O75533 (SF3B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. 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, 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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
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.1 Ref.7
Sequence similarities	Belongs to the SF3B1 family. Contains 11 HEAT repeats.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara mRNA splicing, via spliceosome Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	U12-type spliceosomal complex Inferred from direct assay Ref.10. Source: UniProtKB catalytic step 2 spliceosome Inferred from direct assay Ref.8. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75533-1)

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.

Isoform 2 (identifier: O75533-2)

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

Note: No experimental confirmation available.

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

40

HEAT 1

Repeat

569 – 603

35

HEAT 2

Repeat

604 – 641

38

HEAT 3

Repeat

643 – 677

35

HEAT 4

Repeat

680 – 718

39

HEAT 5

Repeat

763 – 801

39

HEAT 6

Repeat

843 – 881

39

HEAT 7

Repeat

1010 – 1048

39

HEAT 8

Repeat

1052 – 1090

39

HEAT 9

Repeat

1122 – 1160

39

HEAT 10

Repeat

1163 – 1201

39

HEAT 11

Region

223 – 491

269

Interaction with PPP1R8

Region

529 – 568

40

Interaction with SF3B14

Amino acid modifications

Modified residue

129

1

Phosphoserine Ref.17 Ref.20 Ref.22

Modified residue

141

1

N6-acetyllysine Ref.19

Modified residue

142

1

Phosphothreonine Ref.14 Ref.17

Modified residue

194

1

Phosphoserine Ref.17 Ref.20

Modified residue

203

1

Phosphothreonine Ref.20

Modified residue

207

1

Phosphothreonine Ref.13 Ref.17 Ref.18 Ref.20

Modified residue

211

1

Phosphothreonine Ref.11 Ref.13 Ref.17 Ref.18 Ref.20 Ref.22

Modified residue

223

1

Phosphothreonine Ref.11 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20

Modified residue

227

1

Phosphothreonine Ref.17 Ref.18

Modified residue

244

1

Phosphothreonine Ref.7

Modified residue

248

1

Phosphothreonine Probable

Modified residue

267

1

Phosphothreonine Ref.15

Modified residue

278

1

Phosphothreonine By similarity

Modified residue

296

1

Phosphothreonine Ref.11

Modified residue

299

1

Phosphothreonine Ref.11

Modified residue

313

1

Phosphothreonine Probable

Modified residue

326

1

Phosphothreonine Ref.17 Ref.18 Ref.20

Modified residue

328

1

Phosphothreonine Ref.13 Ref.17 Ref.20

Modified residue

332

1

Phosphoserine Ref.17

Modified residue

341

1

Phosphothreonine Ref.18 Ref.22

Modified residue

344

1

Phosphoserine Ref.22

Modified residue

349

1

Phosphoserine Ref.18 Ref.22

Modified residue

350

1

Phosphothreonine Ref.18

Modified residue

354

1

Phosphothreonine Ref.16 Ref.22

Modified residue

400

1

Phosphoserine Ref.18

Modified residue

434

1

Phosphothreonine Ref.18

Modified residue

436

1

Phosphothreonine Ref.18

Modified residue

488

1

Phosphoserine Ref.17 Ref.20

Modified residue

554

1

N6-acetyllysine Ref.19

Modified residue

562

1

N6-acetyllysine Ref.19

Modified residue

1067

1

N6-acetyllysine Ref.19

Natural variations

Alternative sequence

140 – 144

5

GKTPD → FYSAA in isoform 2.

VSP_046182

Alternative sequence

145 – 1304

1160

Missing in isoform 2.

VSP_046183

Experimental info

Mutagenesis

223

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

227

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

235

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

244

1

T → A: Slight inhibition of interaction with PPP1R8. Ref.7

Mutagenesis

248

1

T → A: Slight inhibition of interaction with PPP1R8. Ref.7

Mutagenesis

257

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

261

1

T → A: Slight inhibition of interaction with PPP1R8. Ref.7

Mutagenesis

267

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

273

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

278

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

296

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

303

1

T → A: No effect on interaction with PPP1R8. Ref.7

Mutagenesis

313

1

T → A: No effect on interaction with PPP1R8. Ref.7

Sequence conflict

149

1

A → V in AAC97189. Ref.1

Sequence conflict

594

1

R → L in AAC97189. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

1304

Helix Strand Turn

Details...

Helix

380 – 394

15

Helix

401 – 406

6

Beta strand

410 – 414

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 24, 2009. Version 3. Checksum: 12F051757D2B9DEE	FASTA	1,304	145,830
	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 KTPDPKMNAR 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 VEGREIISNL 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
	Isoform 2 [UniParc]. Checksum: 006D4294E06AB51E	FASTA	144	16,020
	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 KHRRTMIISP ERLDPFADGF YSAA

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] [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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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, MASS SPECTROMETRY.
[23]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF054284 mRNA. Translation: AAC97189.1.
AF086296 mRNA. No translation available.
AC010746 Genomic DNA. No translation available.
AF070540 mRNA. Translation: AAC28633.1.

IPI

IPI00026089.
IPI01011024.

RefSeq

NP_036565.2. NM_012433.2.

UniGene

Hs.632554.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3LQV	X-ray	2.38	P/Q	377-415	[»]

ProteinModelPortal

O75533.

SMR

O75533. Positions 377-415, 849-877, 978-1004, 1014-1085.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29411N.

IntAct

O75533. 17 interactions.

MINT

MINT-1185911.

STRING

9606.ENSP00000335321.

PTM databases

PhosphoSite

O75533.

Proteomic databases

PaxDb

O75533.

PRIDE

O75533.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335508; ENSP00000335321; ENSG00000115524.
ENST00000409915; ENSP00000428820; ENSG00000115524.
ENST00000414963; ENSP00000402997; ENSG00000115524.

GeneID

23451.

KEGG

hsa:23451.

UCSC

uc002uue.3. human.

Organism-specific databases

CTD

23451.

GeneCards

GC02M198256.

HGNC

HGNC:10768. SF3B1.

HPA

HPA050275.

MIM

605590. gene.

neXtProt

NX_O75533.

PharmGKB

PA35686.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5181.

HOGENOM

HOG000166737.

HOVERGEN

HBG079173.

InParanoid

O75533.

KO

K12828.

OMA

GVEAQYI.

OrthoDB

EOG4RJG0Q.

PhylomeDB

O75533.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O75533.

Bgee

O75533.

CleanEx

HS_SF3B1.

Genevestigator

O75533.

GermOnline

ENSG00000115524. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 4 hits.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015016. SF3b_su1.
[Graphical view]

Pfam

PF08920. SF3b1. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50077. HEAT_REPEAT. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1229013.

EvolutionaryTrace

O75533.

GenomeRNAi

23451.

NextBio

45735.

PMAP-CutDB

O75533.

SOURCE

Search...

Entry information

Entry name

SF3B1_HUMAN

Accession

Primary (citable) accession number: O75533
Secondary accession number(s): E9PCH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.