KDM5A_MOUSE
ID KDM5A_MOUSE Reviewed; 1690 AA.
AC Q3UXZ9; Q3TM94; Q3UMI5; Q66JZ3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lysine-specific demethylase 5A;
DE EC=1.14.11.67 {ECO:0000305|PubMed:17320161, ECO:0000305|PubMed:17320163};
DE AltName: Full=Histone demethylase JARID1A;
DE AltName: Full=Jumonji/ARID domain-containing protein 1A;
DE AltName: Full=Retinoblastoma-binding protein 2;
DE Short=RBBP-2;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5A {ECO:0000305};
GN Name=Kdm5a; Synonyms=Jarid1a, Rbp2;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1552.
RC STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb;
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 MRNA] OF 1-1099.
RC STRAIN=C57BL/6J; TISSUE=Germ cell;
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 PROTEIN SEQUENCE OF 1538-1546, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17320163; DOI=10.1016/j.cell.2007.02.013;
RA Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H., Tempst P.,
RA Gilliland D.G., Zhang Y., Kaelin W.G. Jr.;
RT "The retinoblastoma binding protein RBP2 is an H3K4 demethylase.";
RL Cell 128:889-900(2007).
RN [6]
RP FUNCTION.
RX PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
RA Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L.,
RA Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
RT "RBP2 belongs to a family of demethylases, specific for tri-and
RT dimethylated lysine 4 on histone 3.";
RL Cell 128:1063-1076(2007).
RN [7]
RP SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, AND INTERACTION WITH SUZ12.
RX PubMed=20064375; DOI=10.1016/j.cell.2009.12.002;
RA Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., Wysocka J.;
RT "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target
RT gene occupancy in pluripotent cells.";
RL Cell 139:1290-1302(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111; THR-1343; SER-1345;
RP TYR-1595; SER-1598; SER-1603 AND SER-1666, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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 [10]
RP FUNCTION, AND INTERACTION WITH ARNTL; CLOCK AND HDAC1.
RX PubMed=21960634; DOI=10.1126/science.1206022;
RA DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
RA Panda S.;
RT "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences
RT the circadian clock.";
RL Science 333:1881-1885(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC histone H3, thereby playing a central role in histone code. Does not
CC demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not
CC monomethylated H3 'Lys-4' (PubMed:17320161, PubMed:17320163). Regulates
CC specific gene transcription through DNA-binding on 5'-CCGCCC-3' motif.
CC May stimulate transcription mediated by nuclear receptors. Involved in
CC transcriptional regulation of Hox proteins during cell differentiation
CC (By similarity). May participate in transcriptional repression of
CC cytokines such as CXCL12. Plays a role in the regulation of the
CC circadian rhythm and in maintaining the normal periodicity of the
CC circadian clock. In a histone demethylase-independent manner, acts as a
CC coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional
CC activation of PER1/2 and other clock-controlled genes and increases
CC histone acetylation at PER1/2 promoters by inhibiting the activity of
CC HDAC1 (PubMed:21960634). Seems to act as a transcriptional corepressor
CC for some genes such as MT1F and to favor the proliferation of cancer
CC cells (By similarity). {ECO:0000250|UniProtKB:P29375,
CC ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17320163,
CC ECO:0000269|PubMed:21960634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000305|PubMed:17320161, ECO:0000305|PubMed:17320163};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By similarity).
CC Interacts with SUZ12; the interaction is direct (PubMed:20064375).
CC Interacts with ARNTL/BMAL1 and CLOCK (PubMed:21960634). Interacts with
CC HDAC1; this interaction impairs histone deacetylation by HDAC1
CC (PubMed:21960634). Interacts (via PHD-type 1 zinc finger) with histone
CC H3 unmodified at 'Lys-4' and (via PHD-type 3 zinc finger) with histone
CC H3 di- and trimethylated at 'Lys-4' (By similarity).
CC {ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:20064375,
CC ECO:0000269|PubMed:21960634}.
CC -!- INTERACTION:
CC Q3UXZ9; Q80U70: Suz12; NbExp=2; IntAct=EBI-2531441, EBI-2526494;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P29375}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:20064375}. Note=Occupies promoters of genes involved
CC in RNA metabolism and mitochondrial function.
CC {ECO:0000269|PubMed:20064375}.
CC -!- DOMAIN: The GSGFP motif is required for the interaction with SUZ12
CC (PubMed:20064375). The ARID domain specifically binds to the CCGCCC
CC motif and is required for the lysine-specific histone demethylase
CC activity. The PHD-type 3 zinc finger is required for the interaction
CC with histone H3 di- and trimethylated at 'Lys-4' (By similarity).
CC {ECO:0000250|UniProtKB:P29375, ECO:0000269|PubMed:20064375}.
CC -!- DISRUPTION PHENOTYPE: Mice are grossly normal, except that they exhibit
CC behavioral abnormalities when held upside down by the tail, and slight
CC hematological defects. {ECO:0000269|PubMed:17320163}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC155720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK135085; BAE22414.1; ALT_INIT; mRNA.
DR EMBL; AK144877; BAE26113.1; -; mRNA.
DR EMBL; AK166055; BAE38548.1; -; mRNA.
DR EMBL; BC080691; AAH80691.1; ALT_TERM; mRNA.
DR CCDS; CCDS51889.1; -.
DR RefSeq; NP_666109.2; NM_145997.2.
DR AlphaFoldDB; Q3UXZ9; -.
DR SMR; Q3UXZ9; -.
DR BioGRID; 229572; 13.
DR IntAct; Q3UXZ9; 7.
DR STRING; 10090.ENSMUSP00000098558; -.
DR BindingDB; Q3UXZ9; -.
DR ChEMBL; CHEMBL3707461; -.
DR iPTMnet; Q3UXZ9; -.
DR PhosphoSitePlus; Q3UXZ9; -.
DR EPD; Q3UXZ9; -.
DR jPOST; Q3UXZ9; -.
DR MaxQB; Q3UXZ9; -.
DR PaxDb; Q3UXZ9; -.
DR PeptideAtlas; Q3UXZ9; -.
DR PRIDE; Q3UXZ9; -.
DR ProteomicsDB; 263524; -.
DR Antibodypedia; 1751; 232 antibodies from 28 providers.
DR DNASU; 214899; -.
DR Ensembl; ENSMUST00000005108; ENSMUSP00000005108; ENSMUSG00000030180.
DR GeneID; 214899; -.
DR KEGG; mmu:214899; -.
DR UCSC; uc009dne.2; mouse.
DR CTD; 5927; -.
DR MGI; MGI:2136980; Kdm5a.
DR VEuPathDB; HostDB:ENSMUSG00000030180; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000157170; -.
DR InParanoid; Q3UXZ9; -.
DR OMA; KWAPVAP; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q3UXZ9; -.
DR TreeFam; TF106476; -.
DR BRENDA; 1.14.11.67; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 214899; 8 hits in 82 CRISPR screens.
DR ChiTaRS; Kdm5a; mouse.
DR PRO; PR:Q3UXZ9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UXZ9; protein.
DR Bgee; ENSMUSG00000030180; Expressed in rostral migratory stream and 233 other tissues.
DR ExpressionAtlas; Q3UXZ9; baseline and differential.
DR Genevisible; Q3UXZ9; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IMP:MGI.
DR GO; GO:1901726; P:negative regulation of histone deacetylase activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISO:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW Activator; Biological rhythms; Chromatin regulator; Developmental protein;
KW Dioxygenase; Direct protein sequencing; Iron; Isopeptide bond;
KW Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1690
FT /note="Lysine-specific demethylase 5A"
FT /id="PRO_0000292411"
FT DOMAIN 19..60
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 84..174
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 437..603
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 293..343
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 676..728
FT /note="C5HC2"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT ZN_FING 1153..1210
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1599..1653
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 203..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1690
FT /note="Interaction with LMO2"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT REGION 1662..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 419..423
FT /note="GSGFP motif"
FT /evidence="ECO:0000269|PubMed:20064375"
FT BINDING 409
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 483
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 485
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 491
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 493
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 501
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 571
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT MOD_RES 1343
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT MOD_RES 1595
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT CROSSLNK 1007
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT CONFLICT 10
FT /note="A -> S (in Ref. 2; BAE38548)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="V -> R (in Ref. 2; BAE38548)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="P -> A (in Ref. 2; BAE38548)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="P -> A (in Ref. 2; BAE38548)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="V -> A (in Ref. 2; BAE38548)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="A -> P (in Ref. 2; BAE22414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1690 AA; 192216 MW; EFCF56AAAA51F0FC CRC64;
MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK IRPPKDWQPP
FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL
SKIVASKGGF EIVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG
VQMPDLDLKE KVEAEVLSTD IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ
IFGAGPKVVG LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE AFGFEQAVRE
YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS
GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF
CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM
NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVVM
SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCSCP MQNKCLRYRY
PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL SASFNHKKDL IELRVMLEDA EDRKYPENDL
FRKLRDAVKE AETCGSVAQL LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI
SQTRQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK
VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGNNYAYL
EQLESLSAKG RPIPVRLDAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI
GVYGSGKNRR KKVKEIIEKE KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA
MHSLRAANLA KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDKA
RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA
FNRVVSSVSS SPHQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP
IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG
AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD
SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK LAKKLAKEEE
RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK
DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN EDYICINCAK KQGPDSPGQA PPPPFLMSYK
LPMEDLKETS
