ID SG223_HUMAN Reviewed; 1406 AA.
AC Q86YV5; Q8N3N5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 4.
DT 18-JAN-2017, entry version 118.
DE RecName: Full=Tyrosine-protein kinase SgK223;
DE EC=2.7.10.2;
DE AltName: Full=Sugen kinase 223;
GN Name=SGK223;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-1406, AND VARIANTS GLN-404; LEU-569;
RP CYS-578 AND THR-1113.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1406, AND VARIANT
RP THR-1113.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP IDENTIFICATION.
RX PubMed=12471243; DOI=10.1126/science.1075762;
RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.;
RT "The protein kinase complement of the human genome.";
RL Science 298:1912-1934(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696 AND SER-745, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND IDENTIFICATION
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-696 AND
RP SER-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-782, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-122; GLY-137; ILE-139; GLN-404;
RP LEU-569; CYS-578; ALA-595; THR-662; LEU-814; ARG-851; LEU-1003;
RP MET-1041; THR-1113 AND HIS-1315.
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 -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC ProRule:PRU10028}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR EMBL; AC068353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122582; BAC56923.1; -; mRNA.
DR EMBL; AL833872; CAD38729.1; -; mRNA.
DR CCDS; CCDS43706.1; -.
DR RefSeq; NP_001074295.2; NM_001080826.2.
DR RefSeq; XP_005272426.2; XM_005272369.4.
DR RefSeq; XP_005272427.2; XM_005272370.4.
DR UniGene; Hs.583863; -.
DR UniGene; Hs.657673; -.
DR ProteinModelPortal; Q86YV5; -.
DR BioGrid; 127591; 6.
DR IntAct; Q86YV5; 7.
DR MINT; MINT-1413315; -.
DR STRING; 9606.ENSP00000330930; -.
DR iPTMnet; Q86YV5; -.
DR PhosphoSitePlus; Q86YV5; -.
DR BioMuta; SGK223; -.
DR DMDM; 327478560; -.
DR EPD; Q86YV5; -.
DR PaxDb; Q86YV5; -.
DR PeptideAtlas; Q86YV5; -.
DR PRIDE; Q86YV5; -.
DR DNASU; 157285; -.
DR GeneID; 157285; -.
DR KEGG; hsa:157285; -.
DR UCSC; uc064kbu.1; human.
DR CTD; 157285; -.
DR DisGeNET; 157285; -.
DR GeneCards; SGK223; -.
DR H-InvDB; HIX0007293; -.
DR HPA; HPA012066; -.
DR neXtProt; NX_Q86YV5; -.
DR OpenTargets; ENSG00000275342; -.
DR eggNOG; ENOG410IJMD; Eukaryota.
DR eggNOG; ENOG4110SRP; LUCA.
DR GeneTree; ENSGT00460000041554; -.
DR HOGENOM; HOG000168455; -.
DR HOVERGEN; HBG055817; -.
DR InParanoid; Q86YV5; -.
DR KO; K17537; -.
DR OMA; TWHRLHP; -.
DR OrthoDB; EOG091G03K2; -.
DR BioCyc; ZFISH:HS11039-MONOMER; -.
DR SignaLink; Q86YV5; -.
DR ChiTaRS; SGK223; human.
DR GenomeRNAi; 157285; -.
DR PRO; PR:Q86YV5; -.
DR Proteomes; UP000005640; Unplaced.
DR Bgee; ENSG00000182319; -.
DR Genevisible; Q86YV5; HS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1 1406 Tyrosine-protein kinase SgK223.
FT /FTId=PRO_0000263008.
FT DOMAIN 978 1329 Protein kinase. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT NP_BIND 984 992 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT COMPBIAS 55 58 Poly-Pro.
FT COMPBIAS 713 718 Poly-Pro.
FT ACT_SITE 1145 1145 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10028}.
FT BINDING 1024 1024 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00159}.
FT MOD_RES 148 148 Phosphoserine.
FT {ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 413 413 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:Q571I4}.
FT MOD_RES 696 696 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 745 745 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:19690332}.
FT MOD_RES 782 782 Phosphoserine.
FT {ECO:0000244|PubMed:24275569}.
FT MOD_RES 826 826 Phosphoserine.
FT {ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT VARIANT 122 122 L -> I (in dbSNP:rs55764617).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041803.
FT VARIANT 137 137 R -> G (in dbSNP:rs56290960).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041804.
FT VARIANT 139 139 V -> I (in dbSNP:rs34346032).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041805.
FT VARIANT 404 404 R -> Q (in dbSNP:rs3896980).
FT {ECO:0000269|PubMed:17344846,
FT ECO:0000269|Ref.2}.
FT /FTId=VAR_041806.
FT VARIANT 569 569 P -> L (in dbSNP:rs4840955).
FT {ECO:0000269|PubMed:17344846,
FT ECO:0000269|Ref.2}.
FT /FTId=VAR_041807.
FT VARIANT 578 578 S -> C (in dbSNP:rs4840953).
FT {ECO:0000269|PubMed:17344846,
FT ECO:0000269|Ref.2}.
FT /FTId=VAR_041808.
FT VARIANT 595 595 P -> A (in dbSNP:rs55994745).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041809.
FT VARIANT 662 662 P -> T (in dbSNP:rs56351643).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041810.
FT VARIANT 814 814 P -> L (in dbSNP:rs56207906).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041811.
FT VARIANT 851 851 H -> R (in dbSNP:rs56215812).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041812.
FT VARIANT 1003 1003 S -> L (in dbSNP:rs56289289).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041813.
FT VARIANT 1041 1041 V -> M (in dbSNP:rs28533138).
FT {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041814.
FT VARIANT 1113 1113 A -> T (in dbSNP:rs12549973).
FT {ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.2}.
FT /FTId=VAR_041815.
FT VARIANT 1315 1315 R -> H. {ECO:0000269|PubMed:17344846}.
FT /FTId=VAR_041816.
FT CONFLICT 1226 1226 G -> S (in Ref. 2; BAC56923 and 3;
FT CAD38729). {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 978 1329 iprf:PROTEIN_KINASE_DOM [T]
FT MYHIT 1117 1322 ipfam:Pkinase [T]
FT MYHIT 1009 1328 ismart:S_TKc [T]
FT MYHIT 1141 1153 ipat:PROTEIN_KINASE_TYR [T]
SQ SEQUENCE 1406 AA; 149624 MW; 941BCF315B826148 CRC64;
MHQTLCLNPE SLKMSACSDF VEHIWKPGSC KNCFCLRSDH QLVAGPPQPR AGSLPPPPRL
PPRPENCRLE DEGVNSSPYS KPTIAVKPTM MSSEASDVWT EANLSAEVSQ VIWRRAPGKL
PLPKQEDAPV VYLGSFRGVQ KPAGPSTSPD GNSRCPPAYT MVGLHNLEPR GERNIAFHPV
SFPEEKAVHK EKPSFPYQDR PSTQESFRQK LAAFAGTTSG CHQGPGPLRE SLPSEDDSDQ
RCSPSGDSEG GEYCSILDCC PGSPVAKAAS QTAGSRGRHG GRDCSPTCWE QGKCSGPAEQ
EKRGPSFPKE CCSQGPTAHP SCLGPKKLSL TSEAAISSDG LSCGSGSGSG SGASSPFVPH
LESDYCSLMK EPAPEKQQDP GCPGVTPSRC LGLTGEPQPP AHPREATQPE PIYAESTKRK
KAAPVPSKSQ AKIEHAAAAQ GQGQVCTGNA WAQKAASGWG RDSPDPTPQV SATITVMAAH
PEEDHRTIYL SSPDSAVGVQ WPRGPVSQNS EVGEEETSAG QGLSSRESHA HSASESKPKE
RPAIPPKLSK SSPVGSPVSP SAGGPPVSPL ADLSDGSSGG SSIGPQPPSQ GPADPAPSCR
TNGVAISDPS RCPQPAASSA SEQRRPRFQA GTWSRQCRIE EEEEVEQELL SHSWGRETKN
GPTDHSNSTT WHRLHPTDGS SGQNSKVGTG MSKSASFAFE FPKDRSGIET FSPPPPPPKS
RHLLKMNKSS SDLEKVSQGS AESLSPSFRG VHVSFTTGST DSLASDSRTC SDGGPSSELA
HSPTNSGKKL FAPVPFPSGS TEDVSPSGPQ QPPPLPQKKI VSRAASSPDG FFWTQGSPKP
GTASPKLNLS HSETNVHDES HFSYSLSPGN RHHPVFSSSD PLEKAFKGSG HWLPAAGLAG
NRGGCGSPGL QCKGAPSASS SQLSVSSQAS TGSTQLQLHG LLSNISSKEG TYAKLGGLYT
QSLARLVAKC EDLFMGGQKK ELHFNENNWS LFKLTCNKPC CDSGDAIYYC ATCSEDPGST
YAVKICKAPE PKTVSYCSPS VPVHFNIQQD CGHFVASVPS SMLSSPDAPK DPVPALPTHP
PAQEQDCVVV ITREVPHQTA SDFVRDSAAS HQAEPEAYER RVCFLLLQLC NGLEHLKEHG
IIHRDLCLEN LLLVHCTLQA GPGPAPAPAP APAPAAAAPP CSSAAPPAGG TLSPAAGPAS
PEGPREKQLP RLIISNFLKA KQKPGGTPNL QQKKSQARLA PEIVSASQYR KFDEFQTGIL
IYELLHQPNP FEVRAQLRER DYRQEDLPPL PALSLYSPGL QQLAHLLLEA DPIKRIRIGE
AKRVLQCLLW GPRRELVQQP GTSEEALCGT LHNWIDMKRA LMMMKFAEKA VDRRRGVELE
DWLCCQYLAS AEPGALLQSL KLLQLL
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