NH2L1_MOUSE
ID NH2L1_MOUSE Reviewed; 128 AA.
AC Q9D0T1; O08754; Q3UY64;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NHP2-like protein 1;
DE AltName: Full=Fertilization antigen 1 {ECO:0000303|PubMed:9114055};
DE Short=FA-1;
DE AltName: Full=High mobility group-like nuclear protein 2 homolog 1;
DE AltName: Full=Sperm-specific antigen 1;
DE AltName: Full=U4/U6.U5 small nuclear ribonucleoprotein SNU13 {ECO:0000250|UniProtKB:P55769};
DE AltName: Full=U4/U6.U5 tri-snRNP 15.5 kDa protein;
DE Contains:
DE RecName: Full=NHP2-like protein 1, N-terminally processed;
GN Name=Snu13 {ECO:0000250|UniProtKB:P55769};
GN Synonyms=Nhp2l1 {ECO:0000312|MGI:MGI:893586}, Ssfa1;
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 {ECO:0000312|EMBL:BAB23329.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9114055; DOI=10.1073/pnas.94.9.4704;
RA Zhu X., Naz R.K.;
RT "Fertilization antigen-1: cDNA cloning, testis-specific expression, and
RT immunocontraceptive effects.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4704-4709(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Retina;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. Binds to the 5'-stem-loop of U4 snRNA and thereby
CC contributes to spliceosome assembly. The protein undergoes a
CC conformational change upon RNA-binding. {ECO:0000250|UniProtKB:P55769}.
CC -!- SUBUNIT: Identified in the spliceosome B complex. Component of the
CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57,
CC SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39.
CC Interacts with RAD17 and PRPF31. The complex formed by SNU13 and PRPF31
CC binds U4 snRNA. The complex formed by SNU13 and PRPF31 binds also
CC U4atac snRNA, a characteristic component of specific, less abundant
CC spliceosomal complexes. {ECO:0000250|UniProtKB:P55769}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55769}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P55769}. Note=Concentrated in the
CC dense fibrillar component of the nucleolus.
CC {ECO:0000250|UniProtKB:P55769}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U95114; AAC53177.1; ALT_FRAME; mRNA.
DR EMBL; AK004489; BAB23329.1; -; mRNA.
DR EMBL; AK134943; BAE22349.1; -; mRNA.
DR EMBL; AK145608; BAE26537.1; -; mRNA.
DR EMBL; AK168930; BAE40743.1; -; mRNA.
DR EMBL; AK169103; BAE40885.1; -; mRNA.
DR EMBL; BC026755; AAH26755.1; -; mRNA.
DR EMBL; BC054450; AAH54450.1; -; mRNA.
DR EMBL; BC083315; AAH83315.1; -; mRNA.
DR CCDS; CCDS37154.1; -.
DR PIR; T10105; T10105.
DR RefSeq; NP_035612.2; NM_011482.4.
DR RefSeq; XP_003689233.1; XM_003689185.5.
DR AlphaFoldDB; Q9D0T1; -.
DR BMRB; Q9D0T1; -.
DR SMR; Q9D0T1; -.
DR BioGRID; 203509; 52.
DR IntAct; Q9D0T1; 52.
DR MINT; Q9D0T1; -.
DR STRING; 10090.ENSMUSP00000091840; -.
DR iPTMnet; Q9D0T1; -.
DR PhosphoSitePlus; Q9D0T1; -.
DR SwissPalm; Q9D0T1; -.
DR EPD; Q9D0T1; -.
DR jPOST; Q9D0T1; -.
DR MaxQB; Q9D0T1; -.
DR PaxDb; Q9D0T1; -.
DR PeptideAtlas; Q9D0T1; -.
DR PRIDE; Q9D0T1; -.
DR ProteomicsDB; 287506; -.
DR TopDownProteomics; Q9D0T1; -.
DR Antibodypedia; 27035; 108 antibodies from 26 providers.
DR DNASU; 20826; -.
DR Ensembl; ENSMUST00000080622; ENSMUSP00000091840; ENSMUSG00000063480.
DR GeneID; 20826; -.
DR KEGG; mmu:20826; -.
DR UCSC; uc007wya.1; mouse.
DR CTD; 4809; -.
DR MGI; MGI:893586; Snu13.
DR VEuPathDB; HostDB:ENSMUSG00000063480; -.
DR eggNOG; KOG3387; Eukaryota.
DR GeneTree; ENSGT00550000074840; -.
DR HOGENOM; CLU_084513_4_1_1; -.
DR InParanoid; Q9D0T1; -.
DR OMA; KPFYVRF; -.
DR OrthoDB; 1497609at2759; -.
DR PhylomeDB; Q9D0T1; -.
DR TreeFam; TF300184; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR BioGRID-ORCS; 20826; 26 hits in 52 CRISPR screens.
DR ChiTaRS; Nhp2l1; mouse.
DR PRO; PR:Q9D0T1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D0T1; protein.
DR Bgee; ENSMUSG00000063480; Expressed in epiblast (generic) and 63 other tissues.
DR Genevisible; Q9D0T1; MM.
DR GO; GO:0031428; C:box C/D RNP complex; IMP:CAFA.
DR GO; GO:0001651; C:dense fibrillar component; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:UniProtKB.
DR GO; GO:0005690; C:U4atac snRNP; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0034512; F:box C/D RNA binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; ISO:MGI.
DR GO; GO:0034511; F:U3 snoRNA binding; ISO:MGI.
DR GO; GO:0030621; F:U4 snRNA binding; ISO:MGI.
DR GO; GO:0030622; F:U4atac snRNA binding; ISS:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:CAFA.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IDA:MGI.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..128
FT /note="NHP2-like protein 1"
FT /id="PRO_0000423262"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT CHAIN 2..128
FT /note="NHP2-like protein 1, N-terminally processed"
FT /id="PRO_0000136779"
FT REGION 36..48
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT REGION 96..128
FT /note="Important for U4 snRNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT SITE 61
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT SITE 86
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT MOD_RES 2
FT /note="N-acetylthreonine; in NHP2-like protein 1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55769"
FT CONFLICT 9
FT /note="K -> R (in Ref. 2; BAB23329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14174 MW; 78849EBB497089ED CRC64;
MTEADVNPKA YPLADAHLTK KLLDLVQQSC NYKQLRKGAN EATKTLNRGI SEFIVMAADA
EPLEIILHLP LLCEDKNVPY VFVRSKQALG RACGVSRPVI ACSVTIKEGS QLKQQIQSIQ
QSIERLLV
