ID ZNF74_HUMAN Reviewed; 644 AA. AC Q16587; B5MCE3; B7Z5Y2; Q6IBV2; Q6PJP1; Q9UC04; Q9UF05; Q9UF06; Q9UF07; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Zinc finger protein 74; DE AltName: Full=Zinc finger protein 520; DE AltName: Full=hZNF7; GN Name=ZNF74; Synonyms=ZNF520; 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). RC TISSUE=Brain; RX PubMed=8663113; DOI=10.1074/jbc.271.26.15458; RA Grondin B., Bazinet M., Aubry M.; RT "The KRAB zinc finger gene ZNF74 encodes an RNA-binding protein tightly RT associated with the nuclear matrix."; RL J. Biol. Chem. 271:15458-15467(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8268910; DOI=10.1093/hmg/2.10.1583; RA Aubry M., Demczuk S., Desmaze C., Aikem M., Aurias M., Julien J.-P., RA Rouleau G.A.; RT "Isolation of a zinc finger gene consistently deleted in DiGeorge RT syndrome."; RL Hum. Mol. Genet. 2:1583-1587(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RA Aubry M., Cote F.; RT "Alternative promoter usage and splicing of ZNF74 gene."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-117. RC TISSUE=Brain; 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 GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). RC TISSUE=Muscle, and Retinoblastoma; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 499-583. RX PubMed=1639391; DOI=10.1016/0888-7543(92)90135-f; RA Aubry M., Marineau C., Zhang F.R., Zahed L., Figlewicz D., Delattre O., RA Thomas G., de Jong P.J., Julien J.-P., Rouleau G.A.; RT "Cloning of six new genes with zinc finger motifs mapping to short and long RT arms of human acrocentric chromosome 22 (p and q11.2)."; RL Genomics 13:641-648(1992). RN [9] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-582, 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). RN [10] RP VARIANTS LYS-117 AND 623-LYS-LEU-624 DELINS ASN-PHE. RX PubMed=11705709; DOI=10.1016/s0920-9964(00)00191-2; RA Takase K., Ohtsuki T., Migita O., Toru M., Inada T., Yamakawa-Kobayashi K., RA Arinami T.; RT "Association of ZNF74 gene genotypes with age-at-onset of schizophrenia."; RL Schizophr. Res. 52:161-165(2001). CC -!- FUNCTION: May play a role in RNA metabolism. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=2; CC IsoId=Q16587-1; Sequence=Displayed; CC Name=1; CC IsoId=Q16587-2; Sequence=VSP_006891; CC Name=3; CC IsoId=Q16587-3; Sequence=VSP_006892; CC Name=4; CC IsoId=Q16587-4; Sequence=VSP_006893; CC Name=5; CC IsoId=Q16587-5; Sequence=VSP_045530, VSP_045531; CC -!- TISSUE SPECIFICITY: Highly expressed in the fetal brain. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF21777.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF21778.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF21779.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF21780.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA50632.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA63379.1; Type=Frameshift; 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; X92715; CAA63379.1; ALT_FRAME; mRNA. DR EMBL; X71623; CAA50632.1; ALT_FRAME; mRNA. DR EMBL; CR456616; CAG30502.1; -; mRNA. DR EMBL; AF072567; AAF21777.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF072557; AAF21777.1; JOINED; Genomic_DNA. DR EMBL; AF072562; AAF21777.1; JOINED; Genomic_DNA. DR EMBL; AF072567; AAF21778.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF072557; AAF21778.1; JOINED; Genomic_DNA. DR EMBL; AF072562; AAF21778.1; JOINED; Genomic_DNA. DR EMBL; AF072567; AAF21779.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF072562; AAF21779.1; JOINED; Genomic_DNA. DR EMBL; AF072567; AAF21780.1; ALT_FRAME; Genomic_DNA. DR EMBL; AF072562; AAF21780.1; JOINED; Genomic_DNA. DR EMBL; AK299569; BAH13068.1; -; mRNA. DR EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013395; AAH13395.1; -; mRNA. DR EMBL; BC056902; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X63182; CAC16149.1; -; Genomic_DNA. DR CCDS; CCDS42982.1; -. [Q16587-1] DR CCDS; CCDS58794.1; -. [Q16587-5] DR PIR; I39311; I39311. DR RefSeq; NP_001243452.1; NM_001256523.1. [Q16587-5] DR RefSeq; NP_001243453.1; NM_001256524.1. [Q16587-1] DR RefSeq; NP_001243454.1; NM_001256525.1. [Q16587-2] DR RefSeq; NP_003417.2; NM_003426.3. [Q16587-1] DR AlphaFoldDB; Q16587; -. DR SMR; Q16587; -. DR BioGRID; 113444; 36. DR IntAct; Q16587; 4. DR MINT; Q16587; -. DR STRING; 9606.ENSP00000383301; -. DR iPTMnet; Q16587; -. DR PhosphoSitePlus; Q16587; -. DR BioMuta; ZNF74; -. DR DMDM; 292495055; -. DR EPD; Q16587; -. DR jPOST; Q16587; -. DR MassIVE; Q16587; -. DR PaxDb; 9606-ENSP00000483077; -. DR PeptideAtlas; Q16587; -. DR ProteomicsDB; 6037; -. DR ProteomicsDB; 60933; -. [Q16587-1] DR ProteomicsDB; 60934; -. [Q16587-2] DR ProteomicsDB; 60935; -. [Q16587-3] DR ProteomicsDB; 60936; -. [Q16587-4] DR Antibodypedia; 316; 80 antibodies from 18 providers. DR DNASU; 7625; -. DR Ensembl; ENST00000400451.7; ENSP00000383301.2; ENSG00000185252.19. [Q16587-1] DR Ensembl; ENST00000403682.7; ENSP00000384750.3; ENSG00000185252.19. [Q16587-5] DR Ensembl; ENST00000405993.2; ENSP00000385855.1; ENSG00000185252.19. [Q16587-3] DR Ensembl; ENST00000611540.4; ENSP00000483077.1; ENSG00000185252.19. [Q16587-1] DR GeneID; 7625; -. DR KEGG; hsa:7625; -. DR MANE-Select; ENST00000400451.7; ENSP00000383301.2; NM_003426.4; NP_003417.2. DR UCSC; uc002zsh.5; human. [Q16587-1] DR AGR; HGNC:13144; -. DR CTD; 7625; -. DR DisGeNET; 7625; -. DR GeneCards; ZNF74; -. DR HGNC; HGNC:13144; ZNF74. DR HPA; ENSG00000185252; Low tissue specificity. DR MIM; 194548; gene. DR neXtProt; NX_Q16587; -. DR OpenTargets; ENSG00000185252; -. DR PharmGKB; PA37718; -. DR VEuPathDB; HostDB:ENSG00000185252; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162000; -. DR HOGENOM; CLU_002678_44_5_1; -. DR InParanoid; Q16587; -. DR OMA; RPEWQLK; -. DR OrthoDB; 4718324at2759; -. DR PhylomeDB; Q16587; -. DR TreeFam; TF341817; -. DR PathwayCommons; Q16587; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q16587; -. DR BioGRID-ORCS; 7625; 29 hits in 1174 CRISPR screens. DR GeneWiki; ZNF74; -. DR GenomeRNAi; 7625; -. DR Pharos; Q16587; Tbio. DR PRO; PR:Q16587; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q16587; Protein. DR Bgee; ENSG00000185252; Expressed in cortical plate and 129 other cell types or tissues. DR ExpressionAtlas; Q16587; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 12. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1. DR PANTHER; PTHR23232:SF140; ZINC FINGER PROTEIN 726; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 8. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 12. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12. DR Genevisible; Q16587; HS. PE 1: Evidence at protein level; KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Reference proteome; Repeat; RNA-binding; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..644 FT /note="Zinc finger protein 74" FT /id="PRO_0000047383" FT DOMAIN 43..114 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 248..270 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 276..298 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 304..326 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 332..354 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 360..382 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 388..410 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 416..438 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 444..466 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 472..494 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 500..522 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 528..550 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 556..578 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT CROSSLNK 582 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..82 FT /note="MEIPAPEPEKTALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDF FT TQEEWGQLDSPQRALYRDVMLENYQNLLAL -> MPSPPFSPRA (in isoform FT 4)" FT /evidence="ECO:0000305" FT /id="VSP_006893" FT VAR_SEQ 1..71 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:8268910, ECO:0000303|PubMed:8663113" FT /id="VSP_006891" FT VAR_SEQ 12..178 FT /note="ALSSQDPALSLKENLEDISGWGLPEARSKESVSFKDVAVDFTQEEWGQLDSP FT QRALYRDVMLENYQNLLALGPPLHKPDVISHLERGEEPWSMQREVPRGPCPEWELKAVP FT SQQQGICKEEPAQEPIMERPLGGAQAWGRQAGALQRSQAAPWAPAPAMVWDVPVEE -> FT GIGEFQGCGCGLHPGGVGSTRLPSEGLVPGCDVGELPEPSCPRTSTAQARCDLSSGTRR FT GAMEHAEGSPQRALSRMGAEGGALSTAGHLQRRTGPGAHHGAAPRRGAGVGAPGRCSAE FT ESGCALGARTCHGLGRPCRGIPPQVSPLRPATRSRGGTLAGHTQERPGH (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045530" FT VAR_SEQ 83..114 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_006892" FT VAR_SEQ 179..644 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045531" FT VARIANT 117 FT /note="E -> K (in dbSNP:rs3747076)" FT /evidence="ECO:0000269|PubMed:11705709, FT ECO:0000269|PubMed:14702039" FT /id="VAR_012993" FT VARIANT 623..624 FT /note="KL -> NF" FT /evidence="ECO:0000269|PubMed:11705709" FT /id="VAR_012994" FT CONFLICT 171 FT /note="V -> A (in Ref. 7; AAH13395)" FT /evidence="ECO:0000305" FT CONFLICT 517 FT /note="V -> M (in Ref. 1; CAA63379, 2; CAA50632 and 4; FT AAF21777/AAF21778/AAF21779/AAF21780)" FT /evidence="ECO:0000305" FT CONFLICT 569 FT /note="S -> P (in Ref. 5; BAH13068)" FT /evidence="ECO:0000305" SQ SEQUENCE 644 AA; 72207 MW; 87E5AA122BBC82F1 CRC64; MEIPAPEPEK TALSSQDPAL SLKENLEDIS GWGLPEARSK ESVSFKDVAV DFTQEEWGQL DSPQRALYRD VMLENYQNLL ALGPPLHKPD VISHLERGEE PWSMQREVPR GPCPEWELKA VPSQQQGICK EEPAQEPIME RPLGGAQAWG RQAGALQRSQ AAPWAPAPAM VWDVPVEEFP LRCPLFAQQR VPEGGPLLDT RKNVQATEGR TKAPARLCAG ENASTPSEPE KFPQVRRQRG AGAGEGEFVC GECGKAFRQS SSLTLHRRWH SREKAYKCDE CGKAFTWSTN LLEHRRIHTG EKPFFCGECG KAFSCHSSLN VHQRIHTGER PYKCSACEKA FSCSSLLSMH LRVHTGEKPY RCGECGKAFN QRTHLTRHHR IHTGEKPYQC GSCGKAFTCH SSLTVHEKIH SGDKPFKCSD CEKAFNSRSR LTLHQRTHTG EKPFKCADCG KGFSCHAYLL VHRRIHSGEK PFKCNECGKA FSSHAYLIVH RRIHTGEKPF DCSQCWKAFS CHSSLIVHQR IHTGEKPYKC SECGRAFSQN HCLIKHQKIH SGEKSFKCEK CGEMFNWSSH LTEHQRLHSE GKPLAIQFNK HLLSTYYVPG SLLGAGDAGL RDVDPIDALD VAKLLCVVPP RAGRNFSLGS KPRN //