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Protein

Splicing factor 3A subunit 1

Gene

Sf3a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei169 – 1691Critical for binding to SF3A3By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. mRNA processing Source: MGI
  2. mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_260226. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3A subunit 1
Alternative name(s):
SF3a120
Gene namesi
Name:Sf3a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1914715. Sf3a1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: MGI
  2. nucleoplasm Source: MGI
  3. spliceosomal complex Source: MGI
  4. U2-type spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 791791Splicing factor 3A subunit 1PRO_0000114918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei320 – 3201PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei449 – 4491PhosphoserineBy similarity
Modified residuei454 – 4541PhosphotyrosineBy similarity
Modified residuei757 – 7571PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K4Z5.
PaxDbiQ8K4Z5.
PRIDEiQ8K4Z5.

PTM databases

PhosphoSiteiQ8K4Z5.

Expressioni

Gene expression databases

BgeeiQ8K4Z5.
CleanExiMM_SF3A1.
GenevestigatoriQ8K4Z5.

Interactioni

Subunit structurei

Identified in the spliceosome C complex (By similarity). 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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212207. 36 interactions.
IntActiQ8K4Z5. 37 interactions.
MINTiMINT-1868050.

Structurei

Secondary structure

1
791
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi685 – 6873Combined sources
Helixi692 – 6987Combined sources
Beta strandi703 – 7097Combined sources
Beta strandi713 – 7153Combined sources
Beta strandi721 – 7299Combined sources
Helixi736 – 74510Combined sources
Turni750 – 7523Combined sources
Beta strandi753 – 7575Combined sources
Beta strandi760 – 7623Combined sources
Helixi768 – 7714Combined sources
Beta strandi778 – 7836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WE7NMR-A685-786[»]
ProteinModelPortaliQ8K4Z5.
SMRiQ8K4Z5. Positions 48-110, 134-288, 685-788.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8K4Z5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati52 – 9443SURP motif 1Add
BLAST
Repeati166 – 20843SURP motif 2Add
BLAST
Domaini705 – 78884Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi10 – 145Poly-Pro
Compositional biasi118 – 1225Poly-Gln
Compositional biasi260 – 2678Poly-Glu
Compositional biasi367 – 3704Poly-Pro
Compositional biasi555 – 5584Poly-Pro
Compositional biasi670 – 6734Poly-Pro

Domaini

SURP motif 2 mediates direct binding to SF3A3.By similarity

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.
InParanoidiQ8K4Z5.
KOiK12825.
OMAiNEMPQPP.
OrthoDBiEOG7JDQX9.
PhylomeDBiQ8K4Z5.
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]

Sequencei

Sequence statusi: Complete.

Q8K4Z5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAGPVQAVP PPPPVATESK QPIEEEASSK EDPTPSKPVV GIIYPPPEVR
60 70 80 90 100
NIVDKTASFV ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE
110 120 130 140 150
FKEGKAQEPS AAIPKVMQQQ QQATQQQLPQ 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 EEDQEKAEET PSQLDQDTQV
360 370 380 390 400
QDMDEGSDDE EEGQKVPPPP ETPMPPPLPP TPDQVIVRKD YDPKASKPLP
410 420 430 440 450
PAPAPDEYLV SPITGEKIPA SKMQEHMRIG LLDPRWLEQR DRSIREKQSD
460 470 480 490 500
DEVYAPGLDI ESSLKQLAER RTDIFGVEET AIGKKIGEEE IQKPEEKVTW
510 520 530 540 550
DGHSGSMART QQAAQANITL QEQIEAIHKA KGLVPEDDTK EKIGPSKPNE
560 570 580 590 600
IPQQPPPPSS ATNIPSSAPP ITSVPRPPAM PPPVRTTVVS AVPVMPRPPM
610 620 630 640 650
ASVVRLPPGS VIAPMPPIIH APRINVVPMP PAAPPIMAPR PPPMIVPTAF
660 670 680 690 700
VPAPPVAPVP APAPMPPVHP PPPMEDEPPS KKLKTEDSLM PEEEFLRRNK
710 720 730 740 750
GPVSIKVQVP NMQDKTEWKL NGQGLVFTLP LTDQVSVIKV KIHEATGMPA
760 770 780 790
GKQKLQYEGI FIKDSNSLAY YNMASGAVIH LALKERGGRK K
Length:791
Mass (Da):88,545
Last modified:October 1, 2002 - v1
Checksum:iD83D0432469C3708
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571R → G in BAC26142 (PubMed:16141072).Curated
Sequence conflicti368 – 3681P → L in BAC26294 (PubMed:16141072).Curated
Sequence conflicti708 – 7081Q → L in BAC26853 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028829 mRNA. Translation: BAC26142.1.
AK029095 mRNA. Translation: BAC26294.1.
AK030223 mRNA. Translation: BAC26853.1.
AL807825 Genomic DNA. Translation: CAI25745.1.
BC010727 mRNA. Translation: AAH10727.1.
BC029753 mRNA. Translation: AAH29753.1.
CCDSiCCDS24380.1.
RefSeqiNP_080451.4. NM_026175.5.
UniGeneiMm.156914.

Genome annotation databases

EnsembliENSMUST00000002198; ENSMUSP00000002198; ENSMUSG00000002129.
GeneIDi67465.
KEGGimmu:67465.
UCSCiuc007hup.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK028829 mRNA. Translation: BAC26142.1.
AK029095 mRNA. Translation: BAC26294.1.
AK030223 mRNA. Translation: BAC26853.1.
AL807825 Genomic DNA. Translation: CAI25745.1.
BC010727 mRNA. Translation: AAH10727.1.
BC029753 mRNA. Translation: AAH29753.1.
CCDSiCCDS24380.1.
RefSeqiNP_080451.4. NM_026175.5.
UniGeneiMm.156914.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WE7NMR-A685-786[»]
ProteinModelPortaliQ8K4Z5.
SMRiQ8K4Z5. Positions 48-110, 134-288, 685-788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212207. 36 interactions.
IntActiQ8K4Z5. 37 interactions.
MINTiMINT-1868050.

PTM databases

PhosphoSiteiQ8K4Z5.

Proteomic databases

MaxQBiQ8K4Z5.
PaxDbiQ8K4Z5.
PRIDEiQ8K4Z5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002198; ENSMUSP00000002198; ENSMUSG00000002129.
GeneIDi67465.
KEGGimmu:67465.
UCSCiuc007hup.2. mouse.

Organism-specific databases

CTDi10291.
MGIiMGI:1914715. Sf3a1.

Phylogenomic databases

eggNOGiNOG300902.
GeneTreeiENSGT00730000111077.
HOGENOMiHOG000238941.
HOVERGENiHBG059993.
InParanoidiQ8K4Z5.
KOiK12825.
OMAiNEMPQPP.
OrthoDBiEOG7JDQX9.
PhylomeDBiQ8K4Z5.
TreeFamiTF105705.

Enzyme and pathway databases

ReactomeiREACT_260226. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSf3a1. mouse.
EvolutionaryTraceiQ8K4Z5.
NextBioi324654.
PROiQ8K4Z5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4Z5.
CleanExiMM_SF3A1.
GenevestigatoriQ8K4Z5.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary gland and Mammary tumor.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 238-246; 471-484 AND 755-763, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "Solution structure of ubiquitin-like domain in Sf3a120."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 685-786.

Entry informationi

Entry nameiSF3A1_MOUSE
AccessioniPrimary (citable) accession number: Q8K4Z5
Secondary accession number(s): Q8C0M7
, Q8C128, Q8C175, Q921T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2002
Last modified: March 4, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.