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P18754

- RCC1_HUMAN

UniProt

P18754 - RCC1_HUMAN

Protein

Regulator of chromosome condensation

Gene

RCC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. histone binding Source: UniProtKB
    3. nucleosomal DNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. Ran guanyl-nucleotide exchange factor activity Source: UniProtKB

    GO - Biological processi

    1. chromosome segregation Source: UniProtKB
    2. G1/S transition of mitotic cell cycle Source: UniProtKB
    3. mitotic nuclear division Source: UniProtKB-KW
    4. mitotic spindle organization Source: UniProtKB
    5. positive regulation of Ran GTPase activity Source: GOC
    6. regulation of mitosis Source: UniProtKB
    7. spindle assembly Source: UniProtKB
    8. viral process Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_9395. Nuclear import of Rev protein.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of chromosome condensation
    Alternative name(s):
    Cell cycle regulatory protein
    Chromosome condensation protein 1
    Gene namesi
    Name:RCC1
    Synonyms:CHC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1913. RCC1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Becomes dispersed throughout the cytoplasm during mitosis.

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. nuclear chromatin Source: UniProtKB
    4. nuclear membrane Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21S → A: Does not abolish N-terminal methylation. 1 Publication
    Mutagenesisi2 – 21S → Q: Does not abolish N-terminal methylation. 1 Publication
    Mutagenesisi3 – 31P → Q: Abolishes N-terminal methylation. 1 Publication
    Mutagenesisi4 – 41K → Q: Abolishes N-terminal methylation. 2 Publications
    Mutagenesisi4 – 41K → R: Stongly impairs N-terminal methylation and subcellular localization. 2 Publications
    Mutagenesisi182 – 1821D → A: Abolishes interaction with Ran and chromosome localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA26449.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 421420Regulator of chromosome condensationPRO_0000206628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N,N-trimethylserine; alternate3 Publications
    Modified residuei2 – 21N,N-dimethylserine; alternate3 Publications
    Modified residuei2 – 21N-methylserine; alternate3 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei11 – 111Phosphoserine3 Publications

    Post-translational modificationi

    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 facilitate electrostatic binding to the phosphate groups on DNA, while inhibiting histone-binding. Methylated tail helps retain RCC1 on chromosomes during nucleotide exchange on Ran.3 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP18754.
    PaxDbiP18754.
    PRIDEiP18754.

    PTM databases

    PhosphoSiteiP18754.

    Expressioni

    Gene expression databases

    ArrayExpressiP18754.
    BgeeiP18754.
    CleanExiHS_RCC1.
    GenevestigatoriP18754.

    Organism-specific databases

    HPAiCAB015413.
    HPA027573.
    HPA027574.

    Interactioni

    Subunit structurei

    Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RANP628266EBI-992720,EBI-286642
    RANBP3Q9H6Z42EBI-992720,EBI-992681

    Protein-protein interaction databases

    BioGridi107529. 68 interactions.
    DIPiDIP-35416N.
    IntActiP18754. 40 interactions.
    MINTiMINT-240062.
    STRINGi9606.ENSP00000362937.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 428
    Beta strandi56 – 638
    Beta strandi69 – 746
    Beta strandi76 – 838
    Beta strandi88 – 925
    Helixi108 – 1103
    Beta strandi121 – 1266
    Beta strandi128 – 1358
    Beta strandi140 – 1445
    Beta strandi146 – 1483
    Beta strandi151 – 1588
    Beta strandi162 – 1687
    Beta strandi174 – 1796
    Beta strandi181 – 1888
    Beta strandi193 – 1975
    Beta strandi205 – 2073
    Helixi208 – 2103
    Beta strandi212 – 2143
    Helixi216 – 2194
    Helixi220 – 2245
    Beta strandi242 – 2487
    Beta strandi251 – 2566
    Beta strandi261 – 2655
    Beta strandi280 – 2856
    Helixi287 – 2893
    Beta strandi296 – 3016
    Beta strandi303 – 3108
    Beta strandi315 – 3195
    Helixi322 – 3243
    Beta strandi335 – 3406
    Beta strandi343 – 35210
    Beta strandi354 – 3618
    Beta strandi366 – 3705
    Beta strandi379 – 3813
    Beta strandi385 – 3906
    Turni394 – 3985
    Beta strandi399 – 4068
    Beta strandi408 – 41710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A12X-ray1.70A/B/C9-421[»]
    1I2MX-ray1.76B/D20-421[»]
    DisProtiDP00691.
    ProteinModelPortaliP18754.
    SMRiP18754. Positions 21-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18754.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati34 – 8451RCC1 1Add
    BLAST
    Repeati85 – 13652RCC1 2Add
    BLAST
    Repeati138 – 18952RCC1 3Add
    BLAST
    Repeati191 – 25767RCC1 4Add
    BLAST
    Repeati258 – 31154RCC1 5Add
    BLAST
    Repeati312 – 36251RCC1 6Add
    BLAST
    Repeati363 – 41654RCC1 7Add
    BLAST

    Sequence similaritiesi

    Contains 7 RCC1 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5184.
    HOGENOMiHOG000234341.
    HOVERGENiHBG017712.
    KOiK11493.
    OMAiDDAWSPV.
    PhylomeDBiP18754.
    TreeFamiTF101139.

    Family and domain databases

    Gene3Di2.130.10.30. 1 hit.
    InterProiIPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view]
    PfamiPF00415. RCC1. 7 hits.
    [Graphical view]
    PRINTSiPR00633. RCCNDNSATION.
    SUPFAMiSSF50985. SSF50985. 1 hit.
    PROSITEiPS00625. RCC1_1. 1 hit.
    PS00626. RCC1_2. 4 hits.
    PS50012. RCC1_3. 7 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P18754-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSPKRIAKRR SPPADAIPKS KKVKVSHRSH STEPGLVLTL GQGDVGQLGL    50
    GENVMERKKP ALVSIPEDVV QAEAGGMHTV CLSKSGQVYS FGCNDEGALG 100
    RDTSVEGSEM VPGKVELQEK VVQVSAGDSH TAALTDDGRV FLWGSFRDNN 150
    GVIGLLEPMK KSMVPVQVQL DVPVVKVASG NDHLVMLTAD GDLYTLGCGE 200
    QGQLGRVPEL FANRGGRQGL ERLLVPKCVM LKSRGSRGHV RFQDAFCGAY 250
    FTFAISHEGH VYGFGLSNYH QLGTPGTESC FIPQNLTSFK NSTKSWVGFS 300
    GGQHHTVCMD SEGKAYSLGR AEYGRLGLGE GAEEKSIPTL ISRLPAVSSV 350
    ACGASVGYAV TKDGRVFAWG MGTNYQLGTG QDEDAWSPVE MMGKQLENRV 400
    VLSVSSGGQH TVLLVKDKEQ S 421
    Length:421
    Mass (Da):44,969
    Last modified:November 1, 1990 - v1
    Checksum:iF6D225AF81928305
    GO
    Isoform 2 (identifier: P18754-2) [UniParc]FASTAAdd to Basket

    Also known as: RCC1-I

    The sequence of this isoform differs from the canonical sequence as follows:
         24-24: K → KDTRAAASRRVPGARSCQGACGPSPPDQKTRP

    Show »
    Length:452
    Mass (Da):48,146
    Checksum:iA31255E99A01A25F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei24 – 241K → KDTRAAASRRVPGARSCQGA CGPSPPDQKTRP in isoform 2. 2 PublicationsVSP_041122

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12654 mRNA. Translation: CAA31182.1.
    X06130 mRNA. Translation: CAA29496.1.
    D00591 Genomic DNA. Translation: BAA00469.1.
    AF498924 mRNA. Translation: AAM21072.1.
    BC007300 mRNA. Translation: AAH07300.1.
    BC010067 mRNA. Translation: AAH10067.1.
    BC036903 mRNA. Translation: AAH36903.1.
    BC069198 mRNA. Translation: AAH69198.1.
    S75708 mRNA. Translation: AAB32653.1.
    CCDSiCCDS323.1. [P18754-1]
    CCDS41295.1. [P18754-2]
    PIRiA26691.
    RefSeqiNP_001041659.1. NM_001048194.2. [P18754-2]
    NP_001041660.1. NM_001048195.2.
    NP_001041664.1. NM_001048199.2. [P18754-1]
    NP_001260.1. NM_001269.4. [P18754-1]
    UniGeneiHs.469723.

    Genome annotation databases

    EnsembliENST00000373831; ENSP00000362937; ENSG00000180198. [P18754-2]
    ENST00000373832; ENSP00000362938; ENSG00000180198. [P18754-1]
    ENST00000373833; ENSP00000362939; ENSG00000180198. [P18754-1]
    ENST00000398958; ENSP00000381931; ENSG00000180198. [P18754-1]
    GeneIDi1104.
    KEGGihsa:1104.
    UCSCiuc001bqa.2. human. [P18754-1]
    uc001bqe.2. human. [P18754-2]

    Polymorphism databases

    DMDMi132170.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12654 mRNA. Translation: CAA31182.1 .
    X06130 mRNA. Translation: CAA29496.1 .
    D00591 Genomic DNA. Translation: BAA00469.1 .
    AF498924 mRNA. Translation: AAM21072.1 .
    BC007300 mRNA. Translation: AAH07300.1 .
    BC010067 mRNA. Translation: AAH10067.1 .
    BC036903 mRNA. Translation: AAH36903.1 .
    BC069198 mRNA. Translation: AAH69198.1 .
    S75708 mRNA. Translation: AAB32653.1 .
    CCDSi CCDS323.1. [P18754-1 ]
    CCDS41295.1. [P18754-2 ]
    PIRi A26691.
    RefSeqi NP_001041659.1. NM_001048194.2. [P18754-2 ]
    NP_001041660.1. NM_001048195.2.
    NP_001041664.1. NM_001048199.2. [P18754-1 ]
    NP_001260.1. NM_001269.4. [P18754-1 ]
    UniGenei Hs.469723.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A12 X-ray 1.70 A/B/C 9-421 [» ]
    1I2M X-ray 1.76 B/D 20-421 [» ]
    DisProti DP00691.
    ProteinModelPortali P18754.
    SMRi P18754. Positions 21-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107529. 68 interactions.
    DIPi DIP-35416N.
    IntActi P18754. 40 interactions.
    MINTi MINT-240062.
    STRINGi 9606.ENSP00000362937.

    PTM databases

    PhosphoSitei P18754.

    Polymorphism databases

    DMDMi 132170.

    Proteomic databases

    MaxQBi P18754.
    PaxDbi P18754.
    PRIDEi P18754.

    Protocols and materials databases

    DNASUi 1104.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373831 ; ENSP00000362937 ; ENSG00000180198 . [P18754-2 ]
    ENST00000373832 ; ENSP00000362938 ; ENSG00000180198 . [P18754-1 ]
    ENST00000373833 ; ENSP00000362939 ; ENSG00000180198 . [P18754-1 ]
    ENST00000398958 ; ENSP00000381931 ; ENSG00000180198 . [P18754-1 ]
    GeneIDi 1104.
    KEGGi hsa:1104.
    UCSCi uc001bqa.2. human. [P18754-1 ]
    uc001bqe.2. human. [P18754-2 ]

    Organism-specific databases

    CTDi 1104.
    GeneCardsi GC01P028834.
    HGNCi HGNC:1913. RCC1.
    HPAi CAB015413.
    HPA027573.
    HPA027574.
    MIMi 179710. gene.
    neXtProti NX_P18754.
    PharmGKBi PA26449.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5184.
    HOGENOMi HOG000234341.
    HOVERGENi HBG017712.
    KOi K11493.
    OMAi DDAWSPV.
    PhylomeDBi P18754.
    TreeFami TF101139.

    Enzyme and pathway databases

    Reactomei REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_9395. Nuclear import of Rev protein.

    Miscellaneous databases

    EvolutionaryTracei P18754.
    GeneWikii RCC1.
    GenomeRNAii 1104.
    NextBioi 4572.
    PROi P18754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P18754.
    Bgeei P18754.
    CleanExi HS_RCC1.
    Genevestigatori P18754.

    Family and domain databases

    Gene3Di 2.130.10.30. 1 hit.
    InterProi IPR009091. RCC1/BLIP-II.
    IPR000408. Reg_chr_condens.
    [Graphical view ]
    Pfami PF00415. RCC1. 7 hits.
    [Graphical view ]
    PRINTSi PR00633. RCCNDNSATION.
    SUPFAMi SSF50985. SSF50985. 1 hit.
    PROSITEi PS00625. RCC1_1. 1 hit.
    PS00626. RCC1_2. 4 hits.
    PS50012. RCC1_3. 7 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the active cDNA of the human cell cycle gene (RCC1) involved in the regulation of onset of chromosome condensation."
      Ohtsubo M., Kai R., Furuno N., Sekiguchi T., Sekiguchi M., Hayashida H., Kuma K., Miyata T., Fukushige S., Murotsu T., Matsubara K., Nishimoto T.
      Genes Dev. 1:585-593(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete nucleotide sequence of the human RCC1 gene involved in coupling between DNA replication and mitosis."
      Furuno N., Nakagawa K., Eguchi U., Ohtsubo M., Nishimoto T., Soeda E.
      Genomics 11:459-461(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Eye, Mammary gland, Muscle and Testis.
    5. "Mammalian cells have two functional RCC1 proteins produced by alternative splicing."
      Miyabashira J., Sekiguchi T., Nishimoto T.
      J. Cell Sci. 107:2203-2208(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-33 (ISOFORM 2), ALTERNATIVE SPLICING.
    6. "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."
      Bischoff F.R., Maier G., Tilz G., Ponstingl H.
      Proc. Natl. Acad. Sci. U.S.A. 87:8617-8621(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    7. "Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1."
      Bischoff F.R., Ponstingl H.
      Nature 354:80-82(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
      Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
      J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    10. "N-terminal alpha-methylation of RCC1 is necessary for stable chromatin association and normal mitosis."
      Chen T., Muratore T.L., Schaner-Tooley C.E., Shabanowitz J., Hunt D.F., Macara I.G.
      Nat. Cell Biol. 9:596-603(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, SUBCELLULAR LOCATION, HISTONE-BINDING, INTERACTION WITH RAN, PHOSPHORYLATION AT SER-2, METHYLATION AT SER-2, MUTAGENESIS OF SER-2; PRO-3; LYS-4 AND ASP-182.
    11. "Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1."
      Hao Y., Macara I.G.
      J. Cell Biol. 182:827-836(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT SER-2.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
      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.
      Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT SER-2, MUTAGENESIS OF LYS-4.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The 1.7-A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller."
      Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A.
      Nature 392:97-101(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-421.
    18. "Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1)."
      Renault L., Kuhlmann J., Henkel A., Wittinghofer A.
      Cell 105:245-255(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 20-421 IN COMPLEX WITH RAN.

    Entry informationi

    Entry nameiRCC1_HUMAN
    AccessioniPrimary (citable) accession number: P18754
    Secondary accession number(s): Q16269, Q6NT97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 158 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Patients with Raynaud disease produce antibodies that bind to RCC1.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3