ID NH2L1_HUMAN Reviewed; 128 AA.
AC P55769;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 222.
DE RecName: Full=NHP2-like protein 1;
DE AltName: Full=High mobility group-like nuclear protein 2 homolog 1;
DE AltName: Full=OTK27;
DE AltName: Full=SNU13 homolog;
DE Short=hSNU13;
DE AltName: Full=U4/U6.U5 small nuclear ribonucleoprotein SNU13 {ECO:0000312|HGNC:HGNC:7819};
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:0000312|HGNC:HGNC:7819}; Synonyms=NHP2L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8978773; DOI=10.1159/000134186;
RA Saito H., Fujiwara T., Shin S., Okui K., Nakamura Y.;
RT "Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a protein
RT highly homologous to yeast nuclear protein NHP2.";
RL Cytogenet. Cell Genet. 72:191-193(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-7 AND 92-106, FUNCTION,
RP AND MUTAGENESIS OF GLY-38; ALA-57; TYR-80 AND 96-SER--VAL-128.
RX PubMed=10545122; DOI=10.1093/emboj/18.21.6119;
RA Nottrott S., Hartmuth K., Fabrizio P., Urlaub H., Vidovic I., Ficner R.,
RA Luehrmann R.;
RT "Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with
RT the 5' stem-loop of U4 snRNA.";
RL EMBO J. 18:6119-6133(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Urinary bladder;
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 [7]
RP PROTEIN SEQUENCE OF 2-20; 22-33; 77-84 AND 114-125, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RAD17.
RX PubMed=10593953; DOI=10.1074/jbc.274.51.36544;
RA Chang M.-S., Sasaki H., Campbell M.S., Kraeft S.-K., Sutherland R.,
RA Yang C.-Y., Liu Y., Auclair D., Hao L., Sonoda H., Ferland L.H., Chen L.B.;
RT "HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes after UV
RT irradiation.";
RL J. Biol. Chem. 274:36544-36549(1999).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [10]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=11163207; DOI=10.1016/s1097-2765(00)00131-3;
RA Vidovic I., Nottrott S., Hartmuth K., Luehrmann R., Ficner R.;
RT "Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA
RT fragment.";
RL Mol. Cell 6:1331-1342(2000).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=18044964; DOI=10.1021/bi701254q;
RA Soss S.E., Flynn P.F.;
RT "Functional implications for a prototypical K-turn binding protein from
RT structural and dynamical studies of 15.5K.";
RL Biochemistry 46:14979-14986(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PRPF31 AND STEM-LOOP
RP RNA OF U4 SNRNA, AND FUNCTION.
RX PubMed=17412961; DOI=10.1126/science.1137924;
RA Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R.,
RA Carlomagno T., Wahl M.C.;
RT "Binding of the human Prp31 Nop domain to a composite RNA-protein platform
RT in U4 snRNP.";
RL Science 316:115-120(2007).
RN [19] {ECO:0007744|PDB:3SIU, ECO:0007744|PDB:3SIV}
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) IN COMPLEX WITH PRPF31 AND STEM-LOOP
RP RNA OF U4ATAC SNRNA, AND INTERACTION WITH PRPF31.
RX PubMed=21784869; DOI=10.1261/rna.2690611;
RA Liu S., Ghalei H., Luhrmann R., Wahl M.C.;
RT "Structural basis for the dual U4 and U4atac snRNA-binding specificity of
RT spliceosomal protein hPrp31.";
RL RNA 17:1655-1663(2011).
RN [20] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [21] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, IDENTIFICATION
RP BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
RN [22] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC of the small eukaryotic ribosomal subunit. During the assembly of the
CC SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC RNA chaperone and ribosomal proteins associate with the nascent pre-
CC rRNA and work in concert to generate RNA folding, modifications,
CC rearrangements and cleavage as well as targeted degradation of pre-
CC ribosomal RNA by the RNA exosome (PubMed:34516797). Involved in pre-
CC mRNA splicing as component of the spliceosome (PubMed:28781166). Binds
CC to the 5'-stem-loop of U4 snRNA and thereby contributes to spliceosome
CC assembly (PubMed:10545122, PubMed:17412961). The protein undergoes a
CC conformational change upon RNA-binding (PubMed:17412961,
CC PubMed:10545122, PubMed:28781166). {ECO:0000269|PubMed:10545122,
CC ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:34516797}.
CC -!- SUBUNIT: Identified in the spliceosome B complex (PubMed:28781166).
CC Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and
CC U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200,
CC TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and
CC USP39 (PubMed:16723661, PubMed:26912367). Interacts with RAD17 and
CC PRPF31 (PubMed:10593953, PubMed:17412961, PubMed:21784869). The complex
CC formed by SNU13 and PRPF31 binds U4 snRNA (PubMed:17412961). The
CC complex formed by SNU13 and PRPF31 binds also U4atac snRNA, a
CC characteristic component of specific, less abundant spliceosomal
CC complexes (PubMed:21784869). Part of the small subunit (SSU)
CC processome, composed of more than 70 proteins and the RNA chaperone
CC small nucleolar RNA (snoRNA) U3 (PubMed:34516797).
CC {ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:17412961, ECO:0000269|PubMed:21784869,
CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:34516797}.
CC -!- INTERACTION:
CC P55769; Q9UHK0: NUFIP1; NbExp=2; IntAct=EBI-712228, EBI-2563549;
CC P55769; Q16637: SMN2; NbExp=3; IntAct=EBI-712228, EBI-395421;
CC P55769; PRO_0000038596 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-712228, EBI-6179727;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:34516797}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:10593953, ECO:0000269|PubMed:12429849,
CC ECO:0000269|Ref.7}. Note=Concentrated in the dense fibrillar component
CC of the nucleolus. {ECO:0000269|PubMed:10593953}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
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DR EMBL; D50420; BAA23363.1; -; mRNA.
DR EMBL; AF155235; AAF06959.1; -; mRNA.
DR EMBL; AF091076; AAC72945.1; -; mRNA.
DR EMBL; CR456531; CAG30417.1; -; mRNA.
DR EMBL; Z83840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005358; AAH05358.1; -; mRNA.
DR EMBL; BC019282; AAH19282.1; -; mRNA.
DR CCDS; CCDS14022.1; -.
DR CCDS; CCDS33653.1; -.
DR RefSeq; NP_001003796.1; NM_001003796.1.
DR RefSeq; NP_004999.1; NM_005008.3.
DR PDB; 1E7K; X-ray; 2.90 A; A/B=1-128.
DR PDB; 2JNB; NMR; -; A=1-128.
DR PDB; 2OZB; X-ray; 2.60 A; A/D=1-128.
DR PDB; 3JCR; EM; 7.00 A; I=1-128.
DR PDB; 3SIU; X-ray; 2.63 A; A/D=1-128.
DR PDB; 3SIV; X-ray; 3.30 A; A/D/G/J=1-128.
DR PDB; 5O9Z; EM; 4.50 A; O=1-128.
DR PDB; 6AH0; EM; 5.70 A; M=1-128.
DR PDB; 6AHD; EM; 3.80 A; M=1-128.
DR PDB; 6QW6; EM; 2.92 A; 4D=1-128.
DR PDB; 6QX9; EM; 3.28 A; 4D=1-128.
DR PDB; 7MQ8; EM; 3.60 A; SE/SF=1-128.
DR PDB; 7MQ9; EM; 3.87 A; SE/SF=1-128.
DR PDB; 7MQA; EM; 2.70 A; SE/SF=1-128.
DR PDBsum; 1E7K; -.
DR PDBsum; 2JNB; -.
DR PDBsum; 2OZB; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 3SIU; -.
DR PDBsum; 3SIV; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P55769; -.
DR BMRB; P55769; -.
DR EMDB; EMD-23936; -.
DR EMDB; EMD-23937; -.
DR EMDB; EMD-23938; -.
DR EMDB; EMD-3766; -.
DR EMDB; EMD-4658; -.
DR EMDB; EMD-4665; -.
DR EMDB; EMD-6581; -.
DR EMDB; EMD-9621; -.
DR EMDB; EMD-9624; -.
DR SMR; P55769; -.
DR BioGRID; 110874; 283.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-2511; Small ribosomal subunit processome.
DR CORUM; P55769; -.
DR IntAct; P55769; 52.
DR MINT; P55769; -.
DR STRING; 9606.ENSP00000383949; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR GlyGen; P55769; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55769; -.
DR PhosphoSitePlus; P55769; -.
DR SwissPalm; P55769; -.
DR BioMuta; SNU13; -.
DR DMDM; 2500345; -.
DR SWISS-2DPAGE; P55769; -.
DR EPD; P55769; -.
DR jPOST; P55769; -.
DR MassIVE; P55769; -.
DR PaxDb; 9606-ENSP00000383949; -.
DR PeptideAtlas; P55769; -.
DR ProteomicsDB; 56859; -.
DR Pumba; P55769; -.
DR TopDownProteomics; P55769; -.
DR Antibodypedia; 27035; 132 antibodies from 26 providers.
DR DNASU; 4809; -.
DR Ensembl; ENST00000215956.10; ENSP00000215956.5; ENSG00000100138.15.
DR Ensembl; ENST00000401959.6; ENSP00000383949.1; ENSG00000100138.15.
DR Ensembl; ENST00000648674.1; ENSP00000497142.1; ENSG00000100138.15.
DR GeneID; 4809; -.
DR KEGG; hsa:4809; -.
DR MANE-Select; ENST00000401959.6; ENSP00000383949.1; NM_001003796.2; NP_001003796.1.
DR AGR; HGNC:7819; -.
DR CTD; 4809; -.
DR DisGeNET; 4809; -.
DR GeneCards; SNU13; -.
DR HGNC; HGNC:7819; SNU13.
DR HPA; ENSG00000100138; Low tissue specificity.
DR MIM; 601304; gene.
DR MIM; 601876; gene.
DR neXtProt; NX_P55769; -.
DR OpenTargets; ENSG00000100138; -.
DR PharmGKB; PA31621; -.
DR VEuPathDB; HostDB:ENSG00000100138; -.
DR eggNOG; KOG3387; Eukaryota.
DR GeneTree; ENSGT00550000074840; -.
DR HOGENOM; CLU_084513_4_1_1; -.
DR InParanoid; P55769; -.
DR OMA; IKNQIYA; -.
DR OrthoDB; 5481533at2759; -.
DR PhylomeDB; P55769; -.
DR TreeFam; TF300184; -.
DR PathwayCommons; P55769; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; P55769; -.
DR SIGNOR; P55769; -.
DR BioGRID-ORCS; 4809; 838 hits in 1152 CRISPR screens.
DR ChiTaRS; SNU13; human.
DR EvolutionaryTrace; P55769; -.
DR GeneWiki; NHP2L1; -.
DR GenomeRNAi; 4809; -.
DR Pharos; P55769; Tbio.
DR PRO; PR:P55769; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P55769; Protein.
DR Bgee; ENSG00000100138; Expressed in adult organism and 219 other cell types or tissues.
DR ExpressionAtlas; P55769; baseline and differential.
DR Genevisible; P55769; HS.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:GO_Central.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0001651; C:dense fibrillar component; IDA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB.
DR GO; GO:0005690; C:U4atac snRNP; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0034512; F:box C/D RNA binding; IDA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:GO_Central.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:GO_Central.
DR GO; GO:0030622; F:U4atac snRNA binding; IDA:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR CDD; cd21104; SNU13; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR InterPro; IPR004037; Ribosomal_eL8-like_CS.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR InterPro; IPR018492; Ribosomal_eL8/Nhp2.
DR PANTHER; PTHR23105:SF38; NHP2-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR23105; RIBOSOMAL PROTEIN L7AE FAMILY MEMBER; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; L30e-like; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..128
FT /note="NHP2-like protein 1"
FT /id="PRO_0000423260"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..128
FT /note="NHP2-like protein 1, N-terminally processed"
FT /id="PRO_0000136778"
FT REGION 36..48
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000269|PubMed:17412961,
FT ECO:0000269|PubMed:21784869"
FT REGION 96..128
FT /note="Important for U4 snRNA-binding"
FT /evidence="ECO:0000269|PubMed:10545122"
FT SITE 61
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000269|PubMed:17412961,
FT ECO:0000269|PubMed:21784869"
FT SITE 86
FT /note="Interaction with U4 snRNA and U4atac snRNA"
FT /evidence="ECO:0000269|PubMed:17412961,
FT ECO:0000269|PubMed:21784869"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylthreonine; in NHP2-like protein 1, N-
FT terminally processed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0T1"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 19
FT /note="T -> N (in dbSNP:rs1802521)"
FT /id="VAR_034155"
FT MUTAGEN 38
FT /note="G->K: Abolishes U4 snRNA-binding."
FT /evidence="ECO:0000269|PubMed:10545122"
FT MUTAGEN 57
FT /note="A->F: Abolishes U4 snRNA-binding."
FT /evidence="ECO:0000269|PubMed:10545122"
FT MUTAGEN 80
FT /note="Y->A: Reduces U4 snRNA-binding by about 50%."
FT /evidence="ECO:0000269|PubMed:10545122"
FT MUTAGEN 96..128
FT /note="Missing: Abolishes U4 snRNA-binding."
FT /evidence="ECO:0000269|PubMed:10545122"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2JNB"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:2OZB"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2OZB"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2OZB"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2OZB"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2OZB"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:2OZB"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2OZB"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:2OZB"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2OZB"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:2OZB"
SQ SEQUENCE 128 AA; 14174 MW; 78849EBB497089ED CRC64;
MTEADVNPKA YPLADAHLTK KLLDLVQQSC NYKQLRKGAN EATKTLNRGI SEFIVMAADA
EPLEIILHLP LLCEDKNVPY VFVRSKQALG RACGVSRPVI ACSVTIKEGS QLKQQIQSIQ
QSIERLLV
//
