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CHP1_SCHPO
ID   CHP1_SCHPO              Reviewed;         960 AA.
AC   Q10103;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Chromo domain-containing protein 1 {ECO:0000303|PubMed:9722643};
GN   Name=chp1 {ECO:0000303|PubMed:9722643};
GN   ORFNames=SPAC18G6.02c {ECO:0000312|PomBase:SPAC18G6.02c};
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, AND SUBCELLULAR LOCATION.
RX   PubMed=9722643; DOI=10.1093/nar/26.18.4222;
RA   Doe C.L., Wang G., Chow C.-M., Fricker M.D., Singh P.B., Mellor E.J.;
RT   "The fission yeast chromo domain encoding gene chp1(+) is required for
RT   chromosome segregation and shows a genetic interaction with alpha-
RT   tubulin.";
RL   Nucleic Acids Res. 26:4222-4229(1998).
RN   [3]
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).
RN   [4]
RP   FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA   Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA   Moazed D.;
RT   "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT   noncoding centromeric RNAs.";
RL   Cell 119:789-802(2004).
RN   [5]
RP   FUNCTION, COMPOSITION OF THE RITS COMPLEX, AND INTERACTION WITH TAS3.
RX   PubMed=14704433; DOI=10.1126/science.1093686;
RA   Verdel A., Jia S., Gerber S., Sugiyama T., Gygi S.P., Grewal S.I.S.,
RA   Moazed D.;
RT   "RNAi-mediated targeting of heterochromatin by the RITS complex.";
RL   Science 303:672-676(2004).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [7]
RP   INTERACTION WITH DRI1.
RX   PubMed=33693625; DOI=10.1093/genetics/iyab032;
RA   Ban H., Sun W., Chen Y.H., Chen Y., Li F.;
RT   "Dri1 mediates heterochromatin assembly via RNAi and histone
RT   deacetylation.";
RL   Genetics 217:iyab032-iyab032(2021).
CC   -!- FUNCTION: Component of the kinetochore which plays a role in
CC       stabilizing microtubules and so allowing accurate chromosome
CC       segregation. Has a role in the RNA interference (RNAi) pathway which is
CC       important for heterochromatin formation and accurate chromosome
CC       segregation. A member of the RNA-induced transcriptional silencing
CC       (RITS) complex which is involved in the biosynthesis of dsRNA from
CC       primer siRNAs provided by the RNA-directed RNA polymerase (RDRC)
CC       complex. {ECO:0000269|PubMed:10835380, ECO:0000269|PubMed:14704433,
CC       ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:9722643}.
CC   -!- SUBUNIT: Ago1, chp1 and tas3 interact to form the core of the RNA-
CC       induced transcriptional silencing (RITS) complex. The RITS complex
CC       interacts with the RDRC complex via interaction between ago1 and hrr1.
CC       Clr4 has a role in mediating this interaction (PubMed:14704433).
CC       Interacts with dri1 (PubMed:33693625). {ECO:0000269|PubMed:14704433,
CC       ECO:0000269|PubMed:33693625}.
CC   -!- INTERACTION:
CC       Q10103; Q10426: rik1; NbExp=2; IntAct=EBI-421832, EBI-1111936;
CC       Q10103; O94687: tas3; NbExp=10; IntAct=EBI-421832, EBI-423002;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15607976,
CC       ECO:0000269|PubMed:9722643}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, spindle pole body {ECO:0000269|PubMed:9722643}.
CC       Note=Associates with telomeric and mating-type region heterochromatin
CC       (PubMed:15607976).
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DR   EMBL; CU329670; CAA92382.1; -; Genomic_DNA.
DR   PIR; T37916; T37916.
DR   RefSeq; NP_593666.1; NM_001019098.2.
DR   PDB; 2RSN; NMR; -; A=1-75.
DR   PDB; 3G7L; X-ray; 2.20 A; A=15-75.
DR   PDB; 3TIX; X-ray; 2.90 A; B/D=504-960.
DR   PDBsum; 2RSN; -.
DR   PDBsum; 3G7L; -.
DR   PDBsum; 3TIX; -.
DR   AlphaFoldDB; Q10103; -.
DR   BMRB; Q10103; -.
DR   SMR; Q10103; -.
DR   BioGRID; 278711; 120.
DR   DIP; DIP-29301N; -.
DR   IntAct; Q10103; 5.
DR   STRING; 4896.SPAC18G6.02c.1; -.
DR   iPTMnet; Q10103; -.
DR   MaxQB; Q10103; -.
DR   PaxDb; Q10103; -.
DR   PRIDE; Q10103; -.
DR   EnsemblFungi; SPAC18G6.02c.1; SPAC18G6.02c.1:pep; SPAC18G6.02c.
DR   GeneID; 2542239; -.
DR   KEGG; spo:SPAC18G6.02c; -.
DR   PomBase; SPAC18G6.02c; chp1.
DR   VEuPathDB; FungiDB:SPAC18G6.02c; -.
DR   eggNOG; KOG1911; Eukaryota.
DR   HOGENOM; CLU_307797_0_0_1; -.
DR   InParanoid; Q10103; -.
DR   OMA; WYDNTWE; -.
DR   Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR   EvolutionaryTrace; Q10103; -.
DR   PRO; PR:Q10103; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0034507; C:chromosome, centromeric outer repeat region; IDA:PomBase.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0030958; C:RITS complex; IDA:PomBase.
DR   GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR   GO; GO:0042393; F:histone binding; IDA:PomBase.
DR   GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
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; TAS:PomBase.
DR   IDEAL; IID50149; -.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Chromosome partition; Cytoplasm; Cytoskeleton;
KW   DNA-binding; Nucleus; Reference proteome; RNA-mediated gene silencing.
FT   CHAIN           1..960
FT                   /note="Chromo domain-containing protein 1"
FT                   /id="PRO_0000080238"
FT   DOMAIN          22..74
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:2RSN"
FT   STRAND          21..32
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:2RSN"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:2RSN"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:3G7L"
FT   STRAND          519..526
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   TURN            527..530
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          531..539
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           541..544
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           550..558
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          566..569
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           570..576
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          582..587
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          589..595
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           596..606
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          608..613
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          618..623
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           627..632
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          641..648
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           653..660
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           675..682
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   TURN            687..691
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           692..694
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          696..701
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           707..718
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          723..727
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           731..734
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          736..744
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           745..747
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   TURN            748..750
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           751..753
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           757..762
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          766..771
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          804..808
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          812..816
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           818..823
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           827..837
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   TURN            838..841
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          842..846
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           850..861
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           867..882
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          889..891
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           894..896
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           903..918
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   TURN            919..921
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          923..928
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           932..934
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   STRAND          941..944
FT                   /evidence="ECO:0007829|PDB:3TIX"
FT   HELIX           946..952
FT                   /evidence="ECO:0007829|PDB:3TIX"
SQ   SEQUENCE   960 AA;  108726 MW;  E92C16BBD0D5957C CRC64;
     MVSVKPLPDI DSNEGETDAD VYEVEDILAD RVNKNGINEY YIKWAGYDWY DNTWEPEQNL
     FGAEKVLKKW KKRKKLIAKG LLEPFDAEDN EAKKMKREKE ILRQQRQKRK SELTQLSQKV
     KEKFKKMRKK PARRIVTIAN DEEEEDDQTM DEDAFERKSM QGELKERNLT DKTSTLSTSF
     GETSPDVNPF YLSEWPTVTD SILLSKSLSS DAIPLKNGEI KSTMLMPSDS DNSVPGIQNS
     NNLENTGAFV ENANSPQSNT PLSTFRHSSP LSLSPVITSD NDVANSLFFS NSTPLPSSLK
     IKKEAPKLET HTILVSDNSG SLTKQDILSY FAFIKGNIEV FFLKSPKKDK VCNMAYIQFD
     SIEQAKLAYD KGHPSWHVTL VKGKISTDME ECKVSKSILK TTPSKKANAR SVSFTQTTTD
     TLSESEKFAS NVDLDENFDF NVNVTNEDAK QLKKSVIGSS WTTVNNDWNS VSKSDQTFEN
     DGASKVVPAG NITLNSDNSL HHSISESEDL SSASTLSDYF RFVLRVGKSL YYAGELSFDI
     SKLKAETEHQ QLLRSLVSCK QVDVLRFVTS QYLEVFGTCL TKVLSGSLCI RSDVDMTHFK
     NILNRGNGAG IVLGSNYTLL LFTEDNNALM NLYDCQGQSN SPFWMVIFEP LESILVEWSA
     KNLRPKKPYH KSQSYLSYLL QLGHIDLHKI GAFQATQILI VSKQPSPEAE ELEDTFREAA
     IPTFRGLEIP ESLFLSQNVF VFLNVSLEDD FDQLQFLTLA KRKSCKFFLF GLSLPLKSPN
     DSHVGTDFKK NNEPLDKLTY SQYLRPMFPK GGVVSVTLSA LIKTPRLLEL ISPFLEIKKD
     SWILILPPSI VDMVKSYFVT NNPDKSLLEI QNLLNTLQRY LTNPALKNVT LYQDWDIVID
     DSADVSLAST LQLYQKKNYD KYRRFVLIHE LKNELTPVNG LDIVDYDEFK ETFMRAIGLK
 
 
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