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UniProtKB/Swiss-Prot entry Q15637


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SF01_HUMAN
Primary accession number Q15637
Secondary accession numbers Q14818 Q14819 Q15913 Q8IY00 Q92744 Q92745 Q969H7 Q9BW01 Q9UEI0
Integrated into Swiss-Prot on November 7, 2003
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 89)
Name and origin of the protein
Protein name Splicing factor 1
Synonyms Zinc finger protein 162
Transcription factor ZFM1
Zinc finger gene in MEN1 locus
Mammalian branch point-binding protein mBBP
BBP
Gene name
Name: SF1
Synonyms: ZFM1, ZNF162
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 20-30 AND 136-150, VARIANT THR-357, FUNCTION, INTERACTION WITH U1 SNRNA, AND RNA-BINDING.
TISSUE=Bone, and Cervix carcinoma;
PubMed=8752089 [NCBI, ExPASy, EBI, Israel, Japan]
Arning S., Grueter P., Bilbe G., Kraemer A.;
"Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA.";
RNA 2:794-810(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6).
TISSUE=Myeloid leukemia cell;
DOI=10.1006/geno.1997.4705; PubMed=9192847 [NCBI, ExPASy, EBI, Israel, Japan]
Caslini C., Spinelli O., Cazzaniga G., Golay J., De Gioia L., Pedretti A., Breviario F., Amaru R., Barbui T., Biondi A., Introna M., Rambaldi A.;
"Identification of two novel isoforms of the ZNF162 gene: a growing family of signal transduction and activator of RNA proteins.";
Genomics 42:268-277(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
TISSUE=Brain cortex, Cerebellum, and Fetal liver;
DOI=10.1093/hmg/3.3.465; PubMed=7912130 [NCBI, ExPASy, EBI, Israel, Japan]
Toda T., Iida A., Miwa T., Nakamura Y., Imai T.;
"Isolation and characterization of a novel gene encoding nuclear protein at a locus (D11S636) tightly linked to multiple endocrine neoplasia type 1 (MEN1).";
Hum. Mol. Genet. 3:465-470(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
TISSUE=Brain, Eye, Kidney, Muscle, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
DOI=10.1016/S0378-1119(98)00058-4; PubMed=9573336 [NCBI, ExPASy, EBI, Israel, Japan]
Kraemer A., Quentin M., Mulhauser F.;
"Diverse modes of alternative splicing of human splicing factor SF1 deduced from the exon-intron structure of the gene.";
Gene 211:29-37(1998).
[6]
PROTEIN SEQUENCE OF 2-15, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION, INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, AND PHOSPHORYLATION AT SER-20.
DOI=10.1093/emboj/18.16.4549; PubMed=10449420 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J.;
"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly.";
EMBO J. 18:4549-4559(1999).
[8]
PROTEIN SEQUENCE OF 110-135, MASS SPECTROMETRY, AND INTERACTION WITH THE SPLICEOSOME.
DOI=10.1101/gr.473902; PubMed=12176931 [NCBI, ExPASy, EBI, Israel, Japan]
Rappsilber J., Ryder U., Lamond A.I., Mann M.;
"Large-scale proteomic analysis of the human spliceosome.";
Genome Res. 12:1231-1245(2002).
[9]
FUNCTION, AND INTERACTION WITH EWSR1; FUS AND TAF15.
DOI=10.1074/jbc.273.29.18086; PubMed=9660765 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang D., Paley A.J., Childs G.;
"The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription.";
J. Biol. Chem. 273:18086-18091(1998).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.";
Electrophoresis 28:2027-2034(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-80; SER-82 AND TYR-87, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
STRUCTURE BY NMR OF 133-255 IN COMPLEX WITH THE BRANCH SITE SEQUENCE 5'-UAUACUAACAA-3', AND MUTAGENESIS OF ASN-151; ARG-160; LYS-184; LEU-244; LEU-247; LEU-254 AND ARG-255.
DOI=10.1126/science.1064719; PubMed=11691992 [NCBI, ExPASy, EBI, Israel, Japan]
Liu Z., Luyten I., Bottomley M.J., Messias A.C., Houngninou-Molango S., Sprangers R., Zanier K., Kraemer A., Sattler M.;
"Structural basis for recognition of the intron branch site RNA by splicing factor 1.";
Science 294:1098-1102(2001).
[17]
STRUCTURE BY NMR OF 13-25 IN COMPLEX WITH U2AF2, AND MUTAGENESIS OF 16-LYS--ARG-18; 17-LYS-LYS-18; ARG-21 AND TRP-22.
DOI=10.1016/S1097-2765(03)00115-1; PubMed=12718882 [NCBI, ExPASy, EBI, Israel, Japan]
Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M.;
"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP.";
Mol. Cell 11:965-976(2003).
Comments
  • FUNCTION: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor.
  • SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS and TAF15.
  • INTERACTION:
    P03120:E2 (xeno); NbExp=2; IntAct=EBI-744603, EBI-1779322;
  • SUBCELLULAR LOCATION: Nucleus.
  • ALTERNATIVE PRODUCTS: 6 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    Name1
    SynonymsSF1-HL1
    Isoform IDQ15637-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsSF1-Bo, Bone
    Isoform IDQ15637-2
    Features which should be applied to build the isoform sequence: VSP_008839.
    Name3
    SynonymsZFM1-A, ZFM1-ABCDEF
    Isoform IDQ15637-3
    Features which should be applied to build the isoform sequence: VSP_008838.
    Name4
    SynonymsZFM1-B, ZFM1-ABCDF
    Isoform IDQ15637-4
    Features which should be applied to build the isoform sequence: VSP_008835, VSP_008836.
    Name5
    Isoform IDQ15637-5
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_008833, VSP_008835.
    Name6
    SynonymsZFM1-D, B6
    Isoform IDQ15637-6
    Note: Phosphorylated on Ser-463.
    Features which should be applied to build the isoform sequence: VSP_008834, VSP_008837.
  • TISSUE SPECIFICITY: Detected in lung, ovary, adrenal gland, colon, kidney, muscle, pancreas, thyroid, placenta, brain, liver and heart.
  • PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly. Isoform 6 is phosphorylated on Ser-463.
  • SIMILARITY: Contains 1 CCHC-type zinc finger.
  • SIMILARITY: Contains 1 KH domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y08765; CAA70018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y08766; CAA70019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L49345; AAB03514.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L49380; AAB04033.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26120; BAA05116.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26120; BAA05117.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000773; AAH00773.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008080; AAH08080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008724; AAH08724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011657; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC020217; AAH20217.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC038446; AAH38446.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000051; CAA03883.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000052; CAA03883.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G02919; G02919.
RefSeq NP_004621.2; -.
NP_973724.1; -.
NP_973727.1; -.
UniGene Hs.502829
3D structure databases
PDB
1K1G; NMR; -; A=133-260.[ExPASy / RCSB / EBI]
PDBsum 1K1G; -.
ModBase Q15637.
Protein-protein interaction databases
IntAct Q15637; -.
Organism-specific databases
HGNC HGNC:12950; SF1.
GenAtlas SF1.
MIM 601516; gene. [NCBI / EBI]
PharmGKB PA26841; -.
GeneCards Q15637.
Gene expression databases
ArrayExpress Q15637; -.
CleanEx HS_SF1; -.
GermOnline ENSG00000168066; Homo sapiens.
Ontologies
GO
GO:0005840; Cellular component: ribosome (non-traceable author statement from UniProtKB).
GO:0005681; Cellular component: spliceosome (inferred from direct assay from HGNC).
GO:0003723; Molecular function: RNA binding (traceable author statement from UniProtKB).
GO:0003702; Molecular function: RNA polymerase II transcription factor activity (traceable author statement from ProtInc).
GO:0003714; Molecular function: transcription corepressor activity (traceable author statement from ProtInc).
GO:0000389; Biological process: nuclear mRNA 3'-splice site recognition (traceable author statement from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR004087; KH.
IPR004088; KH_type_1.
IPR001878; Znf_CCHC.
Graphical view of domain structure.
Pfam PF00013; KH_1; 1.
PF00098; zf-CCHC; 1.
Pfam graphical view of domain structure.
SMART SM00322; KH; 1.
SM00343; ZnF_C2HC; 1.
SMART graphical view of domain structure.
PROSITE PS50084; KH_TYPE_1; 1.
PS50158; ZF_CCHC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q15637.
Genome annotation databases
Ensembl ENSG00000168066; Homo sapiens. [Contig view]
GeneID 7536; -.
KEGG hsa:7536; -.
Phylogenomic databases
HOVERGEN Q15637; -.
Other
SOURCE SF1; Homo sapiens.
ProtoNet Q15637.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Repressor; RNA-binding; Spliceosome; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   639  638     Splicing factor 1. PRO_0000050129
DOMAIN   141   222  82     KH. 
ZN_FING   277   296  20     CCHC-type. 
MOTIF   15    19  5     Nuclear localization signal (Potential). 
COMPBIAS   324   637  314     Pro-rich. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   20    20        Phosphoserine; by PKG. 
MOD_RES   80    80        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   87    87        Phosphotyrosine. 
VAR_SEQ   10    10        L -> LGKLGPPGLPPLPGPKGGFEPGPPPAPGPGAGLLAPGPPP PPPVGSMGALTAAFPFAALPPPPPPPPPPPPQQPPPPPPP PSPGASYPPPQPPPPPPLYQRVSPPQPPPPQPPRKDQQPG PAGGGG (in isoform 5). VSP_008833
VAR_SEQ   448   548        DQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSG QPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQ NTTTTTTSAGTGSIPPWQQQQ -> GKSVPGKYACGLWGLSPASRKRYDAATTYGHDA (in isoform 6). VSP_008834
VAR_SEQ   528   548        NTTTTTTSAGTGSIPPWQQQQ -> RSLPAAAMARAMRVRTFRAHW (in isoform 4 and isoform 5). VSP_008835
VAR_SEQ   549   639        Missing (in isoform 4). VSP_008836
VAR_SEQ   555   639        PGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAG MMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPP PPPQN -> QWAAPTPSLWSSSPMATTAAAASATPSAQQQYGFQYPLAM AAKIPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGW FGKAA (in isoform 6). VSP_008837
VAR_SEQ   587   639        PPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPF GMPPAPPPPPPQN -> RSIECLLCLLSLLTQLPLPLPKPGRQDPSPRRRWPEP (in isoform 3). VSP_008838
VAR_SEQ   597   639        YAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPP PPPQN -> IPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGW FGKAA (in isoform 2). VSP_008839
VARIANT   357   357  1     S -> T. VAR_017196 
MUTAGEN   15    17        KKR->EED: Abolishes interaction with U2AF2. 
MUTAGEN   16    18        KRK->EDE: Abolishes interaction with U2AF2. 
MUTAGEN   20    20        S->A: Strongly decreases interaction with U2AF2 and spliceosome assembly. 
MUTAGEN   20    20        S->T: Decreases interaction with U2AF2. 
MUTAGEN   21    21        R->A: Decreases interaction with U2AF2 and spliceosome assembly. 
MUTAGEN   21    21        R->K: No effect. 
MUTAGEN   22    22        W->A: Abolishes interaction with U2AF2. 
MUTAGEN   22    22        W->F: No effect. 
MUTAGEN   151   151        N->A: Decreases RNA-binding. 
MUTAGEN   160   160        R->A: Strongly reduces RNA-binding. 
MUTAGEN   184   184        K->A: Abolishes RNA-binding. 
MUTAGEN   244   244        L->A: Decreases RNA-binding. 
MUTAGEN   247   247        L->A: Decreases RNA-binding. 
MUTAGEN   254   254        L->A: Slightly decreases RNA-binding. 
MUTAGEN   255   255        R->A: Slightly decreases RNA-binding. 
CONFLICT   269   269        E -> G (in Ref. 3; BAA05116/BAA05117). 
CONFLICT   348   348        A -> R (in Ref. 2; AAB03514/AAB04033). 
CONFLICT   377   377        R -> W (in Ref. 3; BAA05116/BAA05117). 
CONFLICT   591   591        G -> V (in Ref. 2; AAB04033). 
CONFLICT   623   623        M -> I (in Ref. 2; AAB04033). 
STRAND   136   141  6      
TURN   144   146  3      
HELIX   150   157  8      
STRAND   159   161  3      
HELIX   162   170  9      
STRAND   174   190  17      
STRAND   203   211  9      
HELIX   212   226  15      
TURN   227   230  4      
HELIX   238   244  7      
HELIX   245   248  4      
TURN   249   252  4      
Sequence information
Length: 639 AA [This is the length of the unprocessed precursor] Molecular weight: 68330 Da [This is the MW of the unprocessed precursor] CRC64: EEBC6A02B29DAE4D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 

        70         80         90        100        110        120 
LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 

       130        140        150        160        170        180 
PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 

       190        200        210        220        230        240 
GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 

       250        260        270        280        290        300 
KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 

       310        320        330        340        350        360 
QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 

       370        380        390        400        410        420 
TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 

       430        440        450        460        470        480 
PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP 

       490        500        510        520        530        540 
PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS 

       550        560        570        580        590        600 
IPPWQQQQAA AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPPPPP GSAGMMYAPP 

       610        620        630 
PPPPPPMDPS NFVTMMGMGV AGMPPFGMPP APPPPPPQN 

Q15637 in FASTA format

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