MCM2_MOUSE
ID MCM2_MOUSE Reviewed; 904 AA.
AC P97310; O08971; O89057; Q8C2R0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=DNA replication licensing factor MCM2;
DE AltName: Full=Minichromosome maintenance protein 2 homolog;
DE AltName: Full=Nuclear protein BM28;
GN Name=Mcm2; Synonyms=Bm28, Cdcl1, Kiaa0030, Mcmd2;
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 [MRNA], AND PROTEIN SEQUENCE OF 217-224; 376-384 AND
RP 477-487.
RX PubMed=9077461; DOI=10.1046/j.1365-2443.1996.840284.x;
RA Kimura H., Ohtomo T., Yamaguchi M., Ishii A., Sugimoto K.;
RT "Mouse MCM proteins: complex formation and transportation to the nucleus.";
RL Genes Cells 1:977-993(1996).
RN [2]
RP SEQUENCE REVISION.
RA Kimura H.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Melanoma;
RX PubMed=9371513;
RA Spanjaard R.A., Lee P.J., Sarkar S., Goedegebuure P.S., Eberlein T.J.;
RT "Clone 10d/BM28 (CDCL1), an early S-phase protein, is an important growth
RT regulator of melanoma.";
RL Cancer Res. 57:5122-5128(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 477-668.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE MCM2-7 COMPLEX.
RX PubMed=10567526; DOI=10.1128/mcb.19.12.8003;
RA You Z., Komamura Y., Ishimi Y.;
RT "Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase
RT activity.";
RL Mol. Cell. Biol. 19:8003-8015(1999).
RN [9]
RP INTERACTION WITH DBF4.
RC STRAIN=C57BL/6J; TISSUE=Egg, and Embryo;
RX PubMed=10517317; DOI=10.1007/s004380051078;
RA Lepke M., Puetter V., Staib C., Kneissl M., Berger C., Hoehn K., Nanda I.,
RA Schmid M., Grummt F.;
RT "Identification, characterization and chromosomal localization of the
RT cognate human and murine DBF4 genes.";
RL Mol. Gen. Genet. 262:220-229(1999).
RN [10]
RP INTERACTION WITH KAT7, AND MUTAGENESIS OF LEU-237.
RX PubMed=11278932; DOI=10.1074/jbc.m011556200;
RA Burke T.W., Cook J.G., Asano M., Nevins J.R.;
RT "Replication factors MCM2 and ORC1 interact with the histone
RT acetyltransferase HBO1.";
RL J. Biol. Chem. 276:15397-15408(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-27; SER-139 AND
RP SER-140, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12; SER-21; SER-27; SER-139 AND SER-140, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-27; SER-41; SER-108;
RP SER-139 AND SER-140, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells
CC (PubMed:10567526). The active ATPase sites in the MCM2-7 ring are
CC formed through the interaction surfaces of two neighboring subunits
CC such that a critical structure of a conserved arginine finger motif is
CC provided in trans relative to the ATP-binding site of the Walker A box
CC of the adjacent subunit. The six ATPase active sites, however, are
CC likely to contribute differentially to the complex helicase activity.
CC Required for the entry in S phase and for cell division. Plays a role
CC in terminally differentiated hair cells development of the cochlea and
CC induces cells apoptosis. {ECO:0000250|UniProtKB:P49736,
CC ECO:0000269|PubMed:10567526}.
CC -!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5 (By similarity). Interacts with DBF4 (PubMed:10517317).
CC Interacts with KAT7 (PubMed:11278932). May interact with MCM10 (By
CC similarity). Component of the replisome complex composed of at least
CC DONSON, MCM2, MCM7, PCNA and TICRR (By similarity). Component of the
CC CMG helicase complex, composed of the MCM2-7 complex, the GINS complex
CC and CDC45 (By similarity). Forms a co-chaperone complex with DNAJC9 and
CC histone H3.3-H4 heterodimers (By similarity). Within the complex,
CC interacts (via N-terminus) with DNAJC9 (via C-terminus); the
CC interaction is histone-dependent (By similarity).
CC {ECO:0000250|UniProtKB:P49736, ECO:0000250|UniProtKB:P55861,
CC ECO:0000269|PubMed:10517317, ECO:0000269|PubMed:11278932}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49736}.
CC Chromosome {ECO:0000250|UniProtKB:P55861}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P55861}.
CC -!- PTM: Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108
CC proliferation is increased by genotoxic agents. Ser-40 is mediated by
CC the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is
CC only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-
CC DBF4 complex during G1/S phase is required for the initiation of DNA
CC replication (By similarity). {ECO:0000250|UniProtKB:P49736}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000269|PubMed:10567526}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97849.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86725; BAA22148.1; -; mRNA.
DR EMBL; AF004105; AAC16250.1; -; mRNA.
DR EMBL; AK129039; BAC97849.1; ALT_INIT; mRNA.
DR EMBL; AK088156; BAC40178.1; -; mRNA.
DR EMBL; BC055318; AAH55318.1; -; mRNA.
DR EMBL; U89403; AAC36510.1; -; mRNA.
DR CCDS; CCDS39554.1; -.
DR PIR; T10067; T10067.
DR RefSeq; NP_032590.2; NM_008564.2.
DR AlphaFoldDB; P97310; -.
DR SMR; P97310; -.
DR BioGRID; 201346; 23.
DR ComplexPortal; CPX-2941; MCM complex.
DR CORUM; P97310; -.
DR DIP; DIP-33057N; -.
DR IntAct; P97310; 15.
DR STRING; 10090.ENSMUSP00000061923; -.
DR iPTMnet; P97310; -.
DR PhosphoSitePlus; P97310; -.
DR SwissPalm; P97310; -.
DR EPD; P97310; -.
DR jPOST; P97310; -.
DR MaxQB; P97310; -.
DR PaxDb; P97310; -.
DR PeptideAtlas; P97310; -.
DR PRIDE; P97310; -.
DR ProteomicsDB; 295708; -.
DR Antibodypedia; 4369; 1089 antibodies from 43 providers.
DR DNASU; 17216; -.
DR Ensembl; ENSMUST00000058011; ENSMUSP00000061923; ENSMUSG00000002870.
DR GeneID; 17216; -.
DR KEGG; mmu:17216; -.
DR UCSC; uc009cvx.2; mouse.
DR CTD; 4171; -.
DR MGI; MGI:105380; Mcm2.
DR VEuPathDB; HostDB:ENSMUSG00000002870; -.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_0_1_1; -.
DR InParanoid; P97310; -.
DR OMA; DCVKCGY; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P97310; -.
DR TreeFam; TF300772; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69052; Switching of origins to a post-replicative state.
DR BioGRID-ORCS; 17216; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Mcm2; mouse.
DR PRO; PR:P97310; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P97310; protein.
DR Bgee; ENSMUSG00000002870; Expressed in femorotibial joint and 218 other tissues.
DR ExpressionAtlas; P97310; baseline and differential.
DR Genevisible; P97310; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0090102; P:cochlea development; ISS:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; ISO:MGI.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IDA:MGI.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008045; MCM2.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR PANTHER; PTHR11630:SF44; PTHR11630:SF44; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF12619; MCM2_N; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01658; MCMPROTEIN2.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome;
KW Direct protein sequencing; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..904
FT /note="DNA replication licensing factor MCM2"
FT /id="PRO_0000194088"
FT DOMAIN 473..680
FT /note="MCM"
FT ZN_FING 329..355
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..257
FT /note="Interaction with KAT7"
FT /evidence="ECO:0000269|PubMed:11278932"
FT REGION 61..130
FT /note="Interaction with DNJC9"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOTIF 655..658
FT /note="Arginine finger"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 523..530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:17622165, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 40
FT /note="Phosphoserine; by CDC7"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 53
FT /note="Phosphoserine; by CDC7"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 137
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49736"
FT MUTAGEN 237
FT /note="L->P: Impairs interaction with KAT7."
FT /evidence="ECO:0000269|PubMed:11278932"
FT CONFLICT 70
FT /note="E -> G (in Ref. 3; AAC16250)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> P (in Ref. 3; AAC16250)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="W -> R (in Ref. 1; BAA22148)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Y -> H (in Ref. 3; AAC16250)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="N -> D (in Ref. 7; AAC36510)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="L -> S (in Ref. 7; AAC36510)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="D -> N (in Ref. 7; AAC36510)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="L -> I (in Ref. 3; AAC16250)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 102078 MW; 7B61C13DAD1CAC58 CRC64;
MAESSESLSA SSPARQRRRI SDPLTSSPGR SSRRADALTS SPGRDLPPFE DESEGLLGTE
GPMEEEEDGE ELIGDGMERD YRPIPELDVY EAEGLALDDE DVEELTASQR EAAERTMRQR
DREAGRGLGR MRRGLLYDSS EEDEERPARK RRHVERATED GEEDEEMIES IENLEDLKGH
SVREWVSMAG PRLEIHHRFK NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR
EHVLAYFLPE APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCS KCNFVLGPFC QSQNQEVKPG SCPECQSAGP
FEINMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA DLVDSCKPGD EIELTGIYHN
NYDGSLNTAN GFPVFATIIL ANHVAKKDNK VAVGELTDED VKMITGLSKD QQIGEKIFAS
IAPSIYGHED IKRGLALALF GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS
SRAIFTTGQG ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT EPIISRFDVL
CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KKDEGLTNGG TLEPAMPNTY GVEPLPQEVL
KKYIIYAKER VRPKLNQMDQ DKVARMYSDL RKESMATGSI PITVRHIESM IRMAEAHARM
HLRDYVMEDD VNMAIRVMME SFIDTQKFSV MRSMRKTFAR YLSFRRDNND LLLFILKQLV
AEQVTYQRNR FGAQQDTIEI PEKDLMDKAR QINIHNLSAF YDSDLFKFNK FSRDLKRKLI
LQQF
