Full text data of SMC2
SMC2
(CAPE, SMC2L1)
[Confidence: low (only semi-automatic identification from reviews)]
Structural maintenance of chromosomes protein 2; SMC protein 2; SMC-2 (Chromosome-associated protein E; hCAP-E; XCAP-E homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Structural maintenance of chromosomes protein 2; SMC protein 2; SMC-2 (Chromosome-associated protein E; hCAP-E; XCAP-E homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95347
ID SMC2_HUMAN Reviewed; 1197 AA.
AC O95347; Q6IEE0; Q9P1P2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome-associated protein E;
DE Short=hCAP-E;
DE AltName: Full=XCAP-E homolog;
GN Name=SMC2; Synonyms=CAPE, SMC2L1; ORFNames=PRO0324;
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 INTERACTION WITH SMC4.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G.,
RA Zhou W., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [8]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 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 [9]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677;
RP LYS-1158 AND LYS-1160, 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 [11]
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 [12]
RP INTERACTION WITH BRD4.
RX PubMed=23728299; DOI=10.1038/nature12147;
RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C.,
RA Cannell I.G., Bryson B.D., Rameseder J., Lee M.J., Blake E.J.,
RA Fydrych A., Ho R., Greenberger B.A., Chen G.C., Maffa A.,
RA Del Rosario A.M., Root D.E., Carpenter A.E., Hahn W.C., Sabatini D.M.,
RA Chen C.C., White F.M., Bradner J.E., Yaffe M.B.;
RT "The bromodomain protein Brd4 insulates chromatin from DNA damage
RT signalling.";
RL Nature 498:246-250(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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. 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. Interacts with BRD4 (isoform B), leading to
CC insulate chromatin from DNA damage response pathway.
CC -!- INTERACTION:
CC Q15003:NCAPH; NbExp=2; IntAct=EBI-355822, EBI-1046410;
CC Q6IBW4:NCAPH2; NbExp=2; IntAct=EBI-355822, EBI-2548296;
CC Q9NTJ3:SMC4; NbExp=3; IntAct=EBI-355822, EBI-356173;
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=O95347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95347-2; Sequence=VSP_007243, VSP_007244;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC4,
CC forming a V-shaped heterodimer (By similarity).
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72360.1; Type=Frameshift; Positions=890, 908;
CC Sequence=AAF29579.1; Type=Erroneous initiation;
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DR EMBL; AF092563; AAC72360.1; ALT_FRAME; mRNA.
DR EMBL; AL833191; CAI46187.1; -; mRNA.
DR EMBL; AL161791; CAI16866.1; -; Genomic_DNA.
DR EMBL; AL354938; CAI16866.1; JOINED; Genomic_DNA.
DR EMBL; AL354938; CAI16923.1; -; Genomic_DNA.
DR EMBL; AL161791; CAI16923.1; JOINED; Genomic_DNA.
DR EMBL; CH471105; EAW58973.1; -; Genomic_DNA.
DR EMBL; BC130385; AAI30386.1; -; mRNA.
DR EMBL; AF113673; AAF29579.1; ALT_INIT; mRNA.
DR EMBL; BN000163; CAD89875.1; -; mRNA.
DR RefSeq; NP_001036015.1; NM_001042550.1.
DR RefSeq; NP_001036016.1; NM_001042551.1.
DR RefSeq; NP_001252531.1; NM_001265602.1.
DR RefSeq; NP_006435.2; NM_006444.2.
DR RefSeq; XP_005251717.1; XM_005251660.1.
DR RefSeq; XP_005251718.1; XM_005251661.1.
DR UniGene; Hs.119023; -.
DR ProteinModelPortal; O95347; -.
DR SMR; O95347; 1-273, 462-688, 945-1172.
DR DIP; DIP-35422N; -.
DR IntAct; O95347; 15.
DR MINT; MINT-1161754; -.
DR STRING; 9606.ENSP00000286398; -.
DR PhosphoSite; O95347; -.
DR PaxDb; O95347; -.
DR PRIDE; O95347; -.
DR Ensembl; ENST00000286398; ENSP00000286398; ENSG00000136824.
DR Ensembl; ENST00000303219; ENSP00000306152; ENSG00000136824.
DR Ensembl; ENST00000374787; ENSP00000363919; ENSG00000136824.
DR Ensembl; ENST00000374793; ENSP00000363925; ENSG00000136824.
DR Ensembl; ENST00000493955; ENSP00000431534; ENSG00000136824.
DR GeneID; 10592; -.
DR KEGG; hsa:10592; -.
DR UCSC; uc004bbv.3; human.
DR CTD; 10592; -.
DR GeneCards; GC09P106856; -.
DR H-InvDB; HIX0008250; -.
DR HGNC; HGNC:14011; SMC2.
DR MIM; 605576; gene.
DR neXtProt; NX_O95347; -.
DR PharmGKB; PA37833; -.
DR eggNOG; COG1196; -.
DR HOGENOM; HOG000228249; -.
DR HOVERGEN; HBG106605; -.
DR InParanoid; O95347; -.
DR KO; K06674; -.
DR OMA; CQNGKIP; -.
DR OrthoDB; EOG7SR4KV; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; SMC2; human.
DR GeneWiki; SMC2; -.
DR GenomeRNAi; 10592; -.
DR NextBio; 40225; -.
DR PRO; PR:O95347; -.
DR ArrayExpress; O95347; -.
DR Bgee; O95347; -.
DR CleanEx; HS_SMC2; -.
DR Genevestigator; O95347; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027120; Smc2.
DR InterPro; IPR010935; SMC_hinge.
DR PANTHER; PTHR18937:SF9; PTHR18937:SF9; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
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; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1197 Structural maintenance of chromosomes
FT protein 2.
FT /FTId=PRO_0000118995.
FT NP_BIND 32 39 ATP (Potential).
FT REGION 508 671 Flexible hinge.
FT COILED 173 507 Potential.
FT COILED 672 926 Potential.
FT COILED 963 1031 Potential.
FT COMPBIAS 1085 1120 Ala/Asp-rich (DA-box).
FT MOD_RES 114 114 N6-acetyllysine.
FT MOD_RES 222 222 N6-acetyllysine.
FT MOD_RES 677 677 N6-acetyllysine.
FT MOD_RES 1158 1158 N6-acetyllysine.
FT MOD_RES 1160 1160 N6-acetyllysine.
FT VAR_SEQ 1091 1099 SLVALSLIL -> QKQQNHTTG (in isoform 2).
FT /FTId=VSP_007243.
FT VAR_SEQ 1100 1197 Missing (in isoform 2).
FT /FTId=VSP_007244.
FT VARIANT 1009 1009 E -> K (in dbSNP:rs4562395).
FT /FTId=VAR_047489.
FT CONFLICT 294 294 G -> V (in Ref. 1; AAC72360).
FT CONFLICT 916 916 N -> H (in Ref. 1; AAC72360).
FT CONFLICT 998 998 Y -> C (in Ref. 1; AAC72360).
SQ SEQUENCE 1197 AA; 135656 MW; 15EBB56B31FC1364 CRC64;
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA
AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL
LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE
DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH
ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ
MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE
KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA
LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH
GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE
MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM
KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL
EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK
EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN
NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE
DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE
NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF
IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
//
ID SMC2_HUMAN Reviewed; 1197 AA.
AC O95347; Q6IEE0; Q9P1P2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE Short=SMC protein 2;
DE Short=SMC-2;
DE AltName: Full=Chromosome-associated protein E;
DE Short=hCAP-E;
DE AltName: Full=XCAP-E homolog;
GN Name=SMC2; Synonyms=CAPE, SMC2L1; ORFNames=PRO0324;
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 INTERACTION WITH SMC4.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G.,
RA Zhou W., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [8]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 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 [9]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677;
RP LYS-1158 AND LYS-1160, 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 [11]
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 [12]
RP INTERACTION WITH BRD4.
RX PubMed=23728299; DOI=10.1038/nature12147;
RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C.,
RA Cannell I.G., Bryson B.D., Rameseder J., Lee M.J., Blake E.J.,
RA Fydrych A., Ho R., Greenberger B.A., Chen G.C., Maffa A.,
RA Del Rosario A.M., Root D.E., Carpenter A.E., Hahn W.C., Sabatini D.M.,
RA Chen C.C., White F.M., Bradner J.E., Yaffe M.B.;
RT "The bromodomain protein Brd4 insulates chromatin from DNA damage
RT signalling.";
RL Nature 498:246-250(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
CC in the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. 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. Interacts with BRD4 (isoform B), leading to
CC insulate chromatin from DNA damage response pathway.
CC -!- INTERACTION:
CC Q15003:NCAPH; NbExp=2; IntAct=EBI-355822, EBI-1046410;
CC Q6IBW4:NCAPH2; NbExp=2; IntAct=EBI-355822, EBI-2548296;
CC Q9NTJ3:SMC4; NbExp=3; IntAct=EBI-355822, EBI-356173;
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=O95347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95347-2; Sequence=VSP_007243, VSP_007244;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC4,
CC forming a V-shaped heterodimer (By similarity).
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72360.1; Type=Frameshift; Positions=890, 908;
CC Sequence=AAF29579.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF092563; AAC72360.1; ALT_FRAME; mRNA.
DR EMBL; AL833191; CAI46187.1; -; mRNA.
DR EMBL; AL161791; CAI16866.1; -; Genomic_DNA.
DR EMBL; AL354938; CAI16866.1; JOINED; Genomic_DNA.
DR EMBL; AL354938; CAI16923.1; -; Genomic_DNA.
DR EMBL; AL161791; CAI16923.1; JOINED; Genomic_DNA.
DR EMBL; CH471105; EAW58973.1; -; Genomic_DNA.
DR EMBL; BC130385; AAI30386.1; -; mRNA.
DR EMBL; AF113673; AAF29579.1; ALT_INIT; mRNA.
DR EMBL; BN000163; CAD89875.1; -; mRNA.
DR RefSeq; NP_001036015.1; NM_001042550.1.
DR RefSeq; NP_001036016.1; NM_001042551.1.
DR RefSeq; NP_001252531.1; NM_001265602.1.
DR RefSeq; NP_006435.2; NM_006444.2.
DR RefSeq; XP_005251717.1; XM_005251660.1.
DR RefSeq; XP_005251718.1; XM_005251661.1.
DR UniGene; Hs.119023; -.
DR ProteinModelPortal; O95347; -.
DR SMR; O95347; 1-273, 462-688, 945-1172.
DR DIP; DIP-35422N; -.
DR IntAct; O95347; 15.
DR MINT; MINT-1161754; -.
DR STRING; 9606.ENSP00000286398; -.
DR PhosphoSite; O95347; -.
DR PaxDb; O95347; -.
DR PRIDE; O95347; -.
DR Ensembl; ENST00000286398; ENSP00000286398; ENSG00000136824.
DR Ensembl; ENST00000303219; ENSP00000306152; ENSG00000136824.
DR Ensembl; ENST00000374787; ENSP00000363919; ENSG00000136824.
DR Ensembl; ENST00000374793; ENSP00000363925; ENSG00000136824.
DR Ensembl; ENST00000493955; ENSP00000431534; ENSG00000136824.
DR GeneID; 10592; -.
DR KEGG; hsa:10592; -.
DR UCSC; uc004bbv.3; human.
DR CTD; 10592; -.
DR GeneCards; GC09P106856; -.
DR H-InvDB; HIX0008250; -.
DR HGNC; HGNC:14011; SMC2.
DR MIM; 605576; gene.
DR neXtProt; NX_O95347; -.
DR PharmGKB; PA37833; -.
DR eggNOG; COG1196; -.
DR HOGENOM; HOG000228249; -.
DR HOVERGEN; HBG106605; -.
DR InParanoid; O95347; -.
DR KO; K06674; -.
DR OMA; CQNGKIP; -.
DR OrthoDB; EOG7SR4KV; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; SMC2; human.
DR GeneWiki; SMC2; -.
DR GenomeRNAi; 10592; -.
DR NextBio; 40225; -.
DR PRO; PR:O95347; -.
DR ArrayExpress; O95347; -.
DR Bgee; O95347; -.
DR CleanEx; HS_SMC2; -.
DR Genevestigator; O95347; -.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027120; Smc2.
DR InterPro; IPR010935; SMC_hinge.
DR PANTHER; PTHR18937:SF9; PTHR18937:SF9; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
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; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1197 Structural maintenance of chromosomes
FT protein 2.
FT /FTId=PRO_0000118995.
FT NP_BIND 32 39 ATP (Potential).
FT REGION 508 671 Flexible hinge.
FT COILED 173 507 Potential.
FT COILED 672 926 Potential.
FT COILED 963 1031 Potential.
FT COMPBIAS 1085 1120 Ala/Asp-rich (DA-box).
FT MOD_RES 114 114 N6-acetyllysine.
FT MOD_RES 222 222 N6-acetyllysine.
FT MOD_RES 677 677 N6-acetyllysine.
FT MOD_RES 1158 1158 N6-acetyllysine.
FT MOD_RES 1160 1160 N6-acetyllysine.
FT VAR_SEQ 1091 1099 SLVALSLIL -> QKQQNHTTG (in isoform 2).
FT /FTId=VSP_007243.
FT VAR_SEQ 1100 1197 Missing (in isoform 2).
FT /FTId=VSP_007244.
FT VARIANT 1009 1009 E -> K (in dbSNP:rs4562395).
FT /FTId=VAR_047489.
FT CONFLICT 294 294 G -> V (in Ref. 1; AAC72360).
FT CONFLICT 916 916 N -> H (in Ref. 1; AAC72360).
FT CONFLICT 998 998 Y -> C (in Ref. 1; AAC72360).
SQ SEQUENCE 1197 AA; 135656 MW; 15EBB56B31FC1364 CRC64;
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV
NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA
AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL
LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE
DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH
ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ
MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE
KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA
LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH
GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE
MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM
KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL
EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK
EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN
NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE
DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE
NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF
IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
//
MIM
605576
*RECORD*
*FIELD* NO
605576
*FIELD* TI
*605576 STRUCTURAL MAINTENANCE OF CHROMOSOMES 2; SMC2
;;CHROMOSOME-ASSOCIATED PROTEIN E; CAPE
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 SMC2
and SMC4 (605575), which they called CAPE and CAPC, respectively.
Sequence analysis predicted that the 1,197-amino acid CAPE protein is
80% identical to the Xenopus sequence. Northern blot analysis detected a
4.5-kb transcript. Western blot and immunoprecipitation analyses showed
that CAPE is expressed as a 135-kD soluble nuclear protein throughout
the cell cycle in a variety of cell lines and is associated with CAPC 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.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SMC2
gene to chromosome 9 (TMAP SGC33405).
*FIELD* RF
1. 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
605576
*FIELD* TI
*605576 STRUCTURAL MAINTENANCE OF CHROMOSOMES 2; SMC2
;;CHROMOSOME-ASSOCIATED PROTEIN E; CAPE
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 SMC2
and SMC4 (605575), which they called CAPE and CAPC, respectively.
Sequence analysis predicted that the 1,197-amino acid CAPE protein is
80% identical to the Xenopus sequence. Northern blot analysis detected a
4.5-kb transcript. Western blot and immunoprecipitation analyses showed
that CAPE is expressed as a 135-kD soluble nuclear protein throughout
the cell cycle in a variety of cell lines and is associated with CAPC 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.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SMC2
gene to chromosome 9 (TMAP SGC33405).
*FIELD* RF
1. 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