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Q15459

- SF3A1_HUMAN

UniProt

Q15459 - SF3A1_HUMAN

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Protein

Splicing factor 3A subunit 1

Gene

SF3A1

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

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1691Critical for binding to SF3A3

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA 3'-splice site recognition Source: HGNC
  3. mRNA processing Source: HGNC
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3A subunit 1
Alternative name(s):
SF3a120
Spliceosome-associated protein 114
Short name:
SAP 114
Gene namesi
Name:SF3A1
Synonyms:SAP114
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:10765. SF3A1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. spliceosomal complex Source: HGNC
  5. U2-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481E → F: SLURP 1 motif acquires binding to SF3A3; when associated to Leu-55. 1 Publication
Mutagenesisi55 – 551K → L: SLURP 1 motif acquires binding to SF3A3; when associated to Phe-48. 1 Publication
Mutagenesisi162 – 1621F → E: No effect on binding to SF3A3. 1 Publication
Mutagenesisi169 – 1691L → K: Abolishes binding to SF3A3. 1 Publication

Organism-specific databases

PharmGKBiPA35683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 793793Splicing factor 3A subunit 1PRO_0000114917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei320 – 3201Phosphoserine2 Publications
Modified residuei329 – 3291Phosphoserine7 Publications
Modified residuei359 – 3591Phosphoserine4 Publications
Modified residuei413 – 4131Phosphoserine2 Publications
Modified residuei451 – 4511Phosphoserine3 Publications
Modified residuei456 – 4561Phosphotyrosine1 Publication
Modified residuei759 – 7591Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15459.
PaxDbiQ15459.
PeptideAtlasiQ15459.
PRIDEiQ15459.

PTM databases

PhosphoSiteiQ15459.

Miscellaneous databases

PMAP-CutDBQ15459.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiQ15459.
CleanExiHS_SF3A1.
ExpressionAtlasiQ15459. baseline and differential.
GenevestigatoriQ15459.

Organism-specific databases

HPAiHPA000690.
HPA030083.

Interactioni

Subunit structurei

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 SF3A3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAP1LC3CQ9BXW43EBI-1054743,EBI-2603996
PRPF40AO754002EBI-1054743,EBI-473291
RBM10P981752EBI-1054743,EBI-721525
SF3A2Q154283EBI-1054743,EBI-2462271
SF3A3Q128742EBI-1054743,EBI-1051880
SP1P080472EBI-1054743,EBI-298336

Protein-protein interaction databases

BioGridi115580. 129 interactions.
DIPiDIP-29164N.
IntActiQ15459. 28 interactions.
MINTiMINT-144269.
STRINGi9606.ENSP00000215793.

Structurei

Secondary structure

1
793
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 6316
Helixi66 – 749
Helixi79 – 846
Helixi91 – 10313
Helixi161 – 17717
Helixi179 – 18810
Turni189 – 1913
Helixi193 – 1986
Helixi204 – 21512
Beta strandi705 – 7106
Beta strandi715 – 7217
Beta strandi726 – 7316
Helixi737 – 74711
Turni752 – 7543
Beta strandi755 – 7595
Beta strandi762 – 7643
Helixi770 – 7734
Beta strandi779 – 7868

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKHNMR-A704-789[»]
2DT6NMR-A48-110[»]
2DT7NMR-B134-217[»]
ProteinModelPortaliQ15459.
SMRiQ15459. Positions 48-110, 134-288, 704-789.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati52 – 9443SURP motif 1Add
BLAST
Repeati166 – 20843SURP motif 2Add
BLAST
Domaini707 – 79387Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 167Poly-Pro
Compositional biasi118 – 1225Poly-Gln
Compositional biasi260 – 2678Poly-Glu
Compositional biasi369 – 3724Poly-Pro
Compositional biasi557 – 5604Poly-Pro
Compositional biasi672 – 6754Poly-Pro

Domaini

SURP motif 2 mediates direct binding to SF3A3.

Sequence similaritiesi

Contains 2 SURP motif repeats.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG300902.
GeneTreeiENSGT00730000111077.
HOGENOMiHOG000238941.
HOVERGENiHBG059993.
InParanoidiQ15459.
KOiK12825.
OMAiVMQQQQT.
OrthoDBiEOG7JDQX9.
PhylomeDBiQ15459.
TreeFamiTF105705.

Family and domain databases

InterProiIPR022030. PRP21-like.
IPR000061. Surp.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF12230. PRP21_like_P. 1 hit.
PF01805. Surp. 2 hits.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00648. SWAP. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50128. SURP. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15459-1) [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
MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR
60 70 80 90 100
NIVDKTASFV ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE
110 120 130 140 150
FKEGKAQEPS AAIPKVMQQQ QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF
160 170 180 190 200
EFIADPPSIS AFDLDVVKLT AQFVARNGRQ FLTQLMQKEQ RNYQFDFLRP
210 220 230 240 250
QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL DQVCYRVEWA
260 270 280 290 300
KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
310 320 330 340 350
PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT
360 370 380 390 400
QVQDMDEGSD DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP
410 420 430 440 450
LPPAPAPDEY LVSPITGEKI PASKMQEHMR IGLLDPRWLE QRDRSIREKQ
460 470 480 490 500
SDDEVYAPGL DIESSLKQLA ERRTDIFGVE ETAIGKKIGE EEIQKPEEKV
510 520 530 540 550
TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD TKEKIGPSKP
560 570 580 590 600
NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP
610 620 630 640 650
PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT
660 670 680 690 700
AFVPAPPVAP VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR
710 720 730 740 750
NKGPVSIKVQ VPNMQDKTEW KLNGQVLVFT LPLTDQVSVI KVKIHEATGM
760 770 780 790
PAGKQKLQYE GIFIKDSNSL AYYNMANGAV IHLALKERGG RKK
Length:793
Mass (Da):88,886
Last modified:November 1, 1996 - v1
Checksum:i7259F1EC4577305C
GO
Isoform 2 (identifier: Q15459-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-170: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:728
Mass (Da):81,678
Checksum:i53E0FCDFB1CB4616
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti511 – 5111R → W in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036290

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei106 – 17065Missing in isoform 2. CuratedVSP_054090Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85237 mRNA. Translation: CAA59494.1.
CR456575 mRNA. Translation: CAG30461.1.
AC004997 Genomic DNA. Translation: AAC23435.1.
BC001976 mRNA. Translation: AAH01976.1.
BC007684 mRNA. Translation: AAH07684.1.
CCDSiCCDS13875.1. [Q15459-1]
PIRiS60735.
RefSeqiNP_005868.1. NM_005877.5. [Q15459-1]
UniGeneiHs.406277.
Hs.505597.

Genome annotation databases

EnsembliENST00000215793; ENSP00000215793; ENSG00000099995. [Q15459-1]
GeneIDi10291.
KEGGihsa:10291.
UCSCiuc003ahl.3. human. [Q15459-1]

Polymorphism databases

DMDMi2498882.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85237 mRNA. Translation: CAA59494.1 .
CR456575 mRNA. Translation: CAG30461.1 .
AC004997 Genomic DNA. Translation: AAC23435.1 .
BC001976 mRNA. Translation: AAH01976.1 .
BC007684 mRNA. Translation: AAH07684.1 .
CCDSi CCDS13875.1. [Q15459-1 ]
PIRi S60735.
RefSeqi NP_005868.1. NM_005877.5. [Q15459-1 ]
UniGenei Hs.406277.
Hs.505597.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZKH NMR - A 704-789 [» ]
2DT6 NMR - A 48-110 [» ]
2DT7 NMR - B 134-217 [» ]
ProteinModelPortali Q15459.
SMRi Q15459. Positions 48-110, 134-288, 704-789.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115580. 129 interactions.
DIPi DIP-29164N.
IntActi Q15459. 28 interactions.
MINTi MINT-144269.
STRINGi 9606.ENSP00000215793.

PTM databases

PhosphoSitei Q15459.

Polymorphism databases

DMDMi 2498882.

Proteomic databases

MaxQBi Q15459.
PaxDbi Q15459.
PeptideAtlasi Q15459.
PRIDEi Q15459.

Protocols and materials databases

DNASUi 10291.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215793 ; ENSP00000215793 ; ENSG00000099995 . [Q15459-1 ]
GeneIDi 10291.
KEGGi hsa:10291.
UCSCi uc003ahl.3. human. [Q15459-1 ]

Organism-specific databases

CTDi 10291.
GeneCardsi GC22M030727.
HGNCi HGNC:10765. SF3A1.
HPAi HPA000690.
HPA030083.
MIMi 605595. gene.
neXtProti NX_Q15459.
PharmGKBi PA35683.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300902.
GeneTreei ENSGT00730000111077.
HOGENOMi HOG000238941.
HOVERGENi HBG059993.
InParanoidi Q15459.
KOi K12825.
OMAi VMQQQQT.
OrthoDBi EOG7JDQX9.
PhylomeDBi Q15459.
TreeFami TF105705.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi SF3A1. human.
EvolutionaryTracei Q15459.
GeneWikii SF3A1.
GenomeRNAii 10291.
NextBioi 39000.
PMAP-CutDB Q15459.
PROi Q15459.
SOURCEi Search...

Gene expression databases

Bgeei Q15459.
CleanExi HS_SF3A1.
ExpressionAtlasi Q15459. baseline and differential.
Genevestigatori Q15459.

Family and domain databases

InterProi IPR022030. PRP21-like.
IPR000061. Surp.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF12230. PRP21_like_P. 1 hit.
PF01805. Surp. 2 hits.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00648. SWAP. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF109905. SSF109905. 2 hits.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50128. SURP. 2 hits.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian splicing factor SF3a120 represents a new member of the SURP family of proteins and is homologous to the essential splicing factor PRP21p of Saccharomyces cerevisiae."
    Kraemer A., Mulhauser F., Wersig C., Groning K., Bilbe G.
    RNA 1:260-272(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Cervix and Lymph.
  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. "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. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    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.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456 AND TYR-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-329 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-413 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "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].
  13. "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-320; SER-329; SER-359 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-329; SER-359; SER-413 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-320; SER-329 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Solution structure of a human ubiquitin-like domain in SF3A1."
    Structural genomics consortium (SGC)
    Submitted (JUN-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 704-789.
  19. "Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP."
    Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., Yokoyama S.
    Structure 14:1677-1689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 48-110 AND 134-217 IN COMPLEX WITH SF3A3, SUBUNIT, SURP MOTIFS, MUTAGENESIS OF GLU-48; LYS-55; PHE-162 AND LEU-169.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-511.

Entry informationi

Entry nameiSF3A1_HUMAN
AccessioniPrimary (citable) accession number: Q15459
Secondary accession number(s): E9PAW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 155 of the entry and version 1 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 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3