FOG1_HUMAN
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 03-AUG-2022, entry version 163.
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=4; 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}.
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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_153813.2.
DR PDB; 2XU7; X-ray; 1.90 A; C/D=1-15.
DR PDBsum; 2XU7; -.
DR AlphaFoldDB; Q8IX07; -.
DR SMR; Q8IX07; -.
DR BioGRID; 127806; 11.
DR DIP; DIP-48415N; -.
DR ELM; Q8IX07; -.
DR IntAct; Q8IX07; 7.
DR STRING; 9606.ENSP00000326630; -.
DR iPTMnet; Q8IX07; -.
DR PhosphoSitePlus; Q8IX07; -.
DR BioMuta; ZFPM1; -.
DR DMDM; 296434508; -.
DR EPD; Q8IX07; -.
DR jPOST; Q8IX07; -.
DR MassIVE; Q8IX07; -.
DR MaxQB; Q8IX07; -.
DR PaxDb; Q8IX07; -.
DR PeptideAtlas; Q8IX07; -.
DR PRIDE; Q8IX07; -.
DR ProteomicsDB; 70959; -.
DR Antibodypedia; 30722; 122 antibodies from 24 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 CTD; 161882; -.
DR DisGeNET; 161882; -.
DR GeneCards; ZFPM1; -.
DR HGNC; HGNC:19762; ZFPM1.
DR HPA; ENSG00000179588; Low tissue specificity.
DR MIM; 601950; gene.
DR neXtProt; NX_Q8IX07; -.
DR OpenTargets; ENSG00000179588; -.
DR PharmGKB; PA134920282; -.
DR VEuPathDB; HostDB:ENSG00000179588; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00530000063823; -.
DR HOGENOM; CLU_010755_0_0_1; -.
DR InParanoid; Q8IX07; -.
DR OMA; PPCGIRF; -.
DR OrthoDB; 76702at2759; -.
DR PhylomeDB; Q8IX07; -.
DR TreeFam; TF331342; -.
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 BioGRID-ORCS; 161882; 20 hits in 1104 CRISPR screens.
DR ChiTaRS; ZFPM1; human.
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 162 other tissues.
DR ExpressionAtlas; Q8IX07; baseline and differential.
DR Genevisible; Q8IX07; HS.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:BHF-UCL.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISS:BHF-UCL.
DR GO; GO:0003192; P:mitral valve formation; ISS:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; 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:0032091; P:negative regulation of protein binding; 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:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0032642; P:regulation of chemokine production; IEA:Ensembl.
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 IDEAL; IID00324; -.
DR InterPro; IPR039746; FOG.
DR InterPro; IPR034731; ZF_CCHC_FOG.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12958; PTHR12958; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS51810; ZF_CCHC_FOG; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW 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 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..64
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..953
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"
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
