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CND2_XENLA
ID   CND2_XENLA              Reviewed;         699 AA.
AC   O13067;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Condensin complex subunit 2;
DE   AltName: Full=Barren homolog;
DE   AltName: Full=Chromosome assembly protein xCAP-H;
DE   AltName: Full=Chromosome-associated protein H;
DE   AltName: Full=Non-SMC condensin I complex subunit H;
GN   Name=ncaph; Synonyms=brrn1, caph;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 117-132; 135-153; 233-250
RP   AND 632-652, AND IDENTIFICATION IN A CONDENSIN COMPLEX WITH XCAP-C; XCAP-E;
RP   XCAP-D2 AND XCAP-G.
RX   PubMed=9160743; DOI=10.1016/s0092-8674(00)80233-0;
RA   Hirano T., Kobayashi R., Hirano M.;
RT   "Condensins, chromosome condensation protein complexes containing XCAP-C,
RT   XCAP-E and a Xenopus homolog of the Drosophila Barren protein.";
RL   Cell 89:511-521(1997).
RN   [2]
RP   FUNCTION OF THE CONDENSIN COMPLEX, AND PHOSPHORYLATION BY CDK1.
RX   PubMed=9774278; DOI=10.1126/science.282.5388.487;
RA   Kimura K., Hirano M., Kobayashi R., Hirano T.;
RT   "Phosphorylation and activation of 13S condensin by Cdc2 in vitro.";
RL   Science 282:487-490(1998).
RN   [3]
RP   FUNCTION OF THE CONDENSIN COMPLEX.
RX   PubMed=10428035; DOI=10.1016/s0092-8674(00)81018-1;
RA   Kimura K., Rybenkov V.V., Crisona N.J., Hirano T., Cozzarelli N.R.;
RT   "13S condensin actively reconfigures DNA by introducing global positive
RT   writhe: implications for chromosome condensation.";
RL   Cell 98:239-248(1999).
CC   -!- FUNCTION: Regulatory subunit 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 topoisomerase. {ECO:0000269|PubMed:10428035,
CC       ECO:0000269|PubMed:9774278}.
CC   -!- SUBUNIT: Component of the condensin complex, which contains the XCAP-
CC       E/SMC2 and XCAP-C/SMC4 heterodimer, and three non SMC subunits that
CC       probably regulate the complex: XCAP-H/NCAPH, XCAP-D2/NCAPD2 and XCAP-
CC       G/NCAPG. {ECO:0000269|PubMed:9160743}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the
CC       condensin complex is found in the cytoplasm, while a minority of the
CC       complex is associated with chromatin. A subpopulation of the complex
CC       however remains associated with chromosome foci in interphase cells.
CC       During mitosis, most of the condensin complex is associated with the
CC       chromatin. At the onset of prophase, the regulatory subunits of the
CC       complex are phosphorylated by CDK1, leading to condensin's association
CC       with chromosome arms and to chromosome condensation. Dissociation from
CC       chromosomes is observed in late telophase (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC       XCAP-D2 and XCAP-G subunits, activates the condensin complex and is
CC       required for chromosome condensation. {ECO:0000269|PubMed:9774278}.
CC   -!- SIMILARITY: Belongs to the CND2 (condensin subunit 2) family.
CC       {ECO:0000305}.
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DR   EMBL; U90125; AAC60203.1; -; mRNA.
DR   RefSeq; NP_001081818.1; NM_001088349.1.
DR   AlphaFoldDB; O13067; -.
DR   BioGRID; 99404; 2.
DR   DNASU; 398069; -.
DR   GeneID; 398069; -.
DR   KEGG; xla:398069; -.
DR   CTD; 398069; -.
DR   Xenbase; XB-GENE-5738491; ncaph.S.
DR   OrthoDB; 702078at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   GO; GO:0000796; C:condensin complex; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR   InterPro; IPR022816; Condensin_barren_su2.
DR   PANTHER; PTHR13108; PTHR13108; 1.
DR   Pfam; PF05786; Cnd2; 1.
DR   PIRSF; PIRSF017126; Condensin_H; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromosome; Cytoplasm;
KW   Direct protein sequencing; DNA condensation; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..699
FT                   /note="Condensin complex subunit 2"
FT                   /id="PRO_0000095040"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        233
FT                   /note="K -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   699 AA;  77778 MW;  71B7B671A4F415A5 CRC64;
     MSTSTPQSGG RRKPETPDSA FLSPATRPQP ISAAATPTLL NFTSNDDERE RKLRRMSRVI
     DLQLSNANSP ATAISPAQSR GADTPTSLLP KLNNTQISDH YSTCIKLSQE NKITTKNAFG
     LHLIDYMGDI LKHKDSELTN FKVAAGTLDA SAKIYAVRVD AVHADVYKVL GGLGKESQAT
     EDTENQETDT GPQDGRKNPK RRKCSYKTIE RNLNSINRSE TERKSEIDPL FQKAAASFDE
     FSTAGVFLST LKCHSYHSEL HFDADVKPLS TAEETEPPSP GSMDSTELKS LFLQCVEKRP
     LCPSLSGFRF MQWNSDAQNE NLSLLMDKFK KSDHVFDINA EVEDDFVESE APVADEFDAD
     VCEGMDAGDI GEFAEHREAC RLERKGAQLT QIGNGDIGTM CLQLSSCPGE YSYFSPRTMS
     MWAGPEHWRF RPRQKASTDS DQQRVKKAKK VFELNFEDDI DFEVHFRKTR AATTLTKSTL
     ESQNKKSTTL PADFHYDPDN IARMSLRPKD RIRKTTVQES VSEPEDDIGD YDYNNPNDTS
     NFCPALQAAD SDDDDGAFLG PESNSAGFSA ENQMNITSYG ESNLVAGQKV NKIEIQYAKT
     AKKMDMKRLK SSMWSLLANC PESQEEMPSS KEEIDAALIT DEQVFSSVTH GLQKRLPPVM
     AQNLSVPLAF ACLLHLANEK NLKLQGMDDL SDVMIMQDD
 
 
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