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RCC1_DROME
ID   RCC1_DROME              Reviewed;         547 AA.
AC   P25171; A4V1J1; Q9VRR5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Regulator of chromosome condensation;
DE   AltName: Full=Chromatin-binding protein Bj1;
DE   AltName: Full=Regulator of chromosome condensation 1 ortholog;
GN   Name=Rcc1; Synonyms=Bj1; ORFNames=CG10480;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2022188; DOI=10.1002/j.1460-2075.1991.tb08064.x;
RA   Frasch M.;
RT   "The maternally expressed Drosophila gene encoding the chromatin-binding
RT   protein BJ1 is a homolog of the vertebrate gene Regulator of Chromatin
RT   Condensation, RCC1.";
RL   EMBO J. 10:1225-1236(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=2022190; DOI=10.1002/j.1460-2075.1991.tb08068.x;
RA   Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L.,
RA   Sprague G.F. Jr., Frasch M., Nishimoto T.;
RT   "Mutation of the hamster cell cycle gene RCC1 is complemented by the
RT   homologous genes of Drosophila and S.cerevisiae.";
RL   EMBO J. 10:1265-1273(1991).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12121620; DOI=10.1016/s0960-9822(02)00934-x;
RA   Trieselmann N., Wilde A.;
RT   "Ran localizes around the microtubule spindle in vivo during mitosis in
RT   Drosophila embryos.";
RL   Curr. Biol. 12:1124-1129(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; THR-512; SER-526 AND
RP   THR-531, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Promotes the exchange of Ran-bound GDP by GTP. Involved in
CC       the regulation of onset of chromosome condensation in the S phase.
CC       Binds to chromatin. {ECO:0000269|PubMed:2022190}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Becomes dispersed
CC       throughout the cytoplasm during mitosis. Is associated with chromatin
CC       throughout mitosis.
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DR   EMBL; X58530; CAA41417.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF50726.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF50727.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN12235.1; -; Genomic_DNA.
DR   EMBL; AY070540; AAL48011.1; -; mRNA.
DR   PIR; S15028; S15028.
DR   RefSeq; NP_523943.1; NM_079219.3.
DR   RefSeq; NP_729118.1; NM_168151.3.
DR   RefSeq; NP_729119.1; NM_168152.3.
DR   PDB; 3MVD; X-ray; 2.90 A; K/L=2-422.
DR   PDBsum; 3MVD; -.
DR   AlphaFoldDB; P25171; -.
DR   SMR; P25171; -.
DR   BioGRID; 64129; 13.
DR   DIP; DIP-17766N; -.
DR   IntAct; P25171; 6.
DR   STRING; 7227.FBpp0076782; -.
DR   iPTMnet; P25171; -.
DR   PaxDb; P25171; -.
DR   PRIDE; P25171; -.
DR   DNASU; 38669; -.
DR   EnsemblMetazoa; FBtr0077074; FBpp0076782; FBgn0002638.
DR   EnsemblMetazoa; FBtr0077075; FBpp0076783; FBgn0002638.
DR   EnsemblMetazoa; FBtr0077076; FBpp0076784; FBgn0002638.
DR   GeneID; 38669; -.
DR   KEGG; dme:Dmel_CG10480; -.
DR   CTD; 1104; -.
DR   FlyBase; FBgn0002638; Rcc1.
DR   VEuPathDB; VectorBase:FBgn0002638; -.
DR   eggNOG; KOG1426; Eukaryota.
DR   GeneTree; ENSGT00940000174254; -.
DR   HOGENOM; CLU_005210_6_1_1; -.
DR   InParanoid; P25171; -.
DR   OMA; WSWGTND; -.
DR   OrthoDB; 1062377at2759; -.
DR   PhylomeDB; P25171; -.
DR   Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   SignaLink; P25171; -.
DR   BioGRID-ORCS; 38669; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Rcc1; fly.
DR   GenomeRNAi; 38669; -.
DR   PRO; PR:P25171; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0002638; Expressed in cleaving embryo and 47 other tissues.
DR   Genevisible; P25171; DM.
DR   GO; GO:0000793; C:condensed chromosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:FlyBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
DR   GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:FlyBase.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:FlyBase.
DR   GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR   Gene3D; 2.130.10.30; -; 1.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   Pfam; PF00415; RCC1; 4.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; SSF50985; 1.
DR   PROSITE; PS00625; RCC1_1; 1.
DR   PROSITE; PS00626; RCC1_2; 2.
DR   PROSITE; PS50012; RCC1_3; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..547
FT                   /note="Regulator of chromosome condensation"
FT                   /id="PRO_0000206633"
FT   REPEAT          41..91
FT                   /note="RCC1 1"
FT   REPEAT          92..143
FT                   /note="RCC1 2"
FT   REPEAT          145..195
FT                   /note="RCC1 3"
FT   REPEAT          197..257
FT                   /note="RCC1 4"
FT   REPEAT          260..310
FT                   /note="RCC1 5"
FT   REPEAT          311..362
FT                   /note="RCC1 6"
FT   REPEAT          363..416
FT                   /note="RCC1 7"
FT   REPEAT          417..454
FT                   /note="Bj1 1"
FT   REPEAT          455..489
FT                   /note="Bj1 2"
FT   REPEAT          490..519
FT                   /note="Bj1 3"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          423..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         286
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         512
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         531
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        490
FT                   /note="V -> A (in Ref. 1; CAA41417)"
FT                   /evidence="ECO:0000305"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          83..90
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          135..142
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          156..163
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          187..194
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          199..203
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   TURN            215..219
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   TURN            223..229
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          243..249
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          252..257
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   TURN            258..260
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          282..290
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          294..300
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          302..309
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          314..318
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          334..339
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          347..353
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          356..361
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          377..382
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          385..390
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   TURN            394..398
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          401..406
FT                   /evidence="ECO:0007829|PDB:3MVD"
FT   STRAND          408..416
FT                   /evidence="ECO:0007829|PDB:3MVD"
SQ   SEQUENCE   547 AA;  58851 MW;  77D9744EBAF4597A CRC64;
     MPRRKALTNN NNAGEAEQQP PKAKRARIAF HLELPKRRTV LGNVLVCGNG DVGQLGLGED
     ILERKRLSPV AGIPDAVDIS AGGMHNLVLT KSGDIYSFGC NDEGALGRDT SEDGSESKPD
     LIDLPGKALC ISAGDSHSAC LLEDGRVFAW GSFRDSHGNM GLTIDGNKRT PIDLMEGTVC
     CSIASGADHL VILTTAGKVF TVGCAEQGQL GRLSERSISG EGRRGKRDLL RPTQLIITRA
     KPFEAIWATN YCTFMRESQT QVIWATGLNN FKQLAHETKG KEFALTPIKT ELKDIRHIAG
     GQHHTVILTT DLKCSVVGRP EYGRLGLGDV KDVVEKPTIV KKLTEKIVSV GCGEVCSYAV
     TIDGKLYSWG SGVNNQLGVG DGDDELEPIV VVSKNTQGKH MLLASGGGQH AIFLVKADKQ
     DQKENVPVKV SGSSSISKKD KTPPQDNVDK EAENVDKQEQ KENLPAKAST SSKKNKTPPQ
     DNADKEAENV DKQEQKENLP AKASTSSKKI KTPPQDDAAE EVEEESAQEP TPKKAKKPAA
     KRGGKKT
 
 
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