ALPK2_HUMAN
ID ALPK2_HUMAN Reviewed; 2170 AA.
AC Q86TB3; Q6ZUX0; Q8NAT5; Q96L95;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alpha-protein kinase 2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:29888752};
DE AltName: Full=Heart alpha-protein kinase {ECO:0000303|PubMed:10021370};
GN Name=ALPK2; Synonyms=HAK;
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], AND VARIANTS GLN-719; SER-810;
RP THR-825; ILE-891; LYS-916; VAL-1057; PRO-1174; SER-1449; SER-1551 AND
RP VAL-2157.
RC TISSUE=Skeletal muscle;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 552-1770, AND VARIANTS GLN-719;
RP SER-810; THR-825; ILE-891; LYS-916; VAL-1057; PRO-1174; SER-1449 AND
RP VAL-2157.
RC TISSUE=Heart, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 569-2170, AND VARIANTS GLN-719; SER-810;
RP THR-825; ILE-891; LYS-916; VAL-1057; PRO-1174 AND SER-1449.
RX PubMed=10021370; DOI=10.1016/s0960-9822(99)80006-2;
RA Ryazanov A.G., Pavur K.S., Dorovkov M.V.;
RT "Alpha-kinases: a new class of protein kinases with a novel catalytic
RT domain.";
RL Curr. Biol. 9:R43-R45(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29888752; DOI=10.1016/j.isci.2018.03.010;
RA Hofsteen P., Robitaille A.M., Strash N., Palpant N., Moon R.T., Pabon L.,
RA Murry C.E.;
RT "ALPK2 Promotes Cardiogenesis in Zebrafish and Human Pluripotent Stem
RT Cells.";
RL IScience 2:88-100(2018).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-942 AND THR-1476.
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 SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT GLU-1853, AND VARIANTS
RP THR-2; VAL-29; SER-136; THR-202; LEU-388; ILE-397; VAL-457; GLN-719;
RP SER-810; THR-825; ASN-829; PRO-875; LEU-884; ILE-891; LYS-916; THR-969;
RP THR-977; VAL-1057; PRO-1174; SER-1288; SER-1449; SER-1551; ARG-1579;
RP GLU-1730; ASN-1745; TYR-1767; GLU-1853; CYS-1884; THR-1919; THR-1978 AND
RP VAL-2157.
RX PubMed=28668886; DOI=10.21873/anticanres.11765;
RA Nishi K., Luo H., Nakabayashi K., Doi K., Ishikura S., Iwaihara Y.,
RA Yoshida Y., Tanisawa K., Arai T., Mori S., Sawabe M., Muramatsu M.,
RA Tanaka M., Sakata T., Shirasawa S., Tsunoda T.;
RT "An Alpha-kinase 2 Gene Variant Disrupts Filamentous Actin Localization in
RT the Surface Cells of Colorectal Cancer Spheroids.";
RL Anticancer Res. 37:3855-3862(2017).
CC -!- FUNCTION: Protein kinase that recognizes phosphorylation sites in which
CC the surrounding peptides have an alpha-helical conformation
CC (PubMed:10021370). Regulates cardiac development and cardiomyocyte
CC differentiation by negatively regulating Wnt/beta-catenin signaling
CC (PubMed:29888752). {ECO:0000269|PubMed:29888752,
CC ECO:0000303|PubMed:10021370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305|PubMed:29888752};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:28668886}.
CC -!- TISSUE SPECIFICITY: Expressed in developing cardiac tissue and
CC cardiomyocytes (at protein level). {ECO:0000269|PubMed:29888752}.
CC -!- DEVELOPMENTAL STAGE: Detected in cardiac progenitor cells with
CC expression levels increasing as progenitor cells differentiate into
CC cardiomyocytes. {ECO:0000269|PubMed:29888752}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK95952.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK95952.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAC03812.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC03812.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BX647796; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=CAD89922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL832018; CAD89922.1; ALT_INIT; mRNA.
DR EMBL; BX647796; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX647639; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK092133; BAC03812.1; ALT_SEQ; mRNA.
DR EMBL; AY044450; AAK95952.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11966.2; -.
DR RefSeq; NP_443179.3; NM_052947.3.
DR AlphaFoldDB; Q86TB3; -.
DR SMR; Q86TB3; -.
DR BioGRID; 125447; 25.
DR IntAct; Q86TB3; 3.
DR MINT; Q86TB3; -.
DR STRING; 9606.ENSP00000354991; -.
DR iPTMnet; Q86TB3; -.
DR PhosphoSitePlus; Q86TB3; -.
DR BioMuta; ALPK2; -.
DR DMDM; 226694196; -.
DR MassIVE; Q86TB3; -.
DR MaxQB; Q86TB3; -.
DR PaxDb; Q86TB3; -.
DR PeptideAtlas; Q86TB3; -.
DR PRIDE; Q86TB3; -.
DR ProteomicsDB; 69678; -.
DR Antibodypedia; 22947; 96 antibodies from 23 providers.
DR DNASU; 115701; -.
DR Ensembl; ENST00000361673.4; ENSP00000354991.3; ENSG00000198796.7.
DR GeneID; 115701; -.
DR KEGG; hsa:115701; -.
DR MANE-Select; ENST00000361673.4; ENSP00000354991.3; NM_052947.4; NP_443179.3.
DR UCSC; uc002lhj.5; human.
DR CTD; 115701; -.
DR DisGeNET; 115701; -.
DR GeneCards; ALPK2; -.
DR HGNC; HGNC:20565; ALPK2.
DR HPA; ENSG00000198796; Group enriched (heart muscle, skeletal muscle, tongue).
DR neXtProt; NX_Q86TB3; -.
DR OpenTargets; ENSG00000198796; -.
DR PharmGKB; PA134916108; -.
DR VEuPathDB; HostDB:ENSG00000198796; -.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000160524; -.
DR HOGENOM; CLU_002011_0_0_1; -.
DR InParanoid; Q86TB3; -.
DR OMA; NWEAGNK; -.
DR OrthoDB; 32441at2759; -.
DR PhylomeDB; Q86TB3; -.
DR TreeFam; TF332629; -.
DR PathwayCommons; Q86TB3; -.
DR SignaLink; Q86TB3; -.
DR BioGRID-ORCS; 115701; 8 hits in 1086 CRISPR screens.
DR ChiTaRS; ALPK2; human.
DR GenomeRNAi; 115701; -.
DR Pharos; Q86TB3; Tbio.
DR PRO; PR:Q86TB3; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q86TB3; protein.
DR Bgee; ENSG00000198796; Expressed in left ventricle myocardium and 102 other tissues.
DR Genevisible; Q86TB3; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:UniProtKB.
DR GO; GO:1905223; P:epicardium morphogenesis; IMP:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Immunoglobulin domain; Kinase; Membrane;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2170
FT /note="Alpha-protein kinase 2"
FT /id="PRO_0000260030"
FT DOMAIN 10..114
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1786..1874
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1901..2133
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 109..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2136..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2136..2159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1808..1858
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 2
FT /note="K -> T (in dbSNP:rs6566987)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054914"
FT VARIANT 29
FT /note="A -> V (in dbSNP:rs138405027)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082163"
FT VARIANT 136
FT /note="R -> S (in dbSNP:rs9944810)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054915"
FT VARIANT 202
FT /note="A -> T (in dbSNP:rs115979836)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082164"
FT VARIANT 388
FT /note="S -> L (in dbSNP:rs147887741)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082165"
FT VARIANT 397
FT /note="T -> I (in dbSNP:rs79863383)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082166"
FT VARIANT 457
FT /note="A -> V (in dbSNP:rs199872766)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082167"
FT VARIANT 719
FT /note="H -> Q (in dbSNP:rs12103986)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054916"
FT VARIANT 810
FT /note="G -> S (in dbSNP:rs3809970)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054917"
FT VARIANT 825
FT /note="R -> T (in dbSNP:rs3809972)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054918"
FT VARIANT 829
FT /note="K -> N (in dbSNP:rs3809973)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054919"
FT VARIANT 875
FT /note="T -> P (in dbSNP:rs34109891)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082168"
FT VARIANT 884
FT /note="S -> L (in dbSNP:rs3809974)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054920"
FT VARIANT 891
FT /note="T -> I (in dbSNP:rs3826593)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054921"
FT VARIANT 916
FT /note="N -> K (in dbSNP:rs4940404)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054922"
FT VARIANT 942
FT /note="E -> K (in an ovarian undifferentiated carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_045591"
FT VARIANT 969
FT /note="A -> T (in dbSNP:rs371835741)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082169"
FT VARIANT 977
FT /note="S -> T (in dbSNP:rs3809975)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054923"
FT VARIANT 1057
FT /note="L -> V (in dbSNP:rs3809976)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054924"
FT VARIANT 1063
FT /note="G -> V (in dbSNP:rs34347938)"
FT /id="VAR_062168"
FT VARIANT 1134
FT /note="K -> N (in dbSNP:rs35791514)"
FT /id="VAR_054925"
FT VARIANT 1174
FT /note="H -> P (in dbSNP:rs3809977)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054926"
FT VARIANT 1288
FT /note="L -> S (in dbSNP:rs35882005)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082170"
FT VARIANT 1296
FT /note="L -> V (in dbSNP:rs3809976)"
FT /id="VAR_045593"
FT VARIANT 1449
FT /note="P -> S (in dbSNP:rs3809982)"
FT /evidence="ECO:0000269|PubMed:10021370,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054927"
FT VARIANT 1476
FT /note="K -> T (in a melanoma metastatic sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_045594"
FT VARIANT 1551
FT /note="A -> S (in dbSNP:rs3809983)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:28668886"
FT /id="VAR_054928"
FT VARIANT 1579
FT /note="Q -> R (in dbSNP:rs33910491)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054929"
FT VARIANT 1729
FT /note="K -> E (in dbSNP:rs34409558)"
FT /id="VAR_054930"
FT VARIANT 1730
FT /note="K -> E (in dbSNP:rs17065127)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054931"
FT VARIANT 1745
FT /note="K -> N (in dbSNP:rs56206581)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082171"
FT VARIANT 1767
FT /note="H -> Y (in dbSNP:rs7234999)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_054932"
FT VARIANT 1853
FT /note="Q -> E (rare variant found in East Asian patients;
FT decreases luminal apoptosis, cell aggregation and
FT basolateral membrane localization in colorectal cancer
FT cells; dbSNP:rs55674018)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082172"
FT VARIANT 1884
FT /note="R -> C (in dbSNP:rs33969768)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_057742"
FT VARIANT 1919
FT /note="A -> T (in dbSNP:rs374271622)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082173"
FT VARIANT 1969
FT /note="E -> K (in dbSNP:rs1313881443)"
FT /id="VAR_045595"
FT VARIANT 1978
FT /note="A -> T (in dbSNP:rs146618330)"
FT /evidence="ECO:0000269|PubMed:28668886"
FT /id="VAR_082174"
FT VARIANT 2157
FT /note="I -> V (in dbSNP:rs7240666)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:28668886"
FT /id="VAR_054933"
FT CONFLICT 550
FT /note="N -> S (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="K -> S (in Ref. 1; CAD89922)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="A -> T (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="G -> E (in Ref. 4; BAC03812)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="K -> E (in Ref. 1; CAD89922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1165
FT /note="E -> G (in Ref. 1; CAD89922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217
FT /note="I -> T (in Ref. 4; BAC03812)"
FT /evidence="ECO:0000305"
FT CONFLICT 1402
FT /note="S -> P (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
FT CONFLICT 1428
FT /note="Q -> R (in Ref. 4; BAC03812)"
FT /evidence="ECO:0000305"
FT CONFLICT 1443
FT /note="H -> R (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
FT CONFLICT 1784
FT /note="R -> S (in Ref. 1; BX647639)"
FT /evidence="ECO:0000305"
FT CONFLICT 1814
FT /note="H -> R (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
FT CONFLICT 1939
FT /note="M -> V (in Ref. 1; CAD89922)"
FT /evidence="ECO:0000305"
FT CONFLICT 2042
FT /note="I -> V (in Ref. 1; CAD89922)"
FT /evidence="ECO:0000305"
FT CONFLICT 2092
FT /note="G -> D (in Ref. 1; BX647796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2170 AA; 237013 MW; 5C257153F091B08E CRC64;
MKDSEGPQRP PLCFLSTLLS QKVPEKSDAV LRCIISGQPK PEVTWYKNGQ AIDGSGIISN
YEFFENQYIH VLHLSCCTKN DAAVYQISAK NSFGMICCSA SVEVECSSEN PQLSPNLEDD
RDRGWKHETG THEEERANQI DEKEHPYKEE ESISPGTPRS ADSSPSKSNH SLSLQSLGNL
DISVSSSENP LGVKGTRHTG EAYDPSNTEE IANGLLFLNS SHIYEKQDRC CHKTVHSMAS
KFTDGDLNND GPHDEGLRSS QQNPKVQKYI SFSLPLSEAT AHIYPGDSAV ANKQPSPQLS
SEDSDSDYEL CPEITLTYTE EFSDDDLEYL ECSDVMTDYS NAVWQRNLLG TEHVFLLESD
DEEMEFGEHC LGGCEHFLSG MGCGSRVSGD AGPMVATAGF CGHHSQPQEV GVRSSRVSKH
GPSSPQTGMT LILGPHQDGT SSVTEQGRYK LPTAPEAAEN DYPGIQGETR DSHQAREEFA
SDNLLNMDES VRETEMKLLS GESENSGMSQ CWETAADKRV GGKDLWSKRG SRKSARVRQP
GMKGNPKKPN ANLRESTTEG TLHLCSAKES AEPPLTQSDK RETSHTTAAA TGRSSHADAR
ECAISTQAEQ EAKTLQTSTD SVSKEGNTNC KGEGMQVNTL FETSQVPDWS DPPQVQVQET
VRETISCSQM PAFSEPAGEE SPFTGTTTIS FSNLGGVHKE NASLAQHSEV KPCTCGPQHE
EKQDRDGNIP DNFREDLKYE QSISEANDET MSPGVFSRHL PKDARADFRE PVAVSVASPE
PTDTALTLEN VCDEPRDREA VCAMECFEAG DQGTCFDTID SLVGRPVDKY SPQEICSVDT
ELAEGQNKVS DLCSSNDKTL EVFFQTQVSE TSVSTCKSSK DGNSVMSPLF TSTFTLNISH
TASEGATGEN LAKVENSTYP LASTVHAGQE QPSPSNSGGL DETQLLSSEN NPLVQFKEGG
DKSPSPSAAD TTATPASYSS IVSFPWEKPT TLTANNECFQ ATRETEDTST VTIATEVHPA
KYLAVSIPED KHAGGTEERF PRASHEKVSQ FPSQVQLDHI LSGATIKSTK ELLCRAPSVP
GVPHHVLQLP EGEGFCSNSP LQVDNLSGDK SQTVDRADFR SYEENFQERG SETKQGVQQQ
SLSQQGSLSA PDFQQSLPTT SAAQEERNLV PTAHSPASSR EGAGQRSGWG TRVSVVAETA
GEEDSQALSN VPSLSDILLE ESKEYRPGNW EAGNKLKIIT LEASASEIWP PRQLTNSESK
ASDGGLIIPD KVWAVPDSLK ADAVVPELAP SEIAALAHSP EDAESALADS RESHKGEEPT
ISVHWRSLSS RGFSQPRLLE SSVDPVDEKE LSVTDSLSAA SETGGKENVN NVSQDQEEKQ
LKMDHTAFFK KFLTCPKILE SSVDPIDEIS VIEYTRAGKP EPSETTPQGA REGGQSNDGN
MGHEAEIQPA ILQVPCLQGT ILSENRISRS QEGSMKQEAE QIQPEEAKTA IWQVLQPSEG
GERIPSGCSI GQIQESSDGS LGEAEQSKKD KAELISPTSP LSSCLPIMTH ASLGVDTHNS
TGQIHDVPEN DIVEPRKRQY VFPVSQKRGT IENERGKPLP SSPDLTRFPC TSSPEGNVTD
FLISHKMEEP KIEVLQIGET KPPSSSSSSA KTLAFISGER ELEKAPKLLQ DPCQKGTLGC
AKKSREREKS LEARAGKSPG TLTAVTGSEE VKRKPEAPGS GHLAEGVKKK ILSRVAALRL
KLEEKENIRK NSAFLKKMPK LETSLSHTEE KQDPKKPSCK REGRAPVLLK KIQAEMFPEH
SGNVKLSCQF AEIHEDSTIC WTKDSKSIAQ VQRSAGDNST VSFAIVQASP KDQGLYYCCI
KNSYGKVTAE FNLTAEVLKQ LSSRQDTKGC EEIEFSQLIF KEDFLHDSYF GGRLRGQIAT
EELHFGEGVH RKAFRSTVMH GLMPVFKPGH ACVLKVHNAI AYGTRNNDEL IQRNYKLAAQ
ECYVQNTARY YAKIYAAEAQ PLEGFGEVPE IIPIFLIHRP ENNIPYATVE EELIGEFVKY
SIRDGKEINF LRRESEAGQK CCTFQHWVYQ KTSGCLLVTD MQGVGMKLTD VGIATLAKGY
KGFKGNCSMT FIDQFKALHQ CNKYCKMLGL KSLQNNNQKQ KQPSIGKSKV QTNSMTIKKA
GPETPGEKKT
