ID FOG1_HUMAN Reviewed; 1006 AA. AC Q8IX07; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 02-SEP-2026, entry version 182. DE RecName: Full=Zinc finger protein ZFPM1; DE AltName: Full=Friend of GATA protein 1; DE Short=FOG-1; DE Short=Friend of GATA 1; DE AltName: Full=Zinc finger protein 89A; DE AltName: Full=Zinc finger protein multitype 1; GN Name=ZFPM1; Synonyms=FOG1, ZFN89A; 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], TISSUE SPECIFICITY, AND INTERACTION WITH GATA1 RP AND GATA2. RC TISSUE=Megakaryocyte; RX PubMed=12483298; DOI=10.1007/s00439-002-0832-1; RA Freson K., Thys C., Wittewrongel C., Vermylen J., Hoylaerts M.F., RA Van Geet C.; RT "Molecular cloning and characterization of the GATA1 cofactor human FOG1 RT and assessment of its binding to GATA1 proteins carrying D218 RT substitutions."; RL Hum. Genet. 112:42-49(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] 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 [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, 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 [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901 AND SER-909, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-272; SER-384; RP SER-494; SER-638; SER-786; SER-901 AND SER-909, AND IDENTIFICATION BY MASS RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671; SER-786; SER-901 AND RP SER-914, AND 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). CC -!- FUNCTION: Transcription regulator that plays an essential role in CC erythroid and megakaryocytic cell differentiation. Essential cofactor CC that acts via the formation of a heterodimer with transcription factors CC of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both CC activate or repress transcriptional activity, depending on the cell and CC promoter context. The heterodimer formed with GATA proteins is CC essential to activate expression of genes such as NFE2, ITGA2B, CC alpha- and beta-globin, while it represses expression of KLF1. May be CC involved in regulation of some genes in gonads. May also be involved in CC cardiac development, in a non-redundant way with ZFPM2/FOG2 (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with corepressor CTBP2; this interaction is however CC not essential for corepressor activity (By similarity). Interacts with CC the N-terminal zinc-finger of GATA1, GATA2 and probably GATA3. CC {ECO:0000250, ECO:0000269|PubMed:12483298}. CC -!- INTERACTION: CC Q8IX07; P15976: GATA1; NbExp=2; IntAct=EBI-3942619, EBI-3909284; CC Q8IX07; P49841: GSK3B; NbExp=2; IntAct=EBI-3942619, EBI-373586; CC Q8IX07; Q09028: RBBP4; NbExp=6; IntAct=EBI-3942619, EBI-620823; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Mainly expressed in hematopoietic tissues. Also CC expressed in adult cerebellum, stomach, lymph node, liver and pancreas. CC Expressed in fetal heart, liver and spleen. CC {ECO:0000269|PubMed:12483298}. CC -!- DOMAIN: The CCHC FOG-type zinc fingers 1, 2, 3 and 5 directly bind to CC GATA-type zinc fingers. The Tyr residue adjacent to the last Cys of the CC CCHC FOG-type zinc finger is essential for the interaction with GATA- CC type zinc fingers (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family. CC {ECO:0000255|PROSITE-ProRule:PRU01153}. 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; AF488691; AAN45858.1; -; mRNA. DR EMBL; AC116552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC135049; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471184; EAW66806.1; -; Genomic_DNA. DR CCDS; CCDS32502.1; -. DR RefSeq; NP_722520.2; NM_153813.3. DR PDB; 2XU7; X-ray; 1.90 A; C/D=1-15. DR AlphaFoldDB; Q8IX07; -. DR SMR; Q8IX07; -. DR BioGRID; 127806; 17. DR DIP; DIP-48415N; -. DR ELM; Q8IX07; -. DR FunCoup; Q8IX07; 710. DR IntAct; Q8IX07; 8. DR NDEx; IQUERY-CP-ZFPM1; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000326630; -. DR GlyGen; Q8IX07; 2 sites. DR iPTMnet; Q8IX07; -. DR PhosphoSitePlus; Q8IX07; -. DR BioMuta; ZFPM1; -. DR DMDM; 296434508; -. DR jPOST; Q8IX07; -. DR MassIVE; Q8IX07; -. DR PaxDb; 9606-ENSP00000326630; -. DR PeptideAtlas; Q8IX07; -. DR ProteomicsDB; 70959; -. DR Pumba; Q8IX07; -. DR Antibodypedia; 30722; 124 antibodies from 26 providers. DR DNASU; 161882; -. DR Ensembl; ENST00000319555.8; ENSP00000326630.2; ENSG00000179588.9. DR GeneID; 161882; -. DR KEGG; hsa:161882; -. DR MANE-Select; ENST00000319555.8; ENSP00000326630.2; NM_153813.3; NP_722520.2. DR UCSC; uc002fkv.4; human. DR AGR; HGNC:19762; -. DR ClinPGx; PA134920282; -. DR CTD; 161882; -. DR DisGeNET; 161882; -. DR GeneCards; ZFPM1; -. DR HGNC; HGNC:19762; ZFPM1. DR HPA; ENSG00000179588; Low tissue specificity. DR MIM; 601950; gene. DR OpenTargets; ENSG00000179588; -. DR VEuPathDB; HostDB:ENSG00000179588; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00530000063823; -. DR HOGENOM; CLU_010755_0_0_1; -. DR InParanoid; Q8IX07; -. DR OMA; DCGIWFR; -. DR OrthoDB; 8742770at2759; -. DR PAN-GO; Q8IX07; 8 GO annotations based on evolutionary models. DR PhylomeDB; Q8IX07; -. DR PathwayCommons; Q8IX07; -. DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q8IX07; -. DR SIGNOR; Q8IX07; -. DR Agora; ENSG00000179588; -. DR BioGRID-ORCS; 161882; 21 hits in 1182 CRISPR screens. DR ChiTaRS; ZFPM1; human. DR EvolutionaryTrace; Q8IX07; -. DR GeneWiki; ZFPM1; -. DR GenomeRNAi; 161882; -. DR Pharos; Q8IX07; Tbio. DR PRO; PR:Q8IX07; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q8IX07; protein. DR Bgee; ENSG00000179588; Expressed in pancreatic ductal cell and 164 other cell types or tissues. DR ExpressionAtlas; Q8IX07; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL. DR GO; GO:0017053; C:transcription repressor complex; IDA:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IGI:BHF-UCL. DR GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:BHF-UCL. DR GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL. DR GO; GO:0030218; P:erythrocyte differentiation; ISS:BHF-UCL. DR GO; GO:0007507; P:heart development; IBA:GO_Central. DR GO; GO:0030219; P:megakaryocyte differentiation; ISS:BHF-UCL. DR GO; GO:0003192; P:mitral valve formation; ISS:BHF-UCL. DR GO; GO:0032713; P:negative regulation of interleukin-4 production; IDA:BHF-UCL. DR GO; GO:0060377; P:negative regulation of mast cell differentiation; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL. DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL. DR GO; GO:0030220; P:platelet formation; IGI:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:BHF-UCL. DR GO; GO:0010724; P:regulation of definitive erythrocyte differentiation; IDA:BHF-UCL. DR GO; GO:0002295; P:T-helper cell lineage commitment; IC:BHF-UCL. DR GO; GO:0003195; P:tricuspid valve formation; ISS:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL. DR CDD; cd19215; PR-SET_ZFPM1; 1. DR FunFam; 3.30.160.60:FF:001079; zinc finger protein ZFPM1 isoform X2; 1. DR FunFam; 3.30.160.60:FF:000828; Zinc finger protein, FOG family member 1; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR IDEAL; IID00324; -. DR InterPro; IPR059121; CCHC_ZFPM2-like. DR InterPro; IPR039746; FOG. DR InterPro; IPR049361; ZFPM1/2_PR. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR034731; Znf_CCHC_FOG. DR PANTHER; PTHR12958; FRIEND OF GATA2-RELATED; 1. DR PANTHER; PTHR12958:SF4; ZINC FINGER PROTEIN ZFPM1; 1. DR Pfam; PF25445; CCHC_ZFPM2; 1. DR Pfam; PF21182; FOG1-like_PR; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 9. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6. DR PROSITE; PS51810; ZF_CCHC_FOG; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. DR PDBsum; 2XU7; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..1006 FT /note="Zinc finger protein ZFPM1" FT /id="PRO_0000221041" FT ZN_FING 235..268 FT /note="CCHC FOG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 290..314 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 320..342 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 348..371 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 571..604 FT /note="CCHC FOG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 677..710 FT /note="CCHC FOG-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 811..844 FT /note="CCHC FOG-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT ZN_FING 854..877 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 968..1001 FT /note="CCHC FOG-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT REGION 1..93 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 114..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 330..341 FT /note="Interaction with TACC3" FT /evidence="ECO:0000250" FT REGION 384..409 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 438..460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 473..515 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 605..681 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 708..810 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 794..800 FT /note="Interaction with CTBP2" FT /evidence="ECO:0000250" FT REGION 889..971 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..13 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..25 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..62 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 66..79 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..130 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 485..515 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 617..629 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 715..735 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 754..769 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 780..791 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 925..950 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 246 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 579 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 582 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 595 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 600 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 685 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 688 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 701 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 706 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 819 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 822 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 835 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 840 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 976 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 979 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 992 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT BINDING 997 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01153" FT MOD_RES 84 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 128 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35615" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 491 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35615" FT MOD_RES 494 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 638 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 786 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 901 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 909 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 914 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 935 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35615" FT VARIANT 70 FT /note="G -> A (in dbSNP:rs34916016)" FT /id="VAR_057491" FT CONFLICT 22 FT /note="R -> G (in Ref. 1; AAN45858)" FT /evidence="ECO:0000305" FT CONFLICT 444..447 FT /note="EPLA -> AP (in Ref. 1; AAN45858)" FT /evidence="ECO:0000305" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:2XU7" SQ SEQUENCE 1006 AA; 104888 MW; E9C2363503A64898 CRC64; MSRRKQSNPR QIKRSLGDME AREEVQLVGA SHMEQKATAP EAPSPPSADV NSPPPLPPPT SPGGPKELEG QEPEPRPTEE EPGSPWSGPD ELEPVVQDGQ RRIRARLSLA TGLSWGPFHG SVQTRASSPR QAEPSPALTL LLVDEACWLR TLPQALTEAE ANTEIHRKDD ALWCRVTKPV PAGGLLSVLL TAEPHSTPGH PVKKEPAEPT CPAPAHDLQL LPQQAGMASI LATAVINKDV FPCKDCGIWY RSERNLQAHL LYYCASRQGT GSPAAAATDE KPKETYPNER VCPFPQCRKS CPSASSLEIH MRSHSGERPF VCLICLSAFT TKANCERHLK VHTDTLSGVC HSCGFISTTR DILYSHLVTN HMVCQPGSKG EIYSPGAGHP ATKLPPDSLG SFQQQHTALQ GPLASADLGL APTPSPGLDR KALAEATNGE ARAEPLAQNG GSSEPPAAPR SIKVEAVEEP EAAPILGPGE PGPQAPSRTP SPRSPAPARV KAELSSPTPG SSPVPGELGL AGALFLPQYV FGPDAAPPAS EILAKMSELV HSRLQQGAGA GAGGAQTGLF PGAPKGATCF ECEITFSNVN NYYVHKRLYC SGRRAPEDAP AARRPKAPPG PARAPPGQPA EPDAPRSSPG PGAREEGAGG AATPEDGAGG RGSEGSQSPG SSVDDAEDDP SRTLCEACNI RFSRHETYTV HKRYYCASRH DPPPRRPAAP PGPPGPAAPP APSPAAPVRT RRRRKLYELH AAGAPPPPPP GHAPAPESPR PGSGSGSGPG LAPARSPGPA ADGPIDLSKK PRRPLPGAPA PALADYHECT ACRVSFHSLE AYLAHKKYSC PAAPPPGALG LPAAACPYCP PNGPVRGDLL EHFRLAHGLL LGAPLAGPGV EARTPADRGP SPAPAPAASP QPGSRGPRDG LGPEPQEPPP GPPPSPAAAP EAVPPPPAPP SYSDKGVQTP SKGTPAPLPN GNHRYCRLCN IKFSSLSTFI AHKKYYCSSH AAEHVK //