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 P49023


[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 PAXI_HUMAN
Primary accession number P49023
Secondary accession numbers O14970 O14971 O60360
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on January 10, 2003 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 101)
Name and origin of the protein
Protein name Paxillin
Synonyms None
Gene name
Name: PXN
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] (ISOFORM ALPHA).
DOI=10.1074/jbc.270.10.5039; PubMed=7534286 [NCBI, ExPASy, EBI, Israel, Japan]
Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L.B., Griffin J.D.;
"Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL.";
J. Biol. Chem. 270:5039-5047(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.;
"Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA).
TISSUE=Placenta;
DOI=10.1074/jbc.272.11.7437; PubMed=9054445 [NCBI, ExPASy, EBI, Israel, Japan]
Mazaki Y., Hashimoto S., Sabe H.;
"Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins.";
J. Biol. Chem. 272:7437-7444(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04569; PubMed=16541075 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
INTERACTION WITH ITGA4.
DOI=10.1038/45264; PubMed=10604475 [NCBI, ExPASy, EBI, Israel, Japan]
Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H.;
"Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses.";
Nature 402:676-681(1999).
[6]
INTERACTION WITH GIT1.
DOI=10.1128/MCB.20.17.6354-6363.2000; PubMed=10938112 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Z.-S., Manser E., Loo T.-H., Lim L.;
"Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly.";
Mol. Cell. Biol. 20:6354-6363(2000).
[7]
INTERACTION WITH ASAP2.
PubMed=10749932 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.;
"A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration.";
Mol. Biol. Cell 11:1315-1327(2000).
[8]
PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
DOI=10.1002/ijc.1609; PubMed=11774284 [NCBI, ExPASy, EBI, Israel, Japan]
Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E., Akedo H.;
"Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration.";
Int. J. Cancer 97:330-335(2002).
[9]
INTERACTION WITH RNF5.
DOI=10.1128/MCB.23.15.5331-5345.2003; PubMed=12861019 [NCBI, ExPASy, EBI, Israel, Japan]
Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.;
"RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization.";
Mol. Cell. Biol. 23:5331-5345(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr050134h; PubMed=16212419 [NCBI, ExPASy, EBI, Israel, Japan]
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC).";
J. Proteome Res. 4:1661-1671(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126; SER-130 AND SER-137, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
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
U14588; AAC50104.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87946; AAD00648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87941; AAD00648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87942; AAD00648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87943; AAD00648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87944; AAD00648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U87945; AAD00648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D86862; BAA18997.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D86863; BAA18998.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004263; AAC05175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00220030; -.
IPI00220031; -.
IPI00335634; -.
PIR A55933; A55933.
RefSeq NP_001074324.1; -.
NP_002850.2; -.
UniGene Hs.446336
3D structure databases
PDB
1KKY; Model; -; A=142-157.[ExPASy / RCSB / EBI]
1KL0; Model; -; B=142-157.[ExPASy / RCSB / EBI]
2O9V; X-ray; 1.63 A; B=45-54.[ExPASy / RCSB / EBI]
2VZD; X-ray; 2.10 A; C/D=1-20.[ExPASy / RCSB / EBI]
2VZG; X-ray; 1.80 A; A=141-160.[ExPASy / RCSB / EBI]
2VZI; X-ray; 2.20 A; A=262-315.[ExPASy / RCSB / EBI]
3GM1; X-ray; 2.95 A; C/D/E/F=262-274.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KKY; -.
1KL0; -.
2O9V; -.
2VZD; -.
2VZG; -.
2VZI; -.
3GM1; -.
ModBase P49023.
Protein-protein interaction databases
IntAct P49023; 13.
Enzyme and pathway databases
Pathway_Interaction_DB angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
arf6cyclingpathway; Arf6 signaling events.
ephbfwdpathway; EPHB forward signaling.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
igf1_pathway; IGF1 pathway.
avb3_integrin_pathway; Integrins in angiogenesis.
lysophospholipid_pathway; LPA receptor mediated events.
a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway; Paxillin-independent events mediated by a4b1 and a4b7.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway; Signaling events regulated by Ret tyrosine kinase.
Reactome REACT_9417; Signaling by EGFR.
Organism-specific databases
GeneCards GC12M119110; -.
H-InvDB HIX0011059; -.
HIX0037171; -.
HGNC HGNC:9718; PXN.
GenAtlas PXN.
HPA CAB003841; -.
MIM 602505; gene. [NCBI / EBI]
PharmGKB PA30441; -.
Gene expression databases
ArrayExpress P49023; -.
Bgee P49023; -.
CleanEx HS_PXN; -.
GermOnline ENSG00000089159; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005925; Cellular component: focal adhesion (inferred from direct assay from UniProtKB).
GO:0030027; Cellular component: lamellipodium (inferred from direct assay from UniProtKB).
GO:0005875; Cellular component: microtubule associated complex (traceable author statement from ProtInc).
GO:0017166; Molecular function: vinculin binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007160; Biological process: cell-matrix adhesion (inferred from electronic annotation from InterPro).
GO:0034614; Biological process: cellular response to reactive oxygen species (inferred from expression pattern from UniProtKB).
GO:0007172; Biological process: signal complex assembly (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001904; Paxillin.
IPR001781; Znf_LIM.
Graphical view of domain structure.
Gene3D G3DSA:2.10.110.10; Znf_LIM; 3.
Pfam PF00412; LIM; 4.
PF03535; Paxillin; 1.
Pfam graphical view of domain structure.
PRINTS PR00832; PAXILLIN.
ProDom PD000094; LIM; 4.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00132; LIM; 4.
SMART graphical view of domain structure.
PROSITE PS00478; LIM_DOMAIN_1; 4.
PS50023; LIM_DOMAIN_2; 4.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P49023; -.
Genome annotation databases
Ensembl ENSG00000089159; Homo sapiens. [Contig view]
GeneID 5829; -.
KEGG hsa:5829; -.
Phylogenomic databases
HOVERGEN P49023; -.
Other
NextBio 22710; -.
PMAP-CutDB P49023; -.
SOURCE PXN; Homo sapiens.
ProtoNet P49023.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein; Repeat; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   591  591     Paxillin. PRO_0000075853
DOMAIN   356   415  60     LIM zinc-binding 1. 
DOMAIN   416   473  58     LIM zinc-binding 2. 
DOMAIN   474   533  60     LIM zinc-binding 3. 
DOMAIN   534   591  58     LIM zinc-binding 4. 
MOTIF   3    15  13     LD motif 1. 
MOTIF   144   156  13     LD motif 2. 
MOTIF   216   228  13     LD motif 3. 
MOTIF   265   276  12     LD motif 4. 
MOTIF   333   345  13     LD motif 5. 
COMPBIAS   46    53  8     Pro-rich. 
MOD_RES   31    31        Phosphotyrosine. 
MOD_RES   83    83        Phosphoserine (By similarity). 
MOD_RES   85    85        Phosphoserine. 
MOD_RES   88    88        Phosphotyrosine. 
MOD_RES   106   106        Phosphoserine. 
MOD_RES   109   109        Phosphoserine (By similarity). 
MOD_RES   118   118        Phosphotyrosine. 
MOD_RES   126   126        Phosphoserine. 
MOD_RES   130   130        Phosphoserine. 
MOD_RES   137   137        Phosphoserine. 
MOD_RES   181   181        Phosphotyrosine. 
MOD_RES   303   303        Phosphoserine. 
VAR_SEQ   278   311        Missing (in isoform Alpha). VSP_003114
VAR_SEQ   278   311        IQDLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSWPLEEVVLLVSISSSVQEGEKYPHPCAARHRTPSLRSP DQPPPCPQ (in isoform Gamma). VSP_003115
CONFLICT   73    73        G -> S (in Ref. 4; AAC05175). 
HELIX   143   155  13      
Sequence information
Length: 591 AA [This is the length of the unprocessed precursor] Molecular weight: 64533 Da [This is the MW of the unprocessed precursor] CRC64: 0FFDC07047E96636 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 

        70         80         90        100        110        120 
TILDPLDQWQ PSGSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF 

       130        140        150        160        170        180 
PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL 

       190        200        210        220        230        240 
YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 

       250        260        270        280        290        300 
EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQD LEQRADGERC WAAGWPRDGG 

       310        320        330        340        350        360 
RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA 

       370        380        390        400        410        420 
CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC 

       430        440        450        460        470        480 
NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA 

       490        500        510        520        530        540 
RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK 

       550        560        570        580        590 
PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C 

P49023 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!