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 14-DEC-2022, entry version 184. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 180. 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 ProteomicsDB; 83733; -. DR Antibodypedia; 29372; 210 antibodies from 27 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 AGR; HGNC:30297; -. 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; PROTEIN RCC2; 1. DR Pfam; PF00415; RCC1; 4. DR PRINTS; PR00633; RCCNDNSATION. DR SUPFAM; SSF50985; RCC1/BLIP-II; 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 //