SNR27_HUMAN
ID SNR27_HUMAN Reviewed; 155 AA.
AC Q8WVK2; Q15410;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein;
DE Short=U4/U6.U5 snRNP 27 kDa protein;
DE Short=U4/U6.U5-27K;
DE AltName: Full=Nucleic acid-binding protein RY-1;
DE AltName: Full=U4/U6.U5 tri-snRNP-associated 27 kDa protein;
DE Short=27K;
DE AltName: Full=U4/U6.U5 tri-snRNP-associated protein 3;
GN Name=SNRNP27;
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].
RC TISSUE=T-cell;
RX PubMed=7931148; DOI=10.1099/0022-1317-75-10-2625;
RA Nakamura Y., Moriuchi R., Nakayama D., Yamashita I., Higashiyama Y.,
RA Yamamoto T., Kusano Y., Hino S., Miyamoto T., Katamine S.;
RT "Altered expression of the novel cellular gene as a consequence of
RT integration of human T cell lymphotropic virus type 1.";
RL J. Gen. Virol. 75:2625-2633(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 108-110 AND 141-152, IDENTIFICATION BY MASS
RP SPECTROMETRY, VARIANTS ILE-81 AND PHE-114, AND PHOSPHORYLATION.
RX PubMed=9085842;
RA Fetzer S., Lauber J., Will C.L., Luehrmann R.;
RT "The [U4/U6.U5] tri-snRNP-specific 27K protein is a novel SR protein that
RT can be phosphorylated by the snRNP-associated protein kinase.";
RL RNA 3:344-355(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-114 AND SER-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: May play a role in mRNA splicing.
CC -!- SUBUNIT: Part of a tri-snRNP complex.
CC -!- INTERACTION:
CC Q8WVK2; Q8IWX8: CHERP; NbExp=2; IntAct=EBI-2512550, EBI-2555370;
CC Q8WVK2; P78362: SRPK2; NbExp=5; IntAct=EBI-2512550, EBI-593303;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated in vitro by snRNP-associated protein kinase.
CC {ECO:0000269|PubMed:9085842}.
CC -!- SIMILARITY: Belongs to the SNUT3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X76302; CAA53949.1; ALT_INIT; mRNA.
DR EMBL; AC019206; AAY14866.1; -; Genomic_DNA.
DR EMBL; BC017890; AAH17890.1; -; mRNA.
DR CCDS; CCDS33219.1; -.
DR PIR; I38191; I38191.
DR RefSeq; NP_006848.1; NM_006857.2.
DR PDB; 6QW6; EM; 2.92 A; X=1-155.
DR PDB; 6QX9; EM; 3.28 A; X=1-155.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; Q8WVK2; -.
DR SMR; Q8WVK2; -.
DR BioGRID; 116207; 206.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q8WVK2; -.
DR IntAct; Q8WVK2; 110.
DR MINT; Q8WVK2; -.
DR STRING; 9606.ENSP00000244227; -.
DR iPTMnet; Q8WVK2; -.
DR MetOSite; Q8WVK2; -.
DR PhosphoSitePlus; Q8WVK2; -.
DR BioMuta; SNRNP27; -.
DR DMDM; 74760570; -.
DR EPD; Q8WVK2; -.
DR jPOST; Q8WVK2; -.
DR MassIVE; Q8WVK2; -.
DR MaxQB; Q8WVK2; -.
DR PaxDb; Q8WVK2; -.
DR PeptideAtlas; Q8WVK2; -.
DR PRIDE; Q8WVK2; -.
DR ProteomicsDB; 74800; -.
DR Antibodypedia; 31048; 56 antibodies from 15 providers.
DR DNASU; 11017; -.
DR Ensembl; ENST00000244227.8; ENSP00000244227.3; ENSG00000124380.11.
DR Ensembl; ENST00000450162.6; ENSP00000395144.2; ENSG00000124380.11.
DR GeneID; 11017; -.
DR KEGG; hsa:11017; -.
DR MANE-Select; ENST00000244227.8; ENSP00000244227.3; NM_006857.3; NP_006848.1.
DR UCSC; uc002sfw.4; human.
DR CTD; 11017; -.
DR DisGeNET; 11017; -.
DR GeneCards; SNRNP27; -.
DR HGNC; HGNC:30240; SNRNP27.
DR HPA; ENSG00000124380; Low tissue specificity.
DR MIM; 619629; gene.
DR neXtProt; NX_Q8WVK2; -.
DR OpenTargets; ENSG00000124380; -.
DR PharmGKB; PA164726114; -.
DR VEuPathDB; HostDB:ENSG00000124380; -.
DR eggNOG; KOG3263; Eukaryota.
DR GeneTree; ENSGT00730000111237; -.
DR HOGENOM; CLU_075596_2_1_1; -.
DR InParanoid; Q8WVK2; -.
DR OMA; SMKRKYR; -.
DR OrthoDB; 1627375at2759; -.
DR TreeFam; TF314458; -.
DR PathwayCommons; Q8WVK2; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8WVK2; -.
DR BioGRID-ORCS; 11017; 752 hits in 1050 CRISPR screens.
DR ChiTaRS; SNRNP27; human.
DR GenomeRNAi; 11017; -.
DR Pharos; Q8WVK2; Tbio.
DR PRO; PR:Q8WVK2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WVK2; protein.
DR Bgee; ENSG00000124380; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; Q8WVK2; baseline and differential.
DR Genevisible; Q8WVK2; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IPI:ComplexPortal.
DR GO; GO:0003676; F:nucleic acid binding; NAS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR InterPro; IPR013957; SNRNP27.
DR Pfam; PF08648; SNRNP27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..155
FT /note="U4/U6.U5 small nuclear ribonucleoprotein 27 kDa
FT protein"
FT /id="PRO_0000223965"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 81
FT /note="T -> I"
FT /evidence="ECO:0000269|PubMed:9085842"
FT /id="VAR_025363"
FT VARIANT 114
FT /note="S -> F"
FT /evidence="ECO:0000269|PubMed:9085842"
FT /id="VAR_025364"
SQ SEQUENCE 155 AA; 18860 MW; 26BC291950E49B9F CRC64;
MGRSRSRSPR RERRRSRSTS RERERRRRER SRSRERDRRR SRSRSPHRRR SRSPRRHRST
SPSPSRLKER RDEEKKETKE TKSKERQITE EDLEGKTEEE IEMMKLMGFA SFDSTKGKKV
DGSVNAYAIN VSQKRKYRQY MNRKGGFNRP LDFIA
