AKIB1_HUMAN
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 03-AUG-2022, entry version 175.
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; 12.
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; Q9P2G1; -.
DR PeptideAtlas; Q9P2G1; -.
DR PRIDE; Q9P2G1; -.
DR ProteomicsDB; 83810; -.
DR Antibodypedia; 8661; 30 antibodies from 9 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 CTD; 54467; -.
DR DisGeNET; 54467; -.
DR GeneCards; ANKIB1; -.
DR HGNC; HGNC:22215; ANKIB1.
DR HPA; ENSG00000001629; Tissue enhanced (brain).
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; CAKKCKY; -.
DR OrthoDB; 469819at2759; -.
DR PhylomeDB; Q9P2G1; -.
DR TreeFam; TF331104; -.
DR PathwayCommons; Q9P2G1; -.
DR SignaLink; Q9P2G1; -.
DR BioGRID-ORCS; 54467; 19 hits in 1120 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 187 other tissues.
DR ExpressionAtlas; Q9P2G1; baseline and differential.
DR Genevisible; Q9P2G1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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 Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR044066; TRIAD_supradom.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF00023; Ank; 2.
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; SSF48403; 1.
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.
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
