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Q13435 (SF3B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SF3B2
Synonyms:SAP145
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length895 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/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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 SAP domain.

Sequence caution

The sequence AAA97461.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA97461.1 differs from that shown. Reason: Frameshift at position 28.

The sequence AAH53577.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAG61831.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 895895Splicing factor 3B subunit 2
PRO_0000174328

Regions

Domain24 – 5835SAP
Coiled coil140 – 19960 Potential
Compositional bias16 – 216Poly-Pro
Compositional bias91 – 966Poly-Pro
Compositional bias104 – 11310Poly-Pro
Compositional bias129 – 1324Poly-Pro
Compositional bias249 – 2535Poly-Pro
Compositional bias292 – 2976Poly-Glu
Compositional bias331 – 3355Poly-Lys
Compositional bias699 – 7024Poly-Glu
Compositional bias720 – 7267Poly-Glu

Amino acid modifications

Modified residue2751N6-acetyllysine Ref.17
Modified residue2891Phosphoserine Ref.11 Ref.13 Ref.20
Modified residue3071Phosphoserine Ref.13 Ref.16 Ref.18
Modified residue3091Phosphoserine Ref.13 Ref.16 Ref.18
Modified residue3111Phosphothreonine Ref.13
Modified residue3601Phosphoserine Ref.16
Modified residue3621Phosphoserine Ref.16
Modified residue4311Phosphoserine Ref.9 Ref.14 Ref.18 Ref.20
Modified residue4351Phosphoserine Ref.9 Ref.14 Ref.18 Ref.20
Modified residue4361Phosphoserine Ref.9 Ref.14 Ref.18 Ref.20
Modified residue7801Phosphothreonine Ref.13 Ref.16 Ref.18

Experimental info

Sequence conflict6021K → E in BAF83539. Ref.1
Sequence conflict7651E → G in BAF83539. Ref.1

Secondary structure

..... 895
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13435 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: D372AFA679443AD6

FASTA895100,228
        10         20         30         40         50         60 
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ 

        70         80         90        100        110        120 
TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP 

       130        140        150        160        170        180 
MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQQGDH SLKEHELLEQ 

       190        200        210        220        230        240 
QKRAAVLLEQ ERQQEIAKMG TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG 

       250        260        270        280        290        300 
APVPRPRGPP PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA 

       310        320        330        340        350        360 
RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR EKDSTRSRGS 

       370        380        390        400        410        420 
DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK KEKEKEPEKL DKLENSAAPK 

       430        440        450        460        470        480 
KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS KKKLRRMNRF TVAELKQLVA RPDVVEMHDV 

       490        500        510        520        530        540 
TAQDPKLLVH LKATRNSVPV PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL 

       550        560        570        580        590        600 
QEKEEQKTMK SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR 

       610        620        630        640        650        660 
LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI PGLNSPIPES 

       670        680        690        700        710        720 
CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE EEIDRTPWGE LEPSDEESSE 

       730        740        750        760        770        780 
EEEEEESDED KPDETGFITP ADSGLITPGG FSSVPAGMET PELIELRKKK IEEAMDGSET 

       790        800        810        820        830        840 
PQLFTVLPEK RTATVGGAMM GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM 

       850        860        870        880        890 
TQKYEEHVRE QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymphoblast and Peripheral blood.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye, Kidney, Lung and Testis.
[3]"Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A."
Gozani O., Feld R., Reed R.
Genes Dev. 10:233-243(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-895, PROTEIN SEQUENCE OF 174-182 AND 817-840.
Tissue: Cervix carcinoma.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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 SER-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145."
Terada Y., Yasuda Y.
Mol. Cell. Biol. 26:8149-8158(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-289; SER-307; SER-309; THR-311 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"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].
[16]"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 SER-307; SER-309; SER-360; SER-362 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-307; SER-309; SER-431; SER-435; SER-436 AND THR-780, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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-289; SER-431; SER-435 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Solution structure of the SAP domain of human splicing factor 3B subunit 2."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 24-68.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006833.2. NM_006842.2.
UniGeneHs.406423.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO5NMR-A24-68[»]
ProteinModelPortalQ13435.
SMRQ13435. Positions 26-68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116188. 88 interactions.
IntActQ13435. 47 interactions.
MINTMINT-3027706.
STRING9606.ENSP00000318861.

Chemistry

ChEMBLCHEMBL1229011.

PTM databases

PhosphoSiteQ13435.

Polymorphism databases

DMDM296452908.

Proteomic databases

PaxDbQ13435.
PRIDEQ13435.

Protocols and materials databases

DNASU10992.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322535; ENSP00000318861; ENSG00000087365.
GeneID10992.
KEGGhsa:10992.
UCSCuc001ogy.1. human.

Organism-specific databases

CTD10992.
GeneCardsGC11P065827.
H-InvDBHIX0009823.
HGNCHGNC:10769. SF3B2.
HPAHPA045028.
MIM605591. gene.
neXtProtNX_Q13435.
PharmGKBPA35687.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5182.
HOVERGENHBG054023.
InParanoidQ13435.
KOK12829.
OMADRLKGYM.
PhylomeDBQ13435.
TreeFamTF300635.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ13435.
BgeeQ13435.
CleanExHS_SF3B2.
GenevestigatorQ13435.

Family and domain databases

InterProIPR007180. DUF382.
IPR006568. PSP.
IPR003034. SAP_dom.
[Graphical view]
PfamPF04037. DUF382. 1 hit.
PF04046. PSP. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00581. PSP. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13435.
GeneWikiSF3B2.
GenomeRNAi10992.
NextBio41771.
PMAP-CutDBQ13435.
PROQ13435.
SOURCESearch...

Entry information

Entry nameSF3B2_HUMAN
AccessionPrimary (citable) accession number: Q13435
Secondary accession number(s): A8K485 expand/collapse secondary AC list , B4DT19, Q7L4T5, Q7Z627, Q969K1, Q96CM6, Q9BWD2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 129 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM