CDK15_HUMAN
ID CDK15_HUMAN Reviewed; 435 AA.
AC Q96Q40; A8K8R9; B8ZZX0; C9J1N8; C9K003; F8W6H8; Q4ZG86; Q53TV1; Q6ZMR9;
AC Q8IUP1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cyclin-dependent kinase 15;
DE EC=2.7.11.22 {ECO:0000269|PubMed:24866247};
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 7 protein;
DE AltName: Full=Cell division protein kinase 15;
DE AltName: Full=Serine/threonine-protein kinase ALS2CR7;
DE AltName: Full=Serine/threonine-protein kinase PFTAIRE-2;
GN Name=CDK15; Synonyms=ALS2CR7, PFTK2;
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 4).
RC TISSUE=Testis;
RX PubMed=11586298; DOI=10.1038/ng1001-166;
RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A.,
RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr.,
RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.;
RT "A gene encoding a putative GTPase regulator is mutated in familial
RT amyotrophic lateral sclerosis 2.";
RL Nat. Genet. 29:166-173(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC TISSUE=Glial tumor, and Testis;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 3).
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 [6]
RP NOMENCLATURE.
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 [7]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-64; GLU-93; ARG-127; ILE-255 AND
RP ASP-276.
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24866247; DOI=10.1016/j.bbrc.2014.05.070;
RA Park M.H., Kim S.Y., Kim Y.J., Chung Y.H.;
RT "ALS2CR7 (CDK15) attenuates TRAIL induced apoptosis by inducing
RT phosphorylation of survivin Thr34.";
RL Biochem. Biophys. Res. Commun. 450:129-134(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts like an
CC antiapoptotic protein that counters TRAIL/TNFSF10-induced apoptosis by
CC inducing phosphorylation of BIRC5 at 'Thr-34'.
CC {ECO:0000269|PubMed:24866247}.
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=2.7.11.22;
CC Evidence={ECO:0000269|PubMed:24866247};
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=2.7.11.22; Evidence={ECO:0000269|PubMed:24866247};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q96Q40; Q16543: CDC37; NbExp=2; IntAct=EBI-1051975, EBI-295634;
CC Q96Q40; Q13451: FKBP5; NbExp=2; IntAct=EBI-1051975, EBI-306914;
CC Q96Q40; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1051975, EBI-352572;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96Q40-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q96Q40-3; Sequence=VSP_023745;
CC Name=4;
CC IsoId=Q96Q40-4; Sequence=VSP_038765;
CC Name=5;
CC IsoId=Q96Q40-5; Sequence=VSP_047226;
CC Name=6;
CC IsoId=Q96Q40-6; Sequence=VSP_059406, VSP_059407, VSP_059408;
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
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=AAH38807.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB053308; BAB69017.1; -; mRNA.
DR EMBL; AK131512; BAD18656.1; -; mRNA.
DR EMBL; AK292434; BAF85123.1; -; mRNA.
DR EMBL; AC007242; AAX93182.1; -; Genomic_DNA.
DR EMBL; AC007358; AAX88914.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70295.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70297.1; -; Genomic_DNA.
DR EMBL; BC038807; AAH38807.1; ALT_INIT; mRNA.
DR CCDS; CCDS2350.1; -. [Q96Q40-4]
DR CCDS; CCDS58746.1; -. [Q96Q40-3]
DR CCDS; CCDS58747.1; -. [Q96Q40-5]
DR RefSeq; NP_001248364.1; NM_001261435.1. [Q96Q40-5]
DR RefSeq; NP_001248365.1; NM_001261436.1. [Q96Q40-3]
DR RefSeq; NP_631897.1; NM_139158.2. [Q96Q40-4]
DR RefSeq; XP_005246838.1; XM_005246781.3.
DR RefSeq; XP_005246839.1; XM_005246782.4. [Q96Q40-4]
DR AlphaFoldDB; Q96Q40; -.
DR SMR; Q96Q40; -.
DR BioGRID; 122381; 127.
DR IntAct; Q96Q40; 94.
DR MINT; Q96Q40; -.
DR STRING; 9606.ENSP00000406472; -.
DR BindingDB; Q96Q40; -.
DR ChEMBL; CHEMBL5856; -.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB06486; Enzastaurin.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q96Q40; -.
DR iPTMnet; Q96Q40; -.
DR PhosphoSitePlus; Q96Q40; -.
DR BioMuta; CDK15; -.
DR DMDM; 290457634; -.
DR EPD; Q96Q40; -.
DR jPOST; Q96Q40; -.
DR MassIVE; Q96Q40; -.
DR MaxQB; Q96Q40; -.
DR PaxDb; Q96Q40; -.
DR PeptideAtlas; Q96Q40; -.
DR PRIDE; Q96Q40; -.
DR ProteomicsDB; 29785; -.
DR ProteomicsDB; 77819; -. [Q96Q40-1]
DR ProteomicsDB; 77821; -. [Q96Q40-3]
DR ProteomicsDB; 77822; -. [Q96Q40-4]
DR Antibodypedia; 19940; 256 antibodies from 27 providers.
DR DNASU; 65061; -.
DR Ensembl; ENST00000260967.6; ENSP00000260967.2; ENSG00000138395.17. [Q96Q40-4]
DR Ensembl; ENST00000410091.7; ENSP00000386901.3; ENSG00000138395.17. [Q96Q40-4]
DR Ensembl; ENST00000434439.1; ENSP00000412775.1; ENSG00000138395.17. [Q96Q40-3]
DR Ensembl; ENST00000450471.6; ENSP00000406472.2; ENSG00000138395.17. [Q96Q40-5]
DR Ensembl; ENST00000652192.3; ENSP00000498608.2; ENSG00000138395.17. [Q96Q40-1]
DR GeneID; 65061; -.
DR KEGG; hsa:65061; -.
DR MANE-Select; ENST00000652192.3; ENSP00000498608.2; NM_001366386.2; NP_001353315.1.
DR UCSC; uc002uys.4; human. [Q96Q40-1]
DR CTD; 65061; -.
DR DisGeNET; 65061; -.
DR GeneCards; CDK15; -.
DR HGNC; HGNC:14434; CDK15.
DR HPA; ENSG00000138395; Group enriched (epididymis, ovary).
DR MIM; 616147; gene.
DR neXtProt; NX_Q96Q40; -.
DR OpenTargets; ENSG00000138395; -.
DR PharmGKB; PA165696414; -.
DR VEuPathDB; HostDB:ENSG00000138395; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000159606; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q96Q40; -.
DR OMA; YMAQHPG; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q96Q40; -.
DR TreeFam; TF106508; -.
DR BRENDA; 2.7.11.22; 2681.
DR PathwayCommons; Q96Q40; -.
DR SignaLink; Q96Q40; -.
DR BioGRID-ORCS; 65061; 10 hits in 1102 CRISPR screens.
DR ChiTaRS; CDK15; human.
DR GenomeRNAi; 65061; -.
DR Pharos; Q96Q40; Tchem.
DR PRO; PR:Q96Q40; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96Q40; protein.
DR Bgee; ENSG00000138395; Expressed in corpus epididymis and 116 other tissues.
DR ExpressionAtlas; Q96Q40; baseline and differential.
DR Genevisible; Q96Q40; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07870; STKc_PFTAIRE2; 1.
DR InterPro; IPR042761; CDK15_STKc.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..435
FT /note="Cyclin-dependent kinase 15"
FT /id="PRO_0000085619"
FT DOMAIN 103..387
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 109..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11586298"
FT /id="VSP_038765"
FT VAR_SEQ 182..202
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059406"
FT VAR_SEQ 337..366
FT /note="EWFPLPTPRSLHVVWNRLGRVPEAEDLASQ -> GGSKKQHGWHTDIGQHRT
FT AAMQPCSRNVSF (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059407"
FT VAR_SEQ 367..435
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_059408"
FT VAR_SEQ 400..405
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047226"
FT VAR_SEQ 401..435
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023745"
FT VARIANT 64
FT /note="R -> G (in dbSNP:rs34776344)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042016"
FT VARIANT 93
FT /note="K -> E (in a renal clear cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042017"
FT VARIANT 127
FT /note="Q -> R (in dbSNP:rs56135556)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042018"
FT VARIANT 255
FT /note="T -> I (in dbSNP:rs34851370)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042019"
FT VARIANT 276
FT /note="E -> D (in a breast infiltrating ductal carcinoma
FT sample; somatic mutation; dbSNP:rs1490814436)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042020"
SQ SEQUENCE 435 AA; 49023 MW; B415BBBE322EAB33 CRC64;
MGQELCAKTV QPGCSCYHCS EGGEAHSCRR SQPETTEAAF KLTDLKEASC SMTSFHPRGL
QAARAQKFKS KRPRSNSDCF QEEDLRQGFQ WRKSLPFGAA SSYLNLEKLG EGSYATVYKG
ISRINGQLVA LKVISMNAEE GVPFTAIREA SLLKGLKHAN IVLLHDIIHT KETLTFVFEY
MHTDLAQYMS QHPGGLHPHN VRLFMFQLLR GLAYIHHQHV LHRDLKPQNL LISHLGELKL
ADFGLARAKS IPSQTYSSEV VTLWYRPPDA LLGATEYSSE LDIWGAGCIF IEMFQGQPLF
PGVSNILEQL EKIWEVLGVP TEDTWPGVSK LPNYNPEWFP LPTPRSLHVV WNRLGRVPEA
EDLASQMLKG FPRDRVSAQE ALVHDYFSAL PSQLYQLPDE ESLFTVSGVR LKPEMCDLLA
SYQKGHHPAQ FSKCW
