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 13-SEP-2023, entry version 163. 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}. 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; 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 PDB; 7QXW; EM; 4.10 A; v=1-213. DR PDBsum; 7QXW; -. DR AlphaFoldDB; O76080; -. DR BMRB; O76080; -. DR SMR; O76080; -. DR BioGRID; 113546; 27. 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 ProteomicsDB; 50381; -. DR TopDownProteomics; O76080; -. DR Antibodypedia; 12564; 267 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 AGR; HGNC:13008; -. 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; CGEHRYD; -. DR OrthoDB; 5395454at2759; -. DR PhylomeDB; O76080; -. DR TreeFam; TF313612; -. DR PathwayCommons; O76080; -. DR SignaLink; O76080; -. DR BioGRID-ORCS; 7763; 45 hits in 1125 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; 1.20.5.4770; -; 1. DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1. DR InterPro; IPR035896; AN1-like_Znf. DR InterPro; IPR002653; Znf_A20. DR InterPro; IPR000058; Znf_AN1. DR PANTHER; PTHR10634; AN1-TYPE ZINC FINGER PROTEIN; 1. DR PANTHER; PTHR10634:SF26; AN1-TYPE ZINC FINGER PROTEIN 5; 1. 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; AN1-like Zinc finger; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR PROSITE; PS51036; ZF_A20; 1. DR PROSITE; PS51039; ZF_AN1; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Phosphoprotein; KW Reference proteome; 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 //