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Protein

Splicing factor 3B subunit 2

Gene

SF3B2

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

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA processing Source: ProtInc
  • mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087365-MONOMER.
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
SF3b150
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

HGNCiHGNC:10769. SF3B2.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • precatalytic spliceosome Source: GO_Central
  • spliceosomal complex Source: HGNC
  • U12-type spliceosomal complex Source: UniProtKB
  • U2 snRNP Source: GO_Central
  • U2-type spliceosomal complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

DisGeNETi10992.
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
Modified residuei222Omega-N-methylarginineCombined sources1
Modified residuei245Omega-N-methylarginineCombined sources1
Modified residuei247Omega-N-methylarginineCombined sources1
Modified residuei275N6-acetyllysineCombined sources1
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
Modified residuei515Omega-N-methylarginineCombined sources1
Modified residuei780PhosphothreonineCombined sources1
Modified residuei861PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13435.
MaxQBiQ13435.
PaxDbiQ13435.
PeptideAtlasiQ13435.
PRIDEiQ13435.
TopDownProteomicsiQ13435.

PTM databases

iPTMnetiQ13435.
PhosphoSitePlusiQ13435.
SwissPalmiQ13435.

Miscellaneous databases

PMAP-CutDBQ13435.

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. 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/SF3B145, SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B, SF3B10 and SF3B125. SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). SF3B2 interacts directly with SF3B4. Interacts with HIV-1 Vpr.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX16O602312EBI-749111,EBI-311446
FRA10AC1Q70Z532EBI-749111,EBI-710176
KDM1AO603412EBI-749111,EBI-710124
PRPF3O433952EBI-749111,EBI-744322
PRPF8Q6P2Q93EBI-749111,EBI-538479
RNF113AO155412EBI-749111,EBI-2130294
SF3B4Q154273EBI-749111,EBI-348469
SLU7O953912EBI-749111,EBI-750559
U2AF1Q010812EBI-749111,EBI-632461
XAB2Q9HCS72EBI-749111,EBI-295232
ZNF830Q96NB32EBI-749111,EBI-3920997

Protein-protein interaction databases

BioGridi116188. 141 interactors.
IntActiQ13435. 61 interactors.
MINTiMINT-3027706.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DO5NMR-A24-68[»]
ProteinModelPortaliQ13435.
SMRiQ13435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13435.

Family & Domainsi

Domains and Repeats

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

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

Sequence similaritiesi

Contains 1 SAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2330. Eukaryota.
COG5182. LUCA.
GeneTreeiENSGT00390000006734.
HOVERGENiHBG054023.
InParanoidiQ13435.
KOiK12829.
OMAiDKMENSA.
OrthoDBiEOG091G0A5N.
PhylomeDBiQ13435.
TreeFamiTF300635.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DO5NMR-A24-68[»]
ProteinModelPortaliQ13435.
SMRiQ13435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116188. 141 interactors.
IntActiQ13435. 61 interactors.
MINTiMINT-3027706.
STRINGi9606.ENSP00000318861.

Chemistry databases

ChEMBLiCHEMBL1229011.

PTM databases

iPTMnetiQ13435.
PhosphoSitePlusiQ13435.
SwissPalmiQ13435.

Polymorphism and mutation databases

BioMutaiSF3B2.
DMDMi296452908.

Proteomic databases

EPDiQ13435.
MaxQBiQ13435.
PaxDbiQ13435.
PeptideAtlasiQ13435.
PRIDEiQ13435.
TopDownProteomicsiQ13435.

Protocols and materials databases

DNASUi10992.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10992.
DisGeNETi10992.
GeneCardsiSF3B2.
H-InvDBHIX0009823.
HGNCiHGNC:10769. SF3B2.
HPAiHPA045028.
MIMi605591. gene.
neXtProtiNX_Q13435.
OpenTargetsiENSG00000087365.
PharmGKBiPA35687.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2330. Eukaryota.
COG5182. LUCA.
GeneTreeiENSGT00390000006734.
HOVERGENiHBG054023.
InParanoidiQ13435.
KOiK12829.
OMAiDKMENSA.
OrthoDBiEOG091G0A5N.
PhylomeDBiQ13435.
TreeFamiTF300635.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000087365-MONOMER.
ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.

Miscellaneous databases

ChiTaRSiSF3B2. human.
EvolutionaryTraceiQ13435.
GeneWikiiSF3B2.
GenomeRNAii10992.
PMAP-CutDBQ13435.
PROiQ13435.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087365.
CleanExiHS_SF3B2.
ExpressionAtlasiQ13435. baseline and differential.
GenevisibleiQ13435. HS.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSF3B2_HUMAN
AccessioniPrimary (citable) accession number: Q13435
Secondary accession number(s): A8K485
, B4DT19, Q7L4T5, Q7Z627, Q969K1, Q96CM6, Q9BWD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 159 of the entry and version 2 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, 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
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.