SG196_HUMAN
ID SG196_HUMAN Reviewed; 350 AA.
AC Q9H5K3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein O-mannose kinase;
DE Short=POMK;
DE EC=2.7.1.183 {ECO:0000269|PubMed:23929950};
DE AltName: Full=Protein kinase-like protein SgK196;
DE AltName: Full=Sugen kinase 196;
GN Name=POMK; Synonyms=SGK196;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
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., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., 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., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] PRO-48; PHE-140; MET-254; THR-301 AND
RP ILE-342.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION OF VARIANT MDDGA12 ARG-137.
RX PubMed=23929950; DOI=10.1126/science.1239951;
RA Yoshida-Moriguchi T., Willer T., Anderson M.E., Venzke D., Whyte T.,
RA Muntoni F., Lee H., Nelson S.F., Yu L., Campbell K.P.;
RT "SGK196 is a glycosylation-specific O-mannose kinase required for
RT dystroglycan function.";
RL Science 341:896-899(2013).
RN [8]
RP INVOLVEMENT IN MDDGA12.
RX PubMed=24556084; DOI=10.1136/jmedgenet-2013-102236;
RA von Renesse A., Petkova M.V., Luetzkendorf S., Heinemeyer J., Gill E.,
RA Huebner C., von Moers A., Stenzel W., Schuelke M.;
RT "POMK mutation in a family with congenital muscular dystrophy with merosin
RT deficiency, hypomyelination, mild hearing deficit and intellectual
RT disability.";
RL J. Med. Genet. 51:275-282(2014).
RN [9]
RP TISSUE SPECIFICITY, INVOLVEMENT IN MDDGC12, AND VARIANT MDDGA12 ASP-302.
RX PubMed=24925318; DOI=10.1093/hmg/ddu296;
RA Di Costanzo S., Balasubramanian A., Pond H.L., Rozkalne A., Pantaleoni C.,
RA Saredi S., Gupta V.A., Sunu C.M., Yu T.W., Kang P.B., Salih M.A., Mora M.,
RA Gussoni E., Walsh C.A., Manzini M.C.;
RT "POMK mutations disrupt muscle development leading to a spectrum of
RT neuromuscular presentations.";
RL Hum. Mol. Genet. 23:5781-5792(2014).
RN [10]
RP VARIANTS MDDGA12 ARG-137 AND ARG-258, FUNCTION, AND INVOLVEMENT IN MDDGA12.
RX PubMed=23519211; DOI=10.1126/science.1233675;
RA Jae L.T., Raaben M., Riemersma M., van Beusekom E., Blomen V.A., Velds A.,
RA Kerkhoven R.M., Carette J.E., Topaloglu H., Meinecke P., Wessels M.W.,
RA Lefeber D.J., Whelan S.P., van Bokhoven H., Brummelkamp T.R.;
RT "Deciphering the glycosylome of dystroglycanopathies using haploid screens
RT for lassa virus entry.";
RL Science 340:479-483(2013).
CC -!- FUNCTION: Protein O-mannose kinase that specifically mediates
CC phosphorylation at the 6-position of an O-mannose of the trisaccharide
CC (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-
CC beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide
CC (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-
CC (phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a
CC carbohydrate structure present in alpha-dystroglycan (DAG1), which is
CC required for binding laminin G-like domain-containing extracellular
CC proteins with high affinity. Only shows kinase activity when the
CC GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-
CC mannose, suggesting that this disaccharide serves as the substrate
CC recognition motif. {ECO:0000269|PubMed:23519211,
CC ECO:0000269|PubMed:23929950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-alpha-D-Man]-L-
CC Thr-[protein] + ATP = 3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-
CC (O-6-P-alpha-D-Man)]-Thr-[protein] + ADP + H(+);
CC Xref=Rhea:RHEA:52616, Rhea:RHEA-COMP:13308, Rhea:RHEA-COMP:13309,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:136709,
CC ChEBI:CHEBI:136710, ChEBI:CHEBI:456216; EC=2.7.1.183;
CC Evidence={ECO:0000269|PubMed:23929950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 uM for ATP {ECO:0000269|PubMed:23929950};
CC -!- INTERACTION:
CC Q9H5K3; O94766: B3GAT3; NbExp=2; IntAct=EBI-11337900, EBI-3917958;
CC Q9H5K3; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-11337900, EBI-725665;
CC Q9H5K3; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-11337900, EBI-12070086;
CC Q9H5K3; Q8WZA1: POMGNT1; NbExp=2; IntAct=EBI-11337900, EBI-3912424;
CC Q9H5K3; P04843: RPN1; NbExp=2; IntAct=EBI-11337900, EBI-355963;
CC Q9H5K3; P04844: RPN2; NbExp=2; IntAct=EBI-11337900, EBI-719731;
CC Q9H5K3; P46977: STT3A; NbExp=2; IntAct=EBI-11337900, EBI-719212;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highest expression is observed in brain, skeletal
CC muscle, kidney and heart in fetal and adult tissues.
CC {ECO:0000269|PubMed:24925318}.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with brain
CC and eye anomalies A12 (MDDGA12) [MIM:615249]: An autosomal recessive
CC disorder characterized by congenital muscular dystrophy associated with
CC cobblestone lissencephaly and other brain anomalies, eye malformations,
CC profound intellectual disability, and death usually in the first years
CC of life. Included diseases are the more severe Walker-Warburg syndrome
CC and the slightly less severe muscle-eye-brain disease.
CC {ECO:0000269|PubMed:23519211, ECO:0000269|PubMed:23929950,
CC ECO:0000269|PubMed:24556084, ECO:0000269|PubMed:24925318}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C12
CC (MDDGC12) [MIM:616094]: An autosomal recessive limb-girdle congenital
CC muscular dystrophy, characterized by muscle weakness and delayed motor
CC development in association with cognitive impairment.
CC {ECO:0000269|PubMed:24925318}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. STKL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although related to the Ser/Thr protein kinase family, has no
CC protein kinase activity and acts as a mannose kinase instead.
CC {ECO:0000305|PubMed:23929950}.
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DR EMBL; AK027009; BAB15623.1; -; mRNA.
DR EMBL; AC113191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101548; AAI01549.1; -; mRNA.
DR EMBL; BC113703; AAI13704.1; -; mRNA.
DR CCDS; CCDS6141.1; -.
DR RefSeq; NP_001264900.1; NM_001277971.1.
DR RefSeq; NP_115613.1; NM_032237.4.
DR AlphaFoldDB; Q9H5K3; -.
DR SMR; Q9H5K3; -.
DR BioGRID; 123942; 146.
DR IntAct; Q9H5K3; 206.
DR STRING; 9606.ENSP00000331258; -.
DR GlyConnect; 1664; 3 N-Linked glycans (1 site).
DR GlyGen; Q9H5K3; 4 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q9H5K3; -.
DR PhosphoSitePlus; Q9H5K3; -.
DR BioMuta; POMK; -.
DR DMDM; 74761446; -.
DR EPD; Q9H5K3; -.
DR jPOST; Q9H5K3; -.
DR MassIVE; Q9H5K3; -.
DR MaxQB; Q9H5K3; -.
DR PaxDb; Q9H5K3; -.
DR PeptideAtlas; Q9H5K3; -.
DR PRIDE; Q9H5K3; -.
DR ProteomicsDB; 80917; -.
DR Antibodypedia; 24208; 257 antibodies from 22 providers.
DR DNASU; 84197; -.
DR Ensembl; ENST00000331373.10; ENSP00000331258.5; ENSG00000185900.11.
DR Ensembl; ENST00000676193.1; ENSP00000502774.1; ENSG00000185900.11.
DR GeneID; 84197; -.
DR KEGG; hsa:84197; -.
DR MANE-Select; ENST00000331373.10; ENSP00000331258.5; NM_032237.5; NP_115613.1.
DR UCSC; uc003xpw.4; human.
DR CTD; 84197; -.
DR DisGeNET; 84197; -.
DR GeneCards; POMK; -.
DR HGNC; HGNC:26267; POMK.
DR HPA; ENSG00000185900; Low tissue specificity.
DR MalaCards; POMK; -.
DR MIM; 615247; gene.
DR MIM; 615249; phenotype.
DR MIM; 616094; phenotype.
DR neXtProt; NX_Q9H5K3; -.
DR OpenTargets; ENSG00000185900; -.
DR Orphanet; 370959; Congenital muscular dystrophy with cerebellar involvement.
DR Orphanet; 445110; Limb-girdle muscular dystrophy due to POMK deficiency.
DR Orphanet; 899; Walker-Warburg syndrome.
DR VEuPathDB; HostDB:ENSG00000185900; -.
DR eggNOG; ENOG502QQQV; Eukaryota.
DR GeneTree; ENSGT00390000004945; -.
DR HOGENOM; CLU_067581_0_0_1; -.
DR InParanoid; Q9H5K3; -.
DR OMA; GRLVKCG; -.
DR OrthoDB; 805598at2759; -.
DR PhylomeDB; Q9H5K3; -.
DR BioCyc; MetaCyc:G66-30734-MON; -.
DR BRENDA; 2.7.1.183; 2681.
DR PathwayCommons; Q9H5K3; -.
DR Reactome; R-HSA-5173105; O-linked glycosylation.
DR SignaLink; Q9H5K3; -.
DR BioGRID-ORCS; 84197; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; POMK; human.
DR GenomeRNAi; 84197; -.
DR Pharos; Q9H5K3; Tbio.
DR PRO; PR:Q9H5K3; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H5K3; protein.
DR Bgee; ENSG00000185900; Expressed in paraflocculus and 206 other tissues.
DR ExpressionAtlas; Q9H5K3; baseline and differential.
DR Genevisible; Q9H5K3; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019200; F:carbohydrate kinase activity; IBA:GO_Central.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007420; P:brain development; TAS:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039318; POMK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR22618; PTHR22618; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Congenital muscular dystrophy; Disease variant;
KW Dystroglycanopathy; Endoplasmic reticulum; Glycoprotein; Kinase;
KW Limb-girdle muscular dystrophy; Lissencephaly; Membrane;
KW Nucleotide-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Protein O-mannose kinase"
FT /id="PRO_0000262996"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 81..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 48
FT /note="S -> P (in dbSNP:rs34466747)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041372"
FT VARIANT 137
FT /note="L -> R (in MDDGA12; loss of kinase activity;
FT dbSNP:rs397509385)"
FT /evidence="ECO:0000269|PubMed:23519211,
FT ECO:0000269|PubMed:23929950"
FT /id="VAR_069625"
FT VARIANT 140
FT /note="Y -> F (in dbSNP:rs34750053)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041373"
FT VARIANT 254
FT /note="V -> M (in dbSNP:rs34715198)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041374"
FT VARIANT 258
FT /note="Q -> R (in MDDGA12; dbSNP:rs397509386)"
FT /evidence="ECO:0000269|PubMed:23519211"
FT /id="VAR_069626"
FT VARIANT 301
FT /note="M -> T (in dbSNP:rs33920561)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041375"
FT VARIANT 302
FT /note="V -> D (in MDDGA12; dbSNP:rs199756983)"
FT /evidence="ECO:0000269|PubMed:24925318"
FT /id="VAR_072560"
FT VARIANT 342
FT /note="M -> I (in a lung small cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041376"
SQ SEQUENCE 350 AA; 40050 MW; E074FDB2E5861B0F CRC64;
MEKQPQNSRR GLAPREVPPA VGLLLIMALM NTLLYLCLDH FFIAPRQSTV DPTHCPYGHF
RIGQMKNCSP WLSCEELRTE VRQLKRVGEG AVKRVFLSEW KEHKVALSQL TSLEMKDDFL
HGLQMLKSLQ GTHVVTLLGY CEDDNTMLTE YHPLGSLSNL EETLNLSKYQ NVNTWQHRLE
LAMDYVSIIN YLHHSPVGTR VMCDSNDLPK TLSQYLLTSN FSILANDLDA LPLVNHSSGM
LVKCGHRELH GDFVAPEQLW PYGEDVPFHD DLMPSYDEKI DIWKIPDISS FLLGHIEGSD
MVRFHLFDIH KACKSQTPSE RPTAQDVLET YQKVLDTLRD AMMSQAREML
