Splicing factor 3B subunit 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot O75533 (SF3B1_HUMAN)

Last modified July 7, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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 names

Name:	SF3B1
Synonyms:	SAP155

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1304 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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.
Subunit structure	Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. 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, SF3B14A, PHF5A/SF3B14B, SF3B10 and SF3B125.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. Ref.4 Ref.5
Subcellular location	Nucleus speckle. Note: During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm.
Post-translational modification	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. Ref.5 Ref.1 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Sequence similarities	Belongs to the SF3B1 family. Contains 11 HEAT repeats.

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Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosome Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	RNA splicing factor activity, transesterification mechanism Ref.1 Non-traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ATG12	O94817	1	EBI-876542,EBI-746742
BRF2	Q9HAW0	1	EBI-876542,EBI-1055224
GSK3B	P49841	1	EBI-876542,EBI-373586
HDAC3	O15379	1	EBI-876542,EBI-607682
PUF60	Q9UHX1	1	EBI-876542,EBI-1053259
RNPS1	Q15287	1	EBI-876542,EBI-395959
SMNDC1	O75940	1	EBI-876542,EBI-1052641
SNRNP40	Q96DI7	1	EBI-876542,EBI-538492
SNRPN	P63162	1	EBI-876542,EBI-712493
YWHAZ	P63104	1	EBI-876542,EBI-347088

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1304

1304

Splicing factor 3B subunit 1

PRO_0000174323

Regions

Repeat

529 – 568

HEAT 1

Repeat

569 – 603

HEAT 2

Repeat

604 – 641

HEAT 3

Repeat

643 – 677

HEAT 4

Repeat

680 – 718

HEAT 5

Repeat

763 – 801

HEAT 6

Repeat

843 – 881

HEAT 7

Repeat

1010 – 1048

HEAT 8

Repeat

1052 – 1090

HEAT 9

Repeat

1122 – 1160

HEAT 10

Repeat

1163 – 1201

HEAT 11

Region

223 – 491

269

Interaction with PPP1R8

Amino acid modifications

Modified residue

129

Phosphoserine Ref.15

Modified residue

142

Phosphothreonine Ref.12 Ref.15

Modified residue

194

Phosphoserine Ref.15

Modified residue

207

Phosphothreonine Ref.11 Ref.15

Modified residue

211

Phosphothreonine Ref.9 Ref.11 Ref.14 Ref.15

Modified residue

223

Phosphothreonine Ref.9 Ref.12 Ref.13 Ref.15

Modified residue

227

Phosphothreonine Ref.13 Ref.15

Modified residue

235

Phosphothreonine Ref.8 Ref.15

Modified residue

244

Phosphothreonine Ref.5 Ref.12

Modified residue

248

Phosphothreonine Probable

Modified residue

257

Phosphothreonine Ref.13

Modified residue

261

Phosphothreonine Ref.13

Modified residue

267

Phosphothreonine Ref.13

Modified residue

296

Phosphothreonine Ref.9

Modified residue

299

Phosphothreonine Ref.9 Ref.13

Modified residue

313

Phosphothreonine Probable

Modified residue

316

Phosphothreonine Ref.9

Modified residue

326

Phosphothreonine Ref.9 Ref.11 Ref.15

Modified residue

328

Phosphothreonine Ref.11 Ref.15

Modified residue

332

Phosphoserine Ref.15

Modified residue

344

Phosphoserine Ref.7

Modified residue

350

Phosphothreonine Ref.7

Modified residue

354

Phosphothreonine Ref.7 Ref.14

Modified residue

432

Phosphothreonine Ref.13

Modified residue

488

Phosphoserine Ref.14 Ref.15

Experimental info

Mutagenesis

223

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

227

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

235

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

244

T → A: Slight inhibition of interaction with PPP1R8. Ref.5

Mutagenesis

248

T → A: Slight inhibition of interaction with PPP1R8. Ref.5

Mutagenesis

257

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

261

T → A: Slight inhibition of interaction with PPP1R8. Ref.5

Mutagenesis

267

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

273

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

278

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

296

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

303

T → A: No effect on interaction with PPP1R8. Ref.5

Mutagenesis

313

T → A: No effect on interaction with PPP1R8. Ref.5

Secondary structure

1304

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O75533-1 [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: 40DB21A6209165A7
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FASTA

1,304

145,815

        10         20         30         40         50         60 
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA 

        70         80         90        100        110        120 
TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK 

       130        140        150        160        170        180 
KHRRTMIISP ERLDPFADGG KTPDPKMNVR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE 

       190        200        210        220        230        240 
LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK 

       250        260        270        280        290        300 
GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE 

       310        320        330        340        350        360 
RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI 

       370        380        390        400        410        420 
GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG 

       430        440        450        460        470        480 
YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV 

       490        500        510        520        530        540 
DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM 

       550        560        570        580        590        600 
SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGLEIISNL 

       610        620        630        640        650        660 
AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA 

       670        680        690        700        710        720 
RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG 

       730        740        750        760        770        780 
IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP 

       790        800        810        820        830        840 
DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL 

       850        860        870        880        890        900 
ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF 

       910        920        930        940        950        960 
QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV 

       970        980        990       1000       1010       1020 
VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL 

      1030       1040       1050       1060       1070       1080 
TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT 

      1090       1100       1110       1120       1130       1140 
FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE 

      1150       1160       1170       1180       1190       1200 
LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY 

      1210       1220       1230       1240       1250       1260 
GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK 

      1270       1280       1290       1300 
VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL DYIL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9585501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
[2]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1011-1304. Tissue: Brain.
[3]	"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: 10882114] [Abstract] Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
[4]	"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: 12234937] [Abstract] Cited for: SUBUNIT.
[5]	"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: 12105215] [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.
[6]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; THR-350 AND THR-354, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235, MASS SPECTROMETRY.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211; THR-223; THR-296; THR-299; THR-316 AND THR-326, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 16603771] [Abstract] Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[11]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211; THR-326 AND THR-328, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142; THR-223 AND THR-244, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223; THR-227; THR-257; THR-261; THR-267; THR-299 AND THR-432, MASS SPECTROMETRY.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211; THR-354 AND SER-488, MASS SPECTROMETRY.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-142; SER-194; THR-207; THR-211; THR-223; THR-227; THR-235; THR-326; THR-328; SER-332 AND SER-488, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"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.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF054284 mRNA. Translation: AAC97189.1.
AF070540 mRNA. Translation: AAC28633.1.

IPI

IPI00026089.

UniGene

Hs.632554

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F9D	X-ray	2.50	P/Q	373-415	[»]
2F9J	X-ray	3.00	P/Q	381-415	[»]
2FHO	NMR	-	A	379-424	[»]
2PEH	X-ray	2.11	C/D	333-342	[»]

SMR

O75533. Positions 379-424.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75533. 16 interactions.

PTM databases

PhosphoSite

O75533.

Proteomic databases

PRIDE

O75533.

Genome annotation databases

Ensembl

ENSG00000115524. Homo sapiens. [Contig view]

Organism-specific databases

GeneCards

GC02M197964.

H-InvDB

HIX0002706.

HGNC

HGNC:10768. SF3B1.

MIM

605590. gene.

PharmGKB

PA35686.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75533.

HOVERGEN

O75533.

Enzyme and pathway databases

Reactome

REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75533.

Bgee

O75533.

CleanEx

HS_SF3B1.

GermOnline

ENSG00000115524. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR000357. HEAT.
IPR015016. SF3b_su1.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 2 hits.

Pfam

PF02985. HEAT. 2 hits.
PF08920. SF3b1. 1 hit.
[Graphical view]

PROSITE

PS50077. HEAT_REPEAT. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

PMAP-CutDB

O75533.

SOURCE

Search...

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Entry information

Entry name

SF3B1_HUMAN

Accession

Primary (citable) accession number: O75533

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 1, 1999
Last modified:	July 7, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents