SMC4_HUMAN
ID SMC4_HUMAN Reviewed; 1288 AA.
AC Q9NTJ3; A6NLT9; D3DNL8; O95752; Q8NDL4; Q9UNT9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Structural maintenance of chromosomes protein 4;
DE Short=SMC protein 4;
DE Short=SMC-4;
DE AltName: Full=Chromosome-associated polypeptide C;
DE Short=hCAP-C;
DE AltName: Full=XCAP-C homolog;
GN Name=SMC4; Synonyms=CAPC, SMC4L1;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10319587; DOI=10.1007/s100380050142;
RA Nishiwaki T., Daigo Y., Kawasoe T., Nagasawa Y., Ishiguro H., Fujita M.,
RA Furukawa Y., Nakamura Y.;
RT "Isolation and characterization of a human cDNA homologous to the Xenopus
RT laevis XCAP-C gene belonging to the structural maintenance of chromosomes
RT (SMC) family.";
RL J. Hum. Genet. 44:197-202(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-1288 (ISOFORM 1), AND INTERACTION WITH
RP SMC2.
RC TISSUE=Teratocarcinoma;
RX PubMed=9789013; DOI=10.1073/pnas.95.22.12906;
RA Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S.,
RA Yokomori K.;
RT "Identification of two distinct human SMC protein complexes involved in
RT mitotic chromosome dynamics.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998).
RN [7]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND CNAP1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10958694; DOI=10.1128/mcb.20.18.6996-7006.2000;
RA Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.;
RT "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of
RT Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the
RT early stage of mitotic chromosome condensation.";
RL Mol. Cell. Biol. 20:6996-7006(2000).
RN [8]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; BRRN1; CNAP1 AND CAPG, AND
RP FUNCTION OF THE COMPLEX.
RX PubMed=11136719; DOI=10.1074/jbc.c000873200;
RA Kimura K., Cuvier O., Hirano T.;
RT "Chromosome condensation by a human condensin complex in Xenopus egg
RT extracts.";
RL J. Biol. Chem. 276:5417-5420(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-28; THR-39; SER-41
RP AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-679, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-41; SER-143 AND
RP SER-1056, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-28; THR-39; SER-41;
RP SER-50; SER-143 AND SER-982, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG. {ECO:0000269|PubMed:10958694,
CC ECO:0000269|PubMed:11136719}.
CC -!- INTERACTION:
CC Q9NTJ3; Q15003: NCAPH; NbExp=3; IntAct=EBI-356173, EBI-1046410;
CC Q9NTJ3; Q6IBW4: NCAPH2; NbExp=2; IntAct=EBI-356173, EBI-2548296;
CC Q9NTJ3; O95347: SMC2; NbExp=3; IntAct=EBI-356173, EBI-355822;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm
CC {ECO:0000269|PubMed:10958694}. Chromosome
CC {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority
CC of the condensin complex is found in the cytoplasm, while a minority of
CC the complex is associated with chromatin. A subpopulation of the
CC complex however remains associated with chromosome foci in interphase
CC cells. During mitosis, most of the condensin complex is associated with
CC the chromatin. At the onset of prophase, the regulatory subunits of the
CC complex are phosphorylated by CDC2, leading to condensin's association
CC with chromosome arms and to chromosome condensation. Dissociation from
CC chromosomes is observed in late telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NTJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NTJ3-2; Sequence=VSP_007245;
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in testis,
CC colon, thymus. {ECO:0000269|PubMed:10319587}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC2, forming a
CC V-shaped heterodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily. {ECO:0000305}.
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DR EMBL; AB019987; BAA73535.1; -; mRNA.
DR EMBL; AL136877; CAB66811.1; -; mRNA.
DR EMBL; AL833949; CAD38803.1; -; mRNA.
DR EMBL; AC024221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78639.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78640.1; -; Genomic_DNA.
DR EMBL; AF092564; AAC72361.1; -; mRNA.
DR CCDS; CCDS3189.1; -. [Q9NTJ3-1]
DR PIR; T46486; T46486.
DR RefSeq; NP_001002800.1; NM_001002800.2. [Q9NTJ3-1]
DR RefSeq; NP_001275682.1; NM_001288753.1.
DR RefSeq; NP_005487.3; NM_005496.3. [Q9NTJ3-1]
DR RefSeq; XP_011510613.1; XM_011512311.2. [Q9NTJ3-1]
DR PDB; 4U4P; X-ray; 1.89 A; B=566-809.
DR PDBsum; 4U4P; -.
DR AlphaFoldDB; Q9NTJ3; -.
DR SMR; Q9NTJ3; -.
DR BioGRID; 115362; 164.
DR ComplexPortal; CPX-979; Condensin I complex.
DR ComplexPortal; CPX-985; Condensin II complex.
DR CORUM; Q9NTJ3; -.
DR DIP; DIP-32946N; -.
DR IntAct; Q9NTJ3; 71.
DR MINT; Q9NTJ3; -.
DR STRING; 9606.ENSP00000349961; -.
DR GlyConnect; 2082; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NTJ3; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9NTJ3; -.
DR MetOSite; Q9NTJ3; -.
DR PhosphoSitePlus; Q9NTJ3; -.
DR SwissPalm; Q9NTJ3; -.
DR BioMuta; SMC4; -.
DR DMDM; 30173386; -.
DR EPD; Q9NTJ3; -.
DR jPOST; Q9NTJ3; -.
DR MassIVE; Q9NTJ3; -.
DR MaxQB; Q9NTJ3; -.
DR PaxDb; Q9NTJ3; -.
DR PeptideAtlas; Q9NTJ3; -.
DR PRIDE; Q9NTJ3; -.
DR ProteomicsDB; 82617; -. [Q9NTJ3-1]
DR ProteomicsDB; 82618; -. [Q9NTJ3-2]
DR Antibodypedia; 18504; 260 antibodies from 35 providers.
DR DNASU; 10051; -.
DR Ensembl; ENST00000344722.5; ENSP00000341382.5; ENSG00000113810.16. [Q9NTJ3-1]
DR Ensembl; ENST00000357388.8; ENSP00000349961.3; ENSG00000113810.16. [Q9NTJ3-1]
DR Ensembl; ENST00000462787.5; ENSP00000420734.1; ENSG00000113810.16. [Q9NTJ3-2]
DR GeneID; 10051; -.
DR KEGG; hsa:10051; -.
DR MANE-Select; ENST00000357388.8; ENSP00000349961.3; NM_001002800.3; NP_001002800.1.
DR UCSC; uc003fdh.5; human. [Q9NTJ3-1]
DR CTD; 10051; -.
DR DisGeNET; 10051; -.
DR GeneCards; SMC4; -.
DR HGNC; HGNC:14013; SMC4.
DR HPA; ENSG00000113810; Tissue enhanced (lymphoid).
DR MIM; 605575; gene.
DR neXtProt; NX_Q9NTJ3; -.
DR OpenTargets; ENSG00000113810; -.
DR PharmGKB; PA37834; -.
DR VEuPathDB; HostDB:ENSG00000113810; -.
DR eggNOG; KOG0996; Eukaryota.
DR GeneTree; ENSGT00900000141094; -.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; Q9NTJ3; -.
DR OMA; QIYIDEC; -.
DR PhylomeDB; Q9NTJ3; -.
DR TreeFam; TF101158; -.
DR PathwayCommons; Q9NTJ3; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR SignaLink; Q9NTJ3; -.
DR SIGNOR; Q9NTJ3; -.
DR BioGRID-ORCS; 10051; 796 hits in 1094 CRISPR screens.
DR ChiTaRS; SMC4; human.
DR GeneWiki; SMC4; -.
DR GenomeRNAi; 10051; -.
DR Pharos; Q9NTJ3; Tbio.
DR PRO; PR:Q9NTJ3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NTJ3; protein.
DR Bgee; ENSG00000113810; Expressed in ventricular zone and 186 other tissues.
DR ExpressionAtlas; Q9NTJ3; baseline and differential.
DR Genevisible; Q9NTJ3; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051383; P:kinetochore organization; IEA:Ensembl.
DR GO; GO:0010032; P:meiotic chromosome condensation; IEA:Ensembl.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:Ensembl.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; TAS:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IDA:ComplexPortal.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
DR CDD; cd03274; ABC_SMC4_euk; 2.
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; IPR041738; SMC4_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; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Coiled coil; Cytoplasm; DNA condensation;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1288
FT /note="Structural maintenance of chromosomes protein 4"
FT /id="PRO_0000119006"
FT DOMAIN 613..727
FT /note="SMC hinge"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 272..588
FT /evidence="ECO:0000255"
FT COILED 767..1020
FT /evidence="ECO:0000255"
FT COILED 1109..1129
FT /evidence="ECO:0000255"
FT COMPBIAS 14..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG47"
FT MOD_RES 679
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1056
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 980..1037
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007245"
FT VARIANT 181
FT /note="S -> R (in dbSNP:rs35214835)"
FT /id="VAR_052439"
FT VARIANT 356
FT /note="N -> S (in dbSNP:rs33999879)"
FT /id="VAR_052440"
FT VARIANT 415
FT /note="E -> D (in dbSNP:rs2164675)"
FT /id="VAR_059843"
FT CONFLICT 272
FT /note="R -> Q (in Ref. 6; AAC72361)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> D (in Ref. 2; CAB66811)"
FT /evidence="ECO:0000305"
FT CONFLICT 392..393
FT /note="QL -> HV (in Ref. 6; AAC72361)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="R -> S (in Ref. 6; AAC72361)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="V -> G (in Ref. 3; CAD38803)"
FT /evidence="ECO:0000305"
FT HELIX 573..608
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 630..636
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 638..641
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 642..646
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 648..660
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 665..670
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 671..677
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 702..712
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:4U4P"
FT HELIX 721..729
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 730..733
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:4U4P"
FT STRAND 763..765
FT /evidence="ECO:0007829|PDB:4U4P"
SQ SEQUENCE 1288 AA; 147182 MW; 9D164D6EB0602464 CRC64;
MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAETAS EELDNRSLEE
ILNSIPPPPP PAMTNEAGAP RLMITHIVNQ NFKSYAGEKI LGPFHKRFSC IIGPNGSGKS
NVIDSMLFVF GYRAQKIRSK KLSVLIHNSD EHKDIQSCTV EVHFQKIIDK EGDDYEVIPN
SNFYVSRTAC RDNTSVYHIS GKKKTFKDVG NLLRSHGIDL DHNRFLILQG EVEQIAMMKP
KGQTEHDEGM LEYLEDIIGC GRLNEPIKVL CRRVEILNEH RGEKLNRVKM VEKEKDALEG
EKNIAIEFLT LENEIFRKKN HVCQYYIYEL QKRIAEMETQ KEKIHEDTKE INEKSNILSN
EMKAKNKDVK DTEKKLNKIT KFIEENKEKF TQLDLEDVQV REKLKHATSK AKKLEKQLQK
DKEKVEEFKS IPAKSNNIIN ETTTRNNALE KEKEKEEKKL KEVMDSLKQE TQGLQKEKES
REKELMGFSK SVNEARSKMD VAQSELDIYL SRHNTAVSQL TKAKEALIAA SETLKERKAA
IRDIEGKLPQ TEQELKEKEK ELQKLTQEET NFKSLVHDLF QKVEEAKSSL AMNRSRGKVL
DAIIQEKKSG RIPGIYGRLG DLGAIDEKYD VAISSCCHAL DYIVVDSIDI AQECVNFLKR
QNIGVATFIG LDKMAVWAKK MTEIQTPENT PRLFDLVKVK DEKIRQAFYF ALRDTLVADN
LDQATRVAYQ KDRRWRVVTL QGQIIEQSGT MTGGGSKVMK GRMGSSLVIE ISEEEVNKME
SQLQNDSKKA MQIQEQKVQL EERVVKLRHS EREMRNTLEK FTASIQRLIE QEEYLNVQVK
ELEANVLATA PDKKKQKLLE ENVSAFKTEY DAVAEKAGKV EAEVKRLHNT IVEINNHKLK
AQQDKLDKIN KQLDECASAI TKAQVAIKTA DRNLQKAQDS VLRTEKEIKD TEKEVDDLTA
ELKSLEDKAA EVVKNTNAAE ESLPEIQKEH RNLLQELKVI QENEHALQKD ALSIKLKLEQ
IDGHIAEHNS KIKYWHKEIS KISLHPIEDN PIEEISVLSP EDLEAIKNPD SITNQIALLE
ARCHEMKPNL GAIAEYKKKE ELYLQRVAEL DKITYERDSF RQAYEDLRKQ RLNEFMAGFY
IITNKLKENY QMLTLGGDAE LELVDSLDPF SEGIMFSVRP PKKSWKKIFN LSGGEKTLSS
LALVFALHHY KPTPLYFMDE IDAALDFKNV SIVAFYIYEQ TKNAQFIIIS LRNNMFEISD
RLIGIYKTYN ITKSVAVNPK EIASKGLC
