NSA2_MOUSE
ID NSA2_MOUSE Reviewed; 260 AA.
AC Q9CR47; A0JNU8; Q8BHQ6; Q8BHT0; Q9CRQ0; Q9CS34; Q9CYK0; Q9JKF9;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribosome biogenesis protein NSA2 homolog;
DE AltName: Full=L-name-related protein 42;
DE Short=LNR42;
DE AltName: Full=TGF-beta-inducible nuclear protein 1;
GN Name=Nsa2; Synonyms=Tinp1;
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; TISSUE=Embryo, Embryonic head, Kidney, 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 [MRNA].
RC TISSUE=Macrophage;
RA Guo H., Cai Q., Schroeder R., Kuo P.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: Involved in the biogenesis of the 60S ribosomal subunit. May
CC play a part in the quality control of pre-60S particles (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC Ribosome biogenesis protein NSA2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63492.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK002474; BAB22128.2; -; mRNA.
DR EMBL; AK012832; BAB28500.1; -; mRNA.
DR EMBL; AK014275; BAB29237.1; -; mRNA.
DR EMBL; AK017605; BAB30834.1; -; mRNA.
DR EMBL; AK019203; BAB31599.3; -; mRNA.
DR EMBL; AK019279; BAC25587.1; -; mRNA.
DR EMBL; AK019379; BAB31689.1; -; mRNA.
DR EMBL; AK078457; BAC37283.1; -; mRNA.
DR EMBL; AF238866; AAF63492.1; ALT_FRAME; mRNA.
DR EMBL; BC126976; AAI26977.1; -; mRNA.
DR CCDS; CCDS36756.1; -.
DR RefSeq; NP_067527.3; NM_021552.5.
DR AlphaFoldDB; Q9CR47; -.
DR SMR; Q9CR47; -.
DR BioGRID; 208514; 3.
DR IntAct; Q9CR47; 1.
DR STRING; 10090.ENSMUSP00000073161; -.
DR PhosphoSitePlus; Q9CR47; -.
DR EPD; Q9CR47; -.
DR MaxQB; Q9CR47; -.
DR PaxDb; Q9CR47; -.
DR PeptideAtlas; Q9CR47; -.
DR PRIDE; Q9CR47; -.
DR ProteomicsDB; 295526; -.
DR Antibodypedia; 12347; 84 antibodies from 28 providers.
DR DNASU; 59050; -.
DR Ensembl; ENSMUST00000073456; ENSMUSP00000073161; ENSMUSG00000060739.
DR GeneID; 59050; -.
DR KEGG; mmu:59050; -.
DR UCSC; uc007rns.2; mouse.
DR CTD; 10412; -.
DR MGI; MGI:1913883; Nsa2.
DR VEuPathDB; HostDB:ENSMUSG00000060739; -.
DR eggNOG; KOG3163; Eukaryota.
DR GeneTree; ENSGT00390000018706; -.
DR HOGENOM; CLU_1070048_0_0_1; -.
DR InParanoid; Q9CR47; -.
DR OMA; TKSWKRM; -.
DR OrthoDB; 1079827at2759; -.
DR PhylomeDB; Q9CR47; -.
DR TreeFam; TF300766; -.
DR BioGRID-ORCS; 59050; 24 hits in 52 CRISPR screens.
DR ChiTaRS; Nsa2; mouse.
DR PRO; PR:Q9CR47; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CR47; protein.
DR Bgee; ENSMUSG00000060739; Expressed in undifferentiated genital tubercle and 81 other tissues.
DR ExpressionAtlas; Q9CR47; baseline and differential.
DR Genevisible; Q9CR47; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR CDD; cd11381; NSA2; 1.
DR InterPro; IPR039411; NSA2_fam.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR PANTHER; PTHR12642; PTHR12642; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT CHAIN 1..260
FT /note="Ribosome biogenesis protein NSA2 homolog"
FT /id="PRO_0000122260"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95478"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95478"
FT CONFLICT 1..44
FT /note="MPQNEYIELHRKRYGYRLDYHEKKRKKEGREAHERSKKAKKMIG -> MHVQ
FT RRQKNDC (in Ref. 1; BAB22128)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="E -> G (in Ref. 1; BAC25587)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="G -> E (in Ref. 1; BAB30834)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="W -> C (in Ref. 1; BAB30834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 30036 MW; 229B1B4D8F5F8446 CRC64;
MPQNEYIELH RKRYGYRLDY HEKKRKKEGR EAHERSKKAK KMIGLKAKLY HKQRHAEKIQ
MKKTIKMHEK RNTKQKDDEK TPQGAVPAYL LDREGQSRAK VLSNMIKQKR KEKAGKWEVP
LPKVRAQGET EVLKVIRTGK RKKKAWKRMV TKVCFVGDGF TRKPPKYERF IRPMGLRFKK
AHVTHPELKA TFCLPILGVK KNPSSPLYTT LGVITKGTVI EVNVSELGLV TQGGKVIWGK
YAQVTNNPEN DGCINAVLLV
