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Splicing factor 3A subunit 3 (SF3a60) (Spliceosome-associated protein 61) (SAP 61)

 SF3A3_HUMAN             Reviewed;         501 AA.
Q12874; D3DPT5; Q15460; Q5VT87;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 180.
RecName: Full=Splicing factor 3A subunit 3;
AltName: Full=SF3a60;
AltName: Full=Spliceosome-associated protein 61;
Short=SAP 61;
Name=SF3A3; Synonyms=SAP61;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix adenocarcinoma;
PubMed=8022796; DOI=10.1073/pnas.91.14.6403;
Chiara M.D., Champion-Arnaud P., Buvoli M., Nadal-Ginard B., Reed R.;
"Specific protein-protein interactions between the essential mammalian
spliceosome-associated proteins SAP 61 and SAP 114.";
Proc. Natl. Acad. Sci. U.S.A. 91:6403-6407(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cervix adenocarcinoma;
PubMed=7816610; DOI=10.1093/nar/22.24.5223;
Kraemer A., Legrain P., Mulhauser F., Groening K., Brosi R., Bilbe G.;
"Splicing factor SF3a60 is the mammalian homologue of PRP9 of
S.cerevisiae: the conserved zinc finger-like motif is functionally
exchangeable in vivo.";
Nucleic Acids Res. 22:5223-5228(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-9; 265-273 AND 292-303, ACETYLATION AT MET-1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[7]
CHARACTERIZATION OF THE SPLICEOSOME.
PubMed=10882114; DOI=10.1016/S1097-2765(00)80318-4;
Das R., Zhou Z., Reed R.;
"Functional association of U2 snRNP with the ATP-independent
spliceosomal complex E.";
Mol. Cell 5:779-787(2000).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND
SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-365; SER-367
AND SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND
SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-121; SER-295;
SER-299 AND THR-475, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
STRUCTURE BY NMR OF 71-107 IN COMPLEX WITH SF3A1, AND SUBUNIT.
PubMed=17098193; DOI=10.1016/j.str.2006.09.009;
Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P.,
Muto Y., Yokoyama S.;
"Solution structures of the SURP domains and the subunit-assembly
mechanism within the splicing factor SF3a complex in 17S U2 snRNP.";
Structure 14:1677-1689(2006).
-!- FUNCTION: Subunit of the splicing factor SF3A 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.
-!- SUBUNIT: Identified in the spliceosome C complex. Component of
splicing factor SF3A which is composed of three subunits;
SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the
splicing factor SF3B and a 12S RNA unit to form the U2 small
nuclear ribonucleoproteins complex (U2 snRNP). Interacts with
SF3A1, through its N-terminal region.
{ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17098193}.
-!- INTERACTION:
P04792:HSPB1; NbExp=2; IntAct=EBI-1051880, EBI-352682;
Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-1051880, EBI-6248094;
Q15459:SF3A1; NbExp=5; IntAct=EBI-1051880, EBI-1054743;
O75478:TADA2A; NbExp=3; IntAct=EBI-1051880, EBI-742268;
Q86WT6:TRIM69; NbExp=3; IntAct=EBI-1051880, EBI-749955;
Q9UDV6:ZNF212; NbExp=3; IntAct=EBI-1051880, EBI-1640204;
-!- SUBCELLULAR LOCATION: Nucleus speckle.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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EMBL; U08815; AAA19625.1; -; mRNA.
EMBL; X81789; CAA57388.1; -; mRNA.
EMBL; AL603790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07304.1; -; Genomic_DNA.
EMBL; CH471059; EAX07305.1; -; Genomic_DNA.
EMBL; BC002395; AAH02395.1; -; mRNA.
EMBL; BC011523; AAH11523.1; -; mRNA.
CCDS; CCDS428.1; -.
PIR; A55749; A55749.
RefSeq; NP_006793.1; NM_006802.3.
UniGene; Hs.77897; -.
PDB; 2DT7; NMR; -; A=71-107.
PDBsum; 2DT7; -.
ProteinModelPortal; Q12874; -.
SMR; Q12874; -.
BioGrid; 116146; 131.
CORUM; Q12874; -.
DIP; DIP-882N; -.
IntAct; Q12874; 27.
MINT; MINT-1467744; -.
STRING; 9606.ENSP00000362110; -.
iPTMnet; Q12874; -.
PhosphoSitePlus; Q12874; -.
SwissPalm; Q12874; -.
BioMuta; SF3A3; -.
DMDM; 17380310; -.
EPD; Q12874; -.
MaxQB; Q12874; -.
PaxDb; Q12874; -.
PeptideAtlas; Q12874; -.
PRIDE; Q12874; -.
DNASU; 10946; -.
Ensembl; ENST00000373019; ENSP00000362110; ENSG00000183431.
GeneID; 10946; -.
KEGG; hsa:10946; -.
UCSC; uc001cci.4; human.
CTD; 10946; -.
DisGeNET; 10946; -.
EuPathDB; HostDB:ENSG00000183431.11; -.
GeneCards; SF3A3; -.
HGNC; HGNC:10767; SF3A3.
HPA; HPA032054; -.
HPA; HPA032055; -.
MIM; 605596; gene.
neXtProt; NX_Q12874; -.
OpenTargets; ENSG00000183431; -.
PharmGKB; PA35685; -.
eggNOG; KOG2636; Eukaryota.
eggNOG; COG5188; LUCA.
GeneTree; ENSGT00530000063402; -.
HOGENOM; HOG000160935; -.
HOVERGEN; HBG054452; -.
InParanoid; Q12874; -.
KO; K12827; -.
OMA; EFPCEIC; -.
OrthoDB; EOG091G059G; -.
PhylomeDB; Q12874; -.
TreeFam; TF315227; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
ChiTaRS; SF3A3; human.
EvolutionaryTrace; Q12874; -.
GeneWiki; SF3A3; -.
GenomeRNAi; 10946; -.
PRO; PR:Q12874; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000183431; -.
CleanEx; HS_SF3A3; -.
Genevisible; Q12874; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005681; C:spliceosomal complex; IDA:HGNC.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC.
GO; GO:0006397; P:mRNA processing; IMP:HGNC.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
InterPro; IPR024598; DUF3449.
InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
InterPro; IPR031776; SF3A3.
InterPro; IPR031774; SF3A3_dom.
InterPro; IPR021966; SF3a60_bindingd.
PANTHER; PTHR12786:SF2; PTHR12786:SF2; 1.
Pfam; PF11931; DUF3449; 1.
Pfam; PF16837; SF3A3; 1.
Pfam; PF12108; SF3a60_bindingd; 1.
PROSITE; PS50171; ZF_MATRIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Glycoprotein; Metal-binding;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Spliceosome; Zinc; Zinc-finger.
CHAIN 1 501 Splicing factor 3A subunit 3.
/FTId=PRO_0000174318.
ZN_FING 406 437 Matrin-type. {ECO:0000255|PROSITE-
ProRule:PRU00130}.
COMPBIAS 354 362 Poly-Glu.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 475 475 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CONFLICT 176 176 E -> G (in Ref. 2; CAA57388).
{ECO:0000305}.
HELIX 80 96 {ECO:0000244|PDB:2DT7}.
SEQUENCE 501 AA; 58849 MW; 6E6F6EA17777E1E2 CRC64;
METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY MEVSGNLRDL
YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN EICVPMSVEF EELLKARENP
SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI NLKASEKLDY ITYLSIFDQL FDIPKERKNA
EYKRYLEMLL EYLQDYTDRV KPLQDQNELF GKIQAEFEKK WENGTFPGWP KETSSALTHA
GAHLDLSAFS SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL
FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRHL THENVQRKQA RTGEEREEEE
EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH GLNINYNCEI CGNYTYRGPK
AFQRHFAEWR HAHGMRCLGI PNTAHFANVT QIEDAVSLWA KLKLQKASER WQPDTEEEYE
DSSGNVVNKK TYEDLKRQGL L


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18-003-43556 Splicing factor 3B subunit 1 - Spliceosome-associated protein 155; SAP 155; SF3b155; Pre-mRNA-splicing factor SF3b 155 kDa subunit Polyclonal 0.1 mg Protein A
EIAAB37996 Mouse,Mus musculus,SAP 62,Sap62,Sf3a2,SF3a66,Spliceosome-associated protein 62,Splicing factor 3A subunit 2
EIAAB37991 Homo sapiens,Human,SAP 114,SAP114,SF3A1,SF3a120,Spliceosome-associated protein 114,Splicing factor 3A subunit 1
EIAAB37995 Homo sapiens,Human,SAP 62,SAP62,SF3A2,SF3a66,Spliceosome-associated protein 62,Splicing factor 3A subunit 2
29-345 SFPQ is DNA- and RNA binding protein. It is essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as an heteromer with NONO. It binds 0.1 mg
29-346 SFPQ is DNA- and RNA binding protein. It is essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as an heteromer with NONO. It binds 0.1 mg
EIAAB39962 Alternative-splicing factor 1,ASF,ASF-1,Homo sapiens,Human,OK_SW-cl.3,pre-mRNA-splicing factor SF2, P33 subunit,Serine_arginine-rich splicing factor 1,SF2,SF2P33,SFRS1,Splicing factor, arginine_serine
EIAAB38015 DNA-binding p52_p100 complex, 100 kDa subunit,Mouse,Mus musculus,Polypyrimidine tract-binding protein-associated-splicing factor,PSF,PTB-associated-splicing factor,Sfpq,Splicing factor, proline- and g
18-003-43606 Splicing factor. proline- and glutamine-rich - Polypyrimidine tract-binding protein-associated-splicing factor; PTB-associated-splicing factor; PSF; DNA-binding p52_p100 complex. 100 kDa subunit; 100 0.1 mg Protein A
18-003-43605 Splicing factor. proline- and glutamine-rich - Polypyrimidine tract-binding protein-associated-splicing factor; PTB-associated-splicing factor; PSF; DNA-binding p52_p100 complex. 100 kDa subunit; 100 0.1 mg Protein A
29-233 SF3B1 is subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). 0.1 mg
29-408 SF3B1 is subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and a 12S RNA unit, forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). 0.1 mg


 

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