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CHP2_SCHPO
ID   CHP2_SCHPO              Reviewed;         380 AA.
AC   O42934;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Chromo domain-containing protein 2;
GN   Name=chp2; ORFNames=SPBC16C6.10;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=10835380; DOI=10.1093/genetics/155.2.551;
RA   Thon G., Verhein-Hansen J.;
RT   "Four chromo-domain proteins of Schizosaccharomyces pombe differentially
RT   repress transcription at various chromosomal locations.";
RL   Genetics 155:551-568(2000).
CC   -!- FUNCTION: Component of the kinetochore which plays a role in
CC       stabilizing microtubules and so allowing accurate chromosome
CC       segregation. {ECO:0000269|PubMed:10835380}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; CU329671; CAA16917.1; -; Genomic_DNA.
DR   PIR; T39561; T39561.
DR   RefSeq; NP_596808.1; NM_001023829.2.
DR   PDB; 6FTO; X-ray; 1.60 A; A/B=315-380.
DR   PDBsum; 6FTO; -.
DR   AlphaFoldDB; O42934; -.
DR   SMR; O42934; -.
DR   BioGRID; 276585; 13.
DR   STRING; 4896.SPBC16C6.10.1; -.
DR   iPTMnet; O42934; -.
DR   PaxDb; O42934; -.
DR   PRIDE; O42934; -.
DR   EnsemblFungi; SPBC16C6.10.1; SPBC16C6.10.1:pep; SPBC16C6.10.
DR   GeneID; 2540047; -.
DR   KEGG; spo:SPBC16C6.10; -.
DR   PomBase; SPBC16C6.10; chp2.
DR   VEuPathDB; FungiDB:SPBC16C6.10; -.
DR   eggNOG; KOG1911; Eukaryota.
DR   HOGENOM; CLU_727924_0_0_1; -.
DR   InParanoid; O42934; -.
DR   OMA; GMEENSW; -.
DR   PhylomeDB; O42934; -.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:O42934; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; TAS:PomBase.
DR   GO; GO:0031934; C:mating-type region heterochromatin; TAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0110129; C:SHREC2 complex; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; EXP:PomBase.
DR   GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR   GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR   GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:PomBase.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:PomBase.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:PomBase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR008251; Chromo_shadow_dom.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF01393; Chromo_shadow; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00300; ChSh; 1.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Chromo domain-containing protein 2"
FT                   /id="PRO_0000080239"
FT   DOMAIN          176..238
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   REGION          14..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            325..327
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   STRAND          328..336
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   STRAND          342..348
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   HELIX           358..364
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   HELIX           366..374
FT                   /evidence="ECO:0007829|PDB:6FTO"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:6FTO"
SQ   SEQUENCE   380 AA;  42955 MW;  A2D96BD5987807C4 CRC64;
     MVKSADLDLM NSIISESDEN FSPPPFTVEE AENSINNKSS TASLESPQNG SWHPSLYGLS
     VPEKTHIQNS LDLYSHGNSG SQKTHNVSFS CEIRKVKSSK LSPISNMEDS EDKKEEDESS
     SYKNEFKSSS SASVSSNFEK TSGSDDHNSQ SPVPLNEGFE YIASSGSEDK NSDEEFAVEM
     ILDSRMKKDG SGFQYYLKWE GYDDPSDNTW NDEEDCAGCL ELIDAYWESR GGKPDLSSLI
     RLTRSRARSS NEASYVEKDE SSNSDDSISY KRRRSRNAAN RITDYVDSDL SESSMKEKQS
     KIEKYMKSDK SSKNFKPPFQ KKSWEDLVDC VKTVQQLDNG KLIAKIKWKN GYVSTHDNII
     IHQKCPLKII EYYEAHIKFT
 
 
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