ID   AKIB1_HUMAN             Reviewed;        1089 AA.
AC   Q9P2G1; Q6GMS4; Q6P3S9; Q9NTD7; Q9NW49;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Ankyrin repeat and IBR domain-containing protein 1;
DE            EC=2.3.2.31 {ECO:0000250|UniProtKB:O60260};
GN   Name=ANKIB1; Synonyms=KIAA1386;
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 MET-1016.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin, and Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-1089, AND VARIANT MET-1016.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-1089, AND VARIANT MET-1016.
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
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   [10]
RP   MYRISTOYLATION AT GLY-2.
RX   PubMed=20213681; DOI=10.1002/pmic.200900783;
RA   Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA   Tsunasawa S., Utsumi T.;
RT   "Strategy for comprehensive identification of human N-myristoylated
RT   proteins using an insect cell-free protein synthesis system.";
RL   Proteomics 10:1780-1793(2010).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, 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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737 AND SER-884, AND
RP   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: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC       complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC       enzymes and then transfers it to substrates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC   -!- INTERACTION:
CC       Q9P2G1; P22736: NR4A1; NbExp=2; IntAct=EBI-2687890, EBI-721550;
CC   -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC       interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC       type E3 enzymes: they bind E2s via the first RING domain, but require
CC       an obligate trans-thiolation step during the ubiquitin transfer,
CC       requiring a conserved cysteine residue in the second RING domain.
CC       {ECO:0000250|UniProtKB:O60260}.
CC   -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
CC   -!- CAUTION: Lacks one Cys residue in the IBR-type zinc finger domain that
CC       is one of the conserved features of the family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH63861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA91537.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA92624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB037807; BAA92624.1; ALT_INIT; mRNA.
DR   EMBL; AC000118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC000120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC063861; AAH63861.1; ALT_INIT; mRNA.
DR   EMBL; BC073893; AAH73893.1; -; mRNA.
DR   EMBL; AK001179; BAA91537.1; ALT_INIT; mRNA.
DR   EMBL; AL137349; CAB70704.1; -; mRNA.
DR   CCDS; CCDS47639.1; -.
DR   PIR; T46423; T46423.
DR   RefSeq; NP_061877.1; NM_019004.1.
DR   AlphaFoldDB; Q9P2G1; -.
DR   SMR; Q9P2G1; -.
DR   BioGRID; 119973; 13.
DR   ELM; Q9P2G1; -.
DR   IntAct; Q9P2G1; 4.
DR   MINT; Q9P2G1; -.
DR   STRING; 9606.ENSP00000265742; -.
DR   iPTMnet; Q9P2G1; -.
DR   PhosphoSitePlus; Q9P2G1; -.
DR   BioMuta; ANKIB1; -.
DR   DMDM; 158937428; -.
DR   EPD; Q9P2G1; -.
DR   jPOST; Q9P2G1; -.
DR   MassIVE; Q9P2G1; -.
DR   MaxQB; Q9P2G1; -.
DR   PaxDb; 9606-ENSP00000265742; -.
DR   PeptideAtlas; Q9P2G1; -.
DR   ProteomicsDB; 83810; -.
DR   Pumba; Q9P2G1; -.
DR   Antibodypedia; 8661; 35 antibodies from 10 providers.
DR   DNASU; 54467; -.
DR   Ensembl; ENST00000265742.8; ENSP00000265742.3; ENSG00000001629.10.
DR   GeneID; 54467; -.
DR   KEGG; hsa:54467; -.
DR   MANE-Select; ENST00000265742.8; ENSP00000265742.3; NM_019004.2; NP_061877.1.
DR   UCSC; uc003ulw.2; human.
DR   AGR; HGNC:22215; -.
DR   CTD; 54467; -.
DR   DisGeNET; 54467; -.
DR   GeneCards; ANKIB1; -.
DR   HGNC; HGNC:22215; ANKIB1.
DR   HPA; ENSG00000001629; Low tissue specificity.
DR   MIM; 620069; gene.
DR   neXtProt; NX_Q9P2G1; -.
DR   OpenTargets; ENSG00000001629; -.
DR   PharmGKB; PA134941469; -.
DR   VEuPathDB; HostDB:ENSG00000001629; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   GeneTree; ENSGT00940000157621; -.
DR   HOGENOM; CLU_009823_1_0_1; -.
DR   InParanoid; Q9P2G1; -.
DR   OMA; CNPENCC; -.
DR   OrthoDB; 3084186at2759; -.
DR   PhylomeDB; Q9P2G1; -.
DR   TreeFam; TF331104; -.
DR   PathwayCommons; Q9P2G1; -.
DR   SignaLink; Q9P2G1; -.
DR   SIGNOR; Q9P2G1; -.
DR   BioGRID-ORCS; 54467; 20 hits in 1198 CRISPR screens.
DR   ChiTaRS; ANKIB1; human.
DR   GenomeRNAi; 54467; -.
DR   Pharos; Q9P2G1; Tdark.
DR   PRO; PR:Q9P2G1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9P2G1; Protein.
DR   Bgee; ENSG00000001629; Expressed in corpus callosum and 189 other cell types or tissues.
DR   ExpressionAtlas; Q9P2G1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd20361; Rcat_RBR_ANKIB1; 1.
DR   CDD; cd16774; RING-HC_RBR_ANKIB1; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047564; Rcat_RBR_ANKIB1.
DR   InterPro; IPR047563; RING-HC_RBR_ANKIB1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF465; ANKYRIN REPEAT AND IBR DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q9P2G1; HS.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Lipoprotein; Metal-binding; Myristate;
KW   Phosphoprotein; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..1089
FT                   /note="Ankyrin repeat and IBR domain-containing protein 1"
FT                   /id="PRO_0000066892"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          144..173
FT                   /note="ANK 2"
FT   DOMAIN          851..870
FT                   /note="UIM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         333..383
FT                   /note="RING-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         401..478
FT                   /note="IBR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   ZN_FING         519..548
FT                   /note="RING-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          281..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..569
FT                   /note="TRIAD supradomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   REGION          776..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          575..640
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        300..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        532
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         383
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         465
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         468
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         473
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         519
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         522
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         537
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         540
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         545
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         548
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         555
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   BINDING         565
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT   MOD_RES         737
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         884
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         911
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZPS6"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:20213681"
FT   VARIANT         1016
FT                   /note="L -> M (in dbSNP:rs38794)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005"
FT                   /id="VAR_030862"
FT   CONFLICT        929
FT                   /note="N -> S (in Ref. 4; BAA91537)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1089 AA;  122002 MW;  038570CD3887FF44 CRC64;
     MGNTTTKFRK ALINGDENLA CQIYENNPQL KESLDPNTSY GEPYQHNTPL HYAARHGMNK
     ILGTFLGRDG NPNKRNVHNE TSMHLLCMGP QIMISEGALH PRLARPTEDD FRRADCLQMI
     LKWKGAKLDQ GEYERAAIDA VDNKKNTPLH YAAASGMKAC VELLVKHGGD LFAENENKDT
     PCDCAEKQHH KDLALNLESQ MVFSRDPEAE EIEAEYAALD KREPYEGLRP QDLRRLKDML
     IVETADMLQA PLFTAEALLR AHDWDREKLL EAWMSNPENC CQRSGVQMPT PPPSGYNAWD
     TLPSPRTPRT TRSSVTSPDE ISLSPGDLDT SLCDICMCSI SVFEDPVDMP CGHDFCRGCW
     ESFLNLKIQE GEAHNIFCPA YDCFQLVPVD IIESVVSKEM DKRYLQFDIK AFVENNPAIK
     WCPTPGCDRA VRLTKQGSNT SGSDTLSFPL LRAPAVDCGK GHLFCWECLG EAHEPCDCQT
     WKNWLQKITE MKPEELVGVS EAYEDAANCL WLLTNSKPCA NCKSPIQKNE GCNHMQCAKC
     KYDFCWICLE EWKKHSSSTG GYYRCTRYEV IQHVEEQSKE MTVEAEKKHK RFQELDRFMH
     YYTRFKNHEH SYQLEQRLLK TAKEKMEQLS RALKETEGGC PDTTFIEDAV HVLLKTRRIL
     KCSYPYGFFL EPKSTKKEIF ELMQTDLEMV TEDLAQKVNR PYLRTPRHKI IKAACLVQQK
     RQEFLASVAR GVAPADSPEA PRRSFAGGTW DWEYLGFASP EEYAEFQYRR RHRQRRRGDV
     HSLLSNPPDP DEPSESTLDI PEGGSSSRRP GTSVVSSASM SVLHSSSLRD YTPASRSENQ
     DSLQALSSLD EDDPNILLAI QLSLQESGLA LDEETRDFLS NEASLGAIGT SLPSRLDSVP
     RNTDSPRAAL SSSELLELGD SLMRLGAEND PFSTDTLSSH PLSEARSDFC PSSSDPDSAG
     QDPNINDNLL GNIMAWFHDM NPQSIALIPP ATTEISADSQ LPCIKDGSEG VKDVELVLPE
     DSMFEDASVS EGRGTQIEEN PLEENILAGE AASQAGDSGN EAANRGDGSD VSSQTPQTSS
     DWLEQVHLV
//