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O75533 - SF3B1_HUMAN

UniProt

O75533 - SF3B1_HUMAN

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Protein

Splicing factor 3B subunit 1

Gene

SF3B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. 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

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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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. nuclear speck Source: UniProtKB-SubCell
  3. nucleoplasm Source: HPA
  4. nucleus Source: MGI
  5. spliceosomal complex Source: UniProtKB
  6. U12-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

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 – 1291Phosphoserine3 Publications
Modified residuei141 – 1411N6-acetyllysine1 Publication
Modified residuei142 – 1421Phosphothreonine2 Publications
Modified residuei157 – 1571CitrullineBy similarity
Modified residuei194 – 1941Phosphoserine2 Publications
Modified residuei203 – 2031Phosphothreonine1 Publication
Modified residuei207 – 2071Phosphothreonine4 Publications
Modified residuei211 – 2111Phosphothreonine6 Publications
Modified residuei214 – 2141N6-acetyllysineBy similarity
Modified residuei223 – 2231Phosphothreonine6 Publications
Modified residuei227 – 2271Phosphothreonine2 Publications
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei248 – 2481Phosphothreonine1 Publication
Modified residuei267 – 2671Phosphothreonine1 Publication
Modified residuei296 – 2961Phosphothreonine1 Publication
Modified residuei299 – 2991Phosphothreonine1 Publication
Modified residuei313 – 3131Phosphothreonine1 Publication
Modified residuei326 – 3261Phosphothreonine3 Publications
Modified residuei328 – 3281Phosphothreonine3 Publications
Modified residuei332 – 3321Phosphoserine1 Publication
Modified residuei341 – 3411Phosphothreonine2 Publications
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine2 Publications
Modified residuei350 – 3501Phosphothreonine1 Publication
Modified residuei354 – 3541Phosphothreonine2 Publications
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei434 – 4341Phosphothreonine1 Publication
Modified residuei436 – 4361Phosphothreonine1 Publication
Modified residuei488 – 4881Phosphoserine2 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

BgeeiO75533.
CleanExiHS_SF3B1.
ExpressionAtlasiO75533. baseline and differential.
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. 145 interactions.
DIPiDIP-29411N.
IntActiO75533. 42 interactions.
MINTiMINT-1185911.
STRINGi9606.ENSP00000335321.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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.
GeneTreeiENSGT00390000018393.
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

        10         20         30         40         50
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR 
        60         70         80         90        100
FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ 
       110        120        130        140        150
YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGG KTPDPKMNAR 
       160        170        180        190        200
TYMDVMREQH LTKEEREIRQ QLAEKAKAGE LKVVNGAAAS QPPSKRKRRW 
       210        220        230        240        250
DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK GSETPGATPG 
       260        270        280        290        300
SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE 
       310        320        330        340        350
RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST 
       360        370        380        390        400
PVLTPGKTPI GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS 
       410        420        430        440        450
DEELDAMFPE GYKVLPPPAG YVPIRTPARK LTATPTPLGG MTGFHMQTED 
       460        470        480        490        500
RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV DVDESTLSPE EQKERKIMKL 
       510        520        530        540        550
LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM SPTLEDQERH 
       560        570        580        590        600
LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL 
       610        620        630        640        650
AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA 
       660        670        680        690        700
VCKSKKSWQA RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK 
       710        720        730        740        750
VRTISALAIA ALAEAATPYG IESFDSVLKP LWKGIRQHRG KGLAAFLKAI 
       760        770        780        790        800
GYLIPLMDAE YANYYTREVM LILIREFQSP DEEMKKIVLK VVKQCCGTDG 
       810        820        830        840        850
VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL ANKVGAAEII 
       860        870        880        890        900
SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF 
       910        920        930        940        950
QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ 
       960        970        980        990       1000
AADLISRTAV VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI 
      1010       1020       1030       1040       1050
VNVIGMHKMT PPIKDLLPRL TPILKNRHEK VQENCIDLVG RIADRGAEYV 
      1060       1070       1080       1090       1100
SAREWMRICF ELLELLKAHK KAIRRATVNT FGYIAKAIGP HDVLATLLNN 
      1110       1120       1130       1140       1150
LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE LNVQNGVLKS 
      1160       1170       1180       1190       1200
LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY 
      1210       1220       1230       1240       1250
GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC 
      1260       1270       1280       1290       1300
LQGLFHPARK VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL 

DYIL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117017. 145 interactions.
DIPiDIP-29411N.
IntActiO75533. 42 interactions.
MINTiMINT-1185911.
STRINGi9606.ENSP00000335321.

PTM databases

PhosphoSiteiO75533.

Proteomic databases

MaxQBiO75533.
PaxDbiO75533.
PRIDEiO75533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi23451.
GeneCardsiGC02M198256.
HGNCiHGNC:10768. SF3B1.
HPAiHPA050275.
HPA054596.
MIMi605590. gene.
neXtProtiNX_O75533.
PharmGKBiPA35686.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5181.
GeneTreeiENSGT00390000018393.
HOGENOMiHOG000166737.
HOVERGENiHBG079173.
InParanoidiO75533.
KOiK12828.
OMAiAFWVRRM.
OrthoDBiEOG7R2BHR.
PhylomeDBiO75533.
TreeFamiTF105680.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSF3B1. human.
EvolutionaryTraceiO75533.
GeneWikiiSF3B1.
GenomeRNAii23451.
NextBioi45735.
PMAP-CutDBO75533.
PROiO75533.
SOURCEiSearch...

Gene expression databases

BgeeiO75533.
CleanExiHS_SF3B1.
ExpressionAtlasiO75533. baseline and differential.
GenevestigatoriO75533.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 289:17325-17337(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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 145 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

Similar proteinsi

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