M036461; -.
DR HGNC; HGNC:17847; STK38.
DR HPA; CAB004673; -.
DR MIM; 606964; gene.
DR neXtProt; NX_Q15208; -.
DR PharmGKB; PA38251; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233033; -.
DR HOVERGEN; HBG104247; -.
DR InParanoid; Q15208; -.
DR KO; K08790; -.
DR OMA; FCCEEEH; -.
DR OrthoDB; EOG7BZVS1; -.
DR PhylomeDB; Q15208; -.
DR SignaLink; Q15208; -.
DR ChiTaRS; STK38; human.
DR EvolutionaryTrace; Q15208; -.
DR GeneWiki; STK38; -.
DR GenomeRNAi; 11329; -.
DR NextBio; 43035; -.
DR PRO; PR:Q15208; -.
DR Bgee; Q15208; -.
DR CleanEx; HS_STK38; -.
DR Genevestigator; Q15208; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 465 Serine/threonine-protein kinase 38.
FT /FTId=PRO_0000086718.
FT DOMAIN 89 382 Protein kinase.
FT DOMAIN 383 455 AGC-kinase C-terminal.
FT NP_BIND 95 103 ATP (By similarity).
FT REGION 62 87 Interaction with S100B.
FT ACT_SITE 212 212 Proton acceptor (By similarity).
FT BINDING 118 118 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 74 74 Phosphothreonine.
FT MOD_RES 264 264 Phosphoserine.
FT MOD_RES 281 281 Phosphoserine; by autocatalysis.
FT MOD_RES 444 444 Phosphothreonine; by STK24/MST3.
FT VARIANT 18 18 E -> K (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041196.
FT VARIANT 145 145 D -> N (in dbSNP:rs56005153).
FT /FTId=VAR_041197.
FT VARIANT 267 267 K -> R (in dbSNP:rs56105564).
FT /FTId=VAR_041198.
FT MUTAGEN 74 74 T->A: Decreases autophosphorylation and
FT kinase activity. Reduced binding of
FT S100B.
FT MUTAGEN 118 118 K->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 281 281 S->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 444 444 T->A: Decreases autophosphorylation and
FT kinase activity.
FT HELIX 74 85
SQ SEQUENCE 465 AA; 54190 MW; 7262221DBFFAF83C CRC64;
MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK VMEEEGLKDE
EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL
RKADMLEKEQ VGHIRAERDI LVEADSLWVV KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK
KDTLTEEETQ FYIAETVLAI DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA
HRTEFYRNLN HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN
KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS EKAKDLILRF
CCEWEHRIGA PGVEEIKSNS FFEGVDWEHI RERPAAISIE IKSIDDTSNF DEFPESDILK
PTVATSNHPE TDYKNKDWVF INYTYKRFEG LTARGAIPSY MKAAK
//
ID STK38_HUMAN Reviewed; 465 AA.
AC Q15208; Q503A1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Serine/threonine-protein kinase 38;
DE EC=2.7.11.1;
DE AltName: Full=NDR1 protein kinase;
DE AltName: Full=Nuclear Dbf2-related kinase 1;
GN Name=STK38; Synonyms=NDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-118.
RC TISSUE=Fetal brain;
RX PubMed=7761441; DOI=10.1073/pnas.92.11.5022;
RA Millward T.A., Cron P., Hemmings B.A.;
RT "Molecular cloning and characterization of a conserved nuclear
RT serine/threonine protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5022-5026(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-17; 25-44; 51-63; 72-78; 82-97; 110-118;
RP 122-159; 182-239; 248-266; 277-301; 334-391; 394-402 AND 437-454,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-74; SER-281 AND
RP THR-444, AND MUTAGENESIS OF THR-74; LYS-118; SER-281 AND THR-444.
RX PubMed=12493777; DOI=10.1074/jbc.M210590200;
RA Tamaskovic R., Bichsel S.J., Rogniaux H., Stegert M.R., Hemmings B.A.;
RT "Mechanism of Ca2+-mediated regulation of NDR protein kinase through
RT autophosphorylation and phosphorylation by an upstream kinase.";
RL J. Biol. Chem. 278:6710-6718(2003).
RN [6]
RP ENZYME REGULATION, AND INTERACTION WITH MOB1 AND MOB2.
RX PubMed=15067004; DOI=10.1074/jbc.M401999200;
RA Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.;
RT "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine
RT kinases.";
RL J. Biol. Chem. 279:24444-24451(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION,
RP AND INTERACTION WITH MOB1 AND MOB2.
RX PubMed=15197186; DOI=10.1074/jbc.M404542200;
RA Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.;
RT "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase
RT by the hMOB1 protein.";
RL J. Biol. Chem. 279:35228-35235(2004).
RN [8]
RP ISGYLATION.
RX PubMed=16884686; DOI=10.1016/j.bbrc.2006.07.076;
RA Takeuchi T., Inoue S., Yokosawa H.;
RT "Identification and Herc5-mediated ISGylation of novel target
RT proteins.";
RL Biochem. Biophys. Res. Commun. 348:473-477(2006).
RN [9]
RP INTERACTION WITH STK3/MST2 AND MOBKL1B, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION BY STK3/MST2.
RX PubMed=18362890; DOI=10.1038/onc.2008.66;
RA Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M.,
RA Kawata A., Ohno K., Hata Y.;
RT "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2
RT to form the scaffold to activate nuclear Dbf2-related kinase 1.";
RL Oncogene 27:4281-4292(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION IN THE MLL5-L COMPLEX.
RX PubMed=19377461; DOI=10.1038/nature07954;
RA Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
RA Kitagawa H., Kato S.;
RT "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
RT granulopoiesis.";
RL Nature 459:455-459(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP3K1 AND
RP MAP3K2.
RX PubMed=17906693; DOI=10.1038/sj.onc.1210828;
RA Enomoto A., Kido N., Ito M., Morita A., Matsumoto Y., Takamatsu N.,
RA Hosoi Y., Miyagawa K.;
RT "Negative regulation of MEKK1/2 signaling by serine-threonine kinase
RT 38 (STK38).";
RL Oncogene 27:1930-1938(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP STRUCTURE BY NMR OF 62-84, ENZYME REGULATION, AND INTERACTION WITH
RP S100B.
RX PubMed=14661952; DOI=10.1021/bi035089a;
RA Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.;
RT "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into
RT S100 target specificity and activation of the kinase.";
RL Biochemistry 42:14416-14426(2003).
RN [18]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-18; ASN-145 AND ARG-267.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Negative regulator of MAP3K1/2 signaling. Converts
CC MAP3K2 from its phosphorylated form to its non-phosphorylated form
CC and inhibits autophosphorylation of MAP3K2.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by binding of S100B which releases
CC autoinhibitory N-lobe interactions, enabling ATP to bind and the
CC autophosphorylation of Ser-281. Thr-444 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-444 and the N-lobe promote additional
CC structural changes that complete the activation of the kinase.
CC Autoinhibition is also released by the binding of MOB1/MOBKL1A and
CC MOB2/HCCA2 to the N-terminal of STK38.
CC -!- SUBUNIT: Interacts with MICAL1; leading to inhibit the protein
CC kinase activity by antagonizing activation by MST1/STK4 (By
CC similarity). Homodimeric S100B binds two molecules of STK38.
CC Component of the MLL5-L complex, at least composed of KMT2E/MLL5,
CC STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with
CC MOB1 and MOB2. Interacts with MAP3K1 and MAP3K2 (via the kinase
CC catalytic domain). Forms a tripartite complex with MOBKL1B and
CC STK3/MST2.
CC -!- INTERACTION:
CC P49407:ARRB1; NbExp=3; IntAct=EBI-458376, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-458376, EBI-714559;
CC P08238:HSP90AB1; NbExp=2; IntAct=EBI-458376, EBI-352572;
CC Q9H8S9:MOB1A; NbExp=2; IntAct=EBI-458376, EBI-748229;
CC P02638:S100B (xeno); NbExp=3; IntAct=EBI-458376, EBI-458452;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC observed in peripheral blood leukocytes.
CC -!- PTM: ISGylated (Probable).
CC -!- PTM: Phosphorylated by STK3/MST2 and this is enhanced by MOBKL1B.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; Z35102; CAA84485.1; -; mRNA.
DR EMBL; Z85986; CAB39180.1; -; Genomic_DNA.
DR EMBL; BC012085; AAH12085.1; -; mRNA.
DR EMBL; BC095413; AAH95413.1; -; mRNA.
DR PIR; I38133; I38133.
DR RefSeq; NP_009202.1; NM_007271.2.
DR RefSeq; XP_005248896.1; XM_005248839.1.
DR UniGene; Hs.409578; -.
DR PDB; 1PSB; NMR; -; C/D=62-87.
DR PDBsum; 1PSB; -.
DR ProteinModelPortal; Q15208; -.
DR SMR; Q15208; 23-452.
DR IntAct; Q15208; 13.
DR MINT; MINT-1217042; -.
DR STRING; 9606.ENSP00000229812; -.
DR BindingDB; Q15208; -.
DR ChEMBL; CHEMBL1075155; -.
DR GuidetoPHARMACOLOGY; 1517; -.
DR PhosphoSite; Q15208; -.
DR DMDM; 56749457; -.
DR PaxDb; Q15208; -.
DR PRIDE; Q15208; -.
DR DNASU; 11329; -.
DR Ensembl; ENST00000229812; ENSP00000229812; ENSG00000112079.
DR GeneID; 11329; -.
DR KEGG; hsa:11329; -.
DR UCSC; uc003omg.3; human.
DR CTD; 11329; -.
DR GeneCards; GC06M036461; -.
DR HGNC; HGNC:17847; STK38.
DR HPA; CAB004673; -.
DR MIM; 606964; gene.
DR neXtProt; NX_Q15208; -.
DR PharmGKB; PA38251; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233033; -.
DR HOVERGEN; HBG104247; -.
DR InParanoid; Q15208; -.
DR KO; K08790; -.
DR OMA; FCCEEEH; -.
DR OrthoDB; EOG7BZVS1; -.
DR PhylomeDB; Q15208; -.
DR SignaLink; Q15208; -.
DR ChiTaRS; STK38; human.
DR EvolutionaryTrace; Q15208; -.
DR GeneWiki; STK38; -.
DR GenomeRNAi; 11329; -.
DR NextBio; 43035; -.
DR PRO; PR:Q15208; -.
DR Bgee; Q15208; -.
DR CleanEx; HS_STK38; -.
DR Genevestigator; Q15208; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 465 Serine/threonine-protein kinase 38.
FT /FTId=PRO_0000086718.
FT DOMAIN 89 382 Protein kinase.
FT DOMAIN 383 455 AGC-kinase C-terminal.
FT NP_BIND 95 103 ATP (By similarity).
FT REGION 62 87 Interaction with S100B.
FT ACT_SITE 212 212 Proton acceptor (By similarity).
FT BINDING 118 118 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 74 74 Phosphothreonine.
FT MOD_RES 264 264 Phosphoserine.
FT MOD_RES 281 281 Phosphoserine; by autocatalysis.
FT MOD_RES 444 444 Phosphothreonine; by STK24/MST3.
FT VARIANT 18 18 E -> K (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041196.
FT VARIANT 145 145 D -> N (in dbSNP:rs56005153).
FT /FTId=VAR_041197.
FT VARIANT 267 267 K -> R (in dbSNP:rs56105564).
FT /FTId=VAR_041198.
FT MUTAGEN 74 74 T->A: Decreases autophosphorylation and
FT kinase activity. Reduced binding of
FT S100B.
FT MUTAGEN 118 118 K->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 281 281 S->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 444 444 T->A: Decreases autophosphorylation and
FT kinase activity.
FT HELIX 74 85
SQ SEQUENCE 465 AA; 54190 MW; 7262221DBFFAF83C CRC64;
MAMTGSTPCS SMSNHTKERV TMTKVTLENF YSNLIAQHEE REMRQKKLEK VMEEEGLKDE
EKRLRRSAHA RKETEFLRLK RTRLGLEDFE SLKVIGRGAF GEVRLVQKKD TGHVYAMKIL
RKADMLEKEQ VGHIRAERDI LVEADSLWVV KMFYSFQDKL NLYLIMEFLP GGDMMTLLMK
KDTLTEEETQ FYIAETVLAI DSIHQLGFIH RDIKPDNLLL DSKGHVKLSD FGLCTGLKKA
HRTEFYRNLN HSLPSDFTFQ NMNSKRKAET WKRNRRQLAF STVGTPDYIA PEVFMQTGYN
KLCDWWSLGV IMYEMLIGYP PFCSETPQET YKKVMNWKET LTFPPEVPIS EKAKDLILRF
CCEWEHRIGA PGVEEIKSNS FFEGVDWEHI RERPAAISIE IKSIDDTSNF DEFPESDILK
PTVATSNHPE TDYKNKDWVF INYTYKRFEG LTARGAIPSY MKAAK
//
MIM
606964
*RECORD*
*FIELD* NO
606964
*FIELD* TI
*606964 SERINE/THREONINE PROTEIN KINASE 38; STK38
;;NUCLEAR DBF2-RELATED PROTEIN; NDR
read more*FIELD* TX
CLONING
Using degenerate PCR primers corresponding to sequences of fly and worm
serine/threonine kinases to amplify human cDNAs, followed by screening
several cDNA libraries, Millward et al. (1995) isolated a cDNA encoding
STK38, which they called nuclear Dbf2 (yeast)-related protein, or NDR.
The deduced 465-amino acid protein, which is 68% identical to the fly
protein, contains 12 protein kinase catalytic subdomains and a potential
bipartite nuclear localization signal. Northern blot analysis revealed
expression of a 3.9-kb transcript in all tissues tested, with the
possible exception of adult brain. Highest expression was in peripheral
blood leukocytes. Immunoblot and immunofluorescence microscopy
demonstrated predominantly nuclear expression of a 55-kD protein.
GENE FUNCTION
Millward et al. (1995) showed that the kinase activity of STK38 appears
to be restricted to itself.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the STK38
gene to chromosome 6 (TMAP WI-6620).
*FIELD* RF
1. Millward, T.; Cron, P.; Hemmings, B. A.: Molecular cloning and
characterization of a conserved nuclear serine(threonine) protein
kinase. Proc. Nat. Acad. Sci. 92: 5022-5026, 1995.
*FIELD* CD
Paul J. Converse: 5/22/2002
*FIELD* ED
mgross: 05/22/2002
*RECORD*
*FIELD* NO
606964
*FIELD* TI
*606964 SERINE/THREONINE PROTEIN KINASE 38; STK38
;;NUCLEAR DBF2-RELATED PROTEIN; NDR
read more*FIELD* TX
CLONING
Using degenerate PCR primers corresponding to sequences of fly and worm
serine/threonine kinases to amplify human cDNAs, followed by screening
several cDNA libraries, Millward et al. (1995) isolated a cDNA encoding
STK38, which they called nuclear Dbf2 (yeast)-related protein, or NDR.
The deduced 465-amino acid protein, which is 68% identical to the fly
protein, contains 12 protein kinase catalytic subdomains and a potential
bipartite nuclear localization signal. Northern blot analysis revealed
expression of a 3.9-kb transcript in all tissues tested, with the
possible exception of adult brain. Highest expression was in peripheral
blood leukocytes. Immunoblot and immunofluorescence microscopy
demonstrated predominantly nuclear expression of a 55-kD protein.
GENE FUNCTION
Millward et al. (1995) showed that the kinase activity of STK38 appears
to be restricted to itself.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the STK38
gene to chromosome 6 (TMAP WI-6620).
*FIELD* RF
1. Millward, T.; Cron, P.; Hemmings, B. A.: Molecular cloning and
characterization of a conserved nuclear serine(threonine) protein
kinase. Proc. Nat. Acad. Sci. 92: 5022-5026, 1995.
*FIELD* CD
Paul J. Converse: 5/22/2002
*FIELD* ED
mgross: 05/22/2002