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Protein

Splicing factor 3B subunit 2

Gene

SF3B2

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

Functioni

Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643). SF3B complex is 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 (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (PubMed:15146077).4 Publications

GO - Molecular functioni

GO - Biological processi

  • mRNA processing Source: ProtInc
  • mRNA splicing, via spliceosome Source: GO_Central
  • RNA splicing Source: ProtInc
  • viral process Source: UniProtKB-KW

Keywordsi

Biological processHost-virus interaction, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3B subunit 2
Alternative name(s):
Pre-mRNA-splicing factor SF3b 145 kDa subunit
Short name:
SF3b145
Spliceosome-associated protein 145
Short name:
SAP 145
Gene namesi
Name:SF3B2
Synonyms:SAP145
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000087365.14
HGNCiHGNC:10769 SF3B2
MIMi605591 gene
neXtProtiNX_Q13435

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi471R → K: Does not affect methylation by PRMT9. 1 Publication1
Mutagenesisi495R → K: Does not affect methylation by PRMT9. 1 Publication1
Mutagenesisi502R → K: Does not affect methylation by PRMT9. 1 Publication1
Mutagenesisi506F → A: Does not affect methylation by PRMT9; when associated with A-510. 1 Publication1
Mutagenesisi507K → A: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-509. 1 Publication1
Mutagenesisi507K → R: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-509. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-508. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-509. 1 Publication1
Mutagenesisi508R → K: Abolishes interaction with SMN1; Abolishes methylation by PRMT9. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507 and R-509. 2 Publications1
Mutagenesisi509K → A: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-507. 1 Publication1
Mutagenesisi509K → R: Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-507. 1 Publication1
Mutagenesisi510Y → A: Does not affect methylation by PRMT9; when associated with A-506. 1 Publication1
Mutagenesisi515R → K: Does not affect methylation by PRMT9. 1 Publication1
Mutagenesisi530R → K: Does not affect methylation by PRMT9. 1 Publication1
Mutagenesisi537R → K: Does not affect methylation by PRMT9. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000087365
PharmGKBiPA35687

Chemistry databases

ChEMBLiCHEMBL1229011

Polymorphism and mutation databases

BioMutaiSF3B2
DMDMi296452908

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001743281 – 895Splicing factor 3B subunit 2Add BLAST895

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei222Omega-N-methylarginineCombined sources1
Modified residuei245Omega-N-methylarginineCombined sources1
Modified residuei247Omega-N-methylarginineCombined sources1
Modified residuei275N6-acetyllysineCombined sources1
Cross-linki280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei289PhosphoserineCombined sources1
Modified residuei298PhosphothreonineCombined sources1
Modified residuei307PhosphoserineCombined sources1
Modified residuei309PhosphoserineCombined sources1
Modified residuei311PhosphothreonineCombined sources1
Modified residuei317PhosphoserineCombined sources1
Modified residuei360PhosphoserineCombined sources1
Modified residuei362PhosphoserineCombined sources1
Cross-linki400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei431PhosphoserineCombined sources1
Modified residuei435PhosphoserineCombined sources1
Modified residuei436PhosphoserineCombined sources1
Cross-linki492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei508Omega-N-methylarginine; by PRMT9; alternate1 Publication1
Modified residuei508Symmetric dimethylarginine; by PRMT9; alternate1 Publication1
Modified residuei515Omega-N-methylarginineCombined sources1
Cross-linki543Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki770Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei780PhosphothreonineCombined sources1
Cross-linki790Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki843Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei861PhosphoserineCombined sources1

Post-translational modificationi

Methylation at Arg-508 by PRMT9 is required for the interaction with SMN1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13435
MaxQBiQ13435
PaxDbiQ13435
PeptideAtlasiQ13435
PRIDEiQ13435
ProteomicsDBi59431
TopDownProteomicsiQ13435

PTM databases

iPTMnetiQ13435
PhosphoSitePlusiQ13435
SwissPalmiQ13435

Miscellaneous databases

PMAP-CutDBiQ13435

Expressioni

Gene expression databases

BgeeiENSG00000087365
CleanExiHS_SF3B2
ExpressionAtlasiQ13435 baseline and differential
GenevisibleiQ13435 HS

Organism-specific databases

HPAiHPA045028

Interactioni

Subunit structurei

Identified in the spliceosome C complex (PubMed:11991638). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome (PubMed:15146077). Component of splicing factor SF3B which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42 (PubMed:12234937, PubMed:12738865, PubMed:27720643, PubMed:28541300). SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP) (PubMed:12234937). Interacts directly with SF3B4 (PubMed:25737013). The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2 (PubMed:27720643). Found in a complex with PRMT9, SF3B2 and SF3B4 (PubMed:25737013). Interacts (Arg-508-methylated form) with SMN1 (via Tudor domain) (PubMed:25737013). Interacts with RBM7 (PubMed:27905398).8 Publications
(Microbial infection) Interacts with HIV-1 Vpr.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi116188, 219 interactors
CORUMiQ13435
IntActiQ13435, 67 interactors
MINTiQ13435
STRINGi9606.ENSP00000318861

Structurei

Secondary structure

1895
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 39Combined sources11
Helixi47 – 61Combined sources15

3D structure databases

ProteinModelPortaliQ13435
SMRiQ13435
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13435

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 58SAPPROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni401 – 550Required for interaction with PRMT91 PublicationAdd BLAST150

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili140 – 199Sequence analysisAdd BLAST60

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi16 – 21Poly-Pro6
Compositional biasi91 – 96Poly-Pro6
Compositional biasi104 – 113Poly-Pro10
Compositional biasi129 – 132Poly-Pro4
Compositional biasi249 – 253Poly-Pro5
Compositional biasi292 – 297Poly-Glu6
Compositional biasi331 – 335Poly-Lys5
Compositional biasi699 – 702Poly-Glu4
Compositional biasi720 – 726Poly-Glu7

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2330 Eukaryota
COG5182 LUCA
GeneTreeiENSGT00390000006734
HOVERGENiHBG054023
InParanoidiQ13435
KOiK12829
OMAiMYRQFYR
OrthoDBiEOG091G0A5N
PhylomeDBiQ13435
TreeFamiTF300635

Family and domain databases

InterProiView protein in InterPro
IPR007180 DUF382
IPR006568 PSP_pro-rich
IPR003034 SAP_dom
PfamiView protein in Pfam
PF04037 DUF382, 1 hit
PF04046 PSP, 1 hit
PF02037 SAP, 1 hit
SMARTiView protein in SMART
SM00581 PSP, 1 hit
SM00513 SAP, 1 hit
PROSITEiView protein in PROSITE
PS50800 SAP, 1 hit

Sequencei

Sequence statusi: Complete.

Q13435-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL
60 70 80 90 100
VERLQSYTRQ TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP
110 120 130 140 150
PLQPPPPPPP PPPGLGLGFP MAHPPNLGPP PPLRVGEPVA LSEEERLKLA
160 170 180 190 200
QQQAALLMQQ EERAKQQGDH SLKEHELLEQ QKRAAVLLEQ ERQQEIAKMG
210 220 230 240 250
TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG APVPRPRGPP
260 270 280 290 300
PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA
310 320 330 340 350
RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR
360 370 380 390 400
EKDSTRSRGS DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK
410 420 430 440 450
KEKEKEPEKL DKLENSAAPK KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS
460 470 480 490 500
KKKLRRMNRF TVAELKQLVA RPDVVEMHDV TAQDPKLLVH LKATRNSVPV
510 520 530 540 550
PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL QEKEEQKTMK
560 570 580 590 600
SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR
610 620 630 640 650
LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI
660 670 680 690 700
PGLNSPIPES CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE
710 720 730 740 750
EEIDRTPWGE LEPSDEESSE EEEEEESDED KPDETGFITP ADSGLITPGG
760 770 780 790 800
FSSVPAGMET PELIELRKKK IEEAMDGSET PQLFTVLPEK RTATVGGAMM
810 820 830 840 850
GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM TQKYEEHVRE
860 870 880 890
QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF
Length:895
Mass (Da):100,228
Last modified:May 18, 2010 - v2
Checksum:iD372AFA679443AD6
GO

Sequence cautioni

The sequence AAA97461 differs from that shown. Reason: Frameshift at position 28.Curated
The sequence AAA97461 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH53577 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAG61831 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti602K → E in BAF83539 (PubMed:14702039).Curated1
Sequence conflicti765E → G in BAF83539 (PubMed:14702039).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK290850 mRNA Translation: BAF83539.1
AK300016 mRNA Translation: BAG61831.1 Different initiation.
BC000401 mRNA Translation: AAH00401.2
BC007610 mRNA Translation: AAH07610.1
BC014125 mRNA Translation: AAH14125.2
BC053577 mRNA Translation: AAH53577.1 Sequence problems.
U41371 mRNA Translation: AAA97461.1 Frameshift.
CCDSiCCDS31612.1
RefSeqiNP_006833.2, NM_006842.2
UniGeneiHs.406423

Genome annotation databases

EnsembliENST00000322535; ENSP00000318861; ENSG00000087365
GeneIDi10992
KEGGihsa:10992
UCSCiuc001ogy.2 human

Similar proteinsi

Entry informationi

Entry nameiSF3B2_HUMAN
AccessioniPrimary (citable) accession number: Q13435
Secondary accession number(s): A8K485
, B4DT19, Q7L4T5, Q7Z627, Q969K1, Q96CM6, Q9BWD2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: July 18, 2018
This is version 175 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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