SUV92_MOUSE
ID SUV92_MOUSE Reviewed; 477 AA.
AC Q9EQQ0; Q8BNK2; Q9CUK3; Q9JLP7;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H2;
DE EC=2.1.1.355;
DE AltName: Full=Histone H3-K9 methyltransferase 2;
DE Short=H3-K9-HMTase 2;
DE AltName: Full=Suppressor of variegation 3-9 homolog 2;
DE Short=Su(var)3-9 homolog 2;
GN Name=Suv39h2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
RC STRAIN=C57BL/6J;
RX PubMed=11094092; DOI=10.1128/mcb.20.24.9423-9433.2000;
RA O'Carroll D., Scherthan H., Peters A.H.F.M., Opravil S., Haynes A.R.,
RA Laible G., Rea S., Schmid M., Lebersorger A., Jerratsch M., Sattler L.,
RA Mattei M.-G., Denny P., Brown S.D.M., Schweizer D., Jenuwein T.;
RT "Isolation and characterization of Suv39h2, a second histone H3
RT methyltransferase gene that displays testis-specific expression.";
RL Mol. Cell. Biol. 20:9423-9433(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11701123; DOI=10.1016/s0092-8674(01)00542-6;
RA Peters A.H.F.M., O'Carroll D., Scherthan H., Mechtler K., Sauer S.,
RA Schofer C., Weipoltshammer K., Pagani M., Lachner M., Kohlmaier A.,
RA Opravil S., Doyle M., Sibilia M., Jenuwein T.;
RT "Loss of the Suv39h histone methyltransferases impairs mammalian
RT heterochromatin and genome stability.";
RL Cell 107:323-337(2001).
RN [5]
RP FUNCTION.
RX PubMed=14690609; DOI=10.1016/s1097-2765(03)00477-5;
RA Peters A.H.F.M., Kubicek S., Mechtler K., O'Sullivan R.J., Derijck A.A.,
RA Perez-Burgos L., Kohlmaier A., Opravil S., Tachibana M., Shinkai Y.,
RA Martens J.H.A., Jenuwein T.;
RT "Partitioning and plasticity of repressive histone methylation states in
RT mammalian chromatin.";
RL Mol. Cell 12:1577-1589(2003).
RN [6]
RP FUNCTION.
RX PubMed=14690610; DOI=10.1016/s1097-2765(03)00479-9;
RA Rice J.C., Briggs S.D., Ueberheide B., Barber C.M., Shabanowitz J.,
RA Hunt D.F., Shinkai Y., Allis C.D.;
RT "Histone methyltransferases direct different degrees of methylation to
RT define distinct chromatin domains.";
RL Mol. Cell 12:1591-1598(2003).
RN [7]
RP FUNCTION.
RX PubMed=14702045; DOI=10.1038/ng1278;
RA Garcia-Cao M., O'Sullivan R., Peters A.H.F.M., Jenuwein T., Blasco M.A.;
RT "Epigenetic regulation of telomere length in mammalian cells by the Suv39h1
RT and Suv39h2 histone methyltransferases.";
RL Nat. Genet. 36:94-99(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION IN CIRCADIAN RHYTHMS, AND IDENTIFICATION IN A LARGE PER COMPLEX.
RX PubMed=24413057; DOI=10.1038/nsmb.2746;
RA Duong H.A., Weitz C.J.;
RT "Temporal orchestration of repressive chromatin modifiers by circadian
RT clock Period complexes.";
RL Nat. Struct. Mol. Biol. 21:126-132(2014).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC 'Lys-9' trimethylation represents a specific tag for epigenetic
CC transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5)
CC proteins to methylated histones. Mainly functions in heterochromatin
CC regions, thereby playing a central role in the establishment of
CC constitutive heterochromatin at pericentric and telomere regions. H3
CC 'Lys-9' trimethylation is also required to direct DNA methylation at
CC pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC interaction with RB1 and is involved in many processes, such as cell
CC cycle regulation, transcriptional repression and regulation of telomere
CC length. May participate in regulation of higher-order chromatin
CC organization during spermatogenesis. Recruited by the large PER complex
CC to the E-box elements of the circadian target genes such as PER2 itself
CC or PER1, contributes to the conversion of local chromatin to a
CC heterochromatin-like repressive state through H3 'Lys-9'
CC trimethylation. {ECO:0000269|PubMed:11701123,
CC ECO:0000269|PubMed:14690609, ECO:0000269|PubMed:14690610,
CC ECO:0000269|PubMed:14702045, ECO:0000269|PubMed:24413057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC -!- SUBUNIT: Interacts with SMAD5. The large PER complex involved in the
CC histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1
CC and/or SUV39H2; CBX3 mediates the formation of the complex.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC Note=Associates with centromeric constitutive heterochromatin during
CC most stages of spermato- and spermiogenesis. Predominantly accumulates
CC at the sex chromosomes present at the XY body.
CC -!- TISSUE SPECIFICITY: Testis specific; predominant expression in type B
CC spermatogonia and preleptotene spermatocytes.
CC -!- DEVELOPMENTAL STAGE: Strong expression in early embryos with a peak at
CC 10.5 dpc. Expression is down-regulated at 17.5 dpc, and is nearly
CC absent during postnatal development. In adult testes, prominent
CC expression in late but not early spermatocytes.
CC -!- DOMAIN: Although the SET domain contains the active site of enzymatic
CC activity, both pre-SET and post-SET domains are required for
CC methyltransferase activity. The SET domain also participates in stable
CC binding to heterochromatin (By similarity). {ECO:0000250}.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Suv39h1 and Suv39h2 display severely
CC impaired viability and chromosomal instabilities that are associated
CC with an increased tumor risk and perturbed chromosome interactions
CC during male meiosis. They also show a higher level of histone H3 with
CC phosphorylated 'Ser-10' and a reduced number of cells in G1 phase and
CC an increased portion of cells with aberrant nuclear morphologies.
CC {ECO:0000269|PubMed:11701123}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00912}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF73152.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF149204; AAF73152.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF149205; AAG09134.1; -; mRNA.
DR EMBL; AK015728; BAB29948.1; -; mRNA.
DR EMBL; AK083457; BAC38921.1; -; mRNA.
DR EMBL; AL732620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15652.1; -.
DR RefSeq; NP_073561.2; NM_022724.4.
DR AlphaFoldDB; Q9EQQ0; -.
DR SMR; Q9EQQ0; -.
DR BioGRID; 211103; 2.
DR DIP; DIP-32586N; -.
DR IntAct; Q9EQQ0; 3.
DR STRING; 10090.ENSMUSP00000027956; -.
DR iPTMnet; Q9EQQ0; -.
DR PhosphoSitePlus; Q9EQQ0; -.
DR EPD; Q9EQQ0; -.
DR MaxQB; Q9EQQ0; -.
DR PaxDb; Q9EQQ0; -.
DR PeptideAtlas; Q9EQQ0; -.
DR PRIDE; Q9EQQ0; -.
DR ProteomicsDB; 258674; -.
DR DNASU; 64707; -.
DR GeneID; 64707; -.
DR KEGG; mmu:64707; -.
DR UCSC; uc008ied.2; mouse.
DR CTD; 79723; -.
DR MGI; MGI:1890396; Suv39h2.
DR eggNOG; KOG1082; Eukaryota.
DR InParanoid; Q9EQQ0; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q9EQQ0; -.
DR TreeFam; TF106452; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 64707; 5 hits in 75 CRISPR screens.
DR PRO; PR:Q9EQQ0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9EQQ0; protein.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); ISS:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; IGI:MGI.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:0034968; P:histone lysine methylation; IGI:MGI.
DR GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Cell cycle; Centromere; Chromatin regulator;
KW Chromosome; Differentiation; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc.
FT CHAIN 1..477
FT /note="Histone-lysine N-methyltransferase SUV39H2"
FT /id="PRO_0000186060"
FT DOMAIN 118..176
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 256..314
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 317..440
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 461..477
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..41
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 328..330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 397..398
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H5I1"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 3
FT /note="T -> A (in Ref. 2; BAC38921)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Missing (in Ref. 1; AAF73152)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="K -> R (in Ref. 2; BAB29948/BAC38921)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> N (in Ref. 1; AAF73152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 54098 MW; 4008D46CF0F07006 CRC64;
MATARAKARG SEAGARCHRA PGPPPRPKAR RTARRRRAET LTARRSRPSA GERRAGSQRA
WSGAPRAAVF GDECARGALF KAWCVPCLVS LDTLQELCRK EKLTCKSIGI TKRNLNNYEV
EYLCDYKVAK GVEYYLVKWK GWPDSTNTWE PLRNLRCPQL LRQFSDDKKT YLAQERKCKA
VNSKSLQPAI AEYIVQKAKQ RIALQRWQDY LNRRKNHKGM IFVENTVDLE GPPLDFYYIN
EYRPAPGISI NSEATFGCSC TDCFFDKCCP AEAGVVLAYN KKQQIKIQPG TPIYECNSRC
RCGPECPNRI VQKGTQYSLC IFKTSNGCGW GVKTLVKIKR MSFVMEYVGE VITSEEAERR
GQFYDNKGIT YLFDLDYESD EFTVDAARYG NVSHFVNHSC DPNLQVFSVF IDNLDTRLPR
IALFSTRTIN AGEELTFDYQ MKGSGEASSD SIDHSPAKKR VRTQCKCGAE TCRGYLN
