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O75533

- SF3B1_HUMAN

UniProt

O75533 - SF3B1_HUMAN

Protein

Splicing factor 3B subunit 1

Gene

SF3B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    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. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. gene expression Source: Reactome
    3. mRNA splicing, via spliceosome Source: UniProtKB
    4. RNA splicing Source: Reactome
    5. RNA splicing, via transesterification reactions Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Enzyme and pathway databases

    ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor 3B subunit 1
    Alternative name(s):
    Pre-mRNA-splicing factor SF3b 155 kDa subunit
    Short name:
    SF3b155
    Spliceosome-associated protein 155
    Short name:
    SAP 155
    Gene namesi
    Name:SF3B1
    Synonyms:SAP155
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10768. SF3B1.

    Subcellular locationi

    Nucleus speckle
    Note: During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. nuclear speck Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. spliceosomal complex Source: UniProtKB
    7. U12-type spliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi200 – 2001W → A: Abolishes interaction with RMB39; when associated with A-218; A-232; A-254; A-293; A-310 and A-338. 1 Publication
    Mutagenesisi218 – 2181W → A: Abolishes interaction with RMB39; when associated with A-200; A-232; A-254; A-293; A-310 and A-338. 1 Publication
    Mutagenesisi223 – 2231T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi227 – 2271T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi232 – 2321W → A: Abolishes interaction with RMB39; when associated with A-200; A-218; A-254; A-293; A-310 and A-338. 1 Publication
    Mutagenesisi235 – 2351T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi244 – 2441T → A: Slight inhibition of interaction with PPP1R8. 1 Publication
    Mutagenesisi248 – 2481T → A: Slight inhibition of interaction with PPP1R8. 1 Publication
    Mutagenesisi254 – 2541W → A: Abolishes interaction with RMB39; when associated with A-200; A-218; A-232; A-293; A-310 and A-338. 1 Publication
    Mutagenesisi257 – 2571T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi261 – 2611T → A: Slight inhibition of interaction with PPP1R8. 1 Publication
    Mutagenesisi267 – 2671T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi273 – 2731T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi278 – 2781T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi293 – 2931W → A: Abolishes interaction with RMB39; when associated with A-200; A-218; A-232; A-254; A-310 and A-338. 1 Publication
    Mutagenesisi296 – 2961T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi303 – 3031T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi310 – 3101W → A: Abolishes interaction with RMB39; when associated with A-200; A-218; A-232; A-254; A-293 and A-338. 1 Publication
    Mutagenesisi313 – 3131T → A: No effect on interaction with PPP1R8. 1 Publication
    Mutagenesisi338 – 3381W → A: Abolishes interaction with RMB39; when associated with A-200; A-218; A-232; A-254; A-293 and A-310. 1 Publication

    Organism-specific databases

    PharmGKBiPA35686.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13041304Splicing factor 3B subunit 1PRO_0000174323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei129 – 1291Phosphoserine4 Publications
    Modified residuei141 – 1411N6-acetyllysine1 Publication
    Modified residuei142 – 1421Phosphothreonine3 Publications
    Modified residuei157 – 1571CitrullineBy similarity
    Modified residuei194 – 1941Phosphoserine3 Publications
    Modified residuei203 – 2031Phosphothreonine2 Publications
    Modified residuei207 – 2071Phosphothreonine5 Publications
    Modified residuei211 – 2111Phosphothreonine7 Publications
    Modified residuei214 – 2141N6-acetyllysineBy similarity
    Modified residuei223 – 2231Phosphothreonine7 Publications
    Modified residuei227 – 2271Phosphothreonine3 Publications
    Modified residuei244 – 2441Phosphothreonine2 Publications
    Modified residuei248 – 2481Phosphothreonine2 Publications
    Modified residuei267 – 2671Phosphothreonine2 Publications
    Modified residuei296 – 2961Phosphothreonine2 Publications
    Modified residuei299 – 2991Phosphothreonine2 Publications
    Modified residuei313 – 3131Phosphothreonine2 Publications
    Modified residuei326 – 3261Phosphothreonine4 Publications
    Modified residuei328 – 3281Phosphothreonine4 Publications
    Modified residuei332 – 3321Phosphoserine2 Publications
    Modified residuei341 – 3411Phosphothreonine3 Publications
    Modified residuei344 – 3441Phosphoserine2 Publications
    Modified residuei349 – 3491Phosphoserine3 Publications
    Modified residuei350 – 3501Phosphothreonine2 Publications
    Modified residuei354 – 3541Phosphothreonine3 Publications
    Modified residuei400 – 4001Phosphoserine2 Publications
    Modified residuei434 – 4341Phosphothreonine2 Publications
    Modified residuei436 – 4361Phosphothreonine2 Publications
    Modified residuei488 – 4881Phosphoserine3 Publications
    Modified residuei554 – 5541N6-acetyllysine1 Publication
    Modified residuei562 – 5621N6-acetyllysine1 Publication
    Modified residuei1067 – 10671N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation occurs concomitantly with the splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis.11 Publications
    Citrullinated by PADI4.By similarity

    Keywords - PTMi

    Acetylation, Citrullination, Phosphoprotein

    Proteomic databases

    MaxQBiO75533.
    PaxDbiO75533.
    PRIDEiO75533.

    PTM databases

    PhosphoSiteiO75533.

    Miscellaneous databases

    PMAP-CutDBO75533.

    Expressioni

    Gene expression databases

    ArrayExpressiO75533.
    BgeeiO75533.
    CleanExiHS_SF3B1.
    GenevestigatoriO75533.

    Organism-specific databases

    HPAiHPA050275.
    HPA054596.

    Interactioni

    Subunit structurei

    Identified in the spliceosome C complex. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of splicing factor SF3B which is composed of at least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B155, SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B5, SF3B6, PHF5A/SF3B14B, and DDX42. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). SF3B1 interacts directly with the splicing factor U2AF. Phosphorylated form interacts with PPP1R8. Interacts with PQBP1. Interacts with RBM17. Interacts with RBM39. Interacts with SF3B6.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RBM17Q96I252EBI-876542,EBI-740272

    Protein-protein interaction databases

    BioGridi117017. 136 interactions.
    DIPiDIP-29411N.
    IntActiO75533. 41 interactions.
    MINTiMINT-1185911.
    STRINGi9606.ENSP00000335321.

    Structurei

    Secondary structure

    1
    1304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi380 – 39415
    Helixi401 – 4066
    Beta strandi410 – 4145

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F9DX-ray2.50P/Q373-415[»]
    2F9JX-ray3.00P/Q380-415[»]
    2FHONMR-A379-424[»]
    2PEHX-ray2.11C/D333-342[»]
    3LQVX-ray2.38P/Q377-415[»]
    4OZ1X-ray1.74C333-342[»]
    ProteinModelPortaliO75533.
    SMRiO75533. Positions 377-415, 988-1043.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75533.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati529 – 56840HEAT 1Add
    BLAST
    Repeati569 – 60335HEAT 2Add
    BLAST
    Repeati604 – 64138HEAT 3Add
    BLAST
    Repeati643 – 67735HEAT 4Add
    BLAST
    Repeati680 – 71839HEAT 5Add
    BLAST
    Repeati763 – 80139HEAT 6Add
    BLAST
    Repeati843 – 88139HEAT 7Add
    BLAST
    Repeati1010 – 104839HEAT 8Add
    BLAST
    Repeati1052 – 109039HEAT 9Add
    BLAST
    Repeati1122 – 116039HEAT 10Add
    BLAST
    Repeati1163 – 120139HEAT 11Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni190 – 342153U2AF homology region; mediates interaction with RMB39Add
    BLAST
    Regioni223 – 491269Interaction with PPP1R8Add
    BLAST
    Regioni529 – 56840Interaction with SF3B14Add
    BLAST

    Sequence similaritiesi

    Belongs to the SF3B1 family.Curated
    Contains 11 HEAT repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5181.
    HOGENOMiHOG000166737.
    HOVERGENiHBG079173.
    InParanoidiO75533.
    KOiK12828.
    OMAiAFWVRRM.
    OrthoDBiEOG7R2BHR.
    PhylomeDBiO75533.
    TreeFamiTF105680.

    Family and domain databases

    Gene3Di1.25.10.10. 4 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015016. SF3b_su1.
    [Graphical view]
    PfamiPF08920. SF3b1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75533-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR     50
    FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ 100
    YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGG KTPDPKMNAR 150
    TYMDVMREQH LTKEEREIRQ QLAEKAKAGE LKVVNGAAAS QPPSKRKRRW 200
    DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK GSETPGATPG 250
    SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE 300
    RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST 350
    PVLTPGKTPI GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS 400
    DEELDAMFPE GYKVLPPPAG YVPIRTPARK LTATPTPLGG MTGFHMQTED 450
    RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV DVDESTLSPE EQKERKIMKL 500
    LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM SPTLEDQERH 550
    LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL 600
    AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA 650
    VCKSKKSWQA RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK 700
    VRTISALAIA ALAEAATPYG IESFDSVLKP LWKGIRQHRG KGLAAFLKAI 750
    GYLIPLMDAE YANYYTREVM LILIREFQSP DEEMKKIVLK VVKQCCGTDG 800
    VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL ANKVGAAEII 850
    SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF 900
    QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ 950
    AADLISRTAV VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI 1000
    VNVIGMHKMT PPIKDLLPRL TPILKNRHEK VQENCIDLVG RIADRGAEYV 1050
    SAREWMRICF ELLELLKAHK KAIRRATVNT FGYIAKAIGP HDVLATLLNN 1100
    LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE LNVQNGVLKS 1150
    LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY 1200
    GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC 1250
    LQGLFHPARK VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL 1300
    DYIL 1304
    Length:1,304
    Mass (Da):145,830
    Last modified:November 24, 2009 - v3
    Checksum:i12F051757D2B9DEE
    GO
    Isoform 2 (identifier: O75533-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-144: GKTPD → FYSAA
         145-1304: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:144
    Mass (Da):16,020
    Checksum:i006D4294E06AB51E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti149 – 1491A → V in AAC97189. (PubMed:9585501)Curated
    Sequence conflicti594 – 5941R → L in AAC97189. (PubMed:9585501)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei140 – 1445GKTPD → FYSAA in isoform 2. 1 PublicationVSP_046182
    Alternative sequencei145 – 13041160Missing in isoform 2. 1 PublicationVSP_046183Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF054284 mRNA. Translation: AAC97189.1.
    AF086296 mRNA. No translation available.
    AC010746 Genomic DNA. No translation available.
    AF070540 mRNA. Translation: AAC28633.1.
    CCDSiCCDS33356.1. [O75533-1]
    CCDS46479.1. [O75533-2]
    RefSeqiNP_036565.2. NM_012433.2. [O75533-1]
    UniGeneiHs.632554.

    Genome annotation databases

    EnsembliENST00000335508; ENSP00000335321; ENSG00000115524. [O75533-1]
    ENST00000409915; ENSP00000428820; ENSG00000115524. [O75533-2]
    ENST00000414963; ENSP00000402997; ENSG00000115524. [O75533-2]
    GeneIDi23451.
    KEGGihsa:23451.
    UCSCiuc002uue.3. human. [O75533-1]
    uc002uuf.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF054284 mRNA. Translation: AAC97189.1 .
    AF086296 mRNA. No translation available.
    AC010746 Genomic DNA. No translation available.
    AF070540 mRNA. Translation: AAC28633.1 .
    CCDSi CCDS33356.1. [O75533-1 ]
    CCDS46479.1. [O75533-2 ]
    RefSeqi NP_036565.2. NM_012433.2. [O75533-1 ]
    UniGenei Hs.632554.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F9D X-ray 2.50 P/Q 373-415 [» ]
    2F9J X-ray 3.00 P/Q 380-415 [» ]
    2FHO NMR - A 379-424 [» ]
    2PEH X-ray 2.11 C/D 333-342 [» ]
    3LQV X-ray 2.38 P/Q 377-415 [» ]
    4OZ1 X-ray 1.74 C 333-342 [» ]
    ProteinModelPortali O75533.
    SMRi O75533. Positions 377-415, 988-1043.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117017. 136 interactions.
    DIPi DIP-29411N.
    IntActi O75533. 41 interactions.
    MINTi MINT-1185911.
    STRINGi 9606.ENSP00000335321.

    PTM databases

    PhosphoSitei O75533.

    Proteomic databases

    MaxQBi O75533.
    PaxDbi O75533.
    PRIDEi O75533.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335508 ; ENSP00000335321 ; ENSG00000115524 . [O75533-1 ]
    ENST00000409915 ; ENSP00000428820 ; ENSG00000115524 . [O75533-2 ]
    ENST00000414963 ; ENSP00000402997 ; ENSG00000115524 . [O75533-2 ]
    GeneIDi 23451.
    KEGGi hsa:23451.
    UCSCi uc002uue.3. human. [O75533-1 ]
    uc002uuf.3. human.

    Organism-specific databases

    CTDi 23451.
    GeneCardsi GC02M198256.
    HGNCi HGNC:10768. SF3B1.
    HPAi HPA050275.
    HPA054596.
    MIMi 605590. gene.
    neXtProti NX_O75533.
    PharmGKBi PA35686.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5181.
    HOGENOMi HOG000166737.
    HOVERGENi HBG079173.
    InParanoidi O75533.
    KOi K12828.
    OMAi AFWVRRM.
    OrthoDBi EOG7R2BHR.
    PhylomeDBi O75533.
    TreeFami TF105680.

    Enzyme and pathway databases

    Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    EvolutionaryTracei O75533.
    GeneWikii SF3B1.
    GenomeRNAii 23451.
    NextBioi 45735.
    PMAP-CutDB O75533.
    PROi O75533.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75533.
    Bgeei O75533.
    CleanExi HS_SF3B1.
    Genevestigatori O75533.

    Family and domain databases

    Gene3Di 1.25.10.10. 4 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015016. SF3b_su1.
    [Graphical view ]
    Pfami PF08920. SF3b1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis."
      Wang C., Chua K., Seghezzi W., Lees E., Gozani O., Reed R.
      Genes Dev. 12:1409-1414(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION.
    2. "Full clone sequencing of the longest available member from each UniGene cluster."
      Woessner J., Tan F., Marra M., Kucaba T., Yandell M., Martin J., Marth G., Bowles L., Wylie T., Bowers Y., Steptoe M., Theising B., Geisel S., Allen M., Underwood K., Chappell J., Person B., Gibbons M.
      , Harvey N., Pape D., Chamberlain A., Morales R., Schurk R., Ritter E., Kohn S., Swaller T., Behymer K., Hillier L., Wilson R., Waterston R.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1011-1304 (ISOFORM 1).
      Tissue: Brain.
    5. "Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
      Das R., Zhou Z., Reed R.
      Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
    6. "Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein."
      Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.
      EMBO J. 21:4978-4988(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SF3B COMPLEX.
    7. "Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1."
      Boudrez A., Beullens M., Waelkens E., Stalmans W., Bollen M.
      J. Biol. Chem. 277:31834-31841(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R8, PHOSPHORYLATION AT THR-244; THR-248 AND THR-313, MUTAGENESIS OF THR-223; THR-227; THR-235; THR-244; THR-248; THR-257; THR-261; THR-267; THR-273; THR-278; THR-296; THR-303 AND THR-313.
    8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    9. "Molecular architecture of the multiprotein splicing factor SF3b."
      Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.
      Science 300:980-984(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SF3B COMPLEX, ELECTRON MICROSCOPY OF THE SF3B COMPLEX.
    10. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
      Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
      RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211; THR-223; THR-296 AND THR-299, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
      Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
      J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211 AND THR-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-142; SER-194; THR-207; THR-211; THR-223; THR-227; THR-326; THR-328; SER-332 AND SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211; THR-223; THR-227; THR-326; THR-341; SER-349; THR-350; SER-400; THR-434 AND THR-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-554; LYS-562 AND LYS-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-194; THR-203; THR-207; THR-211; THR-223; THR-326; THR-328 AND SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-211; THR-341; SER-344; SER-349 AND THR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth."
      Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.
      Genes Dev. 27:615-626(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PQBP1.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 373-415 IN COMPLEX WITH SF3B6, INTERACTION WITH SF3B6.
    26. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."
      Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., Sattler M.
      Nat. Struct. Mol. Biol. 14:620-629(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 333-342 IN COMPLEX WITH RBM17, INTERACTION WITH RBM17.
    27. "NMR solution structure of the human spliceosomal protein complex p14-SF3B155."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 379-424.
    28. "Structural model of the p14/SF3b155 - branch duplex complex."
      Schellenberg M.J., Dul E.L., MacMillan A.M.
      RNA 17:155-165(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 377-415 IN COMPLEX WITH SF3B6, INTERACTION WITH SF3B6.
    29. "Cancer-relevant splicing factor CAPERalpha engages the essential splicing factor SF3b155 in a specific ternary complex."
      Loerch S., Maucuer A., Manceau V., Green M.R., Kielkopf C.L.
      J. Biol. Chem. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 333-342 IN COMPLEX WITH RBM39, INTERACTION WITH RMB39, MUTAGENESIS OF TRP-200; TRP-218; TRP-232; TRP-254; TRP-293; TRP-310 AND TRP-338.

    Entry informationi

    Entry nameiSF3B1_HUMAN
    AccessioniPrimary (citable) accession number: O75533
    Secondary accession number(s): E9PCH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3