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Regulator of chromosome condensation (Cell cycle regulatory protein) (Chromosome condensation protein 1)

 RCC1_HUMAN              Reviewed;         421 AA.
P18754; Q16269; Q6NT97;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 191.
RecName: Full=Regulator of chromosome condensation;
AltName: Full=Cell cycle regulatory protein;
AltName: Full=Chromosome condensation protein 1;
Name=RCC1; Synonyms=CHC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3678831; DOI=10.1101/gad.1.6.585;
Ohtsubo M., Kai R., Furuno N., Sekiguchi T., Sekiguchi M.,
Hayashida H., Kuma K., Miyata T., Fukushige S., Murotsu T.,
Matsubara K., Nishimoto T.;
"Isolation and characterization of the active cDNA of the human cell
cycle gene (RCC1) involved in the regulation of onset of chromosome
condensation.";
Genes Dev. 1:585-593(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1769659;
Furuno N., Nakagawa K., Eguchi U., Ohtsubo M., Nishimoto T., Soeda E.;
"Complete nucleotide sequence of the human RCC1 gene involved in
coupling between DNA replication and mitosis.";
Genomics 11:459-461(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, Mammary gland, Muscle, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-33 (ISOFORM 2), AND ALTERNATIVE
SPLICING.
PubMed=7983178;
Miyabashira J., Sekiguchi T., Nishimoto T.;
"Mammalian cells have two functional RCC1 proteins produced by
alternative splicing.";
J. Cell Sci. 107:2203-2208(1994).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=2236072; DOI=10.1073/pnas.87.21.8617;
Bischoff F.R., Maier G., Tilz G., Ponstingl H.;
"A 47-kDa human nuclear protein recognized by antikinetochore
autoimmune sera is homologous with the protein encoded by RCC1, a gene
implicated in onset of chromosome condensation.";
Proc. Natl. Acad. Sci. U.S.A. 87:8617-8621(1990).
[7]
FUNCTION.
PubMed=1944575; DOI=10.1038/354080a0;
Bischoff F.R., Ponstingl H.;
"Catalysis of guanine nucleotide exchange on Ran by the mitotic
regulator RCC1.";
Nature 354:80-82(1991).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
INTERACTION WITH ARRB2.
PubMed=16820410; DOI=10.1242/jcs.03046;
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.;
"Novel function of beta-arrestin2 in the nucleus of mature
spermatozoa.";
J. Cell Sci. 119:3047-3056(2006).
[10]
CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION,
HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2,
METHYLATION AT SER-2, AND MUTAGENESIS OF SER-2; PRO-3; LYS-4 AND
ASP-182.
PubMed=17435751; DOI=10.1038/ncb1572;
Chen T., Muratore T.L., Schaner-Tooley C.E., Shabanowitz J.,
Hunt D.F., Macara I.G.;
"N-terminal alpha-methylation of RCC1 is necessary for stable
chromatin association and normal mitosis.";
Nat. Cell Biol. 9:596-603(2007).
[11]
METHYLATION AT SER-2.
PubMed=18762580; DOI=10.1083/jcb.200803110;
Hao Y., Macara I.G.;
"Regulation of chromatin binding by a conformational switch in the
tail of the Ran exchange factor RCC1.";
J. Cell Biol. 182:827-836(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT SER-2, AND
MUTAGENESIS OF LYS-4.
PubMed=20668449; DOI=10.1038/nature09343;
Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
"NRMT is an alpha-N-methyltransferase that methylates RCC1 and
retinoblastoma protein.";
Nature 466:1125-1128(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-421.
PubMed=9510255; DOI=10.1038/32204;
Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M.,
Wittinghofer A.;
"The 1.7-A crystal structure of the regulator of chromosome
condensation (RCC1) reveals a seven-bladed propeller.";
Nature 392:97-101(1998).
[20]
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 20-421 IN COMPLEX WITH RAN.
PubMed=11336674; DOI=10.1016/S0092-8674(01)00315-4;
Renault L., Kuhlmann J., Henkel A., Wittinghofer A.;
"Structural basis for guanine nucleotide exchange on Ran by the
regulator of chromosome condensation (RCC1).";
Cell 105:245-255(2001).
-!- FUNCTION: Guanine-nucleotide releasing factor that promotes the
exchange of Ran-bound GDP by GTP. Involved in the regulation of
onset of chromosome condensation in the S phase. Binds both to the
nucleosomes and double-stranded DNA. RCC1-Ran complex (together
with other proteins) acts as a component of a signal transmission
pathway that detects unreplicated DNA. Plays a key role in nucleo-
cytoplasmic transport, mitosis and nuclear-envelope assembly.
{ECO:0000269|PubMed:1944575}.
-!- SUBUNIT: Interacts with ARRB2; the interaction is detected in the
nucleus upon OR1D2 stimulation. {ECO:0000269|PubMed:11336674,
ECO:0000269|PubMed:16820410, ECO:0000269|PubMed:17435751}.
-!- INTERACTION:
P02281:- (xeno); NbExp=2; IntAct=EBI-992720, EBI-1251201;
Q9BV86:NTMT1; NbExp=4; IntAct=EBI-992720, EBI-373016;
P62826:RAN; NbExp=6; IntAct=EBI-992720, EBI-286642;
Q9H6Z4:RANBP3; NbExp=2; IntAct=EBI-992720, EBI-992681;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17435751}.
Cytoplasm {ECO:0000269|PubMed:17435751}. Note=Becomes dispersed
throughout the cytoplasm during mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P18754-1; Sequence=Displayed;
Name=2; Synonyms=RCC1-I;
IsoId=P18754-2; Sequence=VSP_041122;
-!- PTM: N-terminal methylation by METTL11A/NTM1 is required for
binding double-stranded DNA and stable chromatin association.
Di- and trimethylation produce a permanent positive charge on the
amino group, which facilitates electrostatic binding to the
phosphate groups on DNA, while inhibiting histone-binding.
Methylated tail helps retain RCC1 on chromosomes during nucleotide
exchange on Ran. {ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:18762580, ECO:0000269|PubMed:20668449}.
-!- MISCELLANEOUS: Patients with Raynaud disease produce antibodies
that bind to RCC1.
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EMBL; X12654; CAA31182.1; -; mRNA.
EMBL; X06130; CAA29496.1; -; mRNA.
EMBL; D00591; BAA00469.1; -; Genomic_DNA.
EMBL; AF498924; AAM21072.1; -; mRNA.
EMBL; BC007300; AAH07300.1; -; mRNA.
EMBL; BC010067; AAH10067.1; -; mRNA.
EMBL; BC036903; AAH36903.1; -; mRNA.
EMBL; BC069198; AAH69198.1; -; mRNA.
EMBL; S75708; AAB32653.1; -; mRNA.
CCDS; CCDS323.1; -. [P18754-1]
CCDS; CCDS41295.1; -. [P18754-2]
PIR; A26691; A26691.
RefSeq; NP_001041659.1; NM_001048194.2. [P18754-2]
RefSeq; NP_001041660.1; NM_001048195.2.
RefSeq; NP_001041664.1; NM_001048199.2. [P18754-1]
RefSeq; NP_001260.1; NM_001269.4. [P18754-1]
UniGene; Hs.469723; -.
PDB; 1A12; X-ray; 1.70 A; A/B/C=9-421.
PDB; 1I2M; X-ray; 1.76 A; B/D=20-421.
PDB; 5E1B; X-ray; 1.65 A; D/E=2-7.
PDB; 5E1D; X-ray; 1.45 A; D/E=3-7.
PDB; 5E1M; X-ray; 1.75 A; D/E=3-7.
PDB; 5E1O; X-ray; 2.00 A; D/E=3-7.
PDB; 5E2A; X-ray; 1.75 A; D/E=3-7.
PDB; 5E2B; X-ray; 1.95 A; D/E=3-7.
PDB; 5TBK; X-ray; 3.45 A; I/J/K/L/M/N/O/P=1-421.
PDBsum; 1A12; -.
PDBsum; 1I2M; -.
PDBsum; 5E1B; -.
PDBsum; 5E1D; -.
PDBsum; 5E1M; -.
PDBsum; 5E1O; -.
PDBsum; 5E2A; -.
PDBsum; 5E2B; -.
PDBsum; 5TBK; -.
ProteinModelPortal; P18754; -.
SMR; P18754; -.
BioGrid; 107529; 101.
DIP; DIP-35416N; -.
IntAct; P18754; 62.
MINT; MINT-240062; -.
iPTMnet; P18754; -.
PhosphoSitePlus; P18754; -.
SwissPalm; P18754; -.
BioMuta; RCC1; -.
DMDM; 132170; -.
EPD; P18754; -.
PeptideAtlas; P18754; -.
PRIDE; P18754; -.
TopDownProteomics; P18754-1; -. [P18754-1]
DNASU; 1104; -.
Ensembl; ENST00000373831; ENSP00000362937; ENSG00000180198. [P18754-2]
Ensembl; ENST00000373832; ENSP00000362938; ENSG00000180198. [P18754-1]
Ensembl; ENST00000373833; ENSP00000362939; ENSG00000180198. [P18754-1]
Ensembl; ENST00000398958; ENSP00000381931; ENSG00000180198. [P18754-1]
GeneID; 1104; -.
KEGG; hsa:1104; -.
UCSC; uc001bqf.3; human. [P18754-1]
CTD; 1104; -.
DisGeNET; 1104; -.
EuPathDB; HostDB:ENSG00000180198.15; -.
GeneCards; RCC1; -.
HGNC; HGNC:1913; RCC1.
HPA; CAB015413; -.
HPA; HPA027573; -.
HPA; HPA027574; -.
MIM; 179710; gene.
neXtProt; NX_P18754; -.
OpenTargets; ENSG00000180198; -.
PharmGKB; PA26449; -.
GeneTree; ENSGT00900000140783; -.
HOGENOM; HOG000234341; -.
HOVERGEN; HBG017712; -.
InParanoid; P18754; -.
KO; K11493; -.
OMA; EGTVCCS; -.
OrthoDB; EOG091G05E6; -.
PhylomeDB; P18754; -.
TreeFam; TF101139; -.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
ChiTaRS; RCC1; human.
EvolutionaryTrace; P18754; -.
GeneWiki; RCC1; -.
GenomeRNAi; 1104; -.
PRO; PR:P18754; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000180198; -.
CleanEx; HS_RCC1; -.
ExpressionAtlas; P18754; baseline and differential.
Genevisible; P18754; HS.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
GO; GO:0031491; F:nucleosome binding; IMP:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0008536; F:Ran GTPase binding; IDA:CAFA.
GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0043199; F:sulfate binding; IDA:CAFA.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA.
GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
GO; GO:0016032; P:viral process; TAS:Reactome.
Gene3D; 2.130.10.30; -; 1.
InterPro; IPR009091; RCC1/BLIP-II.
InterPro; IPR000408; Reg_chr_condens.
Pfam; PF00415; RCC1; 7.
PRINTS; PR00633; RCCNDNSATION.
SUPFAM; SSF50985; SSF50985; 1.
PROSITE; PS00625; RCC1_1; 1.
PROSITE; PS00626; RCC1_2; 4.
PROSITE; PS50012; RCC1_3; 7.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Guanine-nucleotide releasing factor; Methylation; Mitosis; Nucleus;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:20668449}.
CHAIN 2 421 Regulator of chromosome condensation.
/FTId=PRO_0000206628.
REPEAT 34 84 RCC1 1.
REPEAT 85 136 RCC1 2.
REPEAT 138 189 RCC1 3.
REPEAT 191 257 RCC1 4.
REPEAT 258 311 RCC1 5.
REPEAT 312 362 RCC1 6.
REPEAT 363 416 RCC1 7.
MOD_RES 2 2 N,N,N-trimethylserine; alternate.
{ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:18762580,
ECO:0000269|PubMed:20668449}.
MOD_RES 2 2 N,N-dimethylserine; alternate.
{ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:18762580,
ECO:0000269|PubMed:20668449}.
MOD_RES 2 2 N-methylserine; alternate.
{ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:18762580,
ECO:0000269|PubMed:20668449}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000269|PubMed:17435751}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 24 24 K -> KDTRAAASRRVPGARSCQGACGPSPPDQKTRP (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7983178}.
/FTId=VSP_041122.
MUTAGEN 2 2 S->A: Does not abolish N-terminal
methylation.
{ECO:0000269|PubMed:17435751}.
MUTAGEN 2 2 S->Q: Does not abolish N-terminal
methylation.
{ECO:0000269|PubMed:17435751}.
MUTAGEN 3 3 P->Q: Abolishes N-terminal methylation.
{ECO:0000269|PubMed:17435751}.
MUTAGEN 4 4 K->Q: Abolishes N-terminal methylation.
{ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:20668449}.
MUTAGEN 4 4 K->R: Stongly impairs N-terminal
methylation and subcellular localization.
{ECO:0000269|PubMed:17435751,
ECO:0000269|PubMed:20668449}.
MUTAGEN 182 182 D->A: Abolishes interaction with Ran and
chromosome localization.
{ECO:0000269|PubMed:17435751}.
STRAND 35 42 {ECO:0000244|PDB:1A12}.
STRAND 56 63 {ECO:0000244|PDB:1A12}.
STRAND 69 74 {ECO:0000244|PDB:1A12}.
STRAND 76 83 {ECO:0000244|PDB:1A12}.
STRAND 88 92 {ECO:0000244|PDB:1A12}.
HELIX 108 110 {ECO:0000244|PDB:1A12}.
STRAND 121 126 {ECO:0000244|PDB:1A12}.
STRAND 128 135 {ECO:0000244|PDB:1A12}.
STRAND 140 144 {ECO:0000244|PDB:1A12}.
STRAND 146 148 {ECO:0000244|PDB:1A12}.
STRAND 151 158 {ECO:0000244|PDB:1A12}.
STRAND 162 168 {ECO:0000244|PDB:1A12}.
STRAND 174 179 {ECO:0000244|PDB:1A12}.
STRAND 181 188 {ECO:0000244|PDB:1A12}.
STRAND 193 197 {ECO:0000244|PDB:1A12}.
STRAND 205 207 {ECO:0000244|PDB:1I2M}.
HELIX 208 210 {ECO:0000244|PDB:1A12}.
STRAND 212 214 {ECO:0000244|PDB:1A12}.
HELIX 216 219 {ECO:0000244|PDB:1A12}.
HELIX 220 224 {ECO:0000244|PDB:1A12}.
STRAND 242 248 {ECO:0000244|PDB:1A12}.
STRAND 251 256 {ECO:0000244|PDB:1A12}.
STRAND 261 265 {ECO:0000244|PDB:1A12}.
STRAND 280 285 {ECO:0000244|PDB:1A12}.
HELIX 287 289 {ECO:0000244|PDB:1A12}.
STRAND 296 301 {ECO:0000244|PDB:1A12}.
STRAND 303 310 {ECO:0000244|PDB:1A12}.
STRAND 315 319 {ECO:0000244|PDB:1A12}.
HELIX 322 324 {ECO:0000244|PDB:1A12}.
STRAND 328 331 {ECO:0000244|PDB:5TBK}.
STRAND 335 340 {ECO:0000244|PDB:1A12}.
STRAND 343 352 {ECO:0000244|PDB:1A12}.
STRAND 354 361 {ECO:0000244|PDB:1A12}.
STRAND 366 370 {ECO:0000244|PDB:1A12}.
STRAND 379 381 {ECO:0000244|PDB:1A12}.
STRAND 385 390 {ECO:0000244|PDB:1A12}.
TURN 394 398 {ECO:0000244|PDB:1A12}.
STRAND 399 406 {ECO:0000244|PDB:1A12}.
STRAND 408 417 {ECO:0000244|PDB:1A12}.
SEQUENCE 421 AA; 44969 MW; F6D225AF81928305 CRC64;
MSPKRIAKRR SPPADAIPKS KKVKVSHRSH STEPGLVLTL GQGDVGQLGL GENVMERKKP
ALVSIPEDVV QAEAGGMHTV CLSKSGQVYS FGCNDEGALG RDTSVEGSEM VPGKVELQEK
VVQVSAGDSH TAALTDDGRV FLWGSFRDNN GVIGLLEPMK KSMVPVQVQL DVPVVKVASG
NDHLVMLTAD GDLYTLGCGE QGQLGRVPEL FANRGGRQGL ERLLVPKCVM LKSRGSRGHV
RFQDAFCGAY FTFAISHEGH VYGFGLSNYH QLGTPGTESC FIPQNLTSFK NSTKSWVGFS
GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPAVSSV ACGASVGYAV
TKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MMGKQLENRV VLSVSSGGQH TVLLVKDKEQ
S


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EIAAB34100 Chc1l,Chromosome condensation 1-like,Rat,Rattus norvegicus,Rcbtb2,RCC1 and BTB domain-containing protein 2,Regulator of chromosome condensation and BTB domain-containing protein 2
EIAAB34099 Chc1l,Chromosome condensation 1-like,Mouse,Mus musculus,Rcbtb2,RCC1 and BTB domain-containing protein 2,Regulator of chromosome condensation and BTB domain-containing protein 2
EIAAB34101 CHC1L,CHC1-L,Chromosome condensation 1-like,Homo sapiens,Human,RCBTB2,RCC1 and BTB domain-containing protein 2,RCC1-like G exchanging factor,Regulator of chromosome condensation and BTB domain-contain
201-20-4821 RCBTB2{regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 2}rabbit.pAb 0.2ml
CSB-EL019504RA Rat regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 2 (RCBTB2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
ARP57290_P050 RCC2(regulator of chromosome condensation 2) 50 µg
ARP57290_P050 RCC2(regulator of chromosome condensation 2) 50 µg
EIAAB34098 Mouse,Mus musculus,Rcbtb1,RCC1 and BTB domain-containing protein 1,Regulator of chromosome condensation and BTB domain-containing protein 1
RCBTB2 RCBTB2 Gene regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 2
RCBTB1 RCBTB1 Gene regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 1
E1667h Human ELISA Kit FOR Regulator of chromosome condensation 96T
G7044 Regulator of chromosome condensation (RCC1), Human, ELISA Kit 96T
CSB-EL019505MO Mouse Regulator of chromosome condensation(RCC1) ELISA kit 96T
G7045 Regulator of chromosome condensation (RCC1), Mouse, ELISA Kit 96T
CSB-EL019505HU Human Regulator of chromosome condensation(RCC1) ELISA kit 96T
CSB-EL019505MO Mouse Regulator of chromosome condensation(RCC1) ELISA kit SpeciesMouse 96T
CSB-EL019505HU Human Regulator of chromosome condensation(RCC1) ELISA kit SpeciesHuman 96T
CSB-EL019503MO Mouse regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 1 (RCBTB1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL019504MO Mouse regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 2 (RCBTB2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL019504HU Human regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 2 (RCBTB2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019503HU Human regulator of chromosome condensation (RCC1) and BTB (POZ) domain containing protein 1 (RCBTB1) ELISA kit, Species Human, Sample Type serum, plasma 96T
201-20-6725 RCC1{regulator of chromosome condensation 1 isoform a [Homo sapiens]}mouse.mAb 0.2ml
201-20-4822 RCC1{regulator of chromosome condensation 1 isoform a [Homo sapiens]}rabbit.pAb 0.2ml


 

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