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UniProtKB/Swiss-Prot entry P09619


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

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Entry information
Entry name PGFRB_HUMAN
Primary accession number P09619
Secondary accession number Q8N5L4
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on July 1, 1989 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 124)
Name and origin of the protein
Protein name Beta-type platelet-derived growth factor receptor [Precursor]
Synonyms EC 2.7.10.1
PDGF-R-beta
CD140 antigen-like family member B
CD140b antigen
Gene name
Name: PDGFRB
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].
DOI=10.1073/pnas.85.10.3435; PubMed=2835772 [NCBI, ExPASy, EBI, Israel, Japan]
Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J., Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J.;
"Cloning and expression of a cDNA coding for the human platelet-derived growth factor receptor: evidence for more than one receptor class.";
Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2850496 [NCBI, ExPASy, EBI, Israel, Japan]
Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B., Oestman A., Betsholtz C., Heldin C.-H.;
"cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules.";
Mol. Cell. Biol. 8:3476-3486(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-180.
TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
DOI=10.1038/sj.onc.1201267; PubMed=9285559 [NCBI, ExPASy, EBI, Israel, Japan]
Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S.;
"Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity.";
Oncogene 15:1051-1057(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
DOI=10.1016/0092-8674(88)90224-3; PubMed=2846185 [NCBI, ExPASy, EBI, Israel, Japan]
Roberts W.M., Look A.T., Roussel M.F., Sherr C.J.;
"Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes.";
Cell 55:655-661(1988).
[6]
PROTEIN SEQUENCE OF 33-47.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
PHOSPHORYLATION AT TYR-751 AND TYR-857.
DOI=10.1016/0092-8674(89)90510-2; PubMed=2550144 [NCBI, ExPASy, EBI, Israel, Japan]
Kazlauskas A., Cooper J.A.;
"Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins.";
Cell 58:1121-1133(1989).
[8]
INTERACTION WITH SHB.
PubMed=8302579 [NCBI, ExPASy, EBI, Israel, Japan]
Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.;
"Shb is a ubiquitously expressed Src homology 2 protein.";
Oncogene 9:19-27(1994).
[9]
CHROMOSOMAL TRANSLOCATION WITH TRIP11.
PubMed=9373237 [NCBI, ExPASy, EBI, Israel, Japan]
Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.;
"Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution.";
Blood 90:4271-4277(1997).
[10]
INTERACTION WITH APS.
DOI=10.1038/sj.onc.1202326; PubMed=9989826 [NCBI, ExPASy, EBI, Israel, Japan]
Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A., Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.;
"APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis.";
Oncogene 18:759-767(1999).
[11]
INTERACTION WITH PIK3C2B.
DOI=10.1128/MCB.20.11.3817-3830.2000; PubMed=10805725 [NCBI, ExPASy, EBI, Israel, Japan]
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.;
"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors.";
Mol. Cell. Biol. 20:3817-3830(2000).
[12]
FUNCTION AS A RECEPTOR FOR PDGFD.
DOI=10.1038/35074588; PubMed=11331881 [NCBI, ExPASy, EBI, Israel, Japan]
Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H., Alitalo K., Eriksson U.;
"PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor.";
Nat. Cell Biol. 3:512-516(2001).
[13]
CHROMOSOMAL TRANSLOCATION WITH ETV6.
DOI=10.1056/NEJMoa020150; PubMed=12181402 [NCBI, ExPASy, EBI, Israel, Japan]
Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J., Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E., Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E., Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.;
"Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor beta.";
N. Engl. J. Med. 347:481-487(2002).
[14]
CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
DOI=10.1182/blood-2003-04-1150; PubMed=12907457 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A., Aguiar R.C.T.;
"Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated with eosinophilia: involvement of PDGFRB and response to imatinib.";
Blood 102:4187-4190(2003).
[15]
CHROMOSOMAL TRANSLOCATION WITH SPECC1.
DOI=10.1158/0008-5472.CAN-03-4026; PubMed=15087372 [NCBI, ExPASy, EBI, Israel, Japan]
Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F., Maserati E., Pasquali F., Panarello C.;
"HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with t(5;17)(q33;p11.2).";
Cancer Res. 64:2649-2651(2004).
[16]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1, AND COMPARISON WITH NMR ANALYSIS.
DOI=10.1107/S0907444901012434; PubMed=11567151 [NCBI, ExPASy, EBI, Israel, Japan]
Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A., Rowsell S., Murshudov G.N.;
"NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex.";
Acta Crystallogr. D 57:1397-1404(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH SLC9A3R1 AND PDGFRA.
DOI=10.1074/jbc.M201507200; PubMed=11882663 [NCBI, ExPASy, EBI, Israel, Japan]
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors.";
J. Biol. Chem. 277:18973-18978(2002).
[18]
VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718 AND ILE-882.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
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
J03278; AAA60049.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21616; AAA36427.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032224; AAH32224.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U33172; AAC51675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00015902; -.
PIR A28206; PFHUGB.
RefSeq NP_002600.1; -.
UniGene Hs.509067
3D structure databases
PDB
1GQ5; X-ray; 2.20 A; A=1102-1106.[ExPASy / RCSB / EBI]
1H9O; X-ray; 1.79 A; B=751-755.[ExPASy / RCSB / EBI]
1LWP; Model; -; A=600-962.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GQ5; -.
1H9O; -.
1LWP; -.
ModBase P09619.
Protein-protein interaction databases
DIP DIP:558N; -.
IntAct P09619; 15.
PTM databases
PhosphoSite P09619; -.
Enzyme and pathway databases
BRENDA 2.7.10.1; 247.
Pathway_Interaction_DB pdgfrbpathway; PDGFR-beta signaling pathway.
s1p_s1p1_pathway; S1P1 pathway.
s1p_s1p3_pathway; S1P3 pathway.
ptp1bpathway; Signaling events mediated by PTP1B.
Organism-specific databases
GeneCards GC05M149473; -.
H-InvDB HIX0024847; -.
HGNC HGNC:8804; PDGFRB.
GenAtlas PDGFRB.
HPA CAB003842; -.
CAB018144; -.
MIM 131440; phenotype. [NCBI / EBI]
173410; gene. [NCBI / EBI]
Orphanet 86832; Adult myelodysplastic/myeloproliferative disease.
98274; Chronic myeloproliferative disease.
86830; Chronic myeloproliferative disease, unclassified.
3260; Idiopathic hypereosinophilic syndrome.
98823; Leukemia, myelomonocytic, chronic.
PharmGKB PA33148; -.
Gene expression databases
ArrayExpress P09619; -.
Bgee P09619; -.
CleanEx HS_PDGFRB; -.
GermOnline ENSG00000113721; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0004992; Molecular function: platelet activating factor receptor activity (traceable author statement from ProtInc).
GO:0005019; Molecular function: platelet-derived growth factor beta-receptor activity (inferred from direct assay from UniProtKB).
GO:0048407; Molecular function: platelet-derived growth factor binding (inferred from physical interaction from UniProtKB).
GO:0005161; Molecular function: platelet-derived growth factor receptor binding (inferred from physical interaction from UniProtKB).
GO:0005021; Molecular function: vascular endothelial growth factor receptor activity (inferred from electronic annotation from InterPro).
GO:0060326; Biological process: cell chemotaxis (inferred from direct assay from UniProtKB).
GO:0018108; Biological process: peptidyl-tyrosine phosphorylation (inferred from direct assay from UniProtKB).
GO:0048008; Biological process: platelet-derived growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0030335; Biological process: positive regulation of cell migration (inferred from direct assay from UniProtKB).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from direct assay from UniProtKB).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR001824; Recept_tyr_kinase-III_CS.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
IPR016243; TyrPK_CSF1-R.
IPR009134; VEGFR_N.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 3.
Pfam PF00047; ig; 2.
PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000615; TyrPK_CSF1-R; 1.
PRINTS PR01832; VEGFRECEPTOR.
ProDom PD000001; Prot_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00409; IG; 2.
SM00408; IGc2; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 2.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS00240; RECEPTOR_TYR_KIN_III; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P09619; -.
Genome annotation databases
Ensembl ENSG00000113721; Homo sapiens. [Contig view]
GeneID 5159; -.
KEGG hsa:5159; -.
Phylogenomic databases
HOGENOM P09619; -.
HOVERGEN P09619; -.
OMA P09619; GACTKGG.
Other
DrugBank DB00102; Becaplermin.
DB01254; Dasatinib.
DB00619; Imatinib.
DB00398; Sorafenib.
DB01268; Sunitinib.
NextBio 19958; -.
SOURCE PDGFRB; Homo sapiens.
ProtoNet P09619.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Chromosomal rearrangement; Direct protein sequencing; Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1     32  32      
CHAIN   33   1106  1074     Beta-type platelet-derived growth factor receptor. PRO_0000016757
TOPO_DOM   33    531  499     Extracellular (Potential). 
TRANSMEM   532    556  25     Potential. 
TOPO_DOM   557   1106  550     Cytoplasmic (Potential). 
DOMAIN   33    120  88     Ig-like C2-type 1. 
DOMAIN   129    210  82     Ig-like C2-type 2. 
DOMAIN   214    309  96     Ig-like C2-type 3. 
DOMAIN   331    403  73     Ig-like C2-type 4. 
DOMAIN   416    524  109     Ig-like C2-type 5. 
DOMAIN   600    962  363     Protein kinase. 
NP_BIND   606    614  9     ATP (By similarity). 
ACT_SITE   826    826        Proton acceptor (By similarity). 
BINDING   634    634        ATP (By similarity). 
SITE   527    528  2     Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein. 
SITE   527    528  2     Breakpoint for translocation to form TRIP11-PDGFRB. 
MOD_RES   751    751        Phosphotyrosine; by autocatalysis. 
MOD_RES   857    857        Phosphotyrosine; by autocatalysis. 
CARBOHYD   45     45        N-linked (GlcNAc...) (Potential). 
CARBOHYD   89     89        N-linked (GlcNAc...) (Potential). 
CARBOHYD   103    103        N-linked (GlcNAc...) (Potential). 
CARBOHYD   215    215        N-linked (GlcNAc...) (Potential). 
CARBOHYD   230    230        N-linked (GlcNAc...) (Potential). 
CARBOHYD   292    292        N-linked (GlcNAc...) (Potential). 
CARBOHYD   307    307        N-linked (GlcNAc...) (Potential). 
CARBOHYD   354    354        N-linked (GlcNAc...) (Potential). 
CARBOHYD   371    371        N-linked (GlcNAc...) (Potential). 
CARBOHYD   468    468        N-linked (GlcNAc...) (Potential). 
CARBOHYD   479    479        N-linked (GlcNAc...) (Potential). 
DISULFID   54    100        Potential. 
DISULFID   149    190        Potential. 
DISULFID   235    291        Potential. 
DISULFID   436    508        Potential. 
VARIANT   29     29  1     I -> F (in dbSNP:rs17110944 [NCBI]). VAR_034377 
VARIANT   180    180  1     S -> F (in dbSNP:rs17853027 [NCBI]). VAR_035125 
VARIANT   282    282  1     E -> K (in dbSNP:rs34586048 [NCBI]). VAR_042027 
VARIANT   345    345  1     P -> S (in dbSNP:rs2229558 [NCBI]). VAR_049717 
VARIANT   485    485  1     E -> K. VAR_042028 
VARIANT   589    589  1     Y -> H (in a gastric adenocarcinoma sample; somatic mutation). VAR_042029 
VARIANT   718    718  1     N -> Y. VAR_042030 
VARIANT   882    882  1     T -> I (in a breast infiltrating ductal carcinoma sample; somatic mutation). VAR_042031 
CONFLICT   241    241        E -> D (in Ref. 2; AAA36427). 
STRAND   601    603  3      
STRAND   606    613  8      
STRAND   615    617  3      
STRAND   620    624  5      
HELIX   628    631  4      
STRAND   632    634  3      
HELIX   641    649  9      
STRAND   671    673  3      
STRAND   675    678  4      
STRAND   681    685  5      
HELIX   686    695  10      
STRAND   700    702  3      
STRAND   713    716  4      
STRAND   726    735  10      
STRAND   740    746  7      
TURN   747    749  3      
STRAND   750    757  8      
HELIX   761    766  6      
STRAND   775    779  5      
STRAND   781    783  3      
STRAND   785    788  4      
HELIX   800    820  21      
HELIX   829    831  3      
STRAND   832    834  3      
HELIX   836    838  3      
STRAND   840    842  3      
HELIX   847    850  4      
HELIX   855    858  4      
STRAND   862    865  4      
TURN   867    869  3      
HELIX   872    877  6      
HELIX   882    897  16      
TURN   898    900  3      
STRAND   903    907  5      
HELIX   910    919  10      
HELIX   931    940  10      
TURN   945    947  3      
HELIX   951    959  9      
Sequence information
Length: 1106 AA [This is the length of the unprocessed precursor] Molecular weight: 123968 Da [This is the MW of the unprocessed precursor] CRC64: 038C15E531D6E89D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF VLTCSGSAPV 

        70         80         90        100        110        120 
VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC THNDSRGLET DERKRLYIFV 

       130        140        150        160        170        180 
PDPTVGFLPN DAEELFIFLT EITEITIPCR VTDPQLVVTL HEKKGDVALP VPYDHQRGFS 

       190        200        210        220        230        240 
GIFEDRSYIC KTTIGDREVD SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN 

       250        260        270        280        290        300 
EVVNFEWTYP RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH 

       310        320        330        340        350        360 
QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW FKDNRTLGDS 

       370        380        390        400        410        420 
SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH EDAEVQLSFQ LQINVPVRVL 

       430        440        450        460        470        480 
ELSESHPDSG EQTVRCRGRG MPQPNIIWSA CRDLKRCPRE LPPTLLGNSS EEESQLETNV 

       490        500        510        520        530        540 
TYWEEEQEFE VVSTLRLQHV DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA 

       550        560        570        580        590        600 
LVVLTIISLI ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL 

       610        620        630        640        650        660 
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP 

       670        680        690        700        710        720 
HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQHHSDKRRP PSAELYSNAL 

       730        740        750        760        770        780 
PVGLPLPSHV SLTGESDGGY MDMSKDESVD YVPMLDMKGD VKYADIESSN YMAPYDNYVP 

       790        800        810        820        830        840 
SAPERTCRAT LINESPVLSY MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV 

       850        860        870        880        890        900 
KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG 

       910        920        930        940        950        960 
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER 

       970        980        990       1000       1010       1020 
LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS PLDTSSVLYT AVQPNEGDND 

      1030       1040       1050       1060       1070       1080 
YIIPLPDPKP EVADEGPLEG SPSLASSTLN EVNTSSTISC DSPLEPQDEP EPEPQLELQV 

      1090       1100 
EPEPELEQLP DSGCPAPRAE AEDSFL 

P09619 in FASTA format

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