Full text data of SMC4
SMC4
(CAPC, SMC4L1)
[Confidence: low (only semi-automatic identification from reviews)]
Structural maintenance of chromosomes protein 4; SMC protein 4; SMC-4 (Chromosome-associated polypeptide C; hCAP-C; XCAP-C homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Structural maintenance of chromosomes protein 4; SMC protein 4; SMC-4 (Chromosome-associated polypeptide C; hCAP-C; XCAP-C homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NTJ3
ID SMC4_HUMAN Reviewed; 1288 AA.
AC Q9NTJ3; A6NLT9; D3DNL8; O95752; Q8NDL4; Q9UNT9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-APR-2003, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Fujita M., Furukawa Y., Nakamura Y.;
RT "Isolation and characterization of a human cDNA homologous to the
RT Xenopus laevis XCAP-C gene belonging to the structural maintenance of
RT chromosomes (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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP WITH 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
RT in 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
RP SUBCELLULAR 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
RT homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3
RT during the 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
RP CAPG, AND 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT phosphorylation 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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;
RP SER-41 AND SER-50, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three
CC non SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG.
CC -!- INTERACTION:
CC O95347:SMC2; NbExp=3; IntAct=EBI-356173, EBI-355822;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found
CC in the cytoplasm, while a minority of the complex is associated
CC with chromatin. A subpopulation of the complex however remains
CC associated with chromosome foci in interphase cells. During
CC mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of
CC the complex are phosphorylated by CDC2, leading to condensin's
CC association with chromosome arms and to chromosome condensation.
CC Dissociation from 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in testis,
CC colon, thymus.
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC2,
CC forming a V-shaped heterodimer (By similarity).
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
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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 PIR; T46486; T46486.
DR RefSeq; NP_001002800.1; NM_001002800.1.
DR RefSeq; NP_005487.3; NM_005496.3.
DR UniGene; Hs.58992; -.
DR ProteinModelPortal; Q9NTJ3; -.
DR SMR; Q9NTJ3; 91-338, 597-754, 1096-1267.
DR DIP; DIP-32946N; -.
DR IntAct; Q9NTJ3; 18.
DR MINT; MINT-5005675; -.
DR STRING; 9606.ENSP00000341382; -.
DR PhosphoSite; Q9NTJ3; -.
DR DMDM; 30173386; -.
DR PaxDb; Q9NTJ3; -.
DR PeptideAtlas; Q9NTJ3; -.
DR PRIDE; Q9NTJ3; -.
DR DNASU; 10051; -.
DR Ensembl; ENST00000344722; ENSP00000341382; ENSG00000113810.
DR Ensembl; ENST00000357388; ENSP00000349961; ENSG00000113810.
DR Ensembl; ENST00000360111; ENSP00000353225; ENSG00000113810.
DR Ensembl; ENST00000462787; ENSP00000420734; ENSG00000113810.
DR GeneID; 10051; -.
DR KEGG; hsa:10051; -.
DR UCSC; uc003fdh.3; human.
DR CTD; 10051; -.
DR GeneCards; GC03P160117; -.
DR HGNC; HGNC:14013; SMC4.
DR HPA; CAB055509; -.
DR HPA; HPA029449; -.
DR MIM; 605575; gene.
DR neXtProt; NX_Q9NTJ3; -.
DR PharmGKB; PA37834; -.
DR eggNOG; COG1196; -.
DR HOGENOM; HOG000184777; -.
DR HOVERGEN; HBG106696; -.
DR InParanoid; Q9NTJ3; -.
DR KO; K06675; -.
DR OMA; IAIEFLT; -.
DR OrthoDB; EOG7RJPQJ; -.
DR PhylomeDB; Q9NTJ3; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; SMC4; -.
DR GenomeRNAi; 10051; -.
DR NextBio; 37969; -.
DR PRO; PR:Q9NTJ3; -.
DR ArrayExpress; Q9NTJ3; -.
DR Bgee; Q9NTJ3; -.
DR CleanEx; HS_SMC4; -.
DR Genevestigator; Q9NTJ3; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1288 Structural maintenance of chromosomes
FT protein 4.
FT /FTId=PRO_0000119006.
FT NP_BIND 113 120 ATP (Potential).
FT REGION 589 766 Flexible hinge.
FT COILED 272 588 Potential.
FT COILED 767 1020 Potential.
FT COILED 1109 1129 Potential.
FT COMPBIAS 18 23 Poly-Pro.
FT COMPBIAS 66 71 Poly-Pro.
FT COMPBIAS 1191 1226 Ala/Asp-rich (DA-box).
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 39 39 Phosphothreonine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 679 679 N6-acetyllysine.
FT MOD_RES 1056 1056 Phosphoserine.
FT VAR_SEQ 980 1037 Missing (in isoform 2).
FT /FTId=VSP_007245.
FT VARIANT 181 181 S -> R (in dbSNP:rs35214835).
FT /FTId=VAR_052439.
FT VARIANT 356 356 N -> S (in dbSNP:rs33999879).
FT /FTId=VAR_052440.
FT VARIANT 415 415 E -> D (in dbSNP:rs2164675).
FT /FTId=VAR_059843.
FT CONFLICT 272 272 R -> Q (in Ref. 6; AAC72361).
FT CONFLICT 283 283 E -> D (in Ref. 2; CAB66811).
FT CONFLICT 392 393 QL -> HV (in Ref. 6; AAC72361).
FT CONFLICT 594 594 R -> S (in Ref. 6; AAC72361).
FT CONFLICT 645 645 V -> G (in Ref. 3; CAD38803).
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
//
ID SMC4_HUMAN Reviewed; 1288 AA.
AC Q9NTJ3; A6NLT9; D3DNL8; O95752; Q8NDL4; Q9UNT9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-APR-2003, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Fujita M., Furukawa Y., Nakamura Y.;
RT "Isolation and characterization of a human cDNA homologous to the
RT Xenopus laevis XCAP-C gene belonging to the structural maintenance of
RT chromosomes (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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP WITH 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
RT in 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
RP SUBCELLULAR 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
RT homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3
RT during the 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
RP CAPG, AND 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT phosphorylation 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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;
RP SER-41 AND SER-50, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC2. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three
CC non SMC subunits that probably regulate the complex: BRRN1/CAPH,
CC CNAP1/CAPD2 and CAPG.
CC -!- INTERACTION:
CC O95347:SMC2; NbExp=3; IntAct=EBI-356173, EBI-355822;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found
CC in the cytoplasm, while a minority of the complex is associated
CC with chromatin. A subpopulation of the complex however remains
CC associated with chromosome foci in interphase cells. During
CC mitosis, most of the condensin complex is associated with the
CC chromatin. At the onset of prophase, the regulatory subunits of
CC the complex are phosphorylated by CDC2, leading to condensin's
CC association with chromosome arms and to chromosome condensation.
CC Dissociation from 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in testis,
CC colon, thymus.
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC2,
CC forming a V-shaped heterodimer (By similarity).
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC -----------------------------------------------------------------------
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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 PIR; T46486; T46486.
DR RefSeq; NP_001002800.1; NM_001002800.1.
DR RefSeq; NP_005487.3; NM_005496.3.
DR UniGene; Hs.58992; -.
DR ProteinModelPortal; Q9NTJ3; -.
DR SMR; Q9NTJ3; 91-338, 597-754, 1096-1267.
DR DIP; DIP-32946N; -.
DR IntAct; Q9NTJ3; 18.
DR MINT; MINT-5005675; -.
DR STRING; 9606.ENSP00000341382; -.
DR PhosphoSite; Q9NTJ3; -.
DR DMDM; 30173386; -.
DR PaxDb; Q9NTJ3; -.
DR PeptideAtlas; Q9NTJ3; -.
DR PRIDE; Q9NTJ3; -.
DR DNASU; 10051; -.
DR Ensembl; ENST00000344722; ENSP00000341382; ENSG00000113810.
DR Ensembl; ENST00000357388; ENSP00000349961; ENSG00000113810.
DR Ensembl; ENST00000360111; ENSP00000353225; ENSG00000113810.
DR Ensembl; ENST00000462787; ENSP00000420734; ENSG00000113810.
DR GeneID; 10051; -.
DR KEGG; hsa:10051; -.
DR UCSC; uc003fdh.3; human.
DR CTD; 10051; -.
DR GeneCards; GC03P160117; -.
DR HGNC; HGNC:14013; SMC4.
DR HPA; CAB055509; -.
DR HPA; HPA029449; -.
DR MIM; 605575; gene.
DR neXtProt; NX_Q9NTJ3; -.
DR PharmGKB; PA37834; -.
DR eggNOG; COG1196; -.
DR HOGENOM; HOG000184777; -.
DR HOVERGEN; HBG106696; -.
DR InParanoid; Q9NTJ3; -.
DR KO; K06675; -.
DR OMA; IAIEFLT; -.
DR OrthoDB; EOG7RJPQJ; -.
DR PhylomeDB; Q9NTJ3; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR GeneWiki; SMC4; -.
DR GenomeRNAi; 10051; -.
DR NextBio; 37969; -.
DR PRO; PR:Q9NTJ3; -.
DR ArrayExpress; Q9NTJ3; -.
DR Bgee; Q9NTJ3; -.
DR CleanEx; HS_SMC4; -.
DR Genevestigator; Q9NTJ3; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR010935; SMC_hinge.
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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 1288 Structural maintenance of chromosomes
FT protein 4.
FT /FTId=PRO_0000119006.
FT NP_BIND 113 120 ATP (Potential).
FT REGION 589 766 Flexible hinge.
FT COILED 272 588 Potential.
FT COILED 767 1020 Potential.
FT COILED 1109 1129 Potential.
FT COMPBIAS 18 23 Poly-Pro.
FT COMPBIAS 66 71 Poly-Pro.
FT COMPBIAS 1191 1226 Ala/Asp-rich (DA-box).
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 39 39 Phosphothreonine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 679 679 N6-acetyllysine.
FT MOD_RES 1056 1056 Phosphoserine.
FT VAR_SEQ 980 1037 Missing (in isoform 2).
FT /FTId=VSP_007245.
FT VARIANT 181 181 S -> R (in dbSNP:rs35214835).
FT /FTId=VAR_052439.
FT VARIANT 356 356 N -> S (in dbSNP:rs33999879).
FT /FTId=VAR_052440.
FT VARIANT 415 415 E -> D (in dbSNP:rs2164675).
FT /FTId=VAR_059843.
FT CONFLICT 272 272 R -> Q (in Ref. 6; AAC72361).
FT CONFLICT 283 283 E -> D (in Ref. 2; CAB66811).
FT CONFLICT 392 393 QL -> HV (in Ref. 6; AAC72361).
FT CONFLICT 594 594 R -> S (in Ref. 6; AAC72361).
FT CONFLICT 645 645 V -> G (in Ref. 3; CAD38803).
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
//
MIM
605575
*RECORD*
*FIELD* NO
605575
*FIELD* TI
*605575 STRUCTURAL MAINTENANCE OF CHROMOSOMES 4; SMC4
;;CHROMOSOME-ASSOCIATED PROTEIN C; CAPC
read more*FIELD* TX
DESCRIPTION
Members of the structural maintenance of chromosomes, or SMC, family
(e.g., SMC1A; 300040) are critical for mitotic chromosome condensation
in frogs and for DNA repair in mammals.
CLONING
By PCR of human cDNA libraries using degenerate primers based on
conserved C-terminal sequences of Xenopus, yeast, and C. elegans SMC
proteins, Schmiesing et al. (1998) obtained cDNAs encoding human SMC4
and SMC2 (605576), which they called CAPC and CAPE, respectively.
Sequence analysis predicted that the 1,202-amino acid CAPC protein lacks
the first 80 residues of the frog sequence but is homologous in the
middle coiled-coil region. Northern blot analysis detected a 5.0-kb
transcript. Western blot and immunoprecipitation analyses showed that
CAPC is expressed as a 165-kD soluble nuclear protein throughout the
cell cycle in a variety of cell lines and is associated with CAPE in a
heterodimeric complex. Immunofluorescence analysis demonstrated that the
proteins are associated with condensed chromosomes in mitotic cells and
show dense speckles in interphase nuclei. Microinjection of anti-CAPC or
anti-CAPE failed to arrest mitosis in metaphase cells, in contrast to
antibody to SMC1A.
Nishiwaki et al. (1999) isolated a full-length cDNA encoding CAPC. The
1,288-amino acid CAPC protein shares 77% identity overall with the
Xenopus sequence, including preservation of the approximately 200-amino
acid N-terminal region containing a nucleotide-binding motif and of the
approximately 200-amino acid C-terminal region containing a DA box.
Northern blot analysis detected a 4.4-kb transcript in all tissues
tested, with most abundant expression in thymus, testis, and colon.
MAPPING
Using FISH analysis, Nishiwaki et al. (1999) mapped the SMC4 gene to
chromosome 3q26.1.
*FIELD* RF
1. Nishiwaki, T.; Daigo, Y.; Kawasoe, T.; Nagasawa, Y.; Ishiguro,
H.; Fujita, M.; Furukawa, Y.; Nakamura, Y.: Isolation and characterization
of a human cDNA homologous to the Xenopus laevis XCAP-C gene belonging
to the structural maintenance of chromosomes (SMC) family. J. Hum.
Genet. 44: 197-202, 1999.
2. Schmiesing, J. A.; Ball, A. R., Jr.; Gregson, H. C.; Alderton,
J. M.; Zhou, S.; Yokomori, K.: Identification of two distinct human
SMC protein complexes involved in mitotic chromosome dynamics. Proc.
Nat. Acad. Sci. 95: 12906-12911, 1998.
*FIELD* CD
Paul J. Converse: 1/23/2001
*FIELD* ED
wwang: 11/09/2010
mgross: 7/19/2007
mgross: 1/23/2001
*RECORD*
*FIELD* NO
605575
*FIELD* TI
*605575 STRUCTURAL MAINTENANCE OF CHROMOSOMES 4; SMC4
;;CHROMOSOME-ASSOCIATED PROTEIN C; CAPC
read more*FIELD* TX
DESCRIPTION
Members of the structural maintenance of chromosomes, or SMC, family
(e.g., SMC1A; 300040) are critical for mitotic chromosome condensation
in frogs and for DNA repair in mammals.
CLONING
By PCR of human cDNA libraries using degenerate primers based on
conserved C-terminal sequences of Xenopus, yeast, and C. elegans SMC
proteins, Schmiesing et al. (1998) obtained cDNAs encoding human SMC4
and SMC2 (605576), which they called CAPC and CAPE, respectively.
Sequence analysis predicted that the 1,202-amino acid CAPC protein lacks
the first 80 residues of the frog sequence but is homologous in the
middle coiled-coil region. Northern blot analysis detected a 5.0-kb
transcript. Western blot and immunoprecipitation analyses showed that
CAPC is expressed as a 165-kD soluble nuclear protein throughout the
cell cycle in a variety of cell lines and is associated with CAPE in a
heterodimeric complex. Immunofluorescence analysis demonstrated that the
proteins are associated with condensed chromosomes in mitotic cells and
show dense speckles in interphase nuclei. Microinjection of anti-CAPC or
anti-CAPE failed to arrest mitosis in metaphase cells, in contrast to
antibody to SMC1A.
Nishiwaki et al. (1999) isolated a full-length cDNA encoding CAPC. The
1,288-amino acid CAPC protein shares 77% identity overall with the
Xenopus sequence, including preservation of the approximately 200-amino
acid N-terminal region containing a nucleotide-binding motif and of the
approximately 200-amino acid C-terminal region containing a DA box.
Northern blot analysis detected a 4.4-kb transcript in all tissues
tested, with most abundant expression in thymus, testis, and colon.
MAPPING
Using FISH analysis, Nishiwaki et al. (1999) mapped the SMC4 gene to
chromosome 3q26.1.
*FIELD* RF
1. Nishiwaki, T.; Daigo, Y.; Kawasoe, T.; Nagasawa, Y.; Ishiguro,
H.; Fujita, M.; Furukawa, Y.; Nakamura, Y.: Isolation and characterization
of a human cDNA homologous to the Xenopus laevis XCAP-C gene belonging
to the structural maintenance of chromosomes (SMC) family. J. Hum.
Genet. 44: 197-202, 1999.
2. Schmiesing, J. A.; Ball, A. R., Jr.; Gregson, H. C.; Alderton,
J. M.; Zhou, S.; Yokomori, K.: Identification of two distinct human
SMC protein complexes involved in mitotic chromosome dynamics. Proc.
Nat. Acad. Sci. 95: 12906-12911, 1998.
*FIELD* CD
Paul J. Converse: 1/23/2001
*FIELD* ED
wwang: 11/09/2010
mgross: 7/19/2007
mgross: 1/23/2001