MARH7_HUMAN
ID MARH7_HUMAN Reviewed; 704 AA.
AC Q9H992; A8K9X1; B7Z7P5; D3DPB0; Q53GQ1; Q9BTR9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase MARCHF7;
DE EC=2.3.2.27;
DE AltName: Full=Axotrophin;
DE AltName: Full=Membrane-associated RING finger protein 7;
DE AltName: Full=Membrane-associated RING-CH protein VII;
DE Short=MARCH-VII;
DE AltName: Full=RING finger protein 177;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF7 {ECO:0000305};
GN Name=MARCHF7 {ECO:0000312|HGNC:HGNC:17393}; Synonyms=AXOT, MARCH7, RNF177;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-379.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, 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 IDENTIFICATION.
RX PubMed=15670816; DOI=10.1016/j.febslet.2004.12.027;
RA Metcalfe S.M., Muthukumarana P.A.D.S., Thompson H.L., Haendel M.A.,
RA Lyons G.E.;
RT "Leukaemia inhibitory factor (LIF) is functionally linked to axotrophin and
RT both LIF and axotrophin are linked to regulatory immune tolerance.";
RL FEBS Lett. 579:609-614(2005).
RN [7]
RP FUNCTION.
RX PubMed=16868077; DOI=10.1073/pnas.0605215103;
RA Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V.;
RT "E2-25K mediates US11-triggered retro-translocation of MHC class I heavy
RT chains in a permeabilized cell system.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11589-11594(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-686; SER-687 AND SER-691, AND
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-389, AND
RP IDENTIFICATION BY 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 [11]
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).
RN [12]
RP FUNCTION.
RX PubMed=31270356; DOI=10.1038/s41598-019-45939-w;
RA Lenk G.M., Park Y.N., Lemons R., Flynn E., Plank M., Frei C.M., Davis M.J.,
RA Gregorka B., Swanson J.A., Meisler M.H., Kitzman J.O.;
RT "CRISPR knockout screen implicates three genes in lysosome function.";
RL Sci. Rep. 9:9609-9609(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance
CC the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfer the ubiquitin to targeted substrates
CC (PubMed:16868077). May be involved in T-cell proliferation by
CC regulating LIF secretion (By similarity). May play a role in lysosome
CC homeostasis (PubMed:31270356). {ECO:0000250|UniProtKB:Q9WV66,
CC ECO:0000269|PubMed:16868077, ECO:0000269|PubMed:31270356}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q9H992; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-949983, EBI-11962928;
CC Q9H992; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-949983, EBI-742102;
CC Q9H992; O75031: HSF2BP; NbExp=3; IntAct=EBI-949983, EBI-7116203;
CC Q9H992; Q15691: MAPRE1; NbExp=3; IntAct=EBI-949983, EBI-1004115;
CC Q9H992; Q9UPY8: MAPRE3; NbExp=5; IntAct=EBI-949983, EBI-726739;
CC Q9H992; P61086: UBE2K; NbExp=3; IntAct=EBI-949983, EBI-473850;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H992-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H992-2; Sequence=VSP_054406;
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity.
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DR EMBL; AK022973; BAB14340.1; -; mRNA.
DR EMBL; AK292836; BAF85525.1; -; mRNA.
DR EMBL; AK302347; BAH13681.1; -; mRNA.
DR EMBL; AK222880; BAD96600.1; -; mRNA.
DR EMBL; AC009961; AAY14941.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11402.1; -; Genomic_DNA.
DR EMBL; BC003404; AAH03404.1; -; mRNA.
DR EMBL; BC065014; AAH65014.1; -; mRNA.
DR CCDS; CCDS2210.1; -. [Q9H992-1]
DR CCDS; CCDS63039.1; -. [Q9H992-2]
DR RefSeq; NP_001269734.1; NM_001282805.1. [Q9H992-1]
DR RefSeq; NP_001269735.1; NM_001282806.1.
DR RefSeq; NP_001269736.1; NM_001282807.1. [Q9H992-2]
DR RefSeq; NP_073737.1; NM_022826.3. [Q9H992-1]
DR RefSeq; XP_005246830.1; XM_005246773.2.
DR AlphaFoldDB; Q9H992; -.
DR SMR; Q9H992; -.
DR BioGRID; 122319; 77.
DR IntAct; Q9H992; 20.
DR STRING; 9606.ENSP00000259050; -.
DR iPTMnet; Q9H992; -.
DR PhosphoSitePlus; Q9H992; -.
DR BioMuta; MARCH7; -.
DR DMDM; 74762745; -.
DR EPD; Q9H992; -.
DR jPOST; Q9H992; -.
DR MassIVE; Q9H992; -.
DR MaxQB; Q9H992; -.
DR PaxDb; Q9H992; -.
DR PeptideAtlas; Q9H992; -.
DR PRIDE; Q9H992; -.
DR ProteomicsDB; 6891; -.
DR ProteomicsDB; 81297; -. [Q9H992-1]
DR Antibodypedia; 33721; 257 antibodies from 29 providers.
DR DNASU; 64844; -.
DR Ensembl; ENST00000259050.8; ENSP00000259050.3; ENSG00000136536.15. [Q9H992-1]
DR Ensembl; ENST00000409175.6; ENSP00000386830.1; ENSG00000136536.15. [Q9H992-1]
DR Ensembl; ENST00000409591.5; ENSP00000387238.1; ENSG00000136536.15. [Q9H992-2]
DR GeneID; 64844; -.
DR KEGG; hsa:64844; -.
DR MANE-Select; ENST00000409175.6; ENSP00000386830.1; NM_001282805.2; NP_001269734.1.
DR UCSC; uc002uax.5; human. [Q9H992-1]
DR CTD; 64844; -.
DR DisGeNET; 64844; -.
DR GeneCards; MARCHF7; -.
DR HGNC; HGNC:17393; MARCHF7.
DR HPA; ENSG00000136536; Low tissue specificity.
DR MIM; 613334; gene.
DR neXtProt; NX_Q9H992; -.
DR OpenTargets; ENSG00000136536; -.
DR VEuPathDB; HostDB:ENSG00000136536; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00530000063836; -.
DR HOGENOM; CLU_019830_0_0_1; -.
DR InParanoid; Q9H992; -.
DR OMA; HIFRREA; -.
DR PhylomeDB; Q9H992; -.
DR TreeFam; TF330816; -.
DR PathwayCommons; Q9H992; -.
DR SignaLink; Q9H992; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 64844; 8 hits in 1056 CRISPR screens.
DR ChiTaRS; MARCH7; human.
DR GeneWiki; MARCH7; -.
DR GenomeRNAi; 64844; -.
DR Pharos; Q9H992; Tbio.
DR PRO; PR:Q9H992; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H992; protein.
DR Bgee; ENSG00000136536; Expressed in calcaneal tendon and 208 other tissues.
DR ExpressionAtlas; Q9H992; baseline and differential.
DR Genevisible; Q9H992; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:1905524; P:negative regulation of protein autoubiquitination; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:CACAO.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0002643; P:regulation of tolerance induction; IEA:Ensembl.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..704
FT /note="E3 ubiquitin-protein ligase MARCHF7"
FT /id="PRO_0000274415"
FT ZN_FING 544..614
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 686
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..51
FT /note="MESKPSRIPRRISVQPSSSLSARMMSGSRGSSLNDTYHSRDSSFRLDSEYQ
FT -> MIGNYDHLMSLVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054406"
FT VARIANT 100
FT /note="T -> S (in dbSNP:rs17813964)"
FT /id="VAR_030284"
FT VARIANT 193
FT /note="T -> I (in dbSNP:rs16844275)"
FT /id="VAR_030285"
FT VARIANT 379
FT /note="G -> S (in dbSNP:rs13024801)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_030286"
FT CONFLICT 376
FT /note="E -> G (in Ref. 2; BAD96600)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="I -> V (in Ref. 2; BAD96600)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 78051 MW; 1271F74D7F389130 CRC64;
MESKPSRIPR RISVQPSSSL SARMMSGSRG SSLNDTYHSR DSSFRLDSEY QSTSASASAS
PFQSAWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT TSAGRNVGNG LNTLSDSSWR
HSQVPRSSSM VLGSFGTDLM RERRDLERRT DSSISNLMDY SHRSGDFTTS SYVQDRVPSY
SQGARPKENS MSTLQLNTSS TNHQLPSEHQ TILSSRDSRN SLRSNFSSRE SESSRSNTQP
GFSYSSSRDE APIISNSERV VSSQRPFQES SDNEGRRTTR RLLSRIASSM SSTFFSRRSS
QDSLNTRSLN SENSYVSPRI LTASQSRSNV PSASEVPDNR ASEASQGFRF LRRRWGLSSL
SHNHSSESDS ENFNQESEGR NTGPWLSSSL RNRCTPLFSR RRREGRDESS RIPTSDTSSR
SHIFRRESNE VVHLEAQNDP LGAAANRPQA SAASSSATTG GSTSDSAQGG RNTGISGILP
GSLFRFAVPP ALGSNLTDNV MITVDIIPSG WNSADGKSDK TKSAPSRDPE RLQKIKESLL
LEDSEEEEGD LCRICQMAAA SSSNLLIEPC KCTGSLQYVH QDCMKKWLQA KINSGSSLEA
VTTCELCKEK LELNLEDFDI HELHRAHANE QAEYEFISSG LYLVVLLHLC EQSFSDMMGN
TNEPSTRVRF INLARTLQAH MEDLETSEDD SEEDGDHNRT FDIA
