KRR1_MOUSE
ID KRR1_MOUSE Reviewed; 380 AA.
AC Q8BGA5; Q3UIG9; Q52KQ6; Q5EBJ5; Q8C029;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=KRR1 small subunit processome component homolog;
DE AltName: Full=HIV-1 Rev-binding protein 2 homolog;
DE AltName: Full=KRR-R motif-containing protein 1;
GN Name=Krr1; Synonyms=Hrb2;
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;
RC TISSUE=Kidney, Liver, Olfactory bulb, Pituitary, and Thymus;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Pituitary;
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).
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13601}. Nucleus
CC {ECO:0000250|UniProtKB:Q13601}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13601}.
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27537.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK030560; BAC27022.1; -; mRNA.
DR EMBL; AK032472; BAC27888.1; -; mRNA.
DR EMBL; AK041854; BAC31083.1; -; mRNA.
DR EMBL; AK146926; BAE27537.1; ALT_FRAME; mRNA.
DR EMBL; AK168675; BAE40525.1; -; mRNA.
DR EMBL; AC167231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466539; EDL21743.1; -; Genomic_DNA.
DR EMBL; BC089510; AAH89510.1; -; mRNA.
DR EMBL; BC094236; AAH94236.1; -; mRNA.
DR CCDS; CCDS24168.1; -.
DR RefSeq; NP_848725.2; NM_178610.4.
DR AlphaFoldDB; Q8BGA5; -.
DR SMR; Q8BGA5; -.
DR BioGRID; 206745; 4.
DR STRING; 10090.ENSMUSP00000125746; -.
DR iPTMnet; Q8BGA5; -.
DR PhosphoSitePlus; Q8BGA5; -.
DR EPD; Q8BGA5; -.
DR MaxQB; Q8BGA5; -.
DR PaxDb; Q8BGA5; -.
DR PeptideAtlas; Q8BGA5; -.
DR PRIDE; Q8BGA5; -.
DR ProteomicsDB; 263464; -.
DR Antibodypedia; 29617; 181 antibodies from 28 providers.
DR DNASU; 52705; -.
DR Ensembl; ENSMUST00000163048; ENSMUSP00000125746; ENSMUSG00000063334.
DR GeneID; 52705; -.
DR KEGG; mmu:52705; -.
DR UCSC; uc007hag.2; mouse.
DR CTD; 11103; -.
DR MGI; MGI:1289274; Krr1.
DR VEuPathDB; HostDB:ENSMUSG00000063334; -.
DR eggNOG; KOG2874; Eukaryota.
DR GeneTree; ENSGT00390000018775; -.
DR HOGENOM; CLU_040185_0_0_1; -.
DR InParanoid; Q8BGA5; -.
DR OMA; HKKEKFV; -.
DR OrthoDB; 944899at2759; -.
DR PhylomeDB; Q8BGA5; -.
DR TreeFam; TF105745; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 52705; 29 hits in 73 CRISPR screens.
DR ChiTaRS; Krr1; mouse.
DR PRO; PR:Q8BGA5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BGA5; protein.
DR Bgee; ENSMUSG00000063334; Expressed in optic fissure and 259 other tissues.
DR ExpressionAtlas; Q8BGA5; baseline and differential.
DR Genevisible; Q8BGA5; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR PANTHER; PTHR12581; PTHR12581; 1.
DR Pfam; PF17903; KH_8; 1.
DR PIRSF; PIRSF006515; KRR1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..380
FT /note="KRR1 small subunit processome component homolog"
FT /id="PRO_0000050115"
FT DOMAIN 153..205
FT /note="KH"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CONFLICT 38
FT /note="G -> V (in Ref. 4; AAH94236)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="P -> Q (in Ref. 1; BAC27888)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="P -> Q (in Ref. 1; BAE27537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43538 MW; B0A0F674F93F3C7D CRC64;
MATSAEAPAK EAQKRDSQPQ KQKRETQDEA ELLTVPDGWK EPAFSKEDNP RGLLEESSFA
TLFPKYREAY LKECWPLVQK ALNEHHVKAT LDLIEGSMTV CTTKKTFDPY IIIRARDLIK
LLARSVSFEQ AVRILQDDVA CDIIKIGSLV RNKERFVKRR QRLIGPKGST LKALELLTNC
YVMVQGNTVS AIGPFSGLKE VRKVVLDTMK NIHPIYNIKT LMIKRELAKD SELRSQSWER
FLPQFKHKNV NKRKEPKKKS VKKEYTPFPP PQPESQIDKE LASGEYFLKA SQKKRQKMEA
IKAKQAEALT KRQEERNKAF IPPKEKPAVK PKEASTETKI DVAAIKEKVK KAKTKKLGAL
TAEEVKLKME ADEKKQKRKK
