ID ZN768_HUMAN Reviewed; 540 AA. AC Q9H5H4; Q569L7; Q96CX4; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 27-MAR-2024, entry version 179. DE RecName: Full=Zinc finger protein 768; GN Name=ZNF768; 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 [LARGE SCALE MRNA], AND VARIANT ASP-181. RC TISSUE=Ovary, and PNS; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-540. RC TISSUE=Epithelium; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-160, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-83, AND RP IDENTIFICATION BY 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-90 AND SER-97, AND 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-90; SER-97; SER-125; RP SER-132; SER-139 AND SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [10] RP FUNCTION, INTERACTION WITH ELF3, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=30476274; DOI=10.1093/nar/gky1148; RA Rohrmoser M., Kluge M., Yahia Y., Gruber-Eber A., Maqbool M.A., Forne I., RA Krebs S., Blum H., Greifenberg A.K., Geyer M., Descostes N., Imhof A., RA Andrau J.C., Friedel C.C., Eick D.; RT "MIR sequences recruit zinc finger protein ZNF768 to expressed genes."; RL Nucleic Acids Res. 47:700-715(2019). RN [11] RP FUNCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT SER-17; SER-18; SER-23; RP TYR-27; SER-33; SER-62; SER-69; SER-76; SER-83; SER-90; SER-97; SER-104; RP SER-107; SER-111; SER-118; SER-125; TYR-128; SER-132; TYR-135; SER-139; RP TYR-142; SER-144; SER-147; THR-158; SER-160; THR-284; TYR-289; SER-295; RP SER-299; THR-396 AND SER-442, AND MUTAGENESIS OF SER-62; SER-69; SER-76; RP SER-83; SER-90; SER-97; SER-125; SER-132; SER-139 AND SER-160. RX PubMed=34404770; DOI=10.1038/s41467-021-24932-w; RA Villot R., Poirier A., Bakan I., Boulay K., Fernandez E., Devillers R., RA Gama-Braga L., Tribouillard L., Gagne A., Duchesne E., Caron D., RA Berube J.S., Berube J.C., Coulombe Y., Orain M., Gelinas Y., Gobeil S., RA Bosse Y., Masson J.Y., Elowe S., Bilodeau S., Manem V., Joubert P., RA Mallette F.A., Laplante M.; RT "ZNF768 links oncogenic RAS to cellular senescence."; RL Nat. Commun. 12:4841-4841(2021). CC -!- FUNCTION: Binds to mammalian-wide interspersed repeat (MIRs) sequences CC in euchromatin and promoter regions of genes at the consensus sequence CC 5'-GCTGTGTG-[N20]-CCTCTCTG-3', consisting of two anchor regions CC connected by a linker region; the linker region probably does not CC contribute to the binding specificity (PubMed:30476274). Required for CC cell homeostasis (PubMed:34404770). May be involved in transcriptional CC regulation (Probable). {ECO:0000269|PubMed:30476274, CC ECO:0000269|PubMed:34404770, ECO:0000305}. CC -!- SUBUNIT: Interacts (via zinc-finger domains) with TP53 (via N- CC terminus); interaction might be facilitated by TP53 oligomerization CC state (PubMed:34404770). Interacts with ELP3 (PubMed:30476274). CC {ECO:0000269|PubMed:30476274, ECO:0000269|PubMed:34404770}. CC -!- INTERACTION: CC Q9H5H4; P49760: CLK2; NbExp=3; IntAct=EBI-1210580, EBI-750020; CC Q9H5H4; O95967: EFEMP2; NbExp=3; IntAct=EBI-1210580, EBI-743414; CC Q9H5H4; Q92979: EMG1; NbExp=3; IntAct=EBI-1210580, EBI-718638; CC Q9H5H4; Q13526: PIN1; NbExp=5; IntAct=EBI-1210580, EBI-714158; CC Q9H5H4; O00560: SDCBP; NbExp=3; IntAct=EBI-1210580, EBI-727004; CC Q9H5H4; P15622-3: ZNF250; NbExp=3; IntAct=EBI-1210580, EBI-10177272; CC Q9H5H4; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-1210580, EBI-373456; CC Q9H5H4; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-1210580, EBI-740727; CC Q9H5H4; Q5T619: ZNF648; NbExp=3; IntAct=EBI-1210580, EBI-11985915; CC Q9H5H4; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-1210580, EBI-5667516; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:30476274}. Chromosome CC {ECO:0000269|PubMed:30476274}. Note=Localizes to euchromatin. CC {ECO:0000269|PubMed:30476274}. CC -!- PTM: May be phosphorylated at residue 'Ser-5' of the tandem CC heptapeptide repeats in the N-terminus (PubMed:30476274). CC Phosphorylation might be increased upon RAS pathway activation and CC negatively regulate protein stability (PubMed:34404770). CC {ECO:0000269|PubMed:30476274, ECO:0000269|PubMed:34404770}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH13760.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH92403.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15652.1; Type=Erroneous initiation; 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; BC013760; AAH13760.1; ALT_INIT; mRNA. DR EMBL; BC092403; AAH92403.2; ALT_INIT; mRNA. DR EMBL; AK027089; BAB15652.1; ALT_INIT; mRNA. DR CCDS; CCDS10681.2; -. DR RefSeq; NP_078947.3; NM_024671.3. DR AlphaFoldDB; Q9H5H4; -. DR SMR; Q9H5H4; -. DR BioGRID; 122839; 182. DR IntAct; Q9H5H4; 42. DR MINT; Q9H5H4; -. DR STRING; 9606.ENSP00000369777; -. DR iPTMnet; Q9H5H4; -. DR PhosphoSitePlus; Q9H5H4; -. DR BioMuta; ZNF768; -. DR DMDM; 158564024; -. DR EPD; Q9H5H4; -. DR jPOST; Q9H5H4; -. DR MassIVE; Q9H5H4; -. DR MaxQB; Q9H5H4; -. DR PaxDb; 9606-ENSP00000369777; -. DR PeptideAtlas; Q9H5H4; -. DR ProteomicsDB; 80905; -. DR Pumba; Q9H5H4; -. DR Antibodypedia; 13715; 160 antibodies from 20 providers. DR DNASU; 79724; -. DR Ensembl; ENST00000380412.7; ENSP00000369777.5; ENSG00000169957.10. DR GeneID; 79724; -. DR KEGG; hsa:79724; -. DR MANE-Select; ENST00000380412.7; ENSP00000369777.5; NM_024671.4; NP_078947.3. DR UCSC; uc002dyk.4; human. DR AGR; HGNC:26273; -. DR CTD; 79724; -. DR GeneCards; ZNF768; -. DR HGNC; HGNC:26273; ZNF768. DR HPA; ENSG00000169957; Low tissue specificity. DR MIM; 618032; gene. DR neXtProt; NX_Q9H5H4; -. DR OpenTargets; ENSG00000169957; -. DR PharmGKB; PA162410327; -. DR VEuPathDB; HostDB:ENSG00000169957; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000162267; -. DR InParanoid; Q9H5H4; -. DR OMA; SPQFEML; -. DR OrthoDB; 2882612at2759; -. DR PhylomeDB; Q9H5H4; -. DR TreeFam; TF350793; -. DR PathwayCommons; Q9H5H4; -. DR SignaLink; Q9H5H4; -. DR BioGRID-ORCS; 79724; 11 hits in 1183 CRISPR screens. DR ChiTaRS; ZNF768; human. DR GenomeRNAi; 79724; -. DR Pharos; Q9H5H4; Tdark. DR PRO; PR:Q9H5H4; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q9H5H4; Protein. DR Bgee; ENSG00000169957; Expressed in apex of heart and 203 other cell types or tissues. DR ExpressionAtlas; Q9H5H4; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; HDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 10. DR InterPro; IPR000684; RNA_pol_II_repeat_euk. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24393:SF100; LOW QUALITY PROTEIN: ZINC FINGER PROTEIN 595-LIKE-RELATED; 1. DR PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1. DR Pfam; PF05001; RNA_pol_Rpb1_R; 4. DR Pfam; PF00096; zf-C2H2; 10. DR SMART; SM00355; ZnF_C2H2; 10. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10. DR Genevisible; Q9H5H4; HS. PE 1: Evidence at protein level; KW Chromosome; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..540 FT /note="Zinc finger protein 768" FT /id="PRO_0000304408" FT ZN_FING 261..283 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 289..311 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 317..339 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 345..367 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 373..395 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 401..423 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 429..451 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 457..479 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 485..507 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 513..535 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..166 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 239..258 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..123 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..166 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:18669648" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 27 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 62 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 97 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 111 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:23186163" FT MOD_RES 128 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:23186163" FT MOD_RES 135 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:23186163" FT MOD_RES 142 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 144 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 158 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770, FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:23186163" FT MOD_RES 284 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 289 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 396 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:34404770" FT MOD_RES 442 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:34404770" FT VARIANT 181 FT /note="E -> D (in dbSNP:rs10871453)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035024" FT VARIANT 488 FT /note="A -> S (in dbSNP:rs3751848)" FT /id="VAR_052900" FT MUTAGEN 62 FT /note="S->A: Increases protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 69 FT /note="S->A: Increases protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 76 FT /note="S->A: Increases protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 83 FT /note="S->A: Increases protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 90 FT /note="S->A: No effect on protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 97 FT /note="S->A: No effect on protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 125 FT /note="S->A: No effect on protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 132 FT /note="S->A: No effect on protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 139 FT /note="S->A: Increases protein stability." FT /evidence="ECO:0000269|PubMed:34404770" FT MUTAGEN 160 FT /note="S->A: No effect on protein stability." FT /evidence="ECO:0000269|PubMed:34404770" SQ SEQUENCE 540 AA; 60229 MW; 7E9299F7C1BEE866 CRC64; MEREALPWGL EPQDVQSSDE MRSPEGYLRG NMSENEEEEI SQQEGSGDYE VEEIPFGLEP QSPGFEPQSP EFEPQSPRFE PESPGFESRS PGLVPPSPEF APRSPESDSQ SPEFESQSPR YEPQSPGYEP RSPGYEPRSP GYESESSRYE SQNTELKTQS PEFEAQSSKF QEGAEMLLNP EEKSPLNISV GVHPLDSFTQ GFGEQPTGDL PIGPPFEMPT GALLSTPQFE MLQNPLGLTG ALRGPGRRGG RARGGQGPRP NICGICGKSF GRGSTLIQHQ RIHTGEKPYK CEVCSKAFSQ SSDLIKHQRT HTGERPYKCP RCGKAFADSS YLLRHQRTHS GQKPYKCPHC GKAFGDSSYL LRHQRTHSHE RPYSCTECGK CYSQNSSLRS HQRVHTGQRP FSCGICGKSF SQRSALIPHA RSHAREKPFK CPECGKRFGQ SSVLAIHART HLPGRTYSCP DCGKTFNRSS TLIQHQRSHT GERPYRCAVC GKGFCRSSTL LQHHRVHSGE RPYKCDDCGK AFSQSSDLIR HQRTHAAGRR //