Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q12872 (SFSWA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor, suppressor of white-apricot homolog
Alternative name(s):
Splicing factor, arginine/serine-rich 8
Suppressor of white apricot protein homolog
Gene names
Name:SFSWAP
Synonyms:SFRS8, SWAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length951 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role as an alternative splicing regulator. Regulate its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10. Ref.5

Subcellular location

Nucleus Potential.

Sequence similarities

Contains 2 SURP motif repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12872-1)

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.
Isoform 2 (identifier: Q12872-2)

The sequence of this isoform differs from the canonical sequence as follows:
     801-801: R → RSRVTASPGTLRAEPCQSSASVTAAAEPGSYQAASTTTRFDSASSFEGKPGKT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 951951Splicing factor, suppressor of white-apricot homolog
PRO_0000081934

Regions

Repeat211 – 25343SURP motif 1
Repeat459 – 49941SURP motif 2
Compositional bias165 – 1684Poly-Glu
Compositional bias287 – 2904Poly-Asp
Compositional bias382 – 3854Poly-Pro
Compositional bias413 – 4164Poly-Pro
Compositional bias420 – 4245Poly-Pro
Compositional bias434 – 4407Poly-Thr
Compositional bias451 – 4544Poly-Pro
Compositional bias616 – 6194Poly-Ser
Compositional bias660 – 6634Poly-Ala
Compositional bias754 – 76310Poly-Lys
Compositional bias789 – 951163Arg/Ser-rich (RS domain)
Compositional bias850 – 8534Poly-Lys

Amino acid modifications

Modified residue2831Phosphoserine Ref.8 Ref.10
Modified residue3151N6-acetyllysine Ref.11
Modified residue6041Phosphoserine Ref.8 Ref.12 Ref.13
Modified residue6421Phosphothreonine Ref.7
Modified residue9091Phosphoserine Ref.8 Ref.10

Natural variations

Alternative sequence8011R → RSRVTASPGTLRAEPCQSSA SVTAAAEPGSYQAASTTTRF DSASSFEGKPGKT in isoform 2.
VSP_044786
Natural variant521L → Q. Ref.1
Corresponds to variant rs1051207 [ dbSNP | Ensembl ].
VAR_046442
Natural variant1221L → F.
Corresponds to variant rs1051314 [ dbSNP | Ensembl ].
VAR_046443
Natural variant1361L → F. Ref.1
Corresponds to variant rs1131564 [ dbSNP | Ensembl ].
VAR_046444
Natural variant4211L → P. Ref.1 Ref.3 Ref.4
Corresponds to variant rs1982528 [ dbSNP | Ensembl ].
VAR_021789
Natural variant5121G → S.
Corresponds to variant rs34541796 [ dbSNP | Ensembl ].
VAR_057248
Natural variant5381E → G.
Corresponds to variant rs34744641 [ dbSNP | Ensembl ].
VAR_057249
Natural variant8871A → E.
Corresponds to variant rs34729193 [ dbSNP | Ensembl ].
VAR_057250

Experimental info

Sequence conflict2361R → P in AAA19604. Ref.1
Sequence conflict4931H → Y in AAA19604. Ref.1

Secondary structure

........................ 951
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 23, 2010. Version 3.
Checksum: A942D589F4B6BF47

FASTA951104,822
        10         20         30         40         50         60 
MYGASGGRAK PERKSGAKEE AGPGGAGGGG SRVELLVFGY ACKLFRDDER ALAQEQGQHL 

        70         80         90        100        110        120 
IPWMGDHKIL IDRYDGRGHL HDLSEYDAEY STWNRDYQLS EEEARIEALC DEERYLALHT 

       130        140        150        160        170        180 
DLLEEEARQE EEYKRLSEAL AEDGSYNAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN 

       190        200        210        220        230        240 
LEENEEPFVA PLGLSVPSDV ELPPTAKMHA IIERTASFVC RQGAQFEIML KAKQARNSQF 

       250        260        270        280        290        300 
DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE NKSDEKKKSG VSSDNEDDDD EEDGNYLHPS 

       310        320        330        340        350        360 
LFASKKCNRL EELMKPLKVV DPDHPLAALV RKAQADSSTP TPHNADGAPV QPSQVEYTAD 

       370        380        390        400        410        420 
STVAAMYYSY YMLPDGTYCL APPPPGIDVT TYYSTLPAGV TVSNSPGVTT TAPPPPGTTP 

       430        440        450        460        470        480 
LPPPTTAETS SGATSTTTTT SALAPVAAII PPPPDVQPVI DKLAEYVARN GLKFETSVRA 

       490        500        510        520        530        540 
KNDQRFEFLQ PWHQYNAYYE FKKQFFLQKE GGDSMQAVSA PEEAPTDSAP EKPSDAGEDG 

       550        560        570        580        590        600 
APEDAAEVGA RAGSGGKKEA SSSKTVPDGK LVKASFAPIS FAIKAKENDL LPLEKNRVKL 

       610        620        630        640        650        660 
DDDSDDDEES KEGQESSSSA ANTNPAVAPP CVVVEEKKPQ LTQEELEAKQ AKQKLEDRLA 

       670        680        690        700        710        720 
AAAREKLAQA SKESKEKQLQ AERKRKAALF LQTLKNPLPE AEAGKIEESP FSVEESSTTP 

       730        740        750        760        770        780 
CPLLTGGRPL PTLEVKPPDR PSSKSKDPPR EEEKEKKKKK HKKRSRTRSR SPKYHSSSKS 

       790        800        810        820        830        840 
RSRSHSKAKH SLPSAYRTVR RSRSRSRSPR RRAHSPERRR EERSVPTAYR VSRSPGASRK 

       850        860        870        880        890        900 
RTRSRSPHEK KKKRRSRSRT KSKARSQSVS PSKQAAPRPA APAAHSAHSA SVSPVESRGS 

       910        920        930        940        950 
SQERSRGVSQ EKEAQISSAI VSSVQSKITQ DLMAKVRAML AASKNLQTSA S 

« Hide

Isoform 2 [UniParc].

Checksum: C67AFFE577FF7CA4
Show »

FASTA1,003110,012

References

« Hide 'large scale' references
[1]"Conservation of regulated alternative splicing and identification of functional domains in vertebrate homologs to the Drosophila splicing regulator, suppressor-of-white-apricot."
Denhez F., Lafyatis R.
J. Biol. Chem. 269:16170-16179(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-52; PHE-136 AND PRO-421.
Tissue: Placenta.
[2]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-421.
[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] (ISOFORMS 1 AND 2), VARIANT PRO-421.
Tissue: Brain and Skin.
[5]"The mammalian homolog of suppressor-of-white-apricot regulates alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS."
Sarkissian M., Winne A., Lafyatis R.
J. Biol. Chem. 271:31106-31114(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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 THR-642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"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-283; SER-604 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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].
[10]"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-283 AND SER-909, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Solution structure of the SURP1 and SURP2 domain in splicing factor, arginine/serine-rich 8."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 189-282 AND 434-522.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08377 mRNA. Translation: AAA19604.1.
AC117500 Genomic DNA. No translation available.
AC131009 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98526.1.
BC008707 mRNA. Translation: AAH08707.1.
BC015953 mRNA. Translation: AAH15953.1.
BC136678 mRNA. Translation: AAI36679.1.
BC144364 mRNA. Translation: AAI44365.1.
PIRA54037.
B54037.
C54037.
RefSeqNP_001248340.1. NM_001261411.1.
NP_004583.2. NM_004592.3.
UniGeneHs.308171.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ZNMR-A434-522[»]
2E60NMR-A189-282[»]
ProteinModelPortalQ12872.
SMRQ12872. Positions 189-282, 455-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112331. 2 interactions.
IntActQ12872. 2 interactions.
STRING9606.ENSP00000261674.

PTM databases

PhosphoSiteQ12872.

Polymorphism databases

DMDM292495067.

Proteomic databases

PaxDbQ12872.
PRIDEQ12872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261674; ENSP00000261674; ENSG00000061936. [Q12872-1]
ENST00000541286; ENSP00000437738; ENSG00000061936. [Q12872-2]
GeneID6433.
KEGGhsa:6433.
UCSCuc001uja.2. human. [Q12872-1]

Organism-specific databases

CTD6433.
GeneCardsGC12P132196.
H-InvDBHIX0036782.
HGNCHGNC:10790. SFSWAP.
HPAHPA039362.
HPA040063.
MIM601945. gene.
neXtProtNX_Q12872.
PharmGKBPA35706.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289028.
HOVERGENHBG079184.
InParanoidQ12872.
OMAMYYSYYM.
OrthoDBEOG786H2Z.
PhylomeDBQ12872.
TreeFamTF106264.

Gene expression databases

ArrayExpressQ12872.
BgeeQ12872.
CleanExHS_SFRS8.
GenevestigatorQ12872.

Family and domain databases

InterProIPR000061. Surp.
IPR019147. SWAP_N_domain.
[Graphical view]
PfamPF09750. DRY_EERY. 1 hit.
PF01805. Surp. 2 hits.
[Graphical view]
SMARTSM00648. SWAP. 2 hits.
[Graphical view]
SUPFAMSSF109905. SSF109905. 2 hits.
PROSITEPS50128. SURP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSFSWAP. human.
EvolutionaryTraceQ12872.
GenomeRNAi6433.
NextBio24987.
PROQ12872.
SOURCESearch...

Entry information

Entry nameSFSWA_HUMAN
AccessionPrimary (citable) accession number: Q12872
Secondary accession number(s): B2RN45 expand/collapse secondary AC list , B7ZM97, F5H6B8, Q6PJF7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 123 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM