ID CDKL1_HUMAN Reviewed; 357 AA. AC Q00532; J3KMW1; Q2M3A4; Q6QUA0; Q8WXQ5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 8. DT 02-SEP-2026, entry version 213. DE RecName: Full=Cyclin-dependent kinase-like 1 {ECO:0000305}; DE EC=2.7.11.22; DE AltName: Full=Protein kinase p42 KKIALRE; DE AltName: Full=Serine/threonine-protein kinase KKIALRE {ECO:0000303|Ref.2}; GN Name=CDKL1 {ECO:0000312|HGNC:HGNC:1781}; 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 1), AND VARIANT GLU-274. RX PubMed=1639063; DOI=10.1002/j.1460-2075.1992.tb05360.x; RA Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., RA Harlow E., Tsai L.-H.; RT "A family of human cdc2-related protein kinases."; RL EMBO J. 11:2909-2917(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Hu W.-X., Tang L.-J., Shi Y.-W.; RT "The cloning of 2nd splicing version of human serine/threonine-protein RT kinase KKIALRE (cyclin-dependent kinase like-1)."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS PRO-66; RP GLU-274; VAL-329 AND ASN-341. RG NIEHS SNPs program; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; 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 [7] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=9000130; RA Taglienti C.A., Wysk M., Davis R.J.; RT "Molecular cloning of the epidermal growth factor-stimulated protein kinase RT p56 KKIAMRE."; RL Oncogene 13:2563-2574(1996). RN [8] {ECO:0007744|PDB:4AGU} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-300 OF VARIANT GLU-274 IN RP COMPLEX WITH SYNTHETIC INHIBITOR. RX PubMed=29420175; DOI=10.1016/j.celrep.2017.12.083; RA Canning P., Park K., Goncalves J., Li C., Howard C.J., Sharpe T.D., RA Holt L.J., Pelletier L., Bullock A.N., Leroux M.R.; RT "CDKL Family Kinases Have Evolved Distinct Structural Features and Ciliary RT Function."; RL Cell Rep. 22:885-894(2018). RN [9] RP VARIANTS [LARGE SCALE ANALYSIS] GLU-274 AND VAL-329. 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 -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=2.7.11.22; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9000130}. Nucleus CC {ECO:0000269|PubMed:9000130}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q00532-1; Sequence=Displayed; CC Name=2; CC IsoId=Q00532-2; Sequence=VSP_041239, VSP_041240, VSP_041241, CC VSP_041242; CC Name=3; CC IsoId=Q00532-3; Sequence=VSP_059391, VSP_059392; CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, and to a lower extent CC in ovary. {ECO:0000269|PubMed:9000130}. CC -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI04978.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAS00095.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA47002.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; X66358; CAA47002.1; ALT_INIT; mRNA. DR EMBL; X66359; CAA47002.1; JOINED; mRNA. DR EMBL; AF390028; AAL58838.1; -; mRNA. DR EMBL; AY525548; AAS00095.1; ALT_INIT; Genomic_DNA. DR EMBL; AL118556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359397; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK308732; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC104977; AAI04978.1; ALT_INIT; mRNA. DR CCDS; CCDS73637.1; -. [Q00532-3] DR CCDS; CCDS9699.2; -. [Q00532-1] DR PIR; S22745; S22745. DR PIR; S23383; S23383. DR RefSeq; NP_001269165.2; NM_001282236.3. [Q00532-3] DR RefSeq; NP_001410690.1; NM_001423761.1. [Q00532-1] DR RefSeq; NP_001410691.1; NM_001423762.1. [Q00532-1] DR RefSeq; NP_001410692.1; NM_001423763.1. [Q00532-1] DR RefSeq; NP_004187.3; NM_004196.7. [Q00532-1] DR PDB; 4AGU; X-ray; 2.40 A; A/B/C=1-300. DR AlphaFoldDB; Q00532; -. DR SMR; Q00532; -. DR BioGRID; 114341; 23. DR FunCoup; Q00532; 1140. DR IntAct; Q00532; 24. DR MINT; Q00532; -. DR STRING; 9606.ENSP00000379176; -. DR BindingDB; Q00532; -. DR ChEMBL; CHEMBL5789; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q00532; -. DR GuidetoPHARMACOLOGY; 1982; -. DR GlyGen; Q00532; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q00532; -. DR PhosphoSitePlus; Q00532; -. DR BioMuta; CDKL1; -. DR DMDM; 229463050; -. DR CPTAC; non-CPTAC-6018; -. DR CPTAC; non-CPTAC-6019; -. DR jPOST; Q00532; -. DR MassIVE; Q00532; -. DR PaxDb; 9606-ENSP00000379176; -. DR PeptideAtlas; Q00532; -. DR ProteomicsDB; 57849; -. [Q00532-1] DR ProteomicsDB; 57850; -. [Q00532-2] DR Antibodypedia; 23644; 363 antibodies from 31 providers. DR DNASU; 8814; -. DR Ensembl; ENST00000395834.6; ENSP00000379176.2; ENSG00000100490.11. [Q00532-1] DR Ensembl; ENST00000906201.1; ENSP00000576260.1; ENSG00000100490.11. [Q00532-1] DR Ensembl; ENST00000906202.1; ENSP00000576261.1; ENSG00000100490.11. [Q00532-1] DR Ensembl; ENST00000941216.1; ENSP00000611275.1; ENSG00000100490.11. [Q00532-1] DR Ensembl; ENST00000941217.1; ENSP00000611276.1; ENSG00000100490.11. [Q00532-1] DR Ensembl; ENST00000941218.1; ENSP00000611277.1; ENSG00000100490.11. [Q00532-1] DR GeneID; 8814; -. DR KEGG; hsa:8814; -. DR MANE-Select; ENST00000395834.6; ENSP00000379176.2; NM_004196.7; NP_004187.3. DR UCSC; uc001wxz.5; human. [Q00532-1] DR UCSC; uc032bbp.2; human. DR AGR; HGNC:1781; -. DR ClinPGx; PA26317; -. DR CTD; 8814; -. DR DisGeNET; 8814; -. DR GeneCards; CDKL1; -. DR HGNC; HGNC:1781; CDKL1. DR HPA; ENSG00000100490; Low tissue specificity. DR MIM; 603441; gene. DR OpenTargets; ENSG00000100490; -. DR VEuPathDB; HostDB:ENSG00000100490; -. DR eggNOG; KOG0593; Eukaryota. DR GeneTree; ENSGT00940000159132; -. DR InParanoid; Q00532; -. DR OMA; LHSTHYN; -. DR OrthoDB; 548217at2759; -. DR PAN-GO; Q00532; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q00532; -. DR BRENDA; 2.7.11.22; 2681. DR PathwayCommons; Q00532; -. DR SignaLink; Q00532; -. DR SIGNOR; Q00532; -. DR Agora; ENSG00000100490; -. DR BioGRID-ORCS; 8814; 9 hits in 1192 CRISPR screens. DR ChiTaRS; CDKL1; human. DR EvolutionaryTrace; Q00532; -. DR GenomeRNAi; 8814; -. DR Pharos; Q00532; Tchem. DR PRO; PR:Q00532; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q00532; protein. DR Bgee; ENSG00000100490; Expressed in right uterine tube and 120 other cell types or tissues. DR ExpressionAtlas; Q00532; baseline and differential. DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB. DR CDD; cd07847; STKc_CDKL1_4; 1. DR FunFam; 1.10.510.10:FF:000191; cyclin-dependent kinase-like 1 isoform X1; 1. DR FunFam; 3.30.200.20:FF:000049; cyclin-dependent kinase-like 1 isoform X1; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR050108; CDK. 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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF192; CYCLIN-DEPENDENT KINASE-LIKE 1; 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 PDBsum; 4AGU; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Nucleus; Proteomics identification; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..357 FT /note="Cyclin-dependent kinase-like 1" FT /id="PRO_0000085810" FT DOMAIN 4..287 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 45..51 FT /note="[NKR]KIAxRE" FT ACT_SITE 126 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 VAR_SEQ 1 FT /note="M -> MELSTDTGWNQKSNFPPCDSRVSKEEAQLPFPTPSSYGADSSNQTYA FT HKSQSEREQHKEVRAVLNHCSGLDGGEESGLCGTSTRIDAGTGNGTDDKVTDQHRHRRC FT LQGTKGNNRGSEVWGLLLQGNVDRSGGAPSAGVLLRRRGYSCALHGLRKFANLAGLLSR FT QQDSARGVSHHSRLKIHFKKIYSSMM (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_041239" FT VAR_SEQ 56 FT /note="K -> KAPSPYAAEPSLCGMKMVRRGKKEFLPAVAEKVDAPSGVGGQGQDSV FT TVGSLGRRSTYGRKQEKQVRQREGIIYCYVAVLLRIYYFDQGCVAREEEQFQELVFGPF FT CHIGSYFTGHRTNVRPYILLLSRPSPFKTAAGTYEAGLVILECSYFLAEQEPYCPTQAL FT QQPHPIIGPWALEGGGVESKEDRHPPPKEAPASCEGFLRSAVPKQAYTPFKTSPDKRLS FT DCVATPPWAPPTPLIISSGVLVAICSMIDPVPEFHSEGLLAKATSGSAGILVWIFLCND FT AFIYGKYILRSGVLWVRGLPGFKSEAAALCHKCYSSADPKREQQQDLLQRVKEQSFHSV FT NGAQARHKGSPSPHQTQEPSWPHPVDPTPGHRWSCLPVPCRAPALLSPWVVDGTGCCGA FT GGGSDRGGSAAQEPT (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_041240" FT VAR_SEQ 98..121 FT /note="VPEHLVKSITWQTLQAVNFCHKHN -> ICNIFVCTGRRLGEHTEALSKKKK FT KGGGGPFLKLRAASCRITLFKNVGCGLETTGDLSLNSGGGAASRGVAAALRALVCGTEL FT TSSDSPQR (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_041241" FT VAR_SEQ 247..357 FT /note="EPLELKFPNISYPALGLLKGCLHMDPTQRLTCEQLLHHPYFENIREIEDLAK FT EHNKPTRKTLRKSRKHHCFTETSKLQYLPQLTGSSILPALDNKKYYCDTKKLNYRFPNI FT -> SLCLSVTLTEGGLLASGAVKRSQMGSSVSQATSWPHPDIVAETAELDDIAMARQTP FT VMLRFNRQKEQEKYLSYGA (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_041242" FT VAR_SEQ 267..275 FT /note="CLHMDPTQR -> RVPIASRTE (in isoform 3)" FT /id="VSP_059391" FT VAR_SEQ 276..357 FT /note="Missing (in isoform 3)" FT /id="VSP_059392" FT VARIANT 66 FT /note="L -> P (in dbSNP:rs11570814)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_020576" FT VARIANT 274 FT /note="Q -> E (in dbSNP:rs7161563)" FT /evidence="ECO:0000269|PubMed:1639063, FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:29420175, FT ECO:0000269|Ref.3" FT /id="VAR_020577" FT VARIANT 329 FT /note="L -> V (in dbSNP:rs9323183)" FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3" FT /id="VAR_020578" FT VARIANT 341 FT /note="K -> N (in dbSNP:rs11570886)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_020579" FT CONFLICT 301 FT /note="N -> D (in Ref. 1; CAA47002)" FT /evidence="ECO:0000305" FT STRAND 4..12 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 14..23 FT /evidence="ECO:0007829|PDB:4AGU" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 42..57 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 100..119 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:4AGU" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 170..174 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 182..197 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 207..218 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 223..230 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 240..243 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 258..267 FT /evidence="ECO:0007829|PDB:4AGU" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 278..282 FT /evidence="ECO:0007829|PDB:4AGU" FT HELIX 285..287 FT /evidence="ECO:0007829|PDB:4AGU" SQ SEQUENCE 357 AA; 41701 MW; 2A0801F1338F58FC CRC64; MEKYEKIGKI GEGSYGVVFK CRNRDTGQIV AIKKFLESED DPVIKKIALR EIRMLKQLKH PNLVNLLEVF RRKRRLHLVF EYCDHTVLHE LDRYQRGVPE HLVKSITWQT LQAVNFCHKH NCIHRDVKPE NILITKHSVI KLCDFGFARL LTGPSDYYTD YVATRWYRSP ELLVGDTQYG PPVDVWAIGC VFAELLSGVP LWPGKSDVDQ LYLIRKTLGD LIPRHQQVFS TNQYFSGVKI PDPEDMEPLE LKFPNISYPA LGLLKGCLHM DPTQRLTCEQ LLHHPYFENI REIEDLAKEH NKPTRKTLRK SRKHHCFTET SKLQYLPQLT GSSILPALDN KKYYCDTKKL NYRFPNI //