REXO4_HUMAN
ID REXO4_HUMAN Reviewed; 422 AA.
AC Q9GZR2; B2RAT2; Q5T8S4; Q5T8S5; Q5T8S6; Q9GZW3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=RNA exonuclease 4;
DE EC=3.1.-.-;
DE AltName: Full=Exonuclease XPMC2;
DE AltName: Full=Prevents mitotic catastrophe 2 protein homolog;
DE Short=hPMC2;
GN Name=REXO4; Synonyms=PMC2, XPMC2H;
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 ALA-283.
RX PubMed=9325058; DOI=10.1006/geno.1997.4874;
RA Kwiatkowska J., Slomski R., Jozwiak S., Short M.P., Kwiatkowski D.J.;
RT "Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and
RT evaluation as TSC1.";
RL Genomics 44:350-354(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ESR1 AND ESR2.
RX PubMed=10908561; DOI=10.1074/jbc.m003880200;
RA Montano M.M., Wittmann B.M., Bianco N.R.;
RT "Identification and characterization of a novel factor that regulates
RT quinone reductase gene transcriptional activity.";
RL J. Biol. Chem. 275:34306-34313(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP IDENTIFICATION BY MASS 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-96 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBUNIT: Can bind ESR1 and ESR2. This interaction is abrogated by
CC estrogen and augmented by tamoxifen treatment.
CC -!- INTERACTION:
CC Q9GZR2; P50570-2: DNM2; NbExp=3; IntAct=EBI-2856313, EBI-10968534;
CC Q9GZR2; O75031: HSF2BP; NbExp=3; IntAct=EBI-2856313, EBI-7116203;
CC Q9GZR2; P42858: HTT; NbExp=3; IntAct=EBI-2856313, EBI-466029;
CC Q9GZR2; P29474: NOS3; NbExp=3; IntAct=EBI-2856313, EBI-1391623;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10908561,
CC ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZR2-2; Sequence=VSP_014796, VSP_014797;
CC -!- SIMILARITY: Belongs to the REXO4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI12845.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI12847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI12848.1; 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; AF295774; AAG02123.1; -; mRNA.
DR EMBL; AF273304; AAF98162.1; -; mRNA.
DR EMBL; AL136894; CAB66828.1; -; mRNA.
DR EMBL; AK025493; BAB15152.1; -; mRNA.
DR EMBL; AK314333; BAG36979.1; -; mRNA.
DR EMBL; AL158826; CAI12845.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL158826; CAI12847.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL158826; CAI12848.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL158826; CAI12849.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88082.1; -; Genomic_DNA.
DR EMBL; BC009274; AAH09274.1; -; mRNA.
DR CCDS; CCDS65179.1; -. [Q9GZR2-2]
DR CCDS; CCDS6969.1; -. [Q9GZR2-1]
DR RefSeq; NP_001266278.1; NM_001279349.1. [Q9GZR2-2]
DR RefSeq; NP_001266279.1; NM_001279350.1.
DR RefSeq; NP_001266280.1; NM_001279351.1.
DR RefSeq; NP_065118.2; NM_020385.3. [Q9GZR2-1]
DR AlphaFoldDB; Q9GZR2; -.
DR SMR; Q9GZR2; -.
DR BioGRID; 121375; 245.
DR IntAct; Q9GZR2; 53.
DR MINT; Q9GZR2; -.
DR STRING; 9606.ENSP00000361010; -.
DR iPTMnet; Q9GZR2; -.
DR PhosphoSitePlus; Q9GZR2; -.
DR BioMuta; REXO4; -.
DR DMDM; 71153418; -.
DR SWISS-2DPAGE; Q9GZR2; -.
DR EPD; Q9GZR2; -.
DR jPOST; Q9GZR2; -.
DR MassIVE; Q9GZR2; -.
DR MaxQB; Q9GZR2; -.
DR PaxDb; Q9GZR2; -.
DR PeptideAtlas; Q9GZR2; -.
DR PRIDE; Q9GZR2; -.
DR ProteomicsDB; 80118; -. [Q9GZR2-1]
DR ProteomicsDB; 80119; -. [Q9GZR2-2]
DR Antibodypedia; 18377; 133 antibodies from 25 providers.
DR DNASU; 57109; -.
DR Ensembl; ENST00000371935.6; ENSP00000361003.2; ENSG00000148300.12. [Q9GZR2-2]
DR Ensembl; ENST00000371942.8; ENSP00000361010.3; ENSG00000148300.12. [Q9GZR2-1]
DR Ensembl; ENST00000628678.2; ENSP00000487504.1; ENSG00000280706.3. [Q9GZR2-2]
DR Ensembl; ENST00000630460.3; ENSP00000486065.1; ENSG00000280706.3. [Q9GZR2-1]
DR GeneID; 57109; -.
DR KEGG; hsa:57109; -.
DR MANE-Select; ENST00000371942.8; ENSP00000361010.3; NM_020385.4; NP_065118.2.
DR UCSC; uc004cdm.5; human. [Q9GZR2-1]
DR CTD; 57109; -.
DR DisGeNET; 57109; -.
DR GeneCards; REXO4; -.
DR HGNC; HGNC:12820; REXO4.
DR HPA; ENSG00000148300; Low tissue specificity.
DR MIM; 602930; gene.
DR neXtProt; NX_Q9GZR2; -.
DR OpenTargets; ENSG00000148300; -.
DR PharmGKB; PA37414; -.
DR VEuPathDB; HostDB:ENSG00000148300; -.
DR eggNOG; KOG2249; Eukaryota.
DR GeneTree; ENSGT00940000159607; -.
DR HOGENOM; CLU_1111086_0_0_1; -.
DR InParanoid; Q9GZR2; -.
DR OMA; CVYDKYI; -.
DR OrthoDB; 1562214at2759; -.
DR PhylomeDB; Q9GZR2; -.
DR TreeFam; TF313504; -.
DR PathwayCommons; Q9GZR2; -.
DR SignaLink; Q9GZR2; -.
DR BioGRID-ORCS; 57109; 8 hits in 1084 CRISPR screens.
DR ChiTaRS; REXO4; human.
DR GeneWiki; REXO4; -.
DR GenomeRNAi; 57109; -.
DR Pharos; Q9GZR2; Tbio.
DR PRO; PR:Q9GZR2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9GZR2; protein.
DR Bgee; ENSG00000148300; Expressed in sural nerve and 98 other tissues.
DR ExpressionAtlas; Q9GZR2; baseline and differential.
DR Genevisible; Q9GZR2; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:LIFEdb.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:ARUK-UCL.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0004519; F:endonuclease activity; IDA:ARUK-UCL.
DR GO; GO:0004527; F:exonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:ARUK-UCL.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IDA:ARUK-UCL.
DR GO; GO:0006281; P:DNA repair; IDA:ARUK-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd06144; REX4_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR034920; Rex4.
DR InterPro; IPR037431; REX4_DEDDh_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR12801:SF130; PTHR12801:SF130; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Exonuclease; Hydrolase; Isopeptide bond; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..422
FT /note="RNA exonuclease 4"
FT /id="PRO_0000131703"
FT DOMAIN 243..394
FT /note="Exonuclease"
FT REGION 1..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 76..132
FT /note="WLLKQKSQAPEKPLVISQMGSKKKPKIIQQNKKETSPQVKGEEMPAGKDQEA
FT SRGSV -> VPRWTGGRQYLAPRPVEQSTIRKEPRKGQMVILFQNEGTSSIRSGKLRRQ
FT PQPHPPR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014796"
FT VAR_SEQ 133..304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014797"
FT VARIANT 141
FT /note="R -> K (in dbSNP:rs6597630)"
FT /id="VAR_023067"
FT VARIANT 283
FT /note="T -> A (in dbSNP:rs2285487)"
FT /evidence="ECO:0000269|PubMed:9325058"
FT /id="VAR_023068"
FT CONFLICT 202
FT /note="A -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46672 MW; 5994D59678B17C21 CRC64;
MGKAKVPASK RAPSSPVAKP GPVKTLTRKK NKKKKRFWKS KAREVSKKPA SGPGAVVRPP
KAPEDFSQNW KALQEWLLKQ KSQAPEKPLV ISQMGSKKKP KIIQQNKKET SPQVKGEEMP
AGKDQEASRG SVPSGSKMDR RAPVPRTKAS GTEHNKKGTK ERTNGDIVPE RGDIEHKKRK
AKEAAPAPPT EEDIWFDDVD PADIEAAIGP EAAKIARKQL GQSEGSVSLS LVKEQAFGGL
TRALALDCEM VGVGPKGEES MAARVSIVNQ YGKCVYDKYV KPTEPVTDYR TAVSGIRPEN
LKQGEELEVV QKEVAEMLKG RILVGHALHN DLKVLFLDHP KKKIRDTQKY KPFKSQVKSG
RPSLRLLSEK ILGLQVQQAE HCSIQDAQAA MRLYVMVKKE WESMARDRRP LLTAPDHCSD
DA
