ID NEK3_HUMAN Reviewed; 506 AA. AC P51956; A8K2J4; Q5TAP2; Q8J023; Q8WUN5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 27-MAR-2024, entry version 211. DE RecName: Full=Serine/threonine-protein kinase Nek3; DE EC=2.7.11.1; DE AltName: Full=HSPK 36; DE AltName: Full=Never in mitosis A-related kinase 3; DE Short=NimA-related protein kinase 3; GN Name=NEK3; 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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=12063396; DOI=10.1159/000059342; RA Kimura M., Okano Y.; RT "Molecular cloning and characterization of the human NIMA-related protein RT kinase 3 gene (NEK3)."; RL Cytogenet. Cell Genet. 95:177-182(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-506 (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=7522034; RA Schultz S.J., Fry A.M., Suetterlin C., Ried T., Nigg E.A.; RT "Cell cycle-dependent expression of Nek2, a novel human protein kinase RT related to the NIMA mitotic regulator of Aspergillus nidulans."; RL Cell Growth Differ. 5:625-635(1994). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-189. RX PubMed=8274451; RA Schultz S.J., Nigg E.A.; RT "Identification of 21 novel human protein kinases, including 3 members of a RT family related to the cell cycle regulator nimA of Aspergillus nidulans."; RL Cell Growth Differ. 4:821-830(1993). RN [8] RP FUNCTION, INTERACTION WITH PRLR; VAV1 AND VAV2, AND ACTIVITY REGULATION. RX PubMed=15618286; DOI=10.1210/me.2004-0443; RA Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.; RT "Novel association of Vav2 and Nek3 modulates signaling through the human RT prolactin receptor."; RL Mol. Endocrinol. 19:939-949(2005). RN [9] RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PXN. RX PubMed=17297458; DOI=10.1038/sj.onc.1210264; RA Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.; RT "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and RT motility of breast cancer cells."; RL Oncogene 26:4668-4678(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] 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 [12] 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-23; ARG-60; HIS-122; LEU-170; GLY-259; RP ASP-305; ASN-461 AND LYS-477. 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). CC -!- FUNCTION: Protein kinase which influences neuronal morphogenesis and CC polarity through effects on microtubules. Regulates microtubule CC acetylation in neurons. Contributes to prolactin-mediated CC phosphorylation of PXN and VAV2. Implicated in prolactin-mediated CC cytoskeletal reorganization and motility of breast cancer cells through CC mechanisms involving RAC1 activation and phosphorylation of PXN and CC VAV2. {ECO:0000269|PubMed:15618286, ECO:0000269|PubMed:17297458}. 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY REGULATION: Prolactin stimulates its activity. CC {ECO:0000269|PubMed:15618286}. CC -!- SUBUNIT: Interacts with PXN, PRLR, VAV1 and VAV2 and this interaction CC is prolactin-dependent. {ECO:0000269|PubMed:15618286, CC ECO:0000269|PubMed:17297458}. CC -!- INTERACTION: CC P51956; P52735: VAV2; NbExp=3; IntAct=EBI-476041, EBI-297549; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, axon CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P51956-1; Sequence=Displayed; CC Name=2; CC IsoId=P51956-2; Sequence=VSP_035427; CC -!- TISSUE SPECIFICITY: Up-regulated in malignant versus normal breast CC tissue. Isoform 2 shows a high level of expression in testis, ovary and CC brain. {ECO:0000269|PubMed:12063396, ECO:0000269|PubMed:17297458}. CC -!- PTM: Phosphorylation at Thr-479 regulates its catalytic activity. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr CC protein kinase family. NIMA subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EAX08907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB072828; BAC15599.1; -; mRNA. DR EMBL; AK290259; BAF82948.1; -; mRNA. DR EMBL; AL139082; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08907.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC019916; AAH19916.2; -; mRNA. DR EMBL; Z29067; CAA82310.1; -; mRNA. DR EMBL; Z25434; CAA80921.1; -; mRNA. DR CCDS; CCDS73576.1; -. [P51956-1] DR PIR; I38224; I38224. DR RefSeq; NP_001139571.1; NM_001146099.1. [P51956-2] DR RefSeq; NP_002489.1; NM_002498.2. [P51956-1] DR RefSeq; NP_689933.1; NM_152720.2. [P51956-1] DR AlphaFoldDB; P51956; -. DR SMR; P51956; -. DR BioGRID; 110827; 21. DR IntAct; P51956; 16. DR STRING; 9606.ENSP00000484443; -. DR BindingDB; P51956; -. DR ChEMBL; CHEMBL5679; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; P51956; -. DR GuidetoPHARMACOLOGY; 2118; -. DR iPTMnet; P51956; -. DR PhosphoSitePlus; P51956; -. DR BioMuta; NEK3; -. DR DMDM; 20178297; -. DR EPD; P51956; -. DR jPOST; P51956; -. DR MassIVE; P51956; -. DR MaxQB; P51956; -. DR PaxDb; 9606-ENSP00000484443; -. DR PeptideAtlas; P51956; -. DR ProteomicsDB; 56457; -. [P51956-1] DR ProteomicsDB; 56458; -. [P51956-2] DR Pumba; P51956; -. DR Antibodypedia; 24171; 260 antibodies from 29 providers. DR DNASU; 4752; -. DR Ensembl; ENST00000610828.5; ENSP00000480328.1; ENSG00000136098.18. [P51956-1] DR Ensembl; ENST00000618534.4; ENSP00000484443.1; ENSG00000136098.18. [P51956-1] DR GeneID; 4752; -. DR KEGG; hsa:4752; -. DR MANE-Select; ENST00000610828.5; ENSP00000480328.1; NM_002498.3; NP_002489.1. DR UCSC; uc032agd.2; human. [P51956-1] DR AGR; HGNC:7746; -. DR CTD; 4752; -. DR DisGeNET; 4752; -. DR GeneCards; NEK3; -. DR HGNC; HGNC:7746; NEK3. DR HPA; ENSG00000136098; Low tissue specificity. DR MIM; 604044; gene. DR neXtProt; NX_P51956; -. DR OpenTargets; ENSG00000136098; -. DR PharmGKB; PA31547; -. DR VEuPathDB; HostDB:ENSG00000136098; -. DR eggNOG; KOG0589; Eukaryota. DR GeneTree; ENSGT00940000159738; -. DR HOGENOM; CLU_000288_63_39_1; -. DR InParanoid; P51956; -. DR OMA; YSYELQY; -. DR OrthoDB; 198307at2759; -. DR PhylomeDB; P51956; -. DR TreeFam; TF106472; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; P51956; -. DR SignaLink; P51956; -. DR SIGNOR; P51956; -. DR BioGRID-ORCS; 4752; 11 hits in 815 CRISPR screens. DR ChiTaRS; NEK3; human. DR GeneWiki; NEK3; -. DR GenomeRNAi; 4752; -. DR Pharos; P51956; Tchem. DR PRO; PR:P51956; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P51956; Protein. DR Bgee; ENSG00000136098; Expressed in sural nerve and 169 other cell types or tissues. DR ExpressionAtlas; P51956; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl. DR GO; GO:0000278; P:mitotic cell cycle; NAS:UniProtKB. DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl. DR CDD; cd08219; STKc_Nek3; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR44984; SERINE/THREONINE-PROTEIN KINASE NEK3; 1. DR PANTHER; PTHR44984:SF1; SERINE_THREONINE-PROTEIN KINASE NEK3; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P51956; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; KW Cell projection; Cytoplasm; Kinase; Magnesium; Metal-binding; Mitosis; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..506 FT /note="Serine/threonine-protein kinase Nek3" FT /id="PRO_0000086423" FT DOMAIN 4..257 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..285 FT /note="Interaction with VAV2" FT /evidence="ECO:0000269|PubMed:15618286" FT REGION 302..325 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 441..490 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 309..323 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 453..470 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..488 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 127 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 161 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 479 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19369195" FT VAR_SEQ 293..309 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12063396" FT /id="VSP_035427" FT VARIANT 23 FT /note="H -> L (in dbSNP:rs17482764)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_033906" FT VARIANT 60 FT /note="P -> R (in dbSNP:rs55946204)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040908" FT VARIANT 122 FT /note="R -> H (in dbSNP:rs56190615)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040909" FT VARIANT 170 FT /note="P -> L (in dbSNP:rs56021040)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040910" FT VARIANT 259 FT /note="R -> G (in dbSNP:rs34077016)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040911" FT VARIANT 305 FT /note="E -> D (in dbSNP:rs55969405)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040912" FT VARIANT 461 FT /note="D -> N (in dbSNP:rs34076988)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040913" FT VARIANT 477 FT /note="E -> K (in dbSNP:rs34488913)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040914" FT CONFLICT 14 FT /note="S -> F (in Ref. 1; BAC15599)" FT /evidence="ECO:0000305" FT CONFLICT 54 FT /note="L -> S (in Ref. 6; CAA82310)" FT /evidence="ECO:0000305" FT CONFLICT 77..78 FT /note="IV -> LY (in Ref. 7; CAA80921)" FT /evidence="ECO:0000305" FT CONFLICT 187..189 FT /note="SLG -> PSV (in Ref. 7; CAA80921)" FT /evidence="ECO:0000305" SQ SEQUENCE 506 AA; 57705 MW; 4437EB4A41A44777 CRC64; MDDYMVLRMI GEGSFGRALL VQHESSNQMF AMKEIRLPKS FSNTQNSRKE AVLLAKMKHP NIVAFKESFE AEGHLYIVME YCDGGDLMQK IKQQKGKLFP EDMILNWFTQ MCLGVNHIHK KRVLHRDIKS KNIFLTQNGK VKLGDFGSAR LLSNPMAFAC TYVGTPYYVP PEIWENLPYN NKSDIWSLGC ILYELCTLKH PFQANSWKNL ILKVCQGCIS PLPSHYSYEL QFLVKQMFKR NPSHRPSATT LLSRGIVARL VQKCLPPEII MEYGEEVLEE IKNSKHNTPR KKTNPSRIRI ALGNEASTVQ EEEQDRKGSH TDLESINENL VESALRRVNR EEKGNKSVHL RKASSPNLHR RQWEKNVPNT ALTALENASI LTSSLTAEDD RGGSVIKYSK NTTRKQWLKE TPDTLLNILK NADLSLAFQT YTIYRPGSEG FLKGPLSEET EASDSVDGGH DSVILDPERL EPGLDEEDTD FEEEDDNPDW VSELKKRAGW QGLCDR //