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Protein data for CND2_SCHPO:

Description:
Condensin complex subunit 2 (p105) (Barren homolog) (CAPH homolog).

Molecular weight: 83254

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-FEB-2006, entry version 38.

Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein CND2_SCHPO:

DatabasePointerAdd. info#1Add. info#2
EMBLAB030213BAA82625.1-
EMBLAL049728CAB41651.1-
PIRT43520T43520.
GeneDB_SpombeSPCC306.03c-.1
BioCycSPOM-XXX-01:SPOM-XXX-01-002161-MONOMER-.1
GOGO:0000796C:condensin complexIDA.
GOGO:0005737C:cytoplasmIDA.
GOGO:0005634C:nucleusIDA.
GOGO:0007076P:mitotic chromosome condensationIMP.
InterProIPR008418Barren.
PfamPF05786Barren1.
PIRSFPIRSF017126Condensin_H1.

General information about the databases mentioned above

Keywords:
Cell cycle; Cell division; Complete proteome; Direct protein sequencing; DNA condensation; DNA damage; DNA repair; Mitosis; Nuclear protein.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 82-113;
RP 123-138; 536-553 AND 674-689, FUNCTION, AND IDENTIFICATION IN A
RP CONDENSIN COMPLEX WITH CUT3; CUT14; CND1 AND CND3.
RX MEDLINE=99415811; PubMed=10485849; DOI=10.1101/gad.13.17.2271;
RA Sutani T., Yuasa T., Tomonaga T., Dohmae N., Takio K., Yanagida M.;
RT "Fission yeast condensin complex: essential roles of non-SMC subunits
RT for condensation and Cdc2 phosphorylation of Cut3/SMC4.";
RL Genes Dev. 13:2271-2283(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTANT CND2-1.
RX MEDLINE=21996421; PubMed=12000964; DOI=10.1038/417197a;
RA Aono N., Sutani T., Tomonaga T., Mochida S., Yanagida M.;
RT "Cnd2 has dual roles in mitotic condensation and interphase.";
RL Nature 417:197-202(2002).

Feature:
CHAIN 1 742 Condensin complex subunit 2.
/FTId=PRO_0000095044.
MUTAGEN 114 114 A->T: In cnd2-1; defects in DNA repair
and cell cycle.

Comments:
-!- FUNCTION: Regulatory subunit of the condensin complex, a complex
required for conversion of interphase chromatin into mitotic-like
condense chromosomes. The condensin complex probably introduces
positive supercoils into relaxed DNA in the presence of type I
topoisomerases and converts nicked DNA into positive knotted forms
in the presence of type II topoisomerases. The condensin complex
probably also plays a role during interphase in processes such as
DNA repair.
-!- SUBUNIT: Component of the condensin complex, which contains the
cut14/smc2 and cut3/smc2 heterodimer, and three non SMC subunits
that probably regulate the complex: cnd1, cnd2 and cnd3.
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic. In interphase
cells, the majority of the condensin complex is found in the
cytoplasm, while a minority of the complex is associated with
chromatin. A subpopulation of the complex however remains
associated with chromosome foci in interphase cells. During
mitosis, most of the condensin complex is associated with the
chromatin. At the onset of prophase, condensin associates with
chromosome arms and to chromosome condensation. Dissociation from
chromosomes is observed in late telophase.
-!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
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Sequence length: 742

     MKRASLGGHA PVSLPSLNDD ALEKKRAKEN SRKQRELRRS SALHSITPRR ESLNNSSPFN
     SSHQVPVLSN FEEWIKLATD NKINSTNTWN FALIDYFHDM SLLRDGEDIN FQKASCTLDG
     CVKIYTSRID SVATETGKLL SGLANDSKVL QQTEEGEDAE NDDEDLQKKK ERKRAQRSVK
     TLVKDFESIR AKKFELECSF DPLFKKMCAD FDEDGAKGLL MNHLCVDQHG RIVFDSSDTV
     IKDLENKDVE AESQEAVVAA PIESHDTEMT NVHDNISRET LNGIYKCYFT DIDQLTICPS
     LQGFEFDSKG NLDVSLLKSL SDEVNMITTT SLVDNTMEKT DADAASLSSD SDGEEGHIVH
     ALEEMAYDEE NPYVDVVPKA MDESENPDFG VDTEVNMADG STMNENYSII STAAANGVYE
     YFDKSMKKNW AGPEHWRIQA LRKNINNAST VFNSSNTAES SDNVSRSLSS TERKKRRELD
     NAIDFLQEVD VEALFTPATS SLKLPKSHWK RHNRCLLPDD YQYDSKRLLQ LFLKPKMSVL
     PNADGEGQLQ LNKALDDEND LDGIQPHGFD SDGSDNVDEG IPPYGFGDSD SPKQTPLLTP
     PSSSGFGDNL LLTARLAKPD MLNYAKRAKK VDVRVLKEKL WKCLDLENTI KENSINSHIE
     GSEMESEETN MPVKSFFSTV NQLEETYEKK ELKDISTSFA FICVLHLANE HNLELTSNED
     FSDVFIRPGP NLTTLEALEN DV

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