ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P20936


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name RASA1_HUMAN
Primary accession number P20936
Secondary accession number B2R6W3
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 121)
Name and origin of the protein
Protein name Ras GTPase-activating protein 1
Synonyms RasGAP
GTPase-activating protein
GAP
Ras p21 protein activator
p120GAP
Gene name
Name: RASA1
Synonyms: RASA
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).
TISSUE=Placenta;
DOI=10.1126/science.3201259; PubMed=3201259 [NCBI, ExPASy, EBI, Israel, Japan]
Trahey M., Wong G., Halenbeck R., Rubinfeld B., Martin G.A., Ladner M., Long C.M., Crosier W.J., Watt K., Koths K., McCormick F.;
"Molecular cloning of two types of GAP complementary DNA from human placenta.";
Science 242:1697-1700(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[4]
PROTEIN SEQUENCE OF 294-303; 326-334; 392-398; 439-457; 458-466; 479-483; 777-790 AND 821-825.
PubMed=8360177 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Zhang G., Mollat P., Carles C., Riva M., Frobert Y., Malassine A., Rostene W., Thang D.C., Beltchev B., Tavitian A., Thane M.N.;
"Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein.";
J. Biol. Chem. 268:18875-18881(1993).
[5]
PROTEIN SEQUENCE OF 1-7 (ISOFORM 2).
PubMed=2123878 [NCBI, ExPASy, EBI, Israel, Japan]
Halenbeck R., Crosier W.J., Clark R., McCormick F., Koths K.;
"Purification, characterization, and western blot analysis of human GTPase-activating protein from native and recombinant sources.";
J. Biol. Chem. 265:21922-21928(1990).
[6]
INTERACTION WITH SQSTM1.
DOI=10.1073/pnas.92.26.12338; PubMed=8618896 [NCBI, ExPASy, EBI, Israel, Japan]
Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.;
"Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region.";
Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[10]
STRUCTURE BY NMR OF 275-350.
PubMed=8137811 [NCBI, ExPASy, EBI, Israel, Japan]
Yang Y.S., Garbay C., Duschesne M., Cornille F., Jullian N., Fromage N., Tocque B., Roques B.P.;
"Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.";
EMBO J. 13:1270-1279(1994).
[11]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 714-1047.
DOI=10.1038/384591a0; PubMed=8955277 [NCBI, ExPASy, EBI, Israel, Japan]
Scheffzek K., Lautwein A., Kabsch W., Reza Ahmadian M., Wittinghofer A.;
"Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras.";
Nature 384:591-596(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 714-1047 IN COMPLEX WITH RAS.
DOI=10.1126/science.277.5324.333; PubMed=9219684 [NCBI, ExPASy, EBI, Israel, Japan]
Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A.;
"The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants.";
Science 277:333-338(1997).
[13]
STRUCTURE BY NMR OF 282-446.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SH3 domain and of the second SH2 domain of human RAS GTPase-activating protein 1.";
Submitted (MAY-2007) to the PDB data bank.
[14]
VARIANTS LEU-398; GLU-400 AND VAL-401.
DOI=10.1038/ng1193-242; PubMed=8275088 [NCBI, ExPASy, EBI, Israel, Japan]
Friedman E., Gejman P.V., Martin G.A., McCormick F.;
"Nonsense mutations in the C-terminal SH2 region of the GTPase activating protein (GAP) gene in human tumours.";
Nat. Genet. 5:242-247(1993).
[15]
VARIANT CMAVM TYR-540.
DOI=10.1086/379793; PubMed=14639529 [NCBI, ExPASy, EBI, Israel, Japan]
Eerola I., Boon L.M., Mulliken J.B., Burrows P.E., Dompmartin A., Watanabe S., Vanwijck R., Vikkula M.;
"Capillary malformation-arteriovenous malformation, a new clinical and genetic disorder caused by RASA1 mutations.";
Am. J. Hum. Genet. 73:1240-1249(2003).
[16]
INTERACTION WITH SPSB1.
DOI=10.1074/jbc.M413897200; PubMed=15713673 [NCBI, ExPASy, EBI, Israel, Japan]
Wang D., Li Z., Messing E.M., Wu G.;
"The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway.";
J. Biol. Chem. 280:16393-16401(2005).
Comments
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
M23379; AAA52517.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M23612; AAA35865.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312739; BAG35610.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033015; AAH33015.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00026262; -.
IPI00220356; -.
PIR A40121; A40121.
B40121; B40121.
RefSeq NP_002881.1; -.
NP_072179.1; -.
UniGene Hs.664080
3D structure databases
PDB
1WER; X-ray; 1.60 A; A=714-1047.[ExPASy / RCSB / EBI]
1WQ1; X-ray; 2.50 A; G=714-1047.[ExPASy / RCSB / EBI]
2GQI; NMR; -; A=282-339.[ExPASy / RCSB / EBI]
2GSB; NMR; -; A=341-446.[ExPASy / RCSB / EBI]
2J05; X-ray; 1.50 A; A/B=281-341.[ExPASy / RCSB / EBI]
2J06; X-ray; 1.80 A; A/B=281-341.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WER; -.
1WQ1; -.
2GQI; -.
2GSB; -.
2J05; -.
2J06; -.
SMR P20936; 340-446.
ModBase P20936.
Protein-protein interaction databases
DIP DIP:144N; -.
IntAct P20936; 2.
PTM databases
PhosphoSite P20936; -.
Enzyme and pathway databases
Pathway_Interaction_DB angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
aurora_a_pathway; Aurora A signaling.
aurora_b_pathway; Aurora B signaling.
bcr_5pathway; BCR signaling pathway.
ephbfwdpathway; EPHB forward signaling.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
il2_1pathway; IL2-mediated signaling events.
insulin_pathway; Insulin Pathway.
trkrpathway; Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway; PDGFR-beta signaling pathway.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
syndecan_2_pathway; Syndecan-2-mediated signaling events.
vegfr1_pathway; VEGFR1 specific signals.
Organism-specific databases
GeneCards GC05P086599; -.
H-InvDB HIX0005015; -.
HGNC HGNC:9871; RASA1.
GenAtlas RASA1.
HPA CAB007789; -.
MIM 139150; gene. [NCBI / EBI]
608354; phenotype. [NCBI / EBI]
608355; phenotype. [NCBI / EBI]
Orphanet 2346; Angio-osteohypertrophic syndrome.
137667; Capillary malformation-arteriovenous malformation.
PharmGKB PA34232; -.
Gene expression databases
ArrayExpress P20936; -.
Bgee P20936; -.
CleanEx HS_RASA1; -.
GermOnline ENSG00000145715; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (non-traceable author statement from UniProtKB).
GO:0001948; Molecular function: glycoprotein binding (inferred from physical interaction from UniProtKB).
GO:0051020; Molecular function: GTPase binding (inferred from physical interaction from UniProtKB).
GO:0019870; Molecular function: potassium channel inhibitor activity (non-traceable author statement from UniProtKB).
GO:0005099; Molecular function: Ras GTPase activator activity (traceable author statement from ProtInc).
GO:0005102; Molecular function: receptor binding (inferred from physical interaction from UniProtKB).
GO:0000910; Biological process: cytokinesis (inferred from sequence or structural similarity from UniProtKB).
GO:0009790; Biological process: embryonic development (inferred from sequence or structural similarity from UniProtKB).
GO:0007242; Biological process: intracellular signaling cascade (non-traceable author statement from UniProtKB).
GO:0001953; Biological process: negative regulation of cell-matrix adhesion (inferred from direct assay from UniProtKB).
GO:0043524; Biological process: negative regulation of neuron apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0045768; Biological process: positive regulation of anti-apoptosis (inferred from direct assay from UniProtKB).
GO:0030833; Biological process: regulation of actin filament polymerization (inferred from direct assay from UniProtKB).
GO:0008360; Biological process: regulation of cell shape (non-traceable author statement from UniProtKB).
GO:0051252; Biological process: regulation of RNA metabolic process (non-traceable author statement from UniProtKB).
GO:0051056; Biological process: regulation of small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
GO:0001570; Biological process: vasculogenesis (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR018029; C2_membr_targeting.
IPR011993; PH_type.
IPR001849; Pleckstrin_homology.
IPR001936; RasGAP.
IPR000980; SH2.
IPR001452; SH3_domain.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
G3DSA:3.30.505.10; SH2; 2.
Pfam PF00168; C2; 1.
PF00169; PH; 1.
PF00616; RasGAP; 1.
PF00017; SH2; 2.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
ProDom PD000093; SH2; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00239; C2; 1.
SM00233; PH; 1.
SM00323; RasGAP; 1.
SM00252; SH2; 2.
SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS50004; C2; 1.
PS50003; PH_DOMAIN; 1.
PS00509; RAS_GTPASE_ACTIV_1; 1.
PS50018; RAS_GTPASE_ACTIV_2; 1.
PS50001; SH2; 2.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P20936; -.
Genome annotation databases
Ensembl ENSG00000145715; Homo sapiens. [Contig view]
GeneID 5921; -.
KEGG hsa:5921; -.
Phylogenomic databases
HOGENOM P20936; -.
HOVERGEN P20936; -.
OMA P20936; VLNDTVD.
Other
NextBio 23056; -.
PMAP-CutDB P20936; -.
SOURCE RASA1; Homo sapiens.
ProtoNet P20936.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing; Disease mutation; GTPase activation; Phosphoprotein; Proto-oncogene; Repeat; SH2 domain; SH3 domain.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1047  1047     Ras GTPase-activating protein 1. PRO_0000056636
DOMAIN   181    272  92     SH2 1. 
DOMAIN   279    341  63     SH3. 
DOMAIN   351    441  91     SH2 2. 
DOMAIN   474    577  104     PH. 
DOMAIN   581    676  96     C2. 
DOMAIN   748    942  195     Ras-GAP. 
COMPBIAS   17     22  6     Poly-Gly. 
COMPBIAS   135    141  7     Poly-Pro. 
COMPBIAS   163    168  6     Poly-Glu. 
MOD_RES   615    615        Phosphotyrosine. 
VAR_SEQ   1    177        Missing (in isoform 2). VSP_001625
VAR_SEQ   178    180        TNQ -> MKG (in isoform 2). VSP_001626
VARIANT   398    398  1     R -> L (in basal cell carcinomas). VAR_002650 
VARIANT   400    400  1     K -> E (in basal cell carcinomas). VAR_002651 
VARIANT   401    401  1     I -> V (in basal cell carcinomas). VAR_002652 
VARIANT   540    540  1     C -> Y (in CMAVM). VAR_017744 
CONFLICT   789    789        R -> A (in Ref. 4; AA sequence). 
STRAND   283    288  6      
STRAND   296    298  3      
STRAND   306    312  7      
STRAND   316    322  7      
TURN   323    325  3      
STRAND   328    332  5      
HELIX   333    335  3      
STRAND   336    338  3      
HELIX   720    723  4      
HELIX   724    730  7      
HELIX   736    744  9      
HELIX   749    762  14      
HELIX   766    780  15      
HELIX   784    786  3      
HELIX   793    805  13      
HELIX   807    823  17      
HELIX   832    834  3      
HELIX   841    860  20      
HELIX   861    865  5      
HELIX   868    884  17      
HELIX   891    900  10      
TURN   901    904  4      
HELIX   905    910  6      
TURN   912    916  5      
HELIX   924    941  18      
HELIX   951    956  6      
HELIX   957    974  18      
HELIX   992   1004  13      
HELIX   1006   1013  8      
HELIX   1020   1038  19      
Sequence information
Length: 1047 AA [This is the length of the unprocessed precursor] Molecular weight: 116403 Da [This is the MW of the unprocessed precursor] CRC64: C35B6567F5BC5370 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPVAAAPYP GLVETGVAGT 

        70         80         90        100        110        120 
LGGGAALGSE FLGAGSVAGA LGGAGLTGGG TAAGVAGAAA GVAGAAVAGP SGDMALTKLP 

       130        140        150        160        170        180 
TSLLAETLGP GGGFPPLPPP PYLPPLGAGL GTVDEGDSLD GPEYEEEEVA IPLTAPPTNQ 

       190        200        210        220        230        240 
WYHGKLDRTI AEERLRQAGK SGSYLIRESD RRPGSFVLSF LSQMNVVNHF RIIAMCGDYY 

       250        260        270        280        290        300 
IGGRRFSSLS DLIGYYSHVS CLLKGEKLLY PVAPPEPVED RRRVRAILPY TKVPDTDEIS 

       310        320        330        340        350        360 
FLKGDMFIVH NELEDGWMWV TNLRTDEQGL IVEDLVEEVG REEDPHEGKI WFHGKISKQE 

       370        380        390        400        410        420 
AYNLLMTVGQ VCSFLVRPSD NTPGDYSLYF RTNENIQRFK ICPTPNNQFM MGGRYYNSIG 

       430        440        450        460        470        480 
DIIDHYRKEQ IVEGYYLKEP VPMQDQEQVL NDTVDGKEIY NTIRRKTKDA FYKNIVKKGY 

       490        500        510        520        530        540 
LLKKGKGKRW KNLYFILEGS DAQLIYFESE KRATKPKGLI DLSVCSVYVV HDSLFGRPNC 

       550        560        570        580        590        600 
FQIVVQHFSE EHYIFYFAGE TPEQAEDWMK GLQAFCNLRK SSPGTSNKRL RQVSSLVLHI 

       610        620        630        640        650        660 
EEAHKLPVKH FTNPYCNIYL NSVQVAKTHA REGQNPVWSE EFVFDDLPPD INRFEITLSN 

       670        680        690        700        710        720 
KTKKSKDPDI LFMRCQLSRL QKGHATDEWF LLSSHIPLKG IEPGSLRVRA RYSMEKIMPE 

       730        740        750        760        770        780 
EEYSEFKELI LQKELHVVYA LSHVCGQDRT LLASILLRIF LHEKLESLLL CTLNDREISM 

       790        800        810        820        830        840 
EDEATTLFRA TTLASTLMEQ YMKATATQFV HHALKDSILK IMESKQSCEL SPSKLEKNED 

       850        860        870        880        890        900 
VNTNLTHLLN ILSELVEKIF MASEILPPTL RYIYGCLQKS VQHKWPTNTT MRTRVVSGFV 

       910        920        930        940        950        960 
FLRLICPAIL NPRMFNIISD SPSPIAARTL ILVAKSVQNL ANLVEFGAKE PYMEGVNPFI 

       970        980        990       1000       1010       1020 
KSNKHRMIMF LDELGNVPEL PDTTEHSRTD LSRDLAALHE ICVAHSDELR TLSNERGAQQ 

      1030       1040 
HVLKKLLAIT ELLQQKQNQY TKTNDVR 

P20936 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!