ZFAN5_HUMAN
ID ZFAN5_HUMAN Reviewed; 213 AA.
AC O76080; A8K484;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=AN1-type zinc finger protein 5;
DE AltName: Full=Zinc finger A20 domain-containing protein 2;
DE AltName: Full=Zinc finger protein 216;
GN Name=ZFAND5; Synonyms=ZA20D2, ZNF216;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9758550; DOI=10.1016/s0378-1119(98)00316-3;
RA Scott D.A., Greinwald J.H. Jr., Marietta J.R., Drury S., Swiderski R.E.,
RA Vinas A., DeAngelis M.M., Carmi R., Ramesh A., Kraft M.L., Elbedour K.,
RA Skworak A.B., Friedman R.A., Srikumari Srisailapathy C.R., Verhoeven K.,
RA Van Camp G., Lovett M., Deininger P.L., Batzer M.A., Morton C.C.,
RA Keats B.J., Smith R.J.H., Sheffield V.C.;
RT "Identification and mutation analysis of a cochlear-expressed, zinc finger
RT protein gene at the DFNB7/11 and dn hearing-loss loci on human chromosome
RT 9q and mouse chromosome 19.";
RL Gene 215:461-469(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Lung, and Skin;
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 [6]
RP TISSUE SPECIFICITY, INTERACTION WITH IKBKG; RIPK1 AND TRAF6, AND FUNCTION.
RX PubMed=14754897; DOI=10.1074/jbc.m309491200;
RA Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z.,
RA Shu H.-B.;
RT "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of
RT NFkappaB activation.";
RL J. Biol. Chem. 279:16847-16853(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Involved in protein degradation via the ubiquitin-proteasome
CC system. May act by anchoring ubiquitinated proteins to the proteasome.
CC Plays a role in ubiquitin-mediated protein degradation during muscle
CC atrophy. Plays a role in the regulation of NF-kappa-B activation and
CC apoptosis. Inhibits NF-kappa-B activation triggered by overexpression
CC of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor
CC (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent
CC manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a
CC potent inhibitory factor for osteoclast differentiation.
CC {ECO:0000269|PubMed:14754897}.
CC -!- SUBUNIT: Interacts with ubiquitin and polyubiquitinated proteins.
CC Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where
CC ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule (By
CC similarity). Homooligomer and/or heterooligomer. Interacts (via A20-
CC type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain).
CC {ECO:0000250, ECO:0000269|PubMed:14754897}.
CC -!- INTERACTION:
CC O76080; P0CG48: UBC; NbExp=3; IntAct=EBI-8028844, EBI-3390054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Expressed in
CC fetal cochlea. Also expressed in infant brain, fetal heart, pancreatic
CC islet, melanocyte, pineal gland, placenta, corneal stroma, and
CC parathyroid tumor. Weakly expressed or undetectable in adult brain,
CC heart, colon, thymus, spleen, kidney, liver, small intestine, placenta,
CC lung and peripheral blood leukocytes. Expressed in rhabdomyosarcoma RD
CC cells (at protein level). {ECO:0000269|PubMed:14754897,
CC ECO:0000269|PubMed:9758550}.
CC -!- DOMAIN: The A20-type zinc finger directly binds polyubiquitin chains
CC and associates with the 26S proteasome. The zinc-finger A20-type domain
CC is essential for inhibition of NF-kappa-B activation (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF062072; AAC61801.1; -; Genomic_DNA.
DR EMBL; AF062346; AAC42601.1; -; mRNA.
DR EMBL; AF062347; AAC42602.1; -; mRNA.
DR EMBL; AK290849; BAF83538.1; -; mRNA.
DR EMBL; AL135924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62533.1; -; Genomic_DNA.
DR EMBL; BC011018; AAH11018.1; -; mRNA.
DR EMBL; BC027707; AAH27707.1; -; mRNA.
DR EMBL; BC073131; AAH73131.1; -; mRNA.
DR CCDS; CCDS6642.1; -.
DR RefSeq; NP_001095890.1; NM_001102420.2.
DR RefSeq; NP_001095891.1; NM_001102421.2.
DR RefSeq; NP_001265172.1; NM_001278243.1.
DR RefSeq; NP_001265173.1; NM_001278244.1.
DR RefSeq; NP_001265174.1; NM_001278245.1.
DR RefSeq; NP_005998.1; NM_006007.3.
DR AlphaFoldDB; O76080; -.
DR BMRB; O76080; -.
DR SMR; O76080; -.
DR BioGRID; 113546; 24.
DR IntAct; O76080; 10.
DR MINT; O76080; -.
DR STRING; 9606.ENSP00000237937; -.
DR iPTMnet; O76080; -.
DR PhosphoSitePlus; O76080; -.
DR BioMuta; ZFAND5; -.
DR EPD; O76080; -.
DR jPOST; O76080; -.
DR MassIVE; O76080; -.
DR MaxQB; O76080; -.
DR PaxDb; O76080; -.
DR PeptideAtlas; O76080; -.
DR PRIDE; O76080; -.
DR ProteomicsDB; 50381; -.
DR TopDownProteomics; O76080; -.
DR Antibodypedia; 12564; 232 antibodies from 17 providers.
DR DNASU; 7763; -.
DR Ensembl; ENST00000237937.7; ENSP00000237937.3; ENSG00000107372.13.
DR Ensembl; ENST00000343431.6; ENSP00000350586.2; ENSG00000107372.13.
DR Ensembl; ENST00000376960.8; ENSP00000366159.4; ENSG00000107372.13.
DR Ensembl; ENST00000376962.10; ENSP00000366161.5; ENSG00000107372.13.
DR GeneID; 7763; -.
DR KEGG; hsa:7763; -.
DR MANE-Select; ENST00000376962.10; ENSP00000366161.5; NM_001102420.3; NP_001095890.1.
DR UCSC; uc004aix.3; human.
DR CTD; 7763; -.
DR DisGeNET; 7763; -.
DR GeneCards; ZFAND5; -.
DR HGNC; HGNC:13008; ZFAND5.
DR HPA; ENSG00000107372; Tissue enhanced (skeletal).
DR MIM; 604761; gene.
DR neXtProt; NX_O76080; -.
DR OpenTargets; ENSG00000107372; -.
DR PharmGKB; PA37587; -.
DR VEuPathDB; HostDB:ENSG00000107372; -.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000156165; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; O76080; -.
DR OMA; AHGCSFD; -.
DR OrthoDB; 1551371at2759; -.
DR PhylomeDB; O76080; -.
DR TreeFam; TF313612; -.
DR PathwayCommons; O76080; -.
DR SignaLink; O76080; -.
DR BioGRID-ORCS; 7763; 43 hits in 1047 CRISPR screens.
DR ChiTaRS; ZFAND5; human.
DR GenomeRNAi; 7763; -.
DR Pharos; O76080; Tbio.
DR PRO; PR:O76080; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O76080; protein.
DR Bgee; ENSG00000107372; Expressed in mucosa of paranasal sinus and 206 other tissues.
DR ExpressionAtlas; O76080; baseline and differential.
DR Genevisible; O76080; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
DR GO; GO:0001944; P:vasculature development; IEA:Ensembl.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR002653; Znf_A20.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01754; zf-A20; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR PROSITE; PS51036; ZF_A20; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..213
FT /note="AN1-type zinc finger protein 5"
FT /id="PRO_0000066557"
FT ZN_FING 8..42
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 148..194
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 39..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88878"
FT MOD_RES 209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88878"
SQ SEQUENCE 213 AA; 23132 MW; E477504B1BA77753 CRC64;
MAQETNQTPG PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QQNSGRMSPM GTASGSNSPT
SDSASVQRAD TSLNNCEGAA GSTSEKSRNV PVAALPVTQQ MTEMSISRED KITTPKTEVS
EPVVTQPSPS VSQPSTSQSE EKAPELPKPK KNRCFMCRKK VGLTGFDCRC GNLFCGLHRY
SDKHNCPYDY KAEAAAKIRK ENPVVVAEKI QRI
