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UniProtKB/Swiss-Prot entry P31749


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

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Entry information
Entry name AKT1_HUMAN
Primary accession number P31749
Secondary accession number Q9BWB6
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on February 1, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 108)
Name and origin of the protein
Protein name RAC-alpha serine/threonine-protein kinase
Synonyms EC 2.7.11.1
RAC-PK-alpha
Protein kinase B
PKB
C-AKT
Gene name
Name: AKT1
Synonyms: PKB, RAC
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], AND CATALYTIC ACTIVITY.
PubMed=1851997 [NCBI, ExPASy, EBI, Israel, Japan]
Jones P.F., Jakubowicz T., Pitossi F.J., Maurer F., Hemmings B.A.;
"Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.";
Proc. Natl. Acad. Sci. U.S.A. 88:4171-4175(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s001250100577; PubMed=11508278 [NCBI, ExPASy, EBI, Israel, Japan]
Matsubara A., Wasson J.C., Donelan S.S., Welling C.M., Glaser B., Permutt M.A.;
"Isolation and characterization of the human AKT1 gene, identification of 13 single nucleotide polymorphisms (SNPs), and their lack of association with Type II diabetes.";
Diabetologia 44:910-913(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Ovary;
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 [MRNA] OF 63-480, FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Foreskin;
PubMed=1718748 [NCBI, ExPASy, EBI, Israel, Japan]
Coffer P.J., Woodgett J.R.;
"Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families.";
Eur. J. Biochem. 201:475-481(1991).
[5]
ERRATUM, AND SEQUENCE REVISION.
PubMed=1533586 [NCBI, ExPASy, EBI, Israel, Japan]
Coffer P.J., Woodgett J.R.;
Eur. J. Biochem. 205:1217-1218(1992).
[6]
ENZYME REGULATION, AND PHOSPHORYLATION AT SER-473.
DOI=10.1073/pnas.95.19.11211; PubMed=9736715 [NCBI, ExPASy, EBI, Israel, Japan]
Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.;
"Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase.";
Proc. Natl. Acad. Sci. U.S.A. 95:11211-11216(1998).
[7]
MUTAGENESIS OF THR-308 AND SER-473, AND PHOSPHORYLATION AT THR-308 AND SER-473.
PubMed=8978681 [NCBI, ExPASy, EBI, Israel, Japan]
Alessi D.R., Andjelkovic M., Caudwell F.B., Cron P., Morrice N., Cohen P., Hemmings B.A.;
"Mechanism of activation of protein kinase B by insulin and IGF-1.";
EMBO J. 15:6541-6551(1996).
[8]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-308 BY PDPK1.
PubMed=9512493 [NCBI, ExPASy, EBI, Israel, Japan]
Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.;
"Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha.";
Biochem. J. 331:299-308(1998).
[9]
INTERACTION WITH MTCP1; TCL1A AND TCL1B.
DOI=10.1016/S1097-2765(00)00039-3; PubMed=10983986 [NCBI, ExPASy, EBI, Israel, Japan]
Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.;
"The protooncogene TCL1 is an Akt kinase coactivator.";
Mol. Cell 6:395-407(2000).
[10]
INTERACTION WITH TCL1A.
DOI=10.1073/pnas.040557697; PubMed=10716693 [NCBI, ExPASy, EBI, Israel, Japan]
Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S., Russo G., Tsichlis P., Croce C.M.;
"Tcl1 enhances Akt kinase activity and mediates its nuclear translocation.";
Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000).
[11]
INTERACTION WITH THEM4, AND SUBCELLULAR LOCATION.
DOI=10.1126/science.1062030; PubMed=11598301 [NCBI, ExPASy, EBI, Israel, Japan]
Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.;
"Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane.";
Science 294:374-380(2001).
[12]
FUNCTION IN PHOSPHORYLATION OF TBC1D4.
DOI=10.1074/jbc.C200198200; PubMed=11994271 [NCBI, ExPASy, EBI, Israel, Japan]
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C., Lienhard G.E.;
"A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.";
J. Biol. Chem. 277:22115-22118(2002).
[13]
PHOSPHORYLATION AT TYR-474, AND MUTAGENESIS OF TYR-474.
DOI=10.1074/jbc.M203387200; PubMed=12149249 [NCBI, ExPASy, EBI, Israel, Japan]
Conus N.M., Hannan K.M., Cristiano B.E., Hemmings B.A., Pearson R.B.;
"Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase.";
J. Biol. Chem. 277:38021-38028(2002).
[14]
INTERACTION WITH TCL1A.
DOI=10.1128/MCB.22.5.1513-1525.2002; PubMed=11839817 [NCBI, ExPASy, EBI, Israel, Japan]
Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M.;
"Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1.";
Mol. Cell. Biol. 22:1513-1525(2002).
[15]
INTERACTION WITH CENTG1, AND PHOSPHORYLATION AT SER-473.
DOI=10.1074/jbc.M312175200; PubMed=14761976 [NCBI, ExPASy, EBI, Israel, Japan]
Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.;
"PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion.";
J. Biol. Chem. 279:16441-16451(2004).
[16]
INTERACTION WITH AKTIP.
DOI=10.1128/MCB.24.4.1493-1504.2004; PubMed=14749367 [NCBI, ExPASy, EBI, Israel, Japan]
Remy I., Michnick S.W.;
"Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt.";
Mol. Cell. Biol. 24:1493-1504(2004).
[17]
INTERACTION WITH CENTG1.
DOI=10.1073/pnas.0400921101; PubMed=15118108 [NCBI, ExPASy, EBI, Israel, Japan]
Ahn J.-Y., Hu Y., Kroll T.G., Allard P., Ye K.;
"PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt.";
Proc. Natl. Acad. Sci. U.S.A. 101:6993-6998(2004).
[18]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CCDC88A.
DOI=10.1016/j.devcel.2005.08.001; PubMed=16139227 [NCBI, ExPASy, EBI, Israel, Japan]
Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.;
"Akt/PKB regulates actin organization and cell motility via Girdin/APE.";
Dev. Cell 9:389-402(2005).
[19]
PHOSPHORYLATION AT THR-308 AND SER-473.
DOI=10.1126/science.1106148; PubMed=15718470 [NCBI, ExPASy, EBI, Israel, Japan]
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex.";
Science 307:1098-1101(2005).
[20]
PHOSPHORYLATION AT SER-473.
DOI=10.1007/s00401-006-0128-y; PubMed=17013611 [NCBI, ExPASy, EBI, Israel, Japan]
Schick V., Majores M., Engels G., Spitoni S., Koch A., Elger C.E., Simon M., Knobbe C., Bluemcke I., Becker A.J.;
"Activation of Akt independent of PTEN and CTMP tumor-suppressor gene mutations in epilepsy-associated Taylor-type focal cortical dysplasias.";
Acta Neuropathol. 112:715-725(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND SER-129, 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).
Comments
  • FUNCTION: General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • ENZYME REGULATION: Three specific sites, one in the kinase domain (Thr-308) and the two other ones in the C-terminal regulatory region (Ser-473 and Tyr-474), need to be phosphorylated for its full activation.
  • SUBUNIT: Interacts with CENTG1 isoform 2 (PIKE-A) in the presence of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN and THEM4. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B.
  • INTERACTION:
    Self; NbExp=1; IntAct=EBI-296087, EBI-296087;
    P29067:Arrb2 (xeno); NbExp=2; IntAct=EBI-296087, EBI-1636616;
    O95999:BCL10; NbExp=3; IntAct=EBI-296087, EBI-958922;
    O43521-1:BCL2L11; NbExp=1; IntAct=EBI-296087, EBI-526416;
    Q16543:CDC37; NbExp=1; IntAct=EBI-296087, EBI-295634;
    P49841:GSK3B; NbExp=1; IntAct=EBI-296087, EBI-373586;
    Q99683:MAP3K5; NbExp=2; IntAct=EBI-296087, EBI-476263;
    O60437:PPL; NbExp=1; IntAct=EBI-296087, EBI-368321;
    Q15047:SETDB1; NbExp=6; IntAct=EBI-296087, EBI-79691;
    Q7Z6J0:SH3RF1; NbExp=1; IntAct=EBI-296087, EBI-1374106;
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A.
  • TISSUE SPECIFICITY: In all human cell types so far analyzed.
  • DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
  • DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
  • PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by the Rictor-mTor complex favors Thr-308 phosphorylation by PDPK1. Ser-473 phosphorylation is enhanced by interaction with CENTG1 isoform 2 (PIKE-A). Ser-473 phosphorylation is enhanced in focal cortical dysplasias with Taylor-type balloon cells.
  • SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.
  • SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
  • SIMILARITY: Contains 1 PH domain.
  • SIMILARITY: Contains 1 protein kinase 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
M63167; AAA36539.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283830; AAL55732.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283819; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283820; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283821; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283822; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283823; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283824; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283825; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283826; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283827; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283828; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF283829; AAL55732.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000479; AAH00479.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC084538; AAH84538.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X61037; CAA43372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39360; A39360.
RefSeq NP_001014431.1; -.
NP_001014432.1; -.
NP_005154.2; -.
UniGene Hs.525622
3D structure databases
PDB
1H10; X-ray; 1.40 A; A=1-123.[ExPASy / RCSB / EBI]
1UNP; X-ray; 1.65 A; A=1-121.[ExPASy / RCSB / EBI]
1UNQ; X-ray; 0.98 A; A=1-123.[ExPASy / RCSB / EBI]
1UNR; X-ray; 1.25 A; A=1-123.[ExPASy / RCSB / EBI]
2UVM; X-ray; 1.94 A; A=1-123.[ExPASy / RCSB / EBI]
2UZR; X-ray; 1.94 A; A=1-123.[ExPASy / RCSB / EBI]
2UZS; X-ray; 2.46 A; A=1-123.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H10; -.
1UNP; -.
1UNQ; -.
1UNR; -.
2UVM; -.
2UZR; -.
2UZS; -.
ModBase P31749.
Protein-protein interaction databases
DIP DIP:24269N; -.
IntAct P31749; -.
PTM databases
PhosphoSite P31749; -.
Enzyme and pathway databases
Reactome REACT_578; Apoptosis.
Organism-specific databases
H-InvDB HIX0012019; -.
HGNC HGNC:391; AKT1.
GenAtlas AKT1.
HPA CAB003765; -.
HPA002891; -.
MIM 164730; gene. [NCBI / EBI]
PharmGKB PA24684; -.
GeneCards P31749.
Gene expression databases
ArrayExpress P31749; -.
CleanEx HS_AKT1; -.
GermOnline ENSG00000142208; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0005524; Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from direct assay from UniProtKB).
GO:0006924; Biological process: activated T cell apoptosis (inferred from mutant phenotype from MGI).
GO:0008633; Biological process: activation of pro-apoptotic gene products (inferred from experiment from Reactome).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0008286; Biological process: insulin receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0048009; Biological process: insulin-like growth factor receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0006809; Biological process: nitric oxide biosynthetic process (traceable author statement from ProtInc).
GO:0018105; Biological process: peptidyl-serine phosphorylation (inferred from direct assay from UniProtKB).
GO:0046777; Biological process: protein amino acid autophosphorylation (traceable author statement from UniProtKB).
GO:0000060; Biological process: protein import into nucleus, translocation (inferred from mutant phenotype from UniProtKB).
GO:0009408; Biological process: response to heat (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR015744; Akt.
IPR001849; PH.
IPR011993; PH_type.
IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
PANTHER PTHR22985:SF69; Akt; 1.
Pfam PF00169; PH; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00233; PH; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31749.
Genome annotation databases
Ensembl ENSG00000142208; Homo sapiens. [Contig view]
GeneID 207; -.
KEGG hsa:207; -.
Phylogenomic databases
HOGENOM P31749; -.
HOVERGEN P31749; -.
Other
BindingDB P31749; -.
DrugBank DB00171; Adenosine triphosphate.
DB01169; Arsenic trioxide.
SOURCE AKT1; Homo sapiens.
ProtoNet P31749.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; ATP-binding; Carbohydrate metabolism; Cell membrane; Cytoplasm; Glucose metabolism; Glycogen biosynthesis; Glycogen metabolism; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Sugar transport; Transferase; Translation regulation; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   480  480     RAC-alpha serine/threonine-protein kinase. PRO_0000085605
DOMAIN   5   108  104     PH. 
DOMAIN   150   408  259     Protein kinase. 
DOMAIN   409   480  72     AGC-kinase C-terminal. 
NP_BIND   156   164  9     ATP (By similarity). 
ACT_SITE   274   274        Proton acceptor (By similarity). 
BINDING   179   179        ATP (By similarity). 
MOD_RES   124   124        Phosphoserine. 
MOD_RES   126   126        Phosphoserine. 
MOD_RES   129   129        Phosphoserine. 
MOD_RES   308   308        Phosphothreonine; by PDPK1. 
MOD_RES   473   473        Phosphoserine. 
MOD_RES   474   474        Phosphotyrosine. 
MUTAGEN   308   308        T->D: 5-fold activation and 18-fold activation; when associated with D-473. 
MUTAGEN   473   473        S->D: 7-fold activation and 25-fold activation; when associated with D-308. 
MUTAGEN   474   474        Y->F: 55% inhibition of activation. 
CONFLICT   173   174        GR -> A (in Ref. 4; CAA43372). 
CONFLICT   202   202        L -> Q (in Ref. 4; CAA43372). 
CONFLICT   212   212        A -> R (in Ref. 4; CAA43372). 
CONFLICT   246   246        S -> A (in Ref. 4; CAA43372). 
CONFLICT   409   409        A -> T (in Ref. 4; CAA43372). 
CONFLICT   476   476        A -> P (in Ref. 4; CAA43372). 
CONFLICT   478   478        G -> A (in Ref. 4; CAA43372). 
CONFLICT   478   478        G -> S (in Ref. 1; AAA36539 and 2; AAL55732). 
STRAND   6    15  10      
STRAND   17    19  3      
STRAND   22    30  9      
STRAND   33    40  8      
STRAND   52    56  5      
STRAND   61    65  5      
STRAND   67    79  13      
STRAND   82    89  8      
HELIX   93   118  26      
Sequence information
Length: 480 AA [This is the length of the unprocessed precursor] Molecular weight: 55686 Da [This is the MW of the unprocessed precursor] CRC64: 6EAFF4F8AD436714 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQREA PLNNFSVAQC 

        70         80         90        100        110        120 
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KKQEEEEMDF 

       130        140        150        160        170        180 
RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI 

       190        200        210        220        230        240 
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS 

       250        260        270        280        290        300 
RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI 

       310        320        330        340        350        360 
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL 

       370        380        390        400        410        420 
ILMEEIRFPR TLGPEAKSLL SGLLKKDPKQ RLGGGSEDAK EIMQHRFFAG IVWQHVYEKK 

       430        440        450        460        470        480 
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA 

P31749 in FASTA format

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

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