PIMRE_MOUSE
ID PIMRE_MOUSE Reviewed; 231 AA.
AC Q8BFY7; Q8K2Z7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein PIMREG {ECO:0000305};
DE AltName: Full=CALM-interactor expressed in thymus and spleen homolog;
DE AltName: Full=PICALM-interacting mitotic regulator {ECO:0000250|UniProtKB:Q9BSJ6};
DE AltName: Full=Regulator of chromosome segregation protein 1;
GN Name=Pimreg {ECO:0000250|UniProtKB:Q9BSJ6};
GN Synonyms=Cats, Fam64a {ECO:0000312|MGI:MGI:1924434}, Rcs1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord, and Wolffian duct;
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] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19383357; DOI=10.1016/j.molonc.2008.08.001;
RA Archangelo L.F., Greif P.A., Hoelzel M., Harasim T., Kremmer E.,
RA Przemeck G.K., Eick D., Deshpande A.J., Buske C., de Angelis M.H.,
RA Saad S.T., Bohlander S.K.;
RT "The CALM and CALM/AF10 interactor CATS is a marker for proliferation.";
RL Mol. Oncol. 2:356-367(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: During mitosis, may play a role in the metaphase-to-anaphase
CC transition. {ECO:0000250|UniProtKB:Q9BSJ6}.
CC -!- SUBUNIT: Interacts with PICALM; this interaction may target PICALM to
CC the nucleus. During mitosis, associates with HDAC2 and MTA2 subunits of
CC the chromatin-remodeling NuRD complex; this association is strongest at
CC prometaphase and decreases as the cell progresses through metaphase and
CC anaphase. {ECO:0000250|UniProtKB:Q9BSJ6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BSJ6}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9BSJ6}. Note=Partially localizes to
CC the nucleolus. {ECO:0000250|UniProtKB:Q9BSJ6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BFY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFY7-2; Sequence=VSP_023998;
CC -!- TISSUE SPECIFICITY: Mainly expressed in thymus and ovary. Expressed in
CC all T-cell subpopulations isolated from the thymus, macrophages, pro-
CC erythrocytes, granulocytes, mast cells and progenitor cells.
CC {ECO:0000269|PubMed:19383357}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed at 9.5 dpc, including high levels
CC in the neural tube, somites, the posterior region of the midbrain,
CC olfactory placode and the branchial arches. At 10.5 dpc, reduction of
CC the widespread expression and stronger expression in the neural tube,
CC branchial arches, developing limbs, telencephalon, nasal process, lense
CC vesicle, anterior and posterior regions of the mid- and hindbrain. From
CC 11.5 dpc on, strongly expressed in the genital tubercle and hair and
CC vibrissae follicles. From 12.5 dpc onwards, expression decreases, with
CC a complete lack of expression in the cephalic region and the neural
CC tube at 14.5 dpc. Strongly expressed during limb development, with
CC higher levels in hindlimbs compared to forelimbs and expression
CC slightly more marked in the posterior region of the limb buds. At 11.5
CC and 12.5 dpc, detected at the distal domain and the underlying
CC mesenchyme, but not in the apical ectodermal ridge. Distally, becomes
CC confined to the digits at 13.5 and 14.5 dpc.
CC {ECO:0000269|PubMed:19383357}.
CC -!- DOMAIN: The N-terminal destruction box 2 (D-box 2) is required for
CC APC/C ubiquitination and proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9BSJ6}.
CC -!- PTM: Ubiquitinated by the anaphase-promoting complex/cyclosome (APC/C)
CC complex in the presence of FZR1, leading to its degradation by the
CC proteasome during mitotic exit. However, degradation is not essential
CC for normal mitotic progression within a single cell cycle (By
CC similarity). {ECO:0000250|UniProtKB:Q9BSJ6}.
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DR EMBL; AK049710; BAC33887.1; -; mRNA.
DR EMBL; AK078429; BAC37270.1; -; mRNA.
DR EMBL; BX119911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029115; AAH29115.1; -; mRNA.
DR CCDS; CCDS48840.1; -. [Q8BFY7-1]
DR RefSeq; NP_653109.2; NM_144526.3. [Q8BFY7-1]
DR RefSeq; XP_006532039.1; XM_006531976.2. [Q8BFY7-1]
DR AlphaFoldDB; Q8BFY7; -.
DR SMR; Q8BFY7; -.
DR BioGRID; 224601; 1.
DR STRING; 10090.ENSMUSP00000021164; -.
DR iPTMnet; Q8BFY7; -.
DR PhosphoSitePlus; Q8BFY7; -.
DR EPD; Q8BFY7; -.
DR jPOST; Q8BFY7; -.
DR MaxQB; Q8BFY7; -.
DR PaxDb; Q8BFY7; -.
DR PeptideAtlas; Q8BFY7; -.
DR PRIDE; Q8BFY7; -.
DR ProteomicsDB; 289425; -. [Q8BFY7-1]
DR ProteomicsDB; 289426; -. [Q8BFY7-2]
DR Antibodypedia; 42756; 76 antibodies from 15 providers.
DR DNASU; 109212; -.
DR Ensembl; ENSMUST00000021164; ENSMUSP00000021164; ENSMUSG00000020808. [Q8BFY7-1]
DR GeneID; 109212; -.
DR KEGG; mmu:109212; -.
DR UCSC; uc007jxz.1; mouse. [Q8BFY7-1]
DR CTD; 54478; -.
DR MGI; MGI:1924434; Pimreg.
DR VEuPathDB; HostDB:ENSMUSG00000020808; -.
DR eggNOG; ENOG502S0SN; Eukaryota.
DR GeneTree; ENSGT00390000008128; -.
DR HOGENOM; CLU_1209428_0_0_1; -.
DR InParanoid; Q8BFY7; -.
DR OMA; QMGPHAH; -.
DR OrthoDB; 1270977at2759; -.
DR PhylomeDB; Q8BFY7; -.
DR TreeFam; TF336322; -.
DR BioGRID-ORCS; 109212; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ctss; mouse.
DR PRO; PR:Q8BFY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BFY7; protein.
DR Bgee; ENSMUSG00000020808; Expressed in ventricular zone and 130 other tissues.
DR ExpressionAtlas; Q8BFY7; baseline and differential.
DR Genevisible; Q8BFY7; MM.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR InterPro; IPR009932; RCS1.
DR PANTHER; PTHR35819; PTHR35819; 1.
DR Pfam; PF07326; RCS1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..231
FT /note="Protein PIMREG"
FT /id="PRO_0000281160"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..17
FT /note="D-box 1"
FT MOTIF 53..56
FT /note="D-box 2"
FT COMPBIAS 13..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ6"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ6"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 128
FT /note="Phosphoserine; by Uhmk1; in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ6"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ6"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSJ6"
FT VAR_SEQ 81..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023998"
FT CONFLICT 163
FT /note="A -> T (in Ref. 3; AAH29115)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="S -> A (in Ref. 3; AAH29115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25686 MW; DD1FE87C5B98664F CRC64;
MASQWQGMRT SVRRRSLLKE EQLEKKEVTR SAGGHPETGP LGSLCRQFQR RLPLRAVSLN
LGNGPSWKRL ESPEPEQQGL QAAARSAKSA LGAMSQRIQE SCQSGTKWLM ETQVKVRRKR
GAQKDRGSPP PSLSQKNTRL CRANRDARVG GHLRLSGQMG PHAHRRQRLR RESALRSPCS
STEPLCSPSE SDSDLEPVGA GIQHLQKLSQ RLDRAIKAEE SGDMTVSLIR E
