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Protein

Regulator of chromosome condensation

Gene

Rcc1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes the exchange of Ran-bound GDP by GTP. Involved in the regulation of onset of chromosome condensation in the S phase. Binds to chromatin.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • Ran guanyl-nucleotide exchange factor activity Source: FlyBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • central nervous system development Source: UniProtKB
  • mitotic chromosome condensation Source: FlyBase
  • neurogenesis Source: FlyBase
  • NLS-bearing protein import into nucleus Source: FlyBase
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of neurogenesis Source: FlyBase
  • regulation of nucleocytoplasmic transport Source: FlyBase
  • ventral cord development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of chromosome condensation
Alternative name(s):
Chromatin-binding protein Bj1
Regulator of chromosome condensation 1 ortholog
Gene namesi
Name:Rcc1
Synonyms:Bj1
ORF Names:CG10480
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002638. Rcc1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Becomes dispersed throughout the cytoplasm during mitosis. Is associated with chromatin throughout mitosis.

GO - Cellular componenti

  • condensed chromosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Regulator of chromosome condensationPRO_0000206633Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Phosphothreonine1 Publication
Modified residuei512 – 5121Phosphothreonine1 Publication
Modified residuei526 – 5261Phosphoserine1 Publication
Modified residuei531 – 5311Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25171.

PTM databases

iPTMnetiP25171.

Expressioni

Gene expression databases

BgeeiP25171.
GenevisibleiP25171. DM.

Interactioni

Protein-protein interaction databases

BioGridi64129. 10 interactions.
DIPiDIP-17766N.
IntActiP25171. 5 interactions.
MINTiMINT-781282.
STRINGi7227.FBpp0076782.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 498Combined sources
Beta strandi63 – 697Combined sources
Beta strandi74 – 818Combined sources
Beta strandi83 – 908Combined sources
Beta strandi95 – 995Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi180 – 1856Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi199 – 2035Combined sources
Turni215 – 2195Combined sources
Turni223 – 2297Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi243 – 2497Combined sources
Beta strandi252 – 2576Combined sources
Turni258 – 2603Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi282 – 2909Combined sources
Beta strandi294 – 3007Combined sources
Beta strandi302 – 3098Combined sources
Beta strandi314 – 3185Combined sources
Helixi321 – 3233Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi334 – 3396Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi356 – 3616Combined sources
Beta strandi366 – 3705Combined sources
Beta strandi377 – 3826Combined sources
Beta strandi385 – 3906Combined sources
Turni394 – 3985Combined sources
Beta strandi401 – 4066Combined sources
Beta strandi408 – 4169Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MVDX-ray2.90K/L2-422[»]
ProteinModelPortaliP25171.
SMRiP25171. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati41 – 9151RCC1 1Add
BLAST
Repeati92 – 14352RCC1 2Add
BLAST
Repeati145 – 19551RCC1 3Add
BLAST
Repeati197 – 25761RCC1 4Add
BLAST
Repeati260 – 31051RCC1 5Add
BLAST
Repeati311 – 36252RCC1 6Add
BLAST
Repeati363 – 41654RCC1 7Add
BLAST
Repeati417 – 45438Bj1 1Add
BLAST
Repeati455 – 48935Bj1 2Add
BLAST
Repeati490 – 51930Bj1 3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi520 – 54728Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
InParanoidiP25171.
KOiK11493.
OMAiSQTEVIW.
OrthoDBiEOG7HQN8F.
PhylomeDBiP25171.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamiPF00415. RCC1. 4 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRRKALTNN NNAGEAEQQP PKAKRARIAF HLELPKRRTV LGNVLVCGNG
60 70 80 90 100
DVGQLGLGED ILERKRLSPV AGIPDAVDIS AGGMHNLVLT KSGDIYSFGC
110 120 130 140 150
NDEGALGRDT SEDGSESKPD LIDLPGKALC ISAGDSHSAC LLEDGRVFAW
160 170 180 190 200
GSFRDSHGNM GLTIDGNKRT PIDLMEGTVC CSIASGADHL VILTTAGKVF
210 220 230 240 250
TVGCAEQGQL GRLSERSISG EGRRGKRDLL RPTQLIITRA KPFEAIWATN
260 270 280 290 300
YCTFMRESQT QVIWATGLNN FKQLAHETKG KEFALTPIKT ELKDIRHIAG
310 320 330 340 350
GQHHTVILTT DLKCSVVGRP EYGRLGLGDV KDVVEKPTIV KKLTEKIVSV
360 370 380 390 400
GCGEVCSYAV TIDGKLYSWG SGVNNQLGVG DGDDELEPIV VVSKNTQGKH
410 420 430 440 450
MLLASGGGQH AIFLVKADKQ DQKENVPVKV SGSSSISKKD KTPPQDNVDK
460 470 480 490 500
EAENVDKQEQ KENLPAKAST SSKKNKTPPQ DNADKEAENV DKQEQKENLP
510 520 530 540
AKASTSSKKI KTPPQDDAAE EVEEESAQEP TPKKAKKPAA KRGGKKT
Length:547
Mass (Da):58,851
Last modified:June 1, 2001 - v2
Checksum:i77D9744EBAF4597A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti490 – 4901V → A in CAA41417 (PubMed:2022188).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58530 Genomic DNA. Translation: CAA41417.1.
AE014296 Genomic DNA. Translation: AAF50726.1.
AE014296 Genomic DNA. Translation: AAF50727.1.
AE014296 Genomic DNA. Translation: AAN12235.1.
AY070540 mRNA. Translation: AAL48011.1.
PIRiS15028.
RefSeqiNP_523943.1. NM_079219.3.
NP_729118.1. NM_168151.3.
NP_729119.1. NM_168152.3.
UniGeneiDm.8023.

Genome annotation databases

EnsemblMetazoaiFBtr0077074; FBpp0076782; FBgn0002638.
FBtr0077075; FBpp0076783; FBgn0002638.
FBtr0077076; FBpp0076784; FBgn0002638.
GeneIDi38669.
KEGGidme:Dmel_CG10480.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58530 Genomic DNA. Translation: CAA41417.1.
AE014296 Genomic DNA. Translation: AAF50726.1.
AE014296 Genomic DNA. Translation: AAF50727.1.
AE014296 Genomic DNA. Translation: AAN12235.1.
AY070540 mRNA. Translation: AAL48011.1.
PIRiS15028.
RefSeqiNP_523943.1. NM_079219.3.
NP_729118.1. NM_168151.3.
NP_729119.1. NM_168152.3.
UniGeneiDm.8023.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MVDX-ray2.90K/L2-422[»]
ProteinModelPortaliP25171.
SMRiP25171. Positions 1-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64129. 10 interactions.
DIPiDIP-17766N.
IntActiP25171. 5 interactions.
MINTiMINT-781282.
STRINGi7227.FBpp0076782.

PTM databases

iPTMnetiP25171.

Proteomic databases

PaxDbiP25171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077074; FBpp0076782; FBgn0002638.
FBtr0077075; FBpp0076783; FBgn0002638.
FBtr0077076; FBpp0076784; FBgn0002638.
GeneIDi38669.
KEGGidme:Dmel_CG10480.

Organism-specific databases

CTDi1104.
FlyBaseiFBgn0002638. Rcc1.

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
InParanoidiP25171.
KOiK11493.
OMAiSQTEVIW.
OrthoDBiEOG7HQN8F.
PhylomeDBiP25171.

Miscellaneous databases

GenomeRNAii38669.
PROiP25171.

Gene expression databases

BgeeiP25171.
GenevisibleiP25171. DM.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
PfamiPF00415. RCC1. 4 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The maternally expressed Drosophila gene encoding the chromatin-binding protein BJ1 is a homolog of the vertebrate gene Regulator of Chromatin Condensation, RCC1."
    Frasch M.
    EMBO J. 10:1225-1236(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Mutation of the hamster cell cycle gene RCC1 is complemented by the homologous genes of Drosophila and S.cerevisiae."
    Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L., Sprague G.F. Jr., Frasch M., Nishimoto T.
    EMBO J. 10:1265-1273(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Ran localizes around the microtubule spindle in vivo during mitosis in Drosophila embryos."
    Trieselmann N., Wilde A.
    Curr. Biol. 12:1124-1129(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; THR-512; SER-526 AND THR-531, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRCC1_DROME
AccessioniPrimary (citable) accession number: P25171
Secondary accession number(s): A4V1J1, Q9VRR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.