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O75533 (SF3B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1304 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the SF3B1 family.

Contains 11 HEAT repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RBM17Q96I252EBI-876542,EBI-740272

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13041304Splicing factor 3B subunit 1
PRO_0000174323

Regions

Repeat529 – 56840HEAT 1
Repeat569 – 60335HEAT 2
Repeat604 – 64138HEAT 3
Repeat643 – 67735HEAT 4
Repeat680 – 71839HEAT 5
Repeat763 – 80139HEAT 6
Repeat843 – 88139HEAT 7
Repeat1010 – 104839HEAT 8
Repeat1052 – 109039HEAT 9
Repeat1122 – 116039HEAT 10
Repeat1163 – 120139HEAT 11
Region223 – 491269Interaction with PPP1R8
Region529 – 56840Interaction with SF3B14

Amino acid modifications

Modified residue1291Phosphoserine Ref.17 Ref.21 Ref.23
Modified residue1411N6-acetyllysine Ref.20
Modified residue1421Phosphothreonine Ref.14 Ref.17
Modified residue1571Citrulline By similarity
Modified residue1941Phosphoserine Ref.17 Ref.21
Modified residue2031Phosphothreonine Ref.21
Modified residue2071Phosphothreonine Ref.13 Ref.17 Ref.19 Ref.21
Modified residue2111Phosphothreonine Ref.11 Ref.13 Ref.17 Ref.19 Ref.21 Ref.23
Modified residue2141N6-acetyllysine By similarity
Modified residue2231Phosphothreonine Ref.11 Ref.14 Ref.15 Ref.17 Ref.19 Ref.21
Modified residue2271Phosphothreonine Ref.17 Ref.19
Modified residue2441Phosphothreonine Ref.7
Modified residue2481Phosphothreonine Probable
Modified residue2671Phosphothreonine Ref.15
Modified residue2961Phosphothreonine Ref.11
Modified residue2991Phosphothreonine Ref.11
Modified residue3131Phosphothreonine Probable
Modified residue3261Phosphothreonine Ref.17 Ref.19 Ref.21
Modified residue3281Phosphothreonine Ref.13 Ref.17 Ref.21
Modified residue3321Phosphoserine Ref.17
Modified residue3411Phosphothreonine Ref.19 Ref.23
Modified residue3441Phosphoserine Ref.23
Modified residue3491Phosphoserine Ref.19 Ref.23
Modified residue3501Phosphothreonine Ref.19
Modified residue3541Phosphothreonine Ref.16 Ref.23
Modified residue4001Phosphoserine Ref.19
Modified residue4341Phosphothreonine Ref.19
Modified residue4361Phosphothreonine Ref.19
Modified residue4881Phosphoserine Ref.17 Ref.21
Modified residue5541N6-acetyllysine Ref.20
Modified residue5621N6-acetyllysine Ref.20
Modified residue10671N6-acetyllysine Ref.20

Natural variations

Alternative sequence140 – 1445GKTPD → FYSAA in isoform 2.
VSP_046182
Alternative sequence145 – 13041160Missing in isoform 2.
VSP_046183

Experimental info

Mutagenesis2231T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2271T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2351T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2441T → A: Slight inhibition of interaction with PPP1R8. Ref.7
Mutagenesis2481T → A: Slight inhibition of interaction with PPP1R8. Ref.7
Mutagenesis2571T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2611T → A: Slight inhibition of interaction with PPP1R8. Ref.7
Mutagenesis2671T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2731T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2781T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis2961T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis3031T → A: No effect on interaction with PPP1R8. Ref.7
Mutagenesis3131T → A: No effect on interaction with PPP1R8. Ref.7
Sequence conflict1491A → V in AAC97189. Ref.1
Sequence conflict5941R → L in AAC97189. Ref.1

Secondary structure

....... 1304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: 12F051757D2B9DEE

FASTA1,304145,830
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 006D4294E06AB51E
Show »

FASTA14416,020

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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, 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]"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].
[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]"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.
RefSeqNP_036565.2. NM_012433.2.
UniGeneHs.632554.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F9DX-ray2.50P/Q373-415[»]
2F9JX-ray3.00P/Q381-415[»]
2FHONMR-A379-424[»]
2PEHX-ray2.11C/D333-342[»]
3LQVX-ray2.38P/Q377-415[»]
ProteinModelPortalO75533.
SMRO75533. Positions 377-415, 587-716, 910-1000, 1143-1196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117017. 126 interactions.
DIPDIP-29411N.
IntActO75533. 40 interactions.
MINTMINT-1185911.
STRING9606.ENSP00000335321.

PTM databases

PhosphoSiteO75533.

Proteomic databases

PaxDbO75533.
PRIDEO75533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335508; ENSP00000335321; ENSG00000115524. [O75533-1]
ENST00000409915; ENSP00000428820; ENSG00000115524. [O75533-2]
ENST00000414963; ENSP00000402997; ENSG00000115524. [O75533-2]
GeneID23451.
KEGGhsa:23451.
UCSCuc002uue.3. human. [O75533-1]
uc002uuf.3. human.

Organism-specific databases

CTD23451.
GeneCardsGC02M198256.
HGNCHGNC:10768. SF3B1.
HPAHPA050275.
HPA054596.
MIM605590. gene.
neXtProtNX_O75533.
PharmGKBPA35686.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5181.
HOGENOMHOG000166737.
HOVERGENHBG079173.
InParanoidO75533.
KOK12828.
OMAAFWVRRM.
OrthoDBEOG7R2BHR.
PhylomeDBO75533.
TreeFamTF105680.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO75533.
BgeeO75533.
CleanExHS_SF3B1.
GenevestigatorO75533.

Family and domain databases

Gene3D1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015016. SF3b_su1.
[Graphical view]
PfamPF08920. SF3b1. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

EvolutionaryTraceO75533.
GeneWikiSF3B1.
GenomeRNAi23451.
NextBio45735.
PMAP-CutDBO75533.
PROO75533.
SOURCESearch...

Entry information

Entry nameSF3B1_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

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