SF3B4_HUMAN
ID SF3B4_HUMAN Reviewed; 424 AA.
AC Q15427; Q5SZ63;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Splicing factor 3B subunit 4;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 49 kDa subunit;
DE AltName: Full=Spliceosome-associated protein 49;
DE Short=SAP 49;
GN Name=SF3B4; Synonyms=SAP49;
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 [GENOMIC DNA].
RX PubMed=7958871; DOI=10.1101/gad.8.16.1974;
RA Champion-Arnaud P., Reed R.;
RT "The prespliceosome components SAP 49 and SAP 145 interact in a complex
RT implicated in tethering U2 snRNP to the branch site.";
RL Genes Dev. 8:1974-1983(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and 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 [5]
RP PROTEIN SEQUENCE OF 2-23, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP CHARACTERIZATION OF THE SPLICEOSOME.
RX PubMed=10882114; DOI=10.1016/s1097-2765(00)80318-4;
RA Das R., Zhou Z., Reed R.;
RT "Functional association of U2 snRNP with the ATP-independent spliceosomal
RT complex E.";
RL Mol. Cell 5:779-787(2000).
RN [7]
RP IDENTIFICATION IN THE SF3B COMPLEX.
RX PubMed=12234937; DOI=10.1093/emboj/cdf480;
RA Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.;
RT "Characterization of novel SF3b and 17S U2 snRNP proteins, including a
RT human Prp5p homologue and an SF3b DEAD-box protein.";
RL EMBO J. 21:4978-4988(2002).
RN [8]
RP IDENTIFICATION IN THE SF3B COMPLEX, AND ELECTRON MICROSCOPY OF THE SF3B
RP COMPLEX.
RX PubMed=12738865; DOI=10.1126/science.1084155;
RA Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.;
RT "Molecular architecture of the multiprotein splicing factor SF3b.";
RL Science 300:980-984(2003).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 INVOLVEMENT IN AFD1.
RX PubMed=22541558; DOI=10.1016/j.ajhg.2012.04.004;
RA Bernier F.P., Caluseriu O., Ng S., Schwartzentruber J., Buckingham K.J.,
RA Innes A.M., Jabs E.W., Innis J.W., Schuette J.L., Gorski J.L., Byers P.H.,
RA Andelfinger G., Siu V., Lauzon J., Fernandez B.A., McMillin M., Scott R.H.,
RA Racher H., Majewski J., Nickerson D.A., Shendure J., Bamshad M.J.,
RA Parboosingh J.S.;
RT "Haploinsufficiency of SF3B4, a component of the pre-mRNA spliceosomal
RT complex, causes Nager syndrome.";
RL Am. J. Hum. Genet. 90:925-933(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP STRUCTURE BY NMR OF 4-184.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domains in splicing factor 3B.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH PRMT9; SF3B2 AND SF3B4.
RX PubMed=25737013; DOI=10.1038/ncomms7428;
RA Yang Y., Hadjikyriacou A., Xia Z., Gayatri S., Kim D., Zurita-Lopez C.,
RA Kelly R., Guo A., Li W., Clarke S.G., Bedford M.T.;
RT "PRMT9 is a type II methyltransferase that methylates the splicing factor
RT SAP145.";
RL Nat. Commun. 6:6428-6428(2015).
RN [18]
RP FUNCTION, IDENTIFICATION IN THE SF3B COMPLEX, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27720643; DOI=10.1016/j.molcel.2016.08.036;
RA Cretu C., Schmitzova J., Ponce-Salvatierra A., Dybkov O.,
RA De Laurentiis E.I., Sharma K., Will C.L., Urlaub H., Luehrmann R., Pena V.;
RT "Molecular architecture of SF3b and structural consequences of its cancer-
RT related mutations.";
RL Mol. Cell 64:307-319(2016).
RN [19]
RP IDENTIFICATION IN THE SF3B COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=28541300; DOI=10.1038/ncomms15522;
RA Teng T., Tsai J.H., Puyang X., Seiler M., Peng S., Prajapati S., Aird D.,
RA Buonamici S., Caleb B., Chan B., Corson L., Feala J., Fekkes P., Gerard B.,
RA Karr C., Korpal M., Liu X., Lowe J.T., Mizui Y., Palacino J., Park E.,
RA Smith P.G., Subramanian V., Wu Z.J., Zou J., Yu L., Chicas A., Warmuth M.,
RA Larsen N., Zhu P.;
RT "Splicing modulators act at the branch point adenosine binding pocket
RT defined by the PHF5A-SF3b complex.";
RL Nat. Commun. 8:15522-15522(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A'
CC complex assembly formed by the stable binding of U2 snRNP to the
CC branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of
CC SF3A/SF3B complex upstream of the branch site is essential, it may
CC anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved
CC in the assembly of the 'E' complex. SF3B4 has been found in complex 'B'
CC and 'C' as well (PubMed:10882114). Belongs also to the minor U12-
CC dependent spliceosome, which is involved in the splicing of rare class
CC of nuclear pre-mRNA intron (PubMed:15146077).
CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643}.
CC -!- SUBUNIT: Component of splicing factor SF3B complex which is composed of
CC at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6,
CC PHF5A and DDX42 (PubMed:12234937, PubMed:12738865, PubMed:27720643,
CC PubMed:28541300). SF3B associates with the splicing factor SF3A and a
CC 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex
CC (U2 snRNP) (PubMed:12234937). Interacts directly with SF3B2. Found in a
CC complex with PRMT9, SF3B2 and SF3B4 (PubMed:25737013). The SF3B complex
CC composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A
CC interacts with U2AF2 (PubMed:27720643). Component of the U11/U12 snRNPs
CC that are part of the U12-type spliceosome (PubMed:15146077).
CC {ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:12738865,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:25737013,
CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300}.
CC -!- INTERACTION:
CC Q15427; O95817: BAG3; NbExp=6; IntAct=EBI-348469, EBI-747185;
CC Q15427; Q9UQB8: BAIAP2; NbExp=3; IntAct=EBI-348469, EBI-525456;
CC Q15427; O75934: BCAS2; NbExp=2; IntAct=EBI-348469, EBI-1050106;
CC Q15427; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-348469, EBI-5453285;
CC Q15427; Q15029: EFTUD2; NbExp=2; IntAct=EBI-348469, EBI-357897;
CC Q15427; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-348469, EBI-10226858;
CC Q15427; P42685: FRK; NbExp=4; IntAct=EBI-348469, EBI-1383583;
CC Q15427; P62993: GRB2; NbExp=2; IntAct=EBI-348469, EBI-401755;
CC Q15427; Q9BUJ2: HNRNPUL1; NbExp=4; IntAct=EBI-348469, EBI-1018153;
CC Q15427; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-348469, EBI-739361;
CC Q15427; P45984: MAPK9; NbExp=7; IntAct=EBI-348469, EBI-713568;
CC Q15427; Q9H7H0: METTL17; NbExp=4; IntAct=EBI-348469, EBI-749353;
CC Q15427; O43639: NCK2; NbExp=7; IntAct=EBI-348469, EBI-713635;
CC Q15427; Q9Y5A7: NUB1; NbExp=3; IntAct=EBI-348469, EBI-3936907;
CC Q15427; Q96T49: PPP1R16B; NbExp=4; IntAct=EBI-348469, EBI-10293968;
CC Q15427; Q6P2P2: PRMT9; NbExp=3; IntAct=EBI-348469, EBI-10962083;
CC Q15427; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-348469, EBI-538479;
CC Q15427; P47897: QARS1; NbExp=3; IntAct=EBI-348469, EBI-347462;
CC Q15427; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-348469, EBI-744023;
CC Q15427; P98175: RBM10; NbExp=8; IntAct=EBI-348469, EBI-721525;
CC Q15427; Q14498: RBM39; NbExp=3; IntAct=EBI-348469, EBI-395290;
CC Q15427; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-348469, EBI-366570;
CC Q15427; O94855: SEC24D; NbExp=3; IntAct=EBI-348469, EBI-748817;
CC Q15427; E9PPJ0: SF3B2; NbExp=3; IntAct=EBI-348469, EBI-10177154;
CC Q15427; Q13435: SF3B2; NbExp=8; IntAct=EBI-348469, EBI-749111;
CC Q15427; O75177: SS18L1; NbExp=4; IntAct=EBI-348469, EBI-744674;
CC Q15427; O75177-5: SS18L1; NbExp=3; IntAct=EBI-348469, EBI-12035119;
CC Q15427; Q9Y4C2: TCAF1; NbExp=5; IntAct=EBI-348469, EBI-750484;
CC Q15427; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-348469, EBI-11974855;
CC Q15427; Q92734: TFG; NbExp=3; IntAct=EBI-348469, EBI-357061;
CC Q15427; Q08117-2: TLE5; NbExp=3; IntAct=EBI-348469, EBI-11741437;
CC Q15427; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-348469, EBI-3650647;
CC Q15427; P57075: UBASH3A; NbExp=3; IntAct=EBI-348469, EBI-2105393;
CC Q15427; Q9BRX9: WDR83; NbExp=2; IntAct=EBI-348469, EBI-7705033;
CC Q15427; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-348469, EBI-597063;
CC Q15427; P17036: ZNF3; NbExp=3; IntAct=EBI-348469, EBI-1640965;
CC Q15427; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-348469, EBI-12006434;
CC Q15427; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-348469, EBI-25475920;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300}.
CC -!- DISEASE: Acrofacial dysostosis 1, Nager type (AFD1) [MIM:154400]: A
CC form of acrofacial dysostosis, a group of disorders which are
CC characterized by malformation of the craniofacial skeleton and the
CC limbs. The major facial features of AFD1 include downslanted palpebral
CC fissures, midface retrusion, and micrognathia, the latter of which
CC often requires the placement of a tracheostomy in early childhood. Limb
CC defects typically involve the anterior (radial) elements of the upper
CC limbs and manifest as small or absent thumbs, triphalangeal thumbs,
CC radial hyoplasia or aplasia, and radioulnar synostosis. Phocomelia of
CC the upper limbs and, occasionally, lower-limb defects have also been
CC reported. {ECO:0000269|PubMed:22541558}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SF3B4 family. {ECO:0000305}.
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DR EMBL; L35013; AAA60300.1; -; Genomic_DNA.
DR EMBL; AL591493; CAI12554.1; -; Genomic_DNA.
DR EMBL; AL590487; CAI12554.1; JOINED; Genomic_DNA.
DR EMBL; AL590487; CAI12648.1; -; Genomic_DNA.
DR EMBL; AL591493; CAI12648.1; JOINED; Genomic_DNA.
DR EMBL; CH471121; EAW53595.1; -; Genomic_DNA.
DR EMBL; BC004273; AAH04273.1; -; mRNA.
DR EMBL; BC013886; AAH13886.1; -; mRNA.
DR EMBL; BC090883; AAH90883.1; -; mRNA.
DR CCDS; CCDS72900.1; -.
DR PIR; A54964; A54964.
DR RefSeq; NP_005841.1; NM_005850.4.
DR PDB; 1X5T; NMR; -; A=102-184.
DR PDB; 5GVQ; NMR; -; A=5-96.
DR PDB; 5Z56; EM; 5.10 A; 4=1-424.
DR PDB; 5Z57; EM; 6.50 A; 4=1-424.
DR PDB; 5Z58; EM; 4.90 A; 4=1-424.
DR PDB; 6AH0; EM; 5.70 A; 4=1-424.
DR PDB; 6AHD; EM; 3.80 A; 4=1-424.
DR PDB; 6QX9; EM; 3.28 A; B4=1-424.
DR PDB; 6Y53; EM; 7.10 A; o=1-424.
DR PDB; 6Y5Q; EM; 7.10 A; o=1-424.
DR PDB; 7ABG; EM; 7.80 A; w=1-424.
DR PDB; 7ABH; EM; 4.50 A; w=1-424.
DR PDB; 7ABI; EM; 8.00 A; w=1-424.
DR PDB; 7DVQ; EM; 2.89 A; 4=1-424.
DR PDB; 7ONB; EM; 3.10 A; K=1-424.
DR PDBsum; 1X5T; -.
DR PDBsum; 5GVQ; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6Y53; -.
DR PDBsum; 6Y5Q; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7ONB; -.
DR AlphaFoldDB; Q15427; -.
DR SMR; Q15427; -.
DR BioGRID; 115554; 339.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR CORUM; Q15427; -.
DR IntAct; Q15427; 88.
DR MINT; Q15427; -.
DR STRING; 9606.ENSP00000271628; -.
DR GlyGen; Q15427; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15427; -.
DR PhosphoSitePlus; Q15427; -.
DR SwissPalm; Q15427; -.
DR BioMuta; SF3B4; -.
DR DMDM; 2500587; -.
DR EPD; Q15427; -.
DR jPOST; Q15427; -.
DR MassIVE; Q15427; -.
DR MaxQB; Q15427; -.
DR PaxDb; Q15427; -.
DR PeptideAtlas; Q15427; -.
DR PRIDE; Q15427; -.
DR ProteomicsDB; 60587; -.
DR Antibodypedia; 20268; 336 antibodies from 37 providers.
DR DNASU; 10262; -.
DR Ensembl; ENST00000271628.9; ENSP00000271628.8; ENSG00000143368.10.
DR GeneID; 10262; -.
DR KEGG; hsa:10262; -.
DR MANE-Select; ENST00000271628.9; ENSP00000271628.8; NM_005850.5; NP_005841.1.
DR UCSC; uc001etk.3; human.
DR CTD; 10262; -.
DR DisGeNET; 10262; -.
DR GeneCards; SF3B4; -.
DR HGNC; HGNC:10771; SF3B4.
DR HPA; ENSG00000143368; Low tissue specificity.
DR MalaCards; SF3B4; -.
DR MIM; 154400; phenotype.
DR MIM; 605593; gene.
DR neXtProt; NX_Q15427; -.
DR OpenTargets; ENSG00000143368; -.
DR Orphanet; 1788; Acrofacial dysostosis, Rodriguez type.
DR Orphanet; 245; Nager syndrome.
DR PharmGKB; PA35689; -.
DR VEuPathDB; HostDB:ENSG00000143368; -.
DR eggNOG; KOG0131; Eukaryota.
DR GeneTree; ENSGT00870000136537; -.
DR HOGENOM; CLU_012062_21_0_1; -.
DR InParanoid; Q15427; -.
DR OMA; HWEQNKE; -.
DR OrthoDB; 1479417at2759; -.
DR PhylomeDB; Q15427; -.
DR TreeFam; TF300890; -.
DR PathwayCommons; Q15427; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q15427; -.
DR SIGNOR; Q15427; -.
DR BioGRID-ORCS; 10262; 781 hits in 1081 CRISPR screens.
DR ChiTaRS; SF3B4; human.
DR EvolutionaryTrace; Q15427; -.
DR GeneWiki; SF3B4; -.
DR GenomeRNAi; 10262; -.
DR Pharos; Q15427; Tbio.
DR PRO; PR:Q15427; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15427; protein.
DR Bgee; ENSG00000143368; Expressed in mucosa of transverse colon and 174 other tissues.
DR ExpressionAtlas; Q15427; baseline and differential.
DR Genevisible; Q15427; HS.
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:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IC:ComplexPortal.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990935; F:splicing factor binding; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:ProtInc.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR CDD; cd12334; RRM1_SF3B4; 1.
DR CDD; cd12335; RRM2_SF3B4; 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; IPR034158; SF3B4_RRM1.
DR InterPro; IPR034159; SF3B4_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; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..424
FT /note="Splicing factor 3B subunit 4"
FT /id="PRO_0000081955"
FT DOMAIN 13..91
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 100..179
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 207..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:5GVQ"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1X5T"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1X5T"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1X5T"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1X5T"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:1X5T"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1X5T"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:1X5T"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1X5T"
SQ SEQUENCE 424 AA; 44386 MW; 212472A25D3FF002 CRC64;
MAAGPISERN QDATVYVGGL DEKVSEPLLW ELFLQAGPVV NTHMPKDRVT GQHQGYGFVE
FLSEEDADYA IKIMNMIKLY GKPIRVNKAS AHNKNLDVGA NIFIGNLDPE IDEKLLYDTF
SAFGVILQTP KIMRDPDTGN SKGYAFINFA SFDASDAAIE AMNGQYLCNR PITVSYAFKK
DSKGERHGSA AERLLAAQNP LSQADRPHQL FADAPPPPSA PNPVVSSLGS GLPPPGMPPP
GSFPPPVPPP GALPPGIPPA MPPPPMPPGA AGHGPPSAGT PGAGHPGHGH SHPHPFPPGG
MPHPGMSQMQ LAHHGPHGLG HPHAGPPGSG GQPPPRPPPG MPHPGPPPMG MPPRGPPFGS
PMGHPGPMPP HGMRGPPPLM PPHGYTGPPR PPPYGYQRGP LPPPRPTPRP PVPPRGPLRG
PLPQ
