SMC3_MOUSE
ID SMC3_MOUSE Reviewed; 1217 AA.
AC Q9CW03; O35667; Q9QUS3;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
DE AltName: Full=Basement membrane-associated chondroitin proteoglycan;
DE Short=Bamacan;
DE AltName: Full=Chondroitin sulfate proteoglycan 6;
DE AltName: Full=Chromosome segregation protein SmcD;
DE AltName: Full=Mad member-interacting protein 1;
GN Name=Smc3; Synonyms=Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd;
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 TISSUE SPECIFICITY.
RX PubMed=10358101; DOI=10.1074/jbc.274.24.17384;
RA Ghiselli G., Siracusa L.D., Iozzo R.V.;
RT "Complete cDNA cloning, genomic organization, chromosomal assignment,
RT functional characterization of the promoter, and expression of the murine
RT Bamacan gene.";
RL J. Biol. Chem. 274:17384-17393(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION IN A COHESIN
RP COMPLEX WITH SMC1A AND RAD21.
RX PubMed=10375619; DOI=10.1016/s0378-1119(99)00160-2;
RA Darwiche N., Freeman L.A., Strunnikov A.;
RT "Characterization of the components of the putative mammalian sister
RT chromatid cohesion complex.";
RL Gene 233:39-47(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 478-1217, INTERACTION WITH MXI1; MXD3 AND
RP MXD4, AND MUTAGENESIS OF LEU-807.
RC TISSUE=Embryo;
RX PubMed=9528857; DOI=10.1038/sj.onc.1201634;
RA Gupta K., Anand G., Yin X.Y., Prochownik E.V.;
RT "Mmip1: a novel leucine zipper protein that reverses the suppressive
RT effects of mad family members on C-myc.";
RL Oncogene 16:1149-1159(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 887-1217.
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 [5]
RP INTERACTION WITH STAG3.
RX PubMed=11483963; DOI=10.1038/35087082;
RA Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S.,
RA Barbero J.L.;
RT "Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis
RT I.";
RL Nat. Cell Biol. 3:761-766(2001).
RN [6]
RP INTERACTION WITH SMC1B.
RX PubMed=11564881; DOI=10.1128/mcb.21.20.6984-6998.2001;
RA Revenkova E., Eijpe M., Heyting C., Gross B., Jessberger R.;
RT "Novel meiosis-specific isoform of mammalian SMC1.";
RL Mol. Cell. Biol. 21:6984-6998(2001).
RN [7]
RP PHOSPHORYLATION AT SER-1013.
RX PubMed=15378723; DOI=10.1002/rcm.1604;
RA Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT "Phosphoproteome analysis of mouse liver using immobilized metal affinity
RT purification and linear ion trap mass spectrometry.";
RL Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-1083.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24287868; DOI=10.1007/s00412-013-0444-7;
RA Visnes T., Giordano F., Kuznetsova A., Suja J.A., Lander A.D., Calof A.L.,
RA Stroem L.;
RT "Localisation of the SMC loading complex Nipbl/Mau2 during mammalian
RT meiotic prophase I.";
RL Chromosoma 123:239-252(2014).
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement. {ECO:0000269|PubMed:10375619}.
CC -!- SUBUNIT: Forms a heterodimer with SMC1A or SMC1B in cohesin complexes
CC (PubMed:11564881). Cohesin complexes are composed of the SMC1 (SMC1A or
CC SMC1B) and SMC3 heterodimer attached via their SMC hinge domain, RAD21
CC which link them, and one STAG protein (STAG1, STAG2 or STAG3), which
CC interacts with RAD21. Also found in meiosis-specific cohesin complexes.
CC Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/SCC-112 and
CC PDS5B/APRIN. Interacts with PDS5A and WAPL; regulated by SMC3
CC acetylation. Interacts with NUMA1, and forms a ternary complex with
CC KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to
CC the spindle pole and a function in chromosome movement. Interacts with
CC SYCP2 and RPGR. Interacts (via SMC hinge domain) with KIAA1328 (via
CC N- and C-terminal domains). Interacts with DDX11. Found in a cohesin
CC complex with SMC1A, STAG1 and RAD21. The SMC1A-SMC3 heterodimer
CC interacts with the NIPBL-MAU2 heterodimer (By similarity). Interacts
CC with MXI1, MXD3 and MXD4 (PubMed:9528857). Interacts with STAG3
CC (PubMed:11483963). Interacts with the NuRD complex component HDAC2; the
CC interaction is direct (By similarity). {ECO:0000250|UniProtKB:P97690,
CC ECO:0000250|UniProtKB:Q9UQE7, ECO:0000269|PubMed:11483963,
CC ECO:0000269|PubMed:11564881, ECO:0000269|PubMed:9528857}.
CC -!- INTERACTION:
CC Q9CW03; Q9Z2D6: Mecp2; NbExp=3; IntAct=EBI-2550068, EBI-1188816;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22346761}. Chromosome
CC {ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:24287868}. Chromosome,
CC centromere {ECO:0000269|PubMed:22346761}. Note=Associates with
CC chromatin. Before prophase it is scattered along chromosome arms.
CC During prophase, most of cohesin complexes dissociate from chromatin
CC probably because of phosphorylation by PLK, except at centromeres,
CC where cohesin complexes remain. At anaphase, the RAD21 subunit of the
CC cohesin complex is cleaved, leading to the dissociation of the complex
CC from chromosomes, allowing chromosome separation. The phosphorylated
CC form at Ser-1083 is preferentially associated with unsynapsed
CC chromosomal regions.
CC -!- TISSUE SPECIFICITY: Spermatocytes (at protein level). Widely expressed,
CC with higher expression in testis and brain.
CC {ECO:0000269|PubMed:10358101, ECO:0000269|PubMed:24287868}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC1A or SMC1B, forming a V-shaped
CC heterodimer. The two heads of the heterodimer are then connected by
CC different ends of the cleavable RAD21 protein, forming a ring structure
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-1083 in a SPO11-dependent manner.
CC {ECO:0000269|PubMed:15378723, ECO:0000269|PubMed:22346761}.
CC -!- PTM: Acetylation at Lys-105 and Lys-106 by ESCO1 is important for
CC genome stability and S phase sister chromatid cohesion. Regulated by
CC DSCC1, it is required for processive DNA synthesis, coupling sister
CC chromatid cohesion establishment during S phase to DNA replication (By
CC similarity). Deacetylation by HDAC8, regulates release of the cohesin
CC complex from chromatin (By similarity). {ECO:0000250|UniProtKB:Q9UQE7}.
CC -!- PTM: Ubiquitinated by the DCX(DCAF15) complex, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q9UQE7}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally isolated as a proteoglycan protein (explaining
CC its name). Although not excluded, such secreted function is not clear.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA75400.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF141294; AAD42073.1; -; mRNA.
DR EMBL; AF047601; AAD27754.1; -; mRNA.
DR EMBL; Y15128; CAA75400.1; ALT_FRAME; mRNA.
DR EMBL; AK005647; BAB24167.1; -; mRNA.
DR CCDS; CCDS38025.1; -.
DR RefSeq; NP_031816.2; NM_007790.3.
DR PDB; 2WD5; X-ray; 2.70 A; B=484-696.
DR PDB; 7DG5; X-ray; 2.00 A; B/D=484-696.
DR PDBsum; 2WD5; -.
DR PDBsum; 7DG5; -.
DR AlphaFoldDB; Q9CW03; -.
DR SMR; Q9CW03; -.
DR BioGRID; 198951; 56.
DR CORUM; Q9CW03; -.
DR DIP; DIP-57028N; -.
DR IntAct; Q9CW03; 51.
DR MINT; Q9CW03; -.
DR STRING; 10090.ENSMUSP00000025930; -.
DR MoonProt; Q9CW03; -.
DR iPTMnet; Q9CW03; -.
DR PhosphoSitePlus; Q9CW03; -.
DR EPD; Q9CW03; -.
DR MaxQB; Q9CW03; -.
DR PaxDb; Q9CW03; -.
DR PRIDE; Q9CW03; -.
DR ProteomicsDB; 257264; -.
DR Antibodypedia; 18357; 353 antibodies from 39 providers.
DR DNASU; 13006; -.
DR Ensembl; ENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974.
DR GeneID; 13006; -.
DR KEGG; mmu:13006; -.
DR UCSC; uc008hwy.2; mouse.
DR CTD; 9126; -.
DR MGI; MGI:1339795; Smc3.
DR VEuPathDB; HostDB:ENSMUSG00000024974; -.
DR eggNOG; KOG0964; Eukaryota.
DR GeneTree; ENSGT00580000081628; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; Q9CW03; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q9CW03; -.
DR TreeFam; TF105602; -.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 13006; 48 hits in 113 CRISPR screens.
DR ChiTaRS; Smc3; mouse.
DR EvolutionaryTrace; Q9CW03; -.
DR PRO; PR:Q9CW03; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CW03; protein.
DR Bgee; ENSMUSG00000024974; Expressed in undifferentiated genital tubercle and 253 other tissues.
DR ExpressionAtlas; Q9CW03; baseline and differential.
DR Genevisible; Q9CW03; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IDA:CAFA.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
DR GO; GO:0036033; F:mediator complex binding; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IPI:MGI.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; ISO:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; DNA damage; DNA repair; Meiosis;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1217
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119002"
FT DOMAIN 530..642
FT /note="SMC hinge"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..350
FT /evidence="ECO:0000255"
FT COILED 393..503
FT /evidence="ECO:0000255"
FT COILED 669..916
FT /evidence="ECO:0000255"
FT COILED 958..989
FT /evidence="ECO:0000255"
FT COMPBIAS 1067..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 783
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15378723"
FT MOD_RES 1065
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97690"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22346761"
FT MOD_RES 1190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQE7"
FT MUTAGEN 807
FT /note="L->P: Abolishes interaction with MXI1."
FT /evidence="ECO:0000269|PubMed:9528857"
FT CONFLICT 999
FT /note="K -> R (in Ref. 3; CAA75400)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175
FT /note="F -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 503..521
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:2WD5"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 566..578
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:7DG5"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 636..645
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:7DG5"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:7DG5"
FT HELIX 675..682
FT /evidence="ECO:0007829|PDB:7DG5"
SQ SEQUENCE 1217 AA; 141556 MW; 11FF55165BE6A88E CRC64;
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLEHFR RKGINQHVQN GYHGIVMNNF
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV
ITAEMAKDFV EDDTTHG
