RCC2_HUMAN
ID RCC2_HUMAN Reviewed; 522 AA.
AC Q9P258; Q8IVL9; Q9BSN6; Q9NPV8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Protein RCC2;
DE AltName: Full=RCC1-like protein TD-60 {ECO:0000303|PubMed:12919680};
DE AltName: Full=Telophase disk protein of 60 kDa {ECO:0000303|PubMed:1939370};
GN Name=RCC2; Synonyms=KIAA1470, TD60;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MICROTUBULES AND RAC1.
RX PubMed=12919680; DOI=10.1016/s1534-5807(03)00205-3;
RA Mollinari C., Reynaud C., Martineau-Thuillier S., Monier S., Kieffer S.,
RA Garin J., Andreassen P.R., Boulet A., Goud B., Kleman J.-P., Margolis R.L.;
RT "The mammalian passenger protein TD-60 is an RCC1 family member with an
RT essential role in prometaphase to metaphase progression.";
RL Dev. Cell 5:295-307(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, Natural killer cell, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-477.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=1939370; DOI=10.1242/jcs.99.3.523;
RA Andreassen P.R., Palmer D.K., Wener M.H., Margolis R.L.;
RT "Telophase disc: a new mammalian mitotic organelle that bisects telophase
RT cells with a possible function in cytokinesis.";
RL J. Cell Sci. 99:523-534(1991).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=7559776; DOI=10.1083/jcb.131.1.191;
RA Martineau S.N., Andreassen P.R., Margolis R.L.;
RT "Delay of HeLa cell cleavage into interphase using dihydrocytochalasin B:
RT retention of a postmitotic spindle and telophase disc correlates with
RT synchronous cleavage recovery.";
RL J. Cell Biol. 131:191-205(1995).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9914378; DOI=10.1007/s004120050330;
RA Martineau-Thuillier S., Andreassen P.R., Margolis R.L.;
RT "Colocalization of TD-60 and INCENP throughout G2 and mitosis: evidence for
RT their possible interaction in signalling cytokinesis.";
RL Chromosoma 107:461-470(1998).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-44; SER-45; SER-46;
RP SER-50 AND SER-51, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-342, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92; LYS-293 AND LYS-377, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23388455; DOI=10.4161/cc.23821;
RA Yenjerla M., Panopoulos A., Reynaud C., Fotedar R., Margolis R.L.;
RT "TD-60 is required for interphase cell cycle progression.";
RL Cell Cycle 12:837-841(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION, INTERACTION WITH RAC1 AND CORO1C, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-439.
RX PubMed=25074804; DOI=10.1242/jcs.154864;
RA Williamson R.C., Cowell C.A., Hammond C.L., Bergen D.J., Roper J.A.,
RA Feng Y., Rendall T.C., Race P.R., Bass M.D.;
RT "Coronin-1C and RCC2 guide mesenchymal migration by trafficking Rac1 and
RT controlling GEF exposure.";
RL J. Cell Sci. 127:4292-4307(2014).
RN [20]
RP FUNCTION.
RX PubMed=26158537; DOI=10.1038/ncomms8678;
RA Papini D., Langemeyer L., Abad M.A., Kerr A., Samejima I., Eyers P.A.,
RA Jeyaprakash A.A., Higgins J.M., Barr F.A., Earnshaw W.C.;
RT "TD-60 links RalA GTPase function to the CPC in mitosis.";
RL Nat. Commun. 6:7678-7678(2015).
RN [21] {ECO:0007744|PDB:5GWN}
RP X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 89-522, FUNCTION, INTERACTION
RP WITH RAC1, INDUCTION, AND MUTAGENESIS OF 318-LYS--LEU-325.
RX PubMed=28869598; DOI=10.1038/onc.2017.306;
RA Song C., Liang L., Jin Y., Li Y., Liu Y., Guo L., Wu C., Yun C.H., Yin Y.;
RT "RCC2 is a novel p53 target in suppressing metastasis.";
RL Oncogene 37:8-17(2018).
CC -!- FUNCTION: Multifunctional protein that may affect its functions by
CC regulating the activity of small GTPases, such as RAC1 and RALA
CC (PubMed:12919680, PubMed:25074804, PubMed:26158537, PubMed:28869598).
CC Required for normal progress through the cell cycle, both during
CC interphase and during mitosis (PubMed:23388455, PubMed:12919680,
CC PubMed:26158537). Required for the presence of normal levels of MAD2L1,
CC AURKB and BIRC5 on inner centromeres during mitosis, and for normal
CC attachment of kinetochores to mitotic spindles (PubMed:12919680,
CC PubMed:26158537). Required for normal organization of the microtubule
CC cytoskeleton in interphase cells (PubMed:23388455). Functions as
CC guanine nucleotide exchange factor (GEF) for RALA (PubMed:26158537).
CC Interferes with the activation of RAC1 by guanine nucleotide exchange
CC factors (PubMed:25074804). Prevents accumulation of active, GTP-bound
CC RAC1, and suppresses RAC1-mediated reorganization of the actin
CC cytoskeleton and formation of membrane protrusions (PubMed:25074804,
CC PubMed:28869598). Required for normal cellular responses to contacts
CC with the extracellular matrix of adjacent cells, and for directional
CC cell migration in response to a fibronectin gradient (in vitro)
CC (PubMed:25074804, PubMed:28869598). {ECO:0000269|PubMed:12919680,
CC ECO:0000269|PubMed:23388455, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:26158537, ECO:0000269|PubMed:28869598}.
CC -!- SUBUNIT: Interacts with RAC1 (PubMed:12919680, PubMed:25074804,
CC PubMed:28869598). Interacts with nucleotide-free and with GDP and GTP-
CC bound forms of RAC1, with a slight preference for GDP-bound RAC1
CC (PubMed:25074804). Binds preferentially to the nucleotide-free form of
CC RAC1 (PubMed:12919680). Interacts with CORO1C (PubMed:25074804).
CC Interacts with microtubules (PubMed:12919680).
CC {ECO:0000269|PubMed:12919680, ECO:0000269|PubMed:25074804,
CC ECO:0000269|PubMed:28869598}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305|PubMed:12429849}.
CC Nucleus {ECO:0000269|PubMed:23388455}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23388455}. Chromosome, centromere
CC {ECO:0000269|PubMed:12919680, ECO:0000269|PubMed:1939370,
CC ECO:0000269|PubMed:9914378}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:1939370, ECO:0000269|PubMed:9914378}. Chromosome
CC {ECO:0000269|PubMed:12919680, ECO:0000269|PubMed:1939370,
CC ECO:0000269|PubMed:9914378}. Midbody {ECO:0000269|PubMed:12919680,
CC ECO:0000269|PubMed:1939370, ECO:0000269|PubMed:9914378}. Cell membrane
CC {ECO:0000269|PubMed:25074804}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25074804}; Cytoplasmic side
CC {ECO:0000305|PubMed:25074804}. Note=Appears in the nucleus at G2, then
CC concentrates at the inner centromere region of chromosomes during
CC prophase. Redistributes to the midzone of the mitotic spindle during
CC anaphase. Here, the protein covers the entire equatorial diameter from
CC cortex to cortex (PubMed:12919680, PubMed:1939370, PubMed:7559776,
CC PubMed:9914378). Colocalizes with cytoplasmic microtubules in
CC interphase cells (PubMed:23388455). Colocalizes with RAC1 at the cell
CC membrane (PubMed:25074804). {ECO:0000269|PubMed:12919680,
CC ECO:0000269|PubMed:1939370, ECO:0000269|PubMed:23388455,
CC ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:7559776,
CC ECO:0000269|PubMed:9914378}.
CC -!- INDUCTION: Induced by TP53/p53 in response to oxidative stress and DNA
CC damage. {ECO:0000269|PubMed:28869598}.
CC -!- CAUTION: Its precise role in the regulation of RAC1 activity is under
CC debate. Was originally proposed to function as a guanine nucleotide
CC exchange factor for RAC1, but later publications indicate it attenuates
CC RAC1 activation by guanine nucleotide exchange factors and prevents
CC accumulation of active, GTP-bound RAC1 (PubMed:12919680,
CC PubMed:25074804, PubMed:28869598). Conflicting results have also been
CC reported regarding its preferential interaction with nucleotide-free
CC RAC1, as opposed to GPD or GTP-bound RAC1 (PubMed:12919680,
CC PubMed:25074804). {ECO:0000269|PubMed:12919680,
CC ECO:0000269|PubMed:25074804, ECO:0000269|PubMed:28869598}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95994.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB94882.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ421269; CAD13148.1; -; mRNA.
DR EMBL; AB040903; BAA95994.1; ALT_INIT; mRNA.
DR EMBL; BC004933; AAH04933.1; -; mRNA.
DR EMBL; BC042141; AAH42141.1; -; mRNA.
DR EMBL; BC053908; AAH53908.1; -; mRNA.
DR EMBL; AL359612; CAB94882.1; ALT_FRAME; mRNA.
DR CCDS; CCDS181.1; -.
DR PIR; T50630; T50630.
DR RefSeq; NP_001129676.1; NM_001136204.2.
DR RefSeq; NP_061185.1; NM_018715.3.
DR PDB; 5GWN; X-ray; 1.31 A; A=89-522.
DR PDBsum; 5GWN; -.
DR AlphaFoldDB; Q9P258; -.
DR SMR; Q9P258; -.
DR BioGRID; 121001; 138.
DR IntAct; Q9P258; 41.
DR MINT; Q9P258; -.
DR STRING; 9606.ENSP00000364585; -.
DR GlyGen; Q9P258; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P258; -.
DR MetOSite; Q9P258; -.
DR PhosphoSitePlus; Q9P258; -.
DR SwissPalm; Q9P258; -.
DR BioMuta; RCC2; -.
DR DMDM; 71152033; -.
DR SWISS-2DPAGE; Q9P258; -.
DR EPD; Q9P258; -.
DR jPOST; Q9P258; -.
DR MassIVE; Q9P258; -.
DR MaxQB; Q9P258; -.
DR PaxDb; Q9P258; -.
DR PeptideAtlas; Q9P258; -.
DR PRIDE; Q9P258; -.
DR ProteomicsDB; 83733; -.
DR Antibodypedia; 29372; 212 antibodies from 28 providers.
DR DNASU; 55920; -.
DR Ensembl; ENST00000375433.3; ENSP00000364582.3; ENSG00000179051.14.
DR Ensembl; ENST00000375436.9; ENSP00000364585.4; ENSG00000179051.14.
DR Ensembl; ENST00000628984.1; ENSP00000486099.1; ENSG00000281540.3.
DR Ensembl; ENST00000631021.3; ENSP00000486447.1; ENSG00000281540.3.
DR GeneID; 55920; -.
DR KEGG; hsa:55920; -.
DR MANE-Select; ENST00000375436.9; ENSP00000364585.4; NM_018715.4; NP_061185.1.
DR UCSC; uc001bal.4; human.
DR CTD; 55920; -.
DR DisGeNET; 55920; -.
DR GeneCards; RCC2; -.
DR HGNC; HGNC:30297; RCC2.
DR HPA; ENSG00000179051; Low tissue specificity.
DR MIM; 609587; gene.
DR neXtProt; NX_Q9P258; -.
DR OpenTargets; ENSG00000179051; -.
DR PharmGKB; PA142671091; -.
DR VEuPathDB; HostDB:ENSG00000179051; -.
DR eggNOG; KOG1427; Eukaryota.
DR GeneTree; ENSGT00940000156151; -.
DR HOGENOM; CLU_005210_7_0_1; -.
DR InParanoid; Q9P258; -.
DR OMA; YGCLSGI; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q9P258; -.
DR TreeFam; TF101168; -.
DR PathwayCommons; Q9P258; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9P258; -.
DR BioGRID-ORCS; 55920; 19 hits in 1076 CRISPR screens.
DR ChiTaRS; RCC2; human.
DR GeneWiki; RCC2; -.
DR GenomeRNAi; 55920; -.
DR Pharos; Q9P258; Tbio.
DR PRO; PR:Q9P258; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P258; protein.
DR Bgee; ENSG00000179051; Expressed in lower esophagus mucosa and 101 other tissues.
DR ExpressionAtlas; Q9P258; baseline and differential.
DR Genevisible; Q9P258; HS.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072356; P:chromosome passenger complex localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR028641; RCC2.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR46207; PTHR46207; 1.
DR Pfam; PF00415; RCC1; 4.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Guanine-nucleotide releasing factor; Membrane; Microtubule; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..522
FT /note="Protein RCC2"
FT /id="PRO_0000206652"
FT REPEAT 103..165
FT /note="RCC1 1"
FT REPEAT 168..219
FT /note="RCC1 2"
FT REPEAT 221..271
FT /note="RCC1 3"
FT REPEAT 273..347
FT /note="RCC1 4"
FT REPEAT 348..401
FT /note="RCC1 5"
FT REPEAT 403..447
FT /note="RCC1 6"
FT REPEAT 448..501
FT /note="RCC1 7"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..325
FT /note="Required for interaction with RAC1"
FT /evidence="ECO:0000269|PubMed:28869598"
FT REGION 502..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK67"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 318..325
FT /note="Missing: Loss of interaction with RAC1."
FT /evidence="ECO:0000269|PubMed:28869598"
FT MUTAGEN 439
FT /note="K->E: Loss of interaction with RAC1 and loss of
FT regulation of RAC1 activation."
FT /evidence="ECO:0000269|PubMed:25074804"
FT CONFLICT 145..148
FT /note="LAGV -> RTRG (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5GWN"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:5GWN"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:5GWN"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:5GWN"
FT HELIX 505..513
FT /evidence="ECO:0007829|PDB:5GWN"
SQ SEQUENCE 522 AA; 56085 MW; 7065F70AEA98EDC3 CRC64;
MPRKKAAAAA WEEPSSGNGT ARAGPRKRGG PAGRKRERPE RCSSSSGGGS SGDEDGLELD
GAPGGGKRAA RPATAGKAGG AAVVITEPEH TKERVKLEGS KCKGQLLIFG ATNWDLIGRK
EVPKQQAAYR NLGQNLWGPH RYGCLAGVRV RTVVSGSCAA HSLLITTEGK LWSWGRNEKG
QLGHGDTKRV EAPRLIEGLS HEVIVSAACG RNHTLALTET GSVFAFGENK MGQLGLGNQT
DAVPSPAQIM YNGQPITKMA CGAEFSMIMD CKGNLYSFGC PEYGQLGHNS DGKFIARAQR
IEYDCELVPR RVAIFIEKTK DGQILPVPNV VVRDVACGAN HTLVLDSQKR VFSWGFGGYG
RLGHAEQKDE MVPRLVKLFD FPGRGASQIY AGYTCSFAVS EVGGLFFWGA TNTSRESTMY
PKAVQDLCGW RIRSLACGKS SIIVAADEST ISWGPSPTFG ELGYGDHKPK SSTAAQEVKT
LDGIFSEQVA MGYSHSLVIA RDESETEKEK IKKLPEYNPR TL
