NH2L1_MACFA
ID NH2L1_MACFA Reviewed; 128 AA.
AC Q4R5C6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=NHP2-like protein 1;
DE AltName: Full=High mobility group-like nuclear protein 2 homolog 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}; Synonyms=NHP2L1;
GN ORFNames=QtrA-11204;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AB169618; BAE01699.1; -; mRNA.
DR RefSeq; NP_001271884.1; NM_001284955.1.
DR RefSeq; XP_005567197.1; XM_005567140.2.
DR AlphaFoldDB; Q4R5C6; -.
DR BMRB; Q4R5C6; -.
DR SMR; Q4R5C6; -.
DR STRING; 9541.XP_005567196.1; -.
DR Ensembl; ENSMFAT00000066331; ENSMFAP00000015804; ENSMFAG00000031096.
DR GeneID; 101926085; -.
DR CTD; 4809; -.
DR VEuPathDB; HostDB:ENSMFAG00000031096; -.
DR eggNOG; KOG3387; Eukaryota.
DR GeneTree; ENSGT00550000074840; -.
DR OrthoDB; 1497609at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR Bgee; ENSMFAG00000031096; Expressed in pituitary gland and 13 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0030622; F:U4atac snRNA binding; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
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 2: Evidence at transcript 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_0000423261"
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_0000319315"
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:0000250|UniProtKB:Q9D0T1"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55769"
SQ SEQUENCE 128 AA; 14174 MW; 78849EBB497089ED CRC64;
MTEADVNPKA YPLADAHLTK KLLDLVQQSC NYKQLRKGAN EATKTLNRGI SEFIVMAADA
EPLEIILHLP LLCEDKNVPY VFVRSKQALG RACGVSRPVI ACSVTIKEGS QLKQQIQSIQ
QSIERLLV
