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Q9P258

- RCC2_HUMAN

UniProt

Q9P258 - RCC2_HUMAN

Protein

Protein RCC2

Gene

RCC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1.1 Publication

    GO - Molecular functioni

    1. microtubule binding Source: UniProt
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProt
    4. Rac GTPase binding Source: UniProt

    GO - Biological processi

    1. chromosome passenger complex localization to kinetochore Source: UniProt
    2. endosome organization Source: InterPro
    3. focal adhesion assembly Source: UniProt
    4. integrin-mediated signaling pathway Source: UniProt
    5. mitotic cell cycle Source: Reactome
    6. mitotic nuclear division Source: UniProtKB-KW
    7. negative regulation of focal adhesion assembly Source: UniProt
    8. negative regulation of GTPase activity Source: UniProt
    9. negative regulation of substrate adhesion-dependent cell spreading Source: UniProt
    10. positive regulation of attachment of spindle microtubules to kinetochore Source: UniProt
    11. positive regulation of G2/M transition of mitotic cell cycle Source: UniProt
    12. regulation of cell migration Source: UniProt

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein RCC2
    Alternative name(s):
    RCC1-like protein TD-60
    Telophase disk protein of 60 kDa
    Gene namesi
    Name:RCC2
    Synonyms:KIAA1470, TD60
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30297. RCC2.

    Subcellular locationi

    Nucleusnucleolus. Chromosomecentromere. Cytoplasmcytoskeletonspindle
    Note: Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during anaphase. Here, the protein covers the entire equatorial diameter from cortex to cortex.

    GO - Cellular componenti

    1. chromosome, centromeric core domain Source: UniProt
    2. cytosol Source: Reactome
    3. microtubule Source: UniProtKB-KW
    4. midbody Source: UniProt
    5. mitotic spindle midzone Source: UniProt
    6. nucleolus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671091.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 522522Protein RCC2PRO_0000206652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei43 – 431Phosphoserine1 Publication
    Modified residuei44 – 441Phosphoserine1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei46 – 461Phosphoserine1 Publication
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei51 – 511Phosphoserine2 Publications
    Modified residuei92 – 921N6-acetyllysine1 Publication
    Modified residuei124 – 1241N6-acetyllysineBy similarity
    Modified residuei293 – 2931N6-acetyllysine1 Publication
    Modified residuei342 – 3421Phosphothreonine1 Publication
    Modified residuei347 – 3471Phosphoserine1 Publication
    Modified residuei377 – 3771N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9P258.
    PaxDbiQ9P258.
    PeptideAtlasiQ9P258.
    PRIDEiQ9P258.

    2D gel databases

    SWISS-2DPAGEQ9P258.

    PTM databases

    PhosphoSiteiQ9P258.

    Expressioni

    Gene expression databases

    BgeeiQ9P258.
    CleanExiHS_RCC2.
    GenevestigatoriQ9P258.

    Organism-specific databases

    HPAiHPA056177.

    Interactioni

    Subunit structurei

    Binds preferentially to the nucleotide-free form of RAC1. Interacts with microtubules.1 Publication

    Protein-protein interaction databases

    BioGridi121001. 17 interactions.
    IntActiQ9P258. 6 interactions.
    MINTiMINT-3037281.
    STRINGi9606.ENSP00000364582.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P258.
    SMRiQ9P258. Positions 101-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati103 – 16563RCC1 1Add
    BLAST
    Repeati168 – 21952RCC1 2Add
    BLAST
    Repeati221 – 27151RCC1 3Add
    BLAST
    Repeati273 – 34775RCC1 4Add
    BLAST
    Repeati348 – 40154RCC1 5Add
    BLAST
    Repeati403 – 44745RCC1 6Add
    BLAST
    Repeati448 – 50154RCC1 7Add
    BLAST

    Sequence similaritiesi

    Contains 7 RCC1 repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5184.
    HOGENOMiHOG000232061.
    HOVERGENiHBG080538.
    InParanoidiQ9P258.
    OMAiVDCKGNL.
    OrthoDBiEOG7TTQ7B.
    PhylomeDBiQ9P258.
    TreeFamiTF101168.

    Family and domain databases

    Gene3Di2.130.10.30. 1 hit.
    InterProiIPR009091. RCC1/BLIP-II.
    IPR028641. RCC2.
    IPR000408. Reg_chr_condens.
    [Graphical view]
    PANTHERiPTHR22870:SF146. PTHR22870:SF146. 1 hit.
    PfamiPF00415. RCC1. 4 hits.
    [Graphical view]
    PRINTSiPR00633. RCCNDNSATION.
    SUPFAMiSSF50985. SSF50985. 1 hit.
    PROSITEiPS00626. RCC1_2. 2 hits.
    PS50012. RCC1_3. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P258-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRKKAAAAA WEEPSSGNGT ARAGPRKRGG PAGRKRERPE RCSSSSGGGS    50
    SGDEDGLELD GAPGGGKRAA RPATAGKAGG AAVVITEPEH TKERVKLEGS 100
    KCKGQLLIFG ATNWDLIGRK EVPKQQAAYR NLGQNLWGPH RYGCLAGVRV 150
    RTVVSGSCAA HSLLITTEGK LWSWGRNEKG QLGHGDTKRV EAPRLIEGLS 200
    HEVIVSAACG RNHTLALTET GSVFAFGENK MGQLGLGNQT DAVPSPAQIM 250
    YNGQPITKMA CGAEFSMIMD CKGNLYSFGC PEYGQLGHNS DGKFIARAQR 300
    IEYDCELVPR RVAIFIEKTK DGQILPVPNV VVRDVACGAN HTLVLDSQKR 350
    VFSWGFGGYG RLGHAEQKDE MVPRLVKLFD FPGRGASQIY AGYTCSFAVS 400
    EVGGLFFWGA TNTSRESTMY PKAVQDLCGW RIRSLACGKS SIIVAADEST 450
    ISWGPSPTFG ELGYGDHKPK SSTAAQEVKT LDGIFSEQVA MGYSHSLVIA 500
    RDESETEKEK IKKLPEYNPR TL 522
    Length:522
    Mass (Da):56,085
    Last modified:July 19, 2005 - v2
    Checksum:i7065F70AEA98EDC3
    GO

    Sequence cautioni

    The sequence CAB94882.1 differs from that shown. Reason: Frameshift at position 477.
    The sequence BAA95994.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1484LAGV → RTRG(PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ421269 mRNA. Translation: CAD13148.1.
    AB040903 mRNA. Translation: BAA95994.1. Different initiation.
    BC004933 mRNA. Translation: AAH04933.1.
    BC042141 mRNA. Translation: AAH42141.1.
    BC053908 mRNA. Translation: AAH53908.1.
    AL359612 mRNA. Translation: CAB94882.1. Frameshift.
    CCDSiCCDS181.1.
    PIRiT50630.
    RefSeqiNP_001129676.1. NM_001136204.2.
    NP_061185.1. NM_018715.3.
    UniGeneiHs.380857.

    Genome annotation databases

    EnsembliENST00000375433; ENSP00000364582; ENSG00000179051.
    ENST00000375436; ENSP00000364585; ENSG00000179051.
    GeneIDi55920.
    KEGGihsa:55920.
    UCSCiuc001bal.3. human.

    Polymorphism databases

    DMDMi71152033.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ421269 mRNA. Translation: CAD13148.1 .
    AB040903 mRNA. Translation: BAA95994.1 . Different initiation.
    BC004933 mRNA. Translation: AAH04933.1 .
    BC042141 mRNA. Translation: AAH42141.1 .
    BC053908 mRNA. Translation: AAH53908.1 .
    AL359612 mRNA. Translation: CAB94882.1 . Frameshift.
    CCDSi CCDS181.1.
    PIRi T50630.
    RefSeqi NP_001129676.1. NM_001136204.2.
    NP_061185.1. NM_018715.3.
    UniGenei Hs.380857.

    3D structure databases

    ProteinModelPortali Q9P258.
    SMRi Q9P258. Positions 101-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121001. 17 interactions.
    IntActi Q9P258. 6 interactions.
    MINTi MINT-3037281.
    STRINGi 9606.ENSP00000364582.

    PTM databases

    PhosphoSitei Q9P258.

    Polymorphism databases

    DMDMi 71152033.

    2D gel databases

    SWISS-2DPAGE Q9P258.

    Proteomic databases

    MaxQBi Q9P258.
    PaxDbi Q9P258.
    PeptideAtlasi Q9P258.
    PRIDEi Q9P258.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375433 ; ENSP00000364582 ; ENSG00000179051 .
    ENST00000375436 ; ENSP00000364585 ; ENSG00000179051 .
    GeneIDi 55920.
    KEGGi hsa:55920.
    UCSCi uc001bal.3. human.

    Organism-specific databases

    CTDi 55920.
    GeneCardsi GC01M017733.
    HGNCi HGNC:30297. RCC2.
    HPAi HPA056177.
    MIMi 609587. gene.
    neXtProti NX_Q9P258.
    PharmGKBi PA142671091.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5184.
    HOGENOMi HOG000232061.
    HOVERGENi HBG080538.
    InParanoidi Q9P258.
    OMAi VDCKGNL.
    OrthoDBi EOG7TTQ7B.
    PhylomeDBi Q9P258.
    TreeFami TF101168.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    GeneWikii RCC2.
    GenomeRNAii 55920.
    NextBioi 61323.
    PROi Q9P258.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9P258.
    CleanExi HS_RCC2.
    Genevestigatori Q9P258.

    Family and domain databases

    Gene3Di 2.130.10.30. 1 hit.
    InterProi IPR009091. RCC1/BLIP-II.
    IPR028641. RCC2.
    IPR000408. Reg_chr_condens.
    [Graphical view ]
    PANTHERi PTHR22870:SF146. PTHR22870:SF146. 1 hit.
    Pfami PF00415. RCC1. 4 hits.
    [Graphical view ]
    PRINTSi PR00633. RCCNDNSATION.
    SUPFAMi SSF50985. SSF50985. 1 hit.
    PROSITEi PS00626. RCC1_2. 2 hits.
    PS50012. RCC1_3. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mammalian passenger protein TD-60 is an RCC1 family member with an essential role in prometaphase to metaphase progression."
      Mollinari C., Reynaud C., Martineau-Thuillier S., Monier S., Kieffer S., Garin J., Andreassen P.R., Boulet A., Goud B., Kleman J.-P., Margolis R.L.
      Dev. Cell 5:295-307(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH MICROTUBULES AND RAC1.
    2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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].
      Tissue: Muscle, Natural killer cell and Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-477.
      Tissue: Melanoma.
    5. "Telophase disc: a new mammalian mitotic organelle that bisects telophase cells with a possible function in cytokinesis."
      Andreassen P.R., Palmer D.K., Wener M.H., Margolis R.L.
      J. Cell Sci. 99:523-534(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Delay of HeLa cell cleavage into interphase using dihydrocytochalasin B: retention of a postmitotic spindle and telophase disc correlates with synchronous cleavage recovery."
      Martineau S.N., Andreassen P.R., Margolis R.L.
      J. Cell Biol. 131:191-205(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Colocalization of TD-60 and INCENP throughout G2 and mitosis: evidence for their possible interaction in signalling cytokinesis."
      Martineau-Thuillier S., Andreassen P.R., Margolis R.L.
      Chromosoma 107:461-470(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-43; SER-44; SER-45; SER-46; SER-50 AND SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-342 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92; LYS-293 AND LYS-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRCC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9P258
    Secondary accession number(s): Q8IVL9, Q9BSN6, Q9NPV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 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

    Keywords - Technical termi

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3