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Protein

Splicing factor 3B subunit 4

Gene

Sf3b4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • positive regulation of mRNA splicing, via spliceosome Source: MGI
  • RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3B subunit 4
Gene namesi
Name:Sf3b4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:109580. Sf3b4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 424423Splicing factor 3B subunit 4PRO_0000328585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei56 – 561PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8QZY9.
MaxQBiQ8QZY9.
PaxDbiQ8QZY9.
PeptideAtlasiQ8QZY9.
PRIDEiQ8QZY9.

PTM databases

iPTMnetiQ8QZY9.
PhosphoSiteiQ8QZY9.

Expressioni

Gene expression databases

BgeeiQ8QZY9.
GenevisibleiQ8QZY9. MM.

Interactioni

Subunit structurei

Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A/SF3B14B, and DDX42/SF3B125. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. SF3B4 interacts directly with SF3B2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi223499. 2 interactions.
IntActiQ8QZY9. 6 interactions.
MINTiMINT-4118170.
STRINGi10090.ENSMUSP00000075709.

Structurei

3D structure databases

ProteinModelPortaliQ8QZY9.
SMRiQ8QZY9. Positions 5-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 9179RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini100 – 17980RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi215 – 2184Poly-Pro
Compositional biasi262 – 2687Poly-Pro

Sequence similaritiesi

Belongs to the SF3B4 family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0131. Eukaryota.
ENOG410XPT4. LUCA.
GeneTreeiENSGT00840000129930.
HOGENOMiHOG000200535.
HOVERGENiHBG002295.
InParanoidiQ8QZY9.
KOiK12831.
OMAiNNNMGMI.
OrthoDBiEOG77Q4XP.
PhylomeDBiQ8QZY9.
TreeFamiTF300890.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8QZY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGPISERN QDATVYVGGL DEKVSEPLLW ELFLQAGPVV NTHMPKDRVT
60 70 80 90 100
GQHQGYGFVE FLSEEDADYA IKIMNMIKLY GKPIRVNKAS AHNKNLDVGA
110 120 130 140 150
NIFIGNLDPE IDEKLLYDTF SAFGVILQTP KIMRDPDTGN SKGYAFINFA
160 170 180 190 200
SFDASDAAIE AMNGQYLCNR PITVSYAFKK DSKGERHGSA AERLLAAQNP
210 220 230 240 250
LSQADRPHQL FADAPPPPSA PNPVVSSLGS GLPPPGMPPP GSFPPPVPPP
260 270 280 290 300
GALPPGIPPA MPPPPMPPGA GGHGPPAAGT PGAGHPGHGH SHPHPFPPGG
310 320 330 340 350
MPHPGMSQMQ LAHHGPHGLG HPHAGPPGSG GQPPPRPPPG MPHPGPPPMG
360 370 380 390 400
MPPRGPPFGS PMGHPGPMPP HGMRGPPPLM PPHGYTGPPR PPPYGYQRGP
410 420
LPPPRPTPRP PVPPRGPLRG PLPQ
Length:424
Mass (Da):44,356
Last modified:June 1, 2002 - v1
Checksum:i7B6B69A2BD95F1E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047751 mRNA. Translation: BAC33145.1.
AK135543 mRNA. Translation: BAE22576.1.
BC024418 mRNA. Translation: AAH24418.3.
BC026567 mRNA. Translation: AAH26567.1.
BC085273 mRNA. Translation: AAH85273.1.
CCDSiCCDS17630.1.
RefSeqiNP_694693.1. NM_153053.4.
UniGeneiMm.219671.

Genome annotation databases

EnsembliENSMUST00000076372; ENSMUSP00000075709; ENSMUSG00000068856.
GeneIDi107701.
KEGGimmu:107701.
UCSCiuc008qme.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK047751 mRNA. Translation: BAC33145.1.
AK135543 mRNA. Translation: BAE22576.1.
BC024418 mRNA. Translation: AAH24418.3.
BC026567 mRNA. Translation: AAH26567.1.
BC085273 mRNA. Translation: AAH85273.1.
CCDSiCCDS17630.1.
RefSeqiNP_694693.1. NM_153053.4.
UniGeneiMm.219671.

3D structure databases

ProteinModelPortaliQ8QZY9.
SMRiQ8QZY9. Positions 5-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223499. 2 interactions.
IntActiQ8QZY9. 6 interactions.
MINTiMINT-4118170.
STRINGi10090.ENSMUSP00000075709.

PTM databases

iPTMnetiQ8QZY9.
PhosphoSiteiQ8QZY9.

Proteomic databases

EPDiQ8QZY9.
MaxQBiQ8QZY9.
PaxDbiQ8QZY9.
PeptideAtlasiQ8QZY9.
PRIDEiQ8QZY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000076372; ENSMUSP00000075709; ENSMUSG00000068856.
GeneIDi107701.
KEGGimmu:107701.
UCSCiuc008qme.1. mouse.

Organism-specific databases

CTDi10262.
MGIiMGI:109580. Sf3b4.

Phylogenomic databases

eggNOGiKOG0131. Eukaryota.
ENOG410XPT4. LUCA.
GeneTreeiENSGT00840000129930.
HOGENOMiHOG000200535.
HOVERGENiHBG002295.
InParanoidiQ8QZY9.
KOiK12831.
OMAiNNNMGMI.
OrthoDBiEOG77Q4XP.
PhylomeDBiQ8QZY9.
TreeFamiTF300890.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

PROiQ8QZY9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8QZY9.
GenevisibleiQ8QZY9. MM.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpus striatum and Muellerian duct.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon and Jaw.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Spleen and Testis.

Entry informationi

Entry nameiSF3B4_MOUSE
AccessioniPrimary (citable) accession number: Q8QZY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.