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P18754

- RCC1_HUMAN

UniProt

P18754 - RCC1_HUMAN

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Protein

Regulator of chromosome condensation

Gene
RCC1, CHC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. regulation of mitosis Source: UniProtKB
  6. regulation of Ran GTPase activity Source: GOC
  7. spindle assembly Source: UniProtKB
  8. viral process Source: Reactome
Complete GO annotation...

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

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
Complete GO annotation...

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.2 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.

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.

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. VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 157 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

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