RCC2_MOUSE
ID RCC2_MOUSE Reviewed; 520 AA.
AC Q8BK67; A2AWQ3; Q6ZPQ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein RCC2;
GN Name=Rcc2; Synonyms=Kiaa1470;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 37-520.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH RAC1.
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 [9]
RP INDUCTION.
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 Required for normal progress through the cell cycle, both during
CC interphase and during mitosis. Required for the presence of normal
CC levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis,
CC and for normal attachment of kinetochores to mitotic spindles. Required
CC for normal organization of the microtubule cytoskeleton in interphase
CC cells. Functions as guanine nucleotide exchange factor (GEF) for RALA.
CC Interferes with the activation of RAC1 by guanine nucleotide exchange
CC factors (By similarity). 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 Required for normal cellular responses to contacts with the
CC extracellular matrix of adjacent cells, and for directional cell
CC migration in response to a fibronectin gradient (in vitro) (By
CC similarity). {ECO:0000250|UniProtKB:Q9P258,
CC ECO:0000269|PubMed:25074804}.
CC -!- SUBUNIT: Interacts with RAC1 (PubMed:25074804). Interacts with
CC nucleotide-free and with GDP and GTP-bound forms of RAC1, with a slight
CC preference for GDP-bound RAC1. Binds preferentially to the nucleotide-
CC free form of RAC1. Interacts with CORO1C. Interacts with microtubules
CC (By similarity). {ECO:0000250|UniProtKB:Q9P258,
CC ECO:0000269|PubMed:25074804}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9P258}. Nucleus {ECO:0000250|UniProtKB:Q9P258}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P258}. Chromosome,
CC centromere {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q9P258}. Chromosome
CC {ECO:0000250|UniProtKB:Q9P258}. Midbody {ECO:0000250|UniProtKB:Q9P258}.
CC Cell membrane {ECO:0000250|UniProtKB:Q9P258}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9P258}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9P258}. 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. Colocalizes with cytoplasmic microtubules in
CC interphase cells. Colocalizes with RAC1 at the cell membrane.
CC {ECO:0000250|UniProtKB:Q9P258}.
CC -!- INDUCTION: Induced by TP53/p53 in response to oxidative stress and DNA
CC damage. {ECO:0000269|PubMed:28869598}.
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DR EMBL; AK076040; BAC36140.1; -; mRNA.
DR EMBL; AL954710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086666; AAH86666.1; -; mRNA.
DR EMBL; AK129370; BAC98180.1; -; mRNA.
DR CCDS; CCDS18852.1; -.
DR RefSeq; NP_776292.1; NM_173867.5.
DR RefSeq; XP_006538534.1; XM_006538471.3.
DR AlphaFoldDB; Q8BK67; -.
DR SMR; Q8BK67; -.
DR BioGRID; 224469; 12.
DR IntAct; Q8BK67; 4.
DR MINT; Q8BK67; -.
DR STRING; 10090.ENSMUSP00000071163; -.
DR iPTMnet; Q8BK67; -.
DR PhosphoSitePlus; Q8BK67; -.
DR SwissPalm; Q8BK67; -.
DR EPD; Q8BK67; -.
DR MaxQB; Q8BK67; -.
DR PaxDb; Q8BK67; -.
DR PeptideAtlas; Q8BK67; -.
DR PRIDE; Q8BK67; -.
DR ProteomicsDB; 255171; -.
DR Antibodypedia; 29372; 212 antibodies from 28 providers.
DR DNASU; 108911; -.
DR Ensembl; ENSMUST00000038893; ENSMUSP00000038144; ENSMUSG00000040945.
DR Ensembl; ENSMUST00000071169; ENSMUSP00000071163; ENSMUSG00000040945.
DR GeneID; 108911; -.
DR KEGG; mmu:108911; -.
DR UCSC; uc008vna.2; mouse.
DR CTD; 55920; -.
DR MGI; MGI:1919784; Rcc2.
DR VEuPathDB; HostDB:ENSMUSG00000040945; -.
DR eggNOG; KOG1427; Eukaryota.
DR GeneTree; ENSGT00940000156151; -.
DR HOGENOM; CLU_005210_7_0_1; -.
DR InParanoid; Q8BK67; -.
DR OMA; YGCLSGI; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q8BK67; -.
DR TreeFam; TF101168; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 108911; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Rcc2; mouse.
DR PRO; PR:Q8BK67; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BK67; protein.
DR Bgee; ENSMUSG00000040945; Expressed in ventricular zone and 272 other tissues.
DR ExpressionAtlas; Q8BK67; baseline and differential.
DR Genevisible; Q8BK67; MM.
DR GO; GO:0034506; C:chromosome, centromeric core domain; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:1990023; C:mitotic spindle midzone; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IGI:UniProtKB.
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; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; IGI:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP: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; IMP:UniProtKB.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:1900027; P:regulation of ruffle assembly; IMP:UniProtKB.
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 Acetylation; Cell cycle; Cell division; Cell membrane; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor;
KW Membrane; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..520
FT /note="Protein RCC2"
FT /id="PRO_0000206653"
FT REPEAT 101..163
FT /note="RCC1 1"
FT REPEAT 166..217
FT /note="RCC1 2"
FT REPEAT 219..269
FT /note="RCC1 3"
FT REPEAT 271..345
FT /note="RCC1 4"
FT REPEAT 346..399
FT /note="RCC1 5"
FT REPEAT 401..445
FT /note="RCC1 6"
FT REPEAT 446..499
FT /note="RCC1 7"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..323
FT /note="Required for interaction with RAC1"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
SQ SEQUENCE 520 AA; 55983 MW; 06E7B90EA721C373 CRC64;
MPRKKGAAWE EPSSGNGTAR AGPRRRGGPA GRKRERPERC SSSSGGGSSG DEDGPELDGA
PGGGKRTARP ATAGKAAGAA AIITEPEHTK ERVKLEGSKC KGQLLIFGAT NWDLIGRKEV
PKQQAAYRNL GQNLWGPHRY GCLSGVRVRT VVSGSCAAHS LLITTEGKLW SWGRNEKGQL
GHGDTKRVEA PRLIEALSHE AIVLAACGRN HTLALTDTGS VFAFGENKMG QLGLGNQTDA
VPSPAQIMYN GQPITKMACG AEFSMLMDCK GNLYSFGCPE YGQLGHNSDG KFIARAQRIE
YDCELVPRRV AIFIEKTKDG QILPVPNVVV RDVACGANHT LVLDSQKRVF SWGFGGYGRL
GHAEQKDEMV PRLVKLFDFP GRGATQIYAG YTCSFAVSEV GGLFFWGATN TSRESTMYPK
AVQDLCGWRI RSLACGKSSI IVAADESTIS WGPSPTFGEL GYGDHKPKSS TAAQEVKTLD
GIFSEQVAMG YSHSLVIARD ESEAEKEKLQ RLPEYTPRTL
