Full text data of STK38L
STK38L
(KIAA0965, NDR2)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein kinase 38-like; 2.7.11.1 (NDR2 protein kinase; Nuclear Dbf2-related kinase 2)
Serine/threonine-protein kinase 38-like; 2.7.11.1 (NDR2 protein kinase; Nuclear Dbf2-related kinase 2)
UniProt
Q9Y2H1
ID ST38L_HUMAN Reviewed; 464 AA.
AC Q9Y2H1; A8K4U0; Q8TBX7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 3.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Serine/threonine-protein kinase 38-like;
DE EC=2.7.11.1;
DE AltName: Full=NDR2 protein kinase;
DE AltName: Full=Nuclear Dbf2-related kinase 2;
GN Name=STK38L; Synonyms=KIAA0965, NDR2;
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, SUBCELLULAR LOCATION, ENZYME
RP REGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; SER-282
RP AND THR-442, AND MUTAGENESIS OF THR-75; LYS-119; SER-282 AND THR-442.
RC TISSUE=Brain;
RX PubMed=15037617; DOI=10.1074/jbc.M402472200;
RA Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A.,
RA Hemmings B.A.;
RT "Regulation of NDR2 protein kinase by multi-site phosphorylation and
RT the S100B calcium-binding protein.";
RL J. Biol. Chem. 279:23806-23812(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 2-18; 26-42; 48-64; 73-79; 83-98; 123-161;
RP 213-224; 229-240; 249-266; 340-392 AND 433-460, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION,
RP 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 [9]
RP PHOSPHORYLATION AT THR-442, ENZYME REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16314523; DOI=10.1128/MCB.25.24.11019-11029.2005;
RA Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J.,
RA Hemmings B.A.;
RT "Regulation of NDR protein kinase by hydrophobic motif phosphorylation
RT mediated by the mammalian Ste20-like kinase MST3.";
RL Mol. Cell. Biol. 25:11019-11029(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11]
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 [12]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-99.
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: Involved in the regulation of structural processes in
CC differentiating and mature neuronal cells (By similarity).
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-282. Thr-442 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-442 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 STK38L.
CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38L.
CC Interacts with MICAL1; leading to inhibit the protein kinase
CC activity by antagonizing activation by MST1/STK4 (By similarity).
CC Interacts with MOB1 and MOB2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Membrane. Note=Associated with the actin cytoskeleton. Co-
CC localizes with STK24/MST3 in the membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC observed in the thymus.
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; AB023182; BAA76809.2; -; mRNA.
DR EMBL; AK291055; BAF83744.1; -; mRNA.
DR EMBL; CH471094; EAW96549.1; -; Genomic_DNA.
DR EMBL; BC028603; AAH28603.1; -; mRNA.
DR RefSeq; NP_055815.1; NM_015000.3.
DR UniGene; Hs.184523; -.
DR ProteinModelPortal; Q9Y2H1; -.
DR SMR; Q9Y2H1; 71-450.
DR IntAct; Q9Y2H1; 4.
DR MINT; MINT-1631355; -.
DR STRING; 9606.ENSP00000373684; -.
DR BindingDB; Q9Y2H1; -.
DR ChEMBL; CHEMBL4851; -.
DR GuidetoPHARMACOLOGY; 1518; -.
DR PhosphoSite; Q9Y2H1; -.
DR DMDM; 56749668; -.
DR PaxDb; Q9Y2H1; -.
DR PeptideAtlas; Q9Y2H1; -.
DR PRIDE; Q9Y2H1; -.
DR DNASU; 23012; -.
DR Ensembl; ENST00000389032; ENSP00000373684; ENSG00000211455.
DR GeneID; 23012; -.
DR KEGG; hsa:23012; -.
DR UCSC; uc001rhr.3; human.
DR CTD; 23012; -.
DR GeneCards; GC12P027396; -.
DR HGNC; HGNC:17848; STK38L.
DR HPA; HPA038623; -.
DR neXtProt; NX_Q9Y2H1; -.
DR PharmGKB; PA38252; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233033; -.
DR HOVERGEN; HBG104247; -.
DR InParanoid; Q9Y2H1; -.
DR KO; K08790; -.
DR OMA; YMKAGKA; -.
DR SignaLink; Q9Y2H1; -.
DR ChiTaRS; STK38L; human.
DR GeneWiki; STK38L; -.
DR GenomeRNAi; 23012; -.
DR NextBio; 43932; -.
DR PRO; PR:Q9Y2H1; -.
DR ArrayExpress; Q9Y2H1; -.
DR Bgee; Q9Y2H1; -.
DR CleanEx; HS_STK38L; -.
DR Genevestigator; Q9Y2H1; -.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
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:0051128; P:regulation of cellular component organization; ISS: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 Acetylation; Actin-binding; ATP-binding; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 464 Serine/threonine-protein kinase 38-like.
FT /FTId=PRO_0000086720.
FT DOMAIN 90 383 Protein kinase.
FT DOMAIN 384 453 AGC-kinase C-terminal.
FT NP_BIND 96 104 ATP (By similarity).
FT REGION 63 88 S100B binding (By similarity).
FT ACT_SITE 213 213 Proton acceptor (By similarity).
FT BINDING 119 119 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 75 75 Phosphothreonine.
FT MOD_RES 282 282 Phosphoserine; by autocatalysis.
FT MOD_RES 442 442 Phosphothreonine; by STK24/MST3.
FT VARIANT 99 99 G -> A (in a aLL TEL/AML1+ sample;
FT somatic mutation).
FT /FTId=VAR_041199.
FT MUTAGEN 75 75 T->A: Decreased kinase activity. Reduced
FT binding of S100B.
FT MUTAGEN 119 119 K->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 282 282 S->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 442 442 T->A: Decreased kinase activity.
SQ SEQUENCE 464 AA; 54003 MW; 71347E80BC3ADCB3 CRC64;
MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD
EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI
LRKSDMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM
KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK
AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY
NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI SEKAKDLILR
FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI EIKSIDDTSN FDDFPESDIL
QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL
//
ID ST38L_HUMAN Reviewed; 464 AA.
AC Q9Y2H1; A8K4U0; Q8TBX7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-DEC-2004, sequence version 3.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Serine/threonine-protein kinase 38-like;
DE EC=2.7.11.1;
DE AltName: Full=NDR2 protein kinase;
DE AltName: Full=Nuclear Dbf2-related kinase 2;
GN Name=STK38L; Synonyms=KIAA0965, NDR2;
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, SUBCELLULAR LOCATION, ENZYME
RP REGULATION, INTERACTION WITH S100, PHOSPHORYLATION AT THR-75; SER-282
RP AND THR-442, AND MUTAGENESIS OF THR-75; LYS-119; SER-282 AND THR-442.
RC TISSUE=Brain;
RX PubMed=15037617; DOI=10.1074/jbc.M402472200;
RA Stegert M.R., Tamaskovic R., Bichsel S.J., Hergovich A.,
RA Hemmings B.A.;
RT "Regulation of NDR2 protein kinase by multi-site phosphorylation and
RT the S100B calcium-binding protein.";
RL J. Biol. Chem. 279:23806-23812(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 2-18; 26-42; 48-64; 73-79; 83-98; 123-161;
RP 213-224; 229-240; 249-266; 340-392 AND 433-460, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Calvo F., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION,
RP 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 [9]
RP PHOSPHORYLATION AT THR-442, ENZYME REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16314523; DOI=10.1128/MCB.25.24.11019-11029.2005;
RA Stegert M.R., Hergovich A., Tamaskovic R., Bichsel S.J.,
RA Hemmings B.A.;
RT "Regulation of NDR protein kinase by hydrophobic motif phosphorylation
RT mediated by the mammalian Ste20-like kinase MST3.";
RL Mol. Cell. Biol. 25:11019-11029(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11]
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 [12]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-99.
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: Involved in the regulation of structural processes in
CC differentiating and mature neuronal cells (By similarity).
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-282. Thr-442 then undergoes calcium-
CC dependent phosphorylation by STK24/MST3. Interactions between
CC phosphorylated Thr-442 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 STK38L.
CC -!- SUBUNIT: Homodimeric S100B binds two molecules of STK38L.
CC Interacts with MICAL1; leading to inhibit the protein kinase
CC activity by antagonizing activation by MST1/STK4 (By similarity).
CC Interacts with MOB1 and MOB2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Membrane. Note=Associated with the actin cytoskeleton. Co-
CC localizes with STK24/MST3 in the membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels
CC observed in the thymus.
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; AB023182; BAA76809.2; -; mRNA.
DR EMBL; AK291055; BAF83744.1; -; mRNA.
DR EMBL; CH471094; EAW96549.1; -; Genomic_DNA.
DR EMBL; BC028603; AAH28603.1; -; mRNA.
DR RefSeq; NP_055815.1; NM_015000.3.
DR UniGene; Hs.184523; -.
DR ProteinModelPortal; Q9Y2H1; -.
DR SMR; Q9Y2H1; 71-450.
DR IntAct; Q9Y2H1; 4.
DR MINT; MINT-1631355; -.
DR STRING; 9606.ENSP00000373684; -.
DR BindingDB; Q9Y2H1; -.
DR ChEMBL; CHEMBL4851; -.
DR GuidetoPHARMACOLOGY; 1518; -.
DR PhosphoSite; Q9Y2H1; -.
DR DMDM; 56749668; -.
DR PaxDb; Q9Y2H1; -.
DR PeptideAtlas; Q9Y2H1; -.
DR PRIDE; Q9Y2H1; -.
DR DNASU; 23012; -.
DR Ensembl; ENST00000389032; ENSP00000373684; ENSG00000211455.
DR GeneID; 23012; -.
DR KEGG; hsa:23012; -.
DR UCSC; uc001rhr.3; human.
DR CTD; 23012; -.
DR GeneCards; GC12P027396; -.
DR HGNC; HGNC:17848; STK38L.
DR HPA; HPA038623; -.
DR neXtProt; NX_Q9Y2H1; -.
DR PharmGKB; PA38252; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233033; -.
DR HOVERGEN; HBG104247; -.
DR InParanoid; Q9Y2H1; -.
DR KO; K08790; -.
DR OMA; YMKAGKA; -.
DR SignaLink; Q9Y2H1; -.
DR ChiTaRS; STK38L; human.
DR GeneWiki; STK38L; -.
DR GenomeRNAi; 23012; -.
DR NextBio; 43932; -.
DR PRO; PR:Q9Y2H1; -.
DR ArrayExpress; Q9Y2H1; -.
DR Bgee; Q9Y2H1; -.
DR CleanEx; HS_STK38L; -.
DR Genevestigator; Q9Y2H1; -.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
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:0051128; P:regulation of cellular component organization; ISS: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 Acetylation; Actin-binding; ATP-binding; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 464 Serine/threonine-protein kinase 38-like.
FT /FTId=PRO_0000086720.
FT DOMAIN 90 383 Protein kinase.
FT DOMAIN 384 453 AGC-kinase C-terminal.
FT NP_BIND 96 104 ATP (By similarity).
FT REGION 63 88 S100B binding (By similarity).
FT ACT_SITE 213 213 Proton acceptor (By similarity).
FT BINDING 119 119 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 75 75 Phosphothreonine.
FT MOD_RES 282 282 Phosphoserine; by autocatalysis.
FT MOD_RES 442 442 Phosphothreonine; by STK24/MST3.
FT VARIANT 99 99 G -> A (in a aLL TEL/AML1+ sample;
FT somatic mutation).
FT /FTId=VAR_041199.
FT MUTAGEN 75 75 T->A: Decreased kinase activity. Reduced
FT binding of S100B.
FT MUTAGEN 119 119 K->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 282 282 S->A: Loss of autophosphorylation and
FT kinase activity.
FT MUTAGEN 442 442 T->A: Decreased kinase activity.
SQ SEQUENCE 464 AA; 54003 MW; 71347E80BC3ADCB3 CRC64;
MAMTAGTTTT FPMSNHTRER VTVAKLTLEN FYSNLILQHE ERETRQKKLE VAMEEEGLAD
EEKKLRRSQH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI
LRKSDMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM
KKDTLTEEET QFYISETVLA IDAIHQLGFI HRDIKPDNLL LDAKGHVKLS DFGLCTGLKK
AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY
NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWKE TLVFPPEVPI SEKAKDLILR
FCIDSENRIG NSGVEEIKGH PFFEGVDWEH IRERPAAIPI EIKSIDDTSN FDDFPESDIL
QPVPNTTEPD YKSKDWVFLN YTYKRFEGLT QRGSIPTYMK AGKL
//