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Database: UniProt
Entry: P08579
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Original site: P08579 
ID   RU2B_HUMAN              Reviewed;         225 AA.
AC   P08579; B2R7J3; D3DW21; Q9UJD4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   29-SEP-2021, entry version 216.
DE   RecName: Full=U2 small nuclear ribonucleoprotein B'';
DE            Short=U2 snRNP B'';
GN   Name=SNRPB2;
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=2951739; DOI=10.1073/pnas.84.8.2421;
RA   Habets W.J., Sillekens P.T.G., Hoet M.H., Schalken J.A., Roebroek A.J.M.,
RA   Leunissen J.A.M., de Ven W.J.M., van Venrooij W.J.;
RT   "Analysis of a cDNA clone expressing a human autoimmune antigen: full-
RT   length sequence of the U2 small nuclear RNA-associated B' antigen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:2421-2425(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Uterus;
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   [6]
RP   IDENTIFICATION IN SPLICEOSOMAL COMPLEX WITH HPRP8BP AND CRNKL1.
RX   PubMed=12084575; DOI=10.1016/s0167-4781(02)00368-8;
RA   Chung S., Zhou Z., Huddleston K.A., Harrison D.A., Reed R., Coleman T.A.,
RA   Rymond B.C.;
RT   "Crooked neck is a component of the human spliceosome and implicated in the
RT   splicing process.";
RL   Biochim. Biophys. Acta 1576:287-297(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP   C COMPLEX.
RX   PubMed=11991638; DOI=10.1017/s1355838202021088;
RA   Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT   "Purification and characterization of native spliceosomes suitable for
RT   three-dimensional structural analysis.";
RL   RNA 8:426-439(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [10]
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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-96 IN COMPLEX WITH SNRPA1 AND
RP   U2 SMALL NUCLEAR RNA, SUBUNIT, AND FUNCTION.
RX   PubMed=9716128; DOI=10.1038/29234;
RA   Price S.R., Evans P.R., Nagai K.;
RT   "Crystal structure of the spliceosomal U2B'-U2A' protein complex bound to a
RT   fragment of U2 small nuclear RNA.";
RL   Nature 394:645-650(1998).
RN   [13] {ECO:0007744|PDB:5XJC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA   Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT   "An Atomic Structure of the Human Spliceosome.";
RL   Cell 169:918-929(2017).
RN   [14] {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   [15] {ECO:0007744|PDB:5MQF}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=28076346; DOI=10.1038/nature21079;
RA   Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA   Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT   "Cryo-EM structure of a human spliceosome activated for step 2 of
RT   splicing.";
RL   Nature 542:318-323(2017).
RN   [16]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-19.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC       (PubMed:11991638, PubMed:28502770, PubMed:28781166, PubMed:28076346).
CC       Associated with sn-RNP U2, where it contributes to the binding of stem
CC       loop IV of U2 snRNA (PubMed:9716128). {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9716128}.
CC   -!- SUBUNIT: Identified in the spliceosome B complex (PubMed:28781166).
CC       Identified in the spliceosome C complex (PubMed:11991638,
CC       PubMed:28502770, PubMed:28076346). Present in a spliceosome complex
CC       assembled in vitro, and composed of SNRPB2, HPRP8BP and CRNKL1
CC       (PubMed:12084575). Contributes to the binding of stem loop IV of U2
CC       snRNA with SNRPP1 (PubMed:9716128). {ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:12084575, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC       ECO:0000269|PubMed:9716128}.
CC   -!- INTERACTION:
CC       P08579; P13196: ALAS1; NbExp=3; IntAct=EBI-1053651, EBI-3905054;
CC       P08579; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-1053651, EBI-1054315;
CC       P08579; Q06547: GABPB1; NbExp=3; IntAct=EBI-1053651, EBI-618165;
CC       P08579; Q8TAK5: GABPB2; NbExp=3; IntAct=EBI-1053651, EBI-8468945;
CC       P08579; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1053651, EBI-618309;
CC       P08579; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-1053651, EBI-2549423;
CC       P08579; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-1053651, EBI-10172004;
CC       P08579; Q14566: MCM6; NbExp=3; IntAct=EBI-1053651, EBI-374900;
CC       P08579; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1053651, EBI-742948;
CC       P08579; Q96NT1: NAP1L5; NbExp=3; IntAct=EBI-1053651, EBI-713627;
CC       P08579; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1053651, EBI-79165;
CC       P08579; Q8ND90: PNMA1; NbExp=5; IntAct=EBI-1053651, EBI-302345;
CC       P08579; P09661: SNRPA1; NbExp=4; IntAct=EBI-1053651, EBI-876439;
CC       P08579; P36406: TRIM23; NbExp=3; IntAct=EBI-1053651, EBI-740098;
CC       P08579; P14373: TRIM27; NbExp=6; IntAct=EBI-1053651, EBI-719493;
CC       P08579; O43829: ZBTB14; NbExp=6; IntAct=EBI-1053651, EBI-10176632;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}.
CC   -!- MISCELLANEOUS: Patients with systemic lupus erythematosus produce
CC       antibodies which interact with snRNP proteins.
CC   -!- SIMILARITY: Belongs to the RRM U1 A/B'' family. {ECO:0000305}.
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DR   EMBL; M15841; AAA36796.1; -; mRNA.
DR   EMBL; AK313004; BAG35840.1; -; mRNA.
DR   EMBL; AL034428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10284.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10285.1; -; Genomic_DNA.
DR   EMBL; BC018022; AAH18022.1; -; mRNA.
DR   EMBL; BC036737; AAH36737.1; -; mRNA.
DR   CCDS; CCDS13123.1; -.
DR   PIR; A25910; A25910.
DR   RefSeq; NP_003083.1; NM_003092.4.
DR   RefSeq; NP_937863.1; NM_198220.2.
DR   PDB; 1A9N; X-ray; 2.38 A; B/D=1-96.
DR   PDB; 5MQF; EM; 5.90 A; X=1-225.
DR   PDB; 5O9Z; EM; 4.50 A; 1=1-225.
DR   PDB; 5XJC; EM; 3.60 A; p=1-225.
DR   PDB; 5YZG; EM; 4.10 A; p=1-225.
DR   PDB; 5Z56; EM; 5.10 A; p=1-225.
DR   PDB; 5Z57; EM; 6.50 A; p=1-225.
DR   PDB; 5Z58; EM; 4.90 A; p=1-225.
DR   PDB; 6AH0; EM; 5.70 A; p=1-225.
DR   PDB; 6AHD; EM; 3.80 A; p=1-225.
DR   PDB; 6FF7; EM; 4.50 A; X=1-225.
DR   PDB; 6ICZ; EM; 3.00 A; p=1-225.
DR   PDB; 6ID0; EM; 2.90 A; p=1-225.
DR   PDB; 6ID1; EM; 2.86 A; p=1-225.
DR   PDB; 6QDV; EM; 3.30 A; Y=3-94.
DR   PDB; 6QX9; EM; 3.28 A; 2B=1-225.
DR   PDB; 6Y53; EM; 7.10 A; b=1-225.
DR   PDB; 6Y5Q; EM; 7.10 A; b=1-225.
DR   PDB; 7A5P; EM; 5.00 A; X=1-225.
DR   PDB; 7ABG; EM; 7.80 A; B=1-225.
DR   PDB; 7ABI; EM; 8.00 A; B=1-225.
DR   PDBsum; 1A9N; -.
DR   PDBsum; 5MQF; -.
DR   PDBsum; 5O9Z; -.
DR   PDBsum; 5XJC; -.
DR   PDBsum; 5YZG; -.
DR   PDBsum; 5Z56; -.
DR   PDBsum; 5Z57; -.
DR   PDBsum; 5Z58; -.
DR   PDBsum; 6AH0; -.
DR   PDBsum; 6AHD; -.
DR   PDBsum; 6FF7; -.
DR   PDBsum; 6ICZ; -.
DR   PDBsum; 6ID0; -.
DR   PDBsum; 6ID1; -.
DR   PDBsum; 6QDV; -.
DR   PDBsum; 6QX9; -.
DR   PDBsum; 6Y53; -.
DR   PDBsum; 6Y5Q; -.
DR   PDBsum; 7A5P; -.
DR   PDBsum; 7ABG; -.
DR   PDBsum; 7ABI; -.
DR   SMR; P08579; -.
DR   BioGRID; 112513; 158.
DR   CORUM; P08579; -.
DR   IntAct; P08579; 61.
DR   MINT; P08579; -.
DR   STRING; 9606.ENSP00000246071; -.
DR   GlyGen; P08579; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P08579; -.
DR   PhosphoSitePlus; P08579; -.
DR   BioMuta; SNRPB2; -.
DR   DMDM; 134095; -.
DR   EPD; P08579; -.
DR   jPOST; P08579; -.
DR   MassIVE; P08579; -.
DR   MaxQB; P08579; -.
DR   PaxDb; P08579; -.
DR   PeptideAtlas; P08579; -.
DR   PRIDE; P08579; -.
DR   ProteomicsDB; 52127; -.
DR   TopDownProteomics; P08579; -.
DR   Antibodypedia; 24425; 227 antibodies.
DR   DNASU; 6629; -.
DR   Ensembl; ENST00000246071; ENSP00000246071; ENSG00000125870.
DR   Ensembl; ENST00000377943; ENSP00000367178; ENSG00000125870.
DR   GeneID; 6629; -.
DR   KEGG; hsa:6629; -.
DR   UCSC; uc002wph.3; human.
DR   CTD; 6629; -.
DR   DisGeNET; 6629; -.
DR   GeneCards; SNRPB2; -.
DR   HGNC; HGNC:11155; SNRPB2.
DR   HPA; ENSG00000125870; Low tissue specificity.
DR   MIM; 603520; gene.
DR   neXtProt; NX_P08579; -.
DR   OpenTargets; ENSG00000125870; -.
DR   PharmGKB; PA35996; -.
DR   VEuPathDB; HostDB:ENSG00000125870; -.
DR   eggNOG; KOG4206; Eukaryota.
DR   GeneTree; ENSGT00390000007046; -.
DR   HOGENOM; CLU_041869_1_1_1; -.
DR   OMA; VISKMRG; -.
DR   OrthoDB; 1608132at2759; -.
DR   PhylomeDB; P08579; -.
DR   TreeFam; TF313834; -.
DR   PathwayCommons; P08579; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 6629; 425 hits in 1012 CRISPR screens.
DR   ChiTaRS; SNRPB2; human.
DR   EvolutionaryTrace; P08579; -.
DR   GeneWiki; SNRPB2; -.
DR   GenomeRNAi; 6629; -.
DR   Pharos; P08579; Tbio.
DR   PRO; PR:P08579; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P08579; protein.
DR   Bgee; ENSG00000125870; Expressed in oocyte and 250 other tissues.
DR   Genevisible; P08579; HS.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR   GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR   GO; GO:0005686; C:U2 snRNP; IDA:GO_Central.
DR   GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR   GO; GO:0070990; F:snRNP binding; IEA:Ensembl.
DR   GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   CDD; cd12478; RRM1_U2B; 1.
DR   CDD; cd12481; RRM2_U2B; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034564; U2B''_RRM1.
DR   InterPro; IPR034562; U2B''_RRM2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Isopeptide bond; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN           1..225
FT                   /note="U2 small nuclear ribonucleoprotein B''"
FT                   /id="PRO_0000081892"
FT   DOMAIN          7..86
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          151..225
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          99..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         111
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQI7"
FT   MOD_RES         151
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   CROSSLNK        111
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         19
FT                   /note="K -> Q (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035487"
FT   STRAND          7..13
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   HELIX           20..32
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   TURN            46..50
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   HELIX           59..68
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:1A9N"
FT   HELIX           89..95
FT                   /evidence="ECO:0007829|PDB:1A9N"
SQ   SEQUENCE   225 AA;  25486 MW;  67C949CC7E14A92A CRC64;
     MDIRPNHTIY INNMNDKIKK EELKRSLYAL FSQFGHVVDI VALKTMKMRG QAFVIFKELG
     SSTNALRQLQ GFPFYGKPMR IQYAKTDSDI ISKMRGTFAD KEKKKEKKKA KTVEQTATTT
     NKKPGQGTPN SANTQGNSTP NPQVPDYPPN YILFLNNLPE ETNEMMLSML FNQFPGFKEV
     RLVPGRHDIA FVEFENDGQA GAARDALQGF KITPSHAMKI TYAKK
//
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