FASTK_HUMAN
ID FASTK_HUMAN Reviewed; 549 AA.
AC Q14296; A8K867; F8VTW9; Q59EM8; Q8IVA0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Fas-activated serine/threonine kinase;
DE Short=FAST kinase;
DE EC=2.7.11.1 {ECO:0000269|PubMed:7544399};
DE EC=2.7.11.8 {ECO:0000269|PubMed:7544399};
GN Name=FASTK;
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), FUNCTION, CATALYTIC ACTIVITY,
RP INTERACTION WITH TIA1 AND TIAR, PHOSPHORYLATION, AND DEPHOSPHORYLATION.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=7544399; DOI=10.1084/jem.182.3.865;
RA Tian Q., Taupin J.-L., Elledge S., Robertson M., Anderson P.;
RT "Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during
RT Fas-mediated apoptosis.";
RL J. Exp. Med. 182:865-874(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Skin;
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 FUNCTION, AND INTERACTION WITH TIA1 AND TIAR.
RX PubMed=17135269; DOI=10.1074/jbc.c600198200;
RA Izquierdo J.M., Valcarcel J.;
RT "Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR
RT proteins to regulate Fas alternative splicing.";
RL J. Biol. Chem. 282:1539-1543(2007).
RN [8]
RP FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4), DOMAIN,
RP RNA-BINDING, MUTAGENESIS OF MET-35, AND ALTERNATIVE INITIATION.
RX PubMed=25704814; DOI=10.1016/j.celrep.2015.01.063;
RA Jourdain A.A., Koppen M., Rodley C.D., Maundrell K., Gueguen N.,
RA Reynier P., Guaras A.M., Enriquez J.A., Anderson P., Simarro M.,
RA Martinou J.C.;
RT "A mitochondria-specific isoform of FASTK is present in mitochondrial RNA
RT granules and regulates gene expression and function.";
RL Cell Rep. 10:1110-1121(2015).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-424.
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: Phosphorylates the splicing regulator TIA1, thereby promoting
CC the inclusion of FAS exon 6, which leads to an mRNA encoding a pro-
CC apoptotic form of the receptor. {ECO:0000269|PubMed:17135269,
CC ECO:0000269|PubMed:7544399}.
CC -!- FUNCTION: [Isoform 4]: Required for the biogenesis of some
CC mitochondrial-encoded mRNAs, specifically stabilizes ND6 (NADH
CC dehydrogenase complex subunit 6) mRNA, and regulates its levels.
CC {ECO:0000269|PubMed:25704814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[Fas-activated protein] = ADP + H(+) + O-
CC phospho-L-seryl-[Fas-activated protein]; Xref=Rhea:RHEA:15881,
CC Rhea:RHEA-COMP:13713, Rhea:RHEA-COMP:13714, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC ChEBI:CHEBI:456216; EC=2.7.11.8;
CC Evidence={ECO:0000269|PubMed:7544399};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[Fas-activated protein] = ADP + H(+) + O-
CC phospho-L-threonyl-[Fas-activated protein]; Xref=Rhea:RHEA:53920,
CC Rhea:RHEA-COMP:13715, Rhea:RHEA-COMP:13716, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.8;
CC Evidence={ECO:0000269|PubMed:7544399};
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:0000269|PubMed:7544399};
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:0000269|PubMed:7544399};
CC -!- SUBUNIT: Interacts with TIA1; the interactions leads to TIA1
CC phosphorylation (PubMed:7544399, PubMed:17135269). Interacts with TIAR
CC (PubMed:7544399, PubMed:17135269). {ECO:0000269|PubMed:17135269,
CC ECO:0000269|PubMed:7544399}.
CC -!- INTERACTION:
CC Q14296; Q86V38: ATN1; NbExp=3; IntAct=EBI-1754067, EBI-11954292;
CC Q14296; Q8IWX8: CHERP; NbExp=3; IntAct=EBI-1754067, EBI-2555370;
CC Q14296; P62508-3: ESRRG; NbExp=3; IntAct=EBI-1754067, EBI-12001340;
CC Q14296; Q92876: KLK6; NbExp=3; IntAct=EBI-1754067, EBI-2432309;
CC Q14296; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-1754067, EBI-1567797;
CC Q14296; O95985: TOP3B; NbExp=3; IntAct=EBI-1754067, EBI-373403;
CC Q14296; O43516: WIPF1; NbExp=3; IntAct=EBI-1754067, EBI-346356;
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion matrix
CC {ECO:0000269|PubMed:25704814}. Note=Colocalizes with mitochondrial RNA
CC granules. {ECO:0000269|PubMed:25704814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=Q14296-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14296-2; Sequence=VSP_042746, VSP_042747;
CC Name=3;
CC IsoId=Q14296-3; Sequence=VSP_044811;
CC Name=4;
CC IsoId=Q14296-4; Sequence=VSP_058246;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas.
CC -!- DOMAIN: The RAP domain is essential for RNA-binding.
CC {ECO:0000269|PubMed:25704814}.
CC -!- PTM: Autophosphorylated on serine/threonine residues. Activated by
CC dephosphorylation. {ECO:0000269|PubMed:7544399}.
CC -!- SIMILARITY: Belongs to the FAST protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93020.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X86779; CAA60448.1; -; mRNA.
DR EMBL; AK292232; BAF84921.1; -; mRNA.
DR EMBL; AB209783; BAD93020.1; ALT_INIT; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471173; EAW54039.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54043.1; -; Genomic_DNA.
DR EMBL; BC011770; AAH11770.1; -; mRNA.
DR EMBL; BC039026; AAH39026.1; -; mRNA.
DR CCDS; CCDS59088.1; -. [Q14296-3]
DR CCDS; CCDS5918.1; -. [Q14296-1]
DR CCDS; CCDS5919.1; -. [Q14296-2]
DR PIR; I37386; I37386.
DR RefSeq; NP_001245390.1; NM_001258461.1. [Q14296-3]
DR RefSeq; NP_006703.1; NM_006712.4. [Q14296-1]
DR RefSeq; NP_148936.2; NM_033015.3. [Q14296-2]
DR RefSeq; XP_005249989.1; XM_005249932.1. [Q14296-4]
DR RefSeq; XP_005249990.1; XM_005249933.3. [Q14296-4]
DR AlphaFoldDB; Q14296; -.
DR BioGRID; 116126; 14.
DR IntAct; Q14296; 23.
DR STRING; 9606.ENSP00000297532; -.
DR GlyGen; Q14296; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14296; -.
DR PhosphoSitePlus; Q14296; -.
DR BioMuta; FASTK; -.
DR DMDM; 13124202; -.
DR EPD; Q14296; -.
DR jPOST; Q14296; -.
DR MassIVE; Q14296; -.
DR MaxQB; Q14296; -.
DR PaxDb; Q14296; -.
DR PeptideAtlas; Q14296; -.
DR PRIDE; Q14296; -.
DR ProteomicsDB; 28667; -.
DR ProteomicsDB; 59957; -. [Q14296-1]
DR ProteomicsDB; 59958; -. [Q14296-2]
DR Antibodypedia; 32964; 288 antibodies from 25 providers.
DR DNASU; 10922; -.
DR Ensembl; ENST00000297532.11; ENSP00000297532.6; ENSG00000164896.21. [Q14296-1]
DR Ensembl; ENST00000353841.6; ENSP00000324817.6; ENSG00000164896.21. [Q14296-2]
DR Ensembl; ENST00000482571.2; ENSP00000418516.1; ENSG00000164896.21. [Q14296-3]
DR GeneID; 10922; -.
DR KEGG; hsa:10922; -.
DR MANE-Select; ENST00000297532.11; ENSP00000297532.6; NM_006712.5; NP_006703.1.
DR UCSC; uc003wix.3; human. [Q14296-1]
DR CTD; 10922; -.
DR DisGeNET; 10922; -.
DR GeneCards; FASTK; -.
DR HGNC; HGNC:24676; FASTK.
DR HPA; ENSG00000164896; Low tissue specificity.
DR MIM; 606965; gene.
DR neXtProt; NX_Q14296; -.
DR OpenTargets; ENSG00000164896; -.
DR PharmGKB; PA142671775; -.
DR VEuPathDB; HostDB:ENSG00000164896; -.
DR eggNOG; ENOG502QXK7; Eukaryota.
DR GeneTree; ENSGT01030000234607; -.
DR HOGENOM; CLU_046861_0_0_1; -.
DR InParanoid; Q14296; -.
DR OMA; KVRTHHY; -.
DR PhylomeDB; Q14296; -.
DR TreeFam; TF331796; -.
DR BRENDA; 2.7.11.8; 2681.
DR PathwayCommons; Q14296; -.
DR SignaLink; Q14296; -.
DR BioGRID-ORCS; 10922; 18 hits in 1110 CRISPR screens.
DR ChiTaRS; FASTK; human.
DR GeneWiki; FASTK; -.
DR GenomeRNAi; 10922; -.
DR Pharos; Q14296; Tbio.
DR PRO; PR:Q14296; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14296; protein.
DR Bgee; ENSG00000164896; Expressed in apex of heart and 188 other tissues.
DR ExpressionAtlas; Q14296; baseline and differential.
DR Genevisible; Q14296; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0035770; C:ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033867; F:Fas-activated serine/threonine kinase activity; IEA:UniProtKB-EC.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR InterPro; IPR013579; FAST_2.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR013584; RAP.
DR InterPro; IPR015715; Ser/Thr_kinase_FAST.
DR PANTHER; PTHR21228:SF4; PTHR21228:SF4; 1.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF08368; FAST_2; 1.
DR Pfam; PF08373; RAP; 1.
DR SMART; SM00952; RAP; 1.
DR PROSITE; PS51286; RAP; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Apoptosis; ATP-binding;
KW Kinase; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; RNA-binding; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..549
FT /note="Fas-activated serine/threonine kinase"
FT /id="PRO_0000087196"
FT DOMAIN 477..535
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:25704814"
FT /id="VSP_058246"
FT VAR_SEQ 28
FT /note="W -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042746"
FT VAR_SEQ 29..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042747"
FT VAR_SEQ 202..228
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044811"
FT VARIANT 424
FT /note="V -> L (in a lung adenocarcinoma sample; somatic
FT mutation; dbSNP:rs758691941)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042200"
FT VARIANT 436
FT /note="A -> V (in dbSNP:rs2288648)"
FT /id="VAR_021970"
FT MUTAGEN 35
FT /note="M->G: Abolishes isoform 4 expression."
FT /evidence="ECO:0000269|PubMed:25704814"
SQ SEQUENCE 549 AA; 61104 MW; 76D38A211B37304A CRC64;
MRRPRGEPGP RAPRPTEGAT CAGPGESWSP SPNSMLRVLL SAQTSPARLS GLLLIPPVQP
CCLGPSKWGD RPVGGGPSAG PVQGLQRLLE QAKSPGELLR WLGQNPSKVR AHHYSVALRR
LGQLLGSRPR PPPVEQVTLQ DLSQLIIRNC PSFDIHTIHV CLHLAVLLGF PSDGPLVCAL
EQERRLRLPP KPPPPLQPLL RGGQGLEAAL SCPRFLRYPR QHLISSLAEA RPEELTPHVM
VLLAQHLARH RLREPQLLEA IAHFLVVQET QLSSKVVQKL VLPFGRLNYL PLEQQFMPCL
ERILAREAGV APLATVNILM SLCQLRCLPF RALHFVFSPG FINYISGTPH ALIVRRYLSL
LDTAVELELP GYRGPRLPRR QQVPIFPQPL ITDRARCKYS HKDIVAEGLR QLLGEEKYRQ
DLTVPPGYCT DFLLCASSSG AVLPVRTQDP FLPYPPRSCP QGQAASSATT RDPAQRVVLV
LRERWHFCRD GRVLLGSRAL RERHLGLMGY QLLPLPFEEL ESQRGLPQLK SYLRQKLQAL
GLRWGPEGG
