[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=T-cell; DOI=10.1089/dna.1993.12.823; PubMed=7692878 [NCBI, ExPASy, EBI, Israel, Japan] Whitney G.S., Chan P.Y., Blake J., Cosand W.L., Neubauer M.G., Aruffo A., Kanner S.B.; "Human T and B lymphocytes express a structurally conserved focal adhesion kinase, pp125FAK."; DNA Cell Biol. 12:823-830(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4). TISSUE=Brain; DOI=10.1006/bbrc.1993.1022; PubMed=8422239 [NCBI, ExPASy, EBI, Israel, Japan] Andre E., Becker-Andre M.; "Expression of an N-terminally truncated form of human focal adhesion kinase in brain."; Biochem. Biophys. Res. Commun. 190:140-147(1993).
[3]	PROTEIN SEQUENCE OF 2-19; 192-199; 222-236; 243-252; 350-364; 414-419; 468-476; 562-569; 674-690; 798-811; 832-838; 904-933; 963-981; 989-1000 AND 1003-1042, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY. TISSUE=Osteosarcoma; Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.; Submitted (JUL-2007) to UniProtKB.
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 552-602, AND TISSUE SPECIFICITY. TISSUE=Melanocyte; PubMed=8247543 [NCBI, ExPASy, EBI, Israel, Japan] Lee S.-T., Strunk K.M., Spritz R.A.; "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."; Oncogene 8:3403-3410(1993).
[5]	INTERACTION WITH TGFB1I1. DOI=10.1074/jbc.273.2.1003; PubMed=9422762 [NCBI, ExPASy, EBI, Israel, Japan] Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T., Ishino M., Takahashi S., Suzuki R., Sasaki T.; "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions."; J. Biol. Chem. 273:1003-1014(1998).
[6]	INTERACTION WITH TGFB1I1, AND MUTAGENESIS OF VAL-928 AND LEU-1034. DOI=10.1074/jbc.273.41.26516; PubMed=9756887 [NCBI, ExPASy, EBI, Israel, Japan] Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C., Tachibana K.; "Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase."; J. Biol. Chem. 273:26516-26521(1998).
[7]	PHOSPHORYLATION AT TYR-397; TYR-407; TYR-577; TYR-861 AND TYR-925. DOI=10.1042/BJ20020410; PubMed=12387730 [NCBI, ExPASy, EBI, Israel, Japan] Relou I.A.M., Bax L.A.B., Van Rijn H.J.M., Akkerman J.-W.N.; "Site-specific phosphorylation of platelet focal adhesion kinase by low-density lipoprotein."; Biochem. J. 369:407-416(2003).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-576, 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).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397 AND SER-840, 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).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-570; TYR-576; TYR-577 AND TYR-861, 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).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397; TYR-576; SER-722; SER-840; SER-843 AND SER-910, AND MASS SPECTROMETRY. DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan] Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.; "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."; Mol. Cell. Proteomics 6:537-547(2007).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-29; SER-568; TYR-570; SER-722; SER-840; SER-887 AND SER-910, 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).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, 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).
[14]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[15]	VARIANTS [LARGE SCALE ANALYSIS] PRO-292; GLN-292; ALA-793; GLU-1030 AND GLU-1044. 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

FUNCTION: Non-receptor protein-tyrosine kinase implicated in signaling pathways involved in cell motility, proliferation and apoptosis. Activated by tyrosine-phosphorylation in response to either integrin clustering induced by cell adhesion or antibody cross-linking, or via G-protein coupled receptor (GPCR) occupancy by ligands such as bombesin or lysophosphatidic acid, or via LDL receptor occupancy. Plays a potential role in oncogenic transformations resulting in increased kinase activity.
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SUBUNIT: Interacts with CAS family members and with GIT1, SORBS1 and BCAR3. Interacts with RGNEF and SHB (By similarity). Interacts with TGFB1I1.
INTERACTION:
P49023:PXN; NbExp=2; IntAct=EBI-702142, EBI-702209;
Q7L0Q8:RHOU; NbExp=1; IntAct=EBI-702142, EBI-1638043;
P12931:SRC; NbExp=1; IntAct=EBI-702142, EBI-621482;
O43294:TGFB1I1; NbExp=1; IntAct=EBI-702142, EBI-1051449;
Q62219:Tgfb1i1 (xeno); NbExp=2; IntAct=EBI-702142, EBI-642844;
P04637:TP53; NbExp=6; IntAct=EBI-702142, EBI-366083;
SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Constituent of focal adhesions.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q05397-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q05397-2
Features which should be applied to build the isoform sequence: VSP_004967, VSP_004968, VSP_004969, VSP_004970.

Name	3
Isoform ID	Q05397-3
Features which should be applied to build the isoform sequence: VSP_004967, VSP_004968, VSP_004969, VSP_004973, VSP_004974.

Name	4
Isoform ID	Q05397-4
Features which should be applied to build the isoform sequence: VSP_004967, VSP_004968, VSP_004969, VSP_004971, VSP_004972.

TISSUE SPECIFICITY: Expressed in all organs tested, in lymphoid cell lines, but most abundantly in brain.
DOMAIN: The first Pro-rich domain interacts with the SH3 domain of CRK-associated substrate (BCAR1) and CASL (By similarity).
DOMAIN: The carboxy-terminal region is the site of focal adhesion targeting (FAT) sequence which mediates the localization of FAK1 to focal adhesions.
PTM: Phosphorylated on 6 tyrosine residues upon activation.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. FAK subfamily.
SIMILARITY: Contains 1 FERM 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

L13616; AAA58469.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L05186; AAA35819.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00012885; -.
IPI00216217; -.
IPI00216218; -.
IPI00789953; -.

PIR

I53012; I53012.
PC1225; PC1225.

RefSeq

NP_005598.3; -.
NP_722560.1; -.

UniGene

Hs.395482

3D structure databases

PDB

1K04; X-ray; 1.95 A; A=891-1052.	[ExPASy / RCSB / EBI]
1K05; X-ray; 2.90 A; A/B/C=891-1052.	[ExPASy / RCSB / EBI]
1MP8; X-ray; 1.60 A; A=411-686.	[ExPASy / RCSB / EBI]
1OW6; X-ray; 2.35 A; A/B/C=892-1052.	[ExPASy / RCSB / EBI]
1OW7; X-ray; 2.60 A; A/B/C=892-1052.	[ExPASy / RCSB / EBI]
1OW8; X-ray; 2.85 A; A/B/C=892-1052.	[ExPASy / RCSB / EBI]
2ETM; X-ray; 2.30 A; A/B=411-689.	[ExPASy / RCSB / EBI]
2IJM; X-ray; 2.19 A; A/B=411-689.	[ExPASy / RCSB / EBI]
2RA7; X-ray; 1.99 A; A=921-1048.	[ExPASy / RCSB / EBI]
3B71; X-ray; 2.82 A; A/B/C=891-1052.	[ExPASy / RCSB / EBI]
3BZ3; X-ray; 2.20 A; A=414-689.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1K04; -.
1K05; -.
1MP8; -.
1OW6; -.
1OW7; -.
1OW8; -.
2ETM; -.
2IJM; -.
2RA7; -.
3B71; -.
3BZ3; -.

SMR

Q05397; 33-383.

ModBase

Q05397.

Protein-protein interaction databases

IntAct

Q05397; 13.

PTM databases

PhosphoSite

Q05397; -.

Enzyme and pathway databases

BRENDA

2.7.10.2; 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
caspase_pathway; Caspase cascade in apoptosis.
epha2_fwdpathway; EPHA2 forward signaling.
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_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.
syndecan_4_pathway; Syndecan-4-mediated signaling events.

Reactome

REACT_578; Apoptosis.

Organism-specific databases

GC08M141737; -.

HIX0020601; -.

HGNC:9611; PTK2.

CAB004036; -.
HPA001842; -.

MIM

600758; gene. [NCBI / EBI]

PharmGKB

PA33955; -.

Gene expression databases

Q05397; -.

Q05397; -.

HS_PTK2; -.

ENSG00000169398; Homo sapiens.

Ontologies

GO:0005856;	Cellular component: cytoskeleton (traceable author statement from ProtInc).
GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005925;	Cellular component: focal adhesion (inferred from direct assay from HPA).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004715;	Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0042169;	Molecular function: SH2 domain binding (inferred from physical interaction from UniProtKB).
GO:0004871;	Molecular function: signal transducer activity (inferred from electronic annotation from InterPro).
GO:0007229;	Biological process: integrin-mediated signaling pathway (traceable author statement from ProtInc).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred by curator from ProtInc).
GO:0007172;	Biological process: signal complex assembly (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR019749; Band_41_domain.
IPR019748; FERM_central.
IPR019747; FERM_CS.
IPR000299; FERM_domain.
IPR005189; Focal_adhesion_target_reg.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Pfam

PF00373; FERM_M; 1.
PF03623; Focal_AT; 1.
PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.

PRINTS

PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00295; B41; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00660; FERM_1; FALSE_NEG.
PS00661; FERM_2; 1.
PS50057; FERM_3; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q05397; -.

Genome annotation databases

Ensembl

ENSG00000169398; Homo sapiens. [Contig view]

GeneID

5747; -.

KEGG

hsa:5747; -.

Phylogenomic databases

HOVERGEN

Q05397; -.

Other

22380; -.

Q05397; -.

PTK2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell junction; Cell membrane; Direct protein sequencing; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Transferase; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 1052`	`1051`	`Focal adhesion kinase 1.`	`PRO_0000088077`
`DOMAIN`	`35 355`	`321`	`FERM.`
`DOMAIN`	`422 680`	`259`	`Protein kinase.`
`NP_BIND`	`428 436`	`9`	`ATP (By similarity).`
`REGION`	`707 1052`	`346`	`Interaction with TGFB1I1.`
`REGION`	`912 1052`	`141`	`Interaction with RGNEF (By similarity).`
`COMPBIAS`	`712 733`	`22`	`Pro-rich.`
`COMPBIAS`	`863 913`	`51`	`Pro-rich.`
`ACT_SITE`	`546 546`		`Proton acceptor (By similarity).`
`BINDING`	`454 454`		`ATP (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`13 13`		`Phosphothreonine.`
`MOD_RES`	`29 29`		`Phosphoserine.`
`MOD_RES`	`397 397`		`Phosphotyrosine.`
`MOD_RES`	`407 407`		`Phosphotyrosine.`
`MOD_RES`	`568 568`		`Phosphoserine.`
`MOD_RES`	`570 570`		`Phosphotyrosine.`
`MOD_RES`	`576 576`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`577 577`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`722 722`		`Phosphoserine.`
`MOD_RES`	`840 840`		`Phosphoserine.`
`MOD_RES`	`843 843`		`Phosphoserine.`
`MOD_RES`	`861 861`		`Phosphotyrosine.`
`MOD_RES`	`887 887`		`Phosphoserine.`
`MOD_RES`	`910 910`		`Phosphoserine.`
`MOD_RES`	`925 925`		`Phosphotyrosine.`
`VAR_SEQ`	`1 181`		`Missing (in isoform 2, isoform 3 and isoform 4).`	`VSP_004967`
`VAR_SEQ`	`182 189`		`EMRGNALE -> MSDYWVVG (in isoform 2, isoform 3 and isoform 4).`	`VSP_004968`
`VAR_SEQ`	`472 472`		`A -> ACHYTSLHWNWCRYISDPNVDACPDPRNAE (in isoform 2, isoform 3 and isoform 4).`	`VSP_004969`
`VAR_SEQ`	`579 583`		`ASKGK -> GKKSG (in isoform 4).`	`VSP_004971`
`VAR_SEQ`	`584 1052`		`Missing (in isoform 4).`	`VSP_004972`
`VAR_SEQ`	`677 706`		`STILEEEKAQQEERMRMESRRQATVSWDSG -> FQNPAQMLPASGRLPNQPCPERENYSFATF (in isoform 3).`	`VSP_004973`
`VAR_SEQ`	`707 1052`		`Missing (in isoform 3).`	`VSP_004974`
`VAR_SEQ`	`834 854`		`Missing (in isoform 2).`	`VSP_004970`
`VARIANT`	`292 292`	`1`	`H -> P.`	`VAR_041682`
`VARIANT`	`292 292`	`1`	`H -> Q.`	`VAR_041683`
`VARIANT`	`793 793`	`1`	`V -> A (in a glioblastoma multiforme sample; somatic mutation).`	`VAR_041684`
`VARIANT`	`1030 1030`	`1`	`D -> E.`	`VAR_041685 [3D]`
`VARIANT`	`1044 1044`	`1`	`K -> E (in a metastatic melanoma sample; somatic mutation).`	`VAR_041686 [3D]`
`MUTAGEN`	`928 928`		`V->G: Loss of interaction with TGFB1I1.`
`MUTAGEN`	`1034 1034`		`L->S: Loss of interaction with TGFB1I1.`
`CONFLICT`	`778 778`		`P -> S (in Ref. 2; AAA35819).`
`HELIX`	`419 421`	`3`
`STRAND`	`422 430`	`9`
`STRAND`	`432 441`	`10`
`STRAND`	`449 455`	`7`
`TURN`	`457 460`	`4`
`HELIX`	`462 476`	`15`
`STRAND`	`486 490`	`5`
`STRAND`	`492 494`	`3`
`STRAND`	`496 500`	`5`
`HELIX`	`507 513`	`7`
`TURN`	`514 517`	`4`
`HELIX`	`520 539`	`20`
`HELIX`	`549 551`	`3`
`STRAND`	`552 556`	`5`
`STRAND`	`559 562`	`4`
`HELIX`	`586 588`	`3`
`HELIX`	`591 596`	`6`
`HELIX`	`601 616`	`16`
`TURN`	`622 625`	`4`
`HELIX`	`628 630`	`3`
`HELIX`	`631 636`	`6`
`HELIX`	`649 658`	`10`
`HELIX`	`663 665`	`3`
`HELIX`	`669 685`	`17`
`STRAND`	`915 917`	`3`
`HELIX`	`923 942`	`20`
`HELIX`	`947 949`	`3`
`HELIX`	`950 971`	`22`
`HELIX`	`972 974`	`3`
`HELIX`	`977 979`	`3`
`HELIX`	`980 1006`	`27`
`TURN`	`1007 1009`	`3`
`STRAND`	`1010 1012`	`3`
`HELIX`	`1013 1045`	`33`

Sequence information

Length: 1052 AA [This is the length of the unprocessed precursor]

Molecular weight: 119233 Da [This is the MW of the unprocessed precursor]

CRC64: D8A4C15138AB0243 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAYLDPNL NHTPNSSTKT HLGTGMERSP GAMERVLKVF HYFESNSEPT TWASIIRHGD 

        70         80         90        100        110        120 
ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW 

       130        140        150        160        170        180 
KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMLEIA DQVDQEIALK LGCLEIRRSY 

       190        200        210        220        230        240 
WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI 

       250        260        270        280        290        300 
LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFTQVQ 

       310        320        330        340        350        360 
TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGTSQSFII 

       370        380        390        400        410        420 
RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSETDDYAEI IDEEDTYTMP STRDYEIQRE 

       430        440        450        460        470        480 
RIELGRCIGE GQFGDVHQGI YMSPENPALA VAIKTCKNCT SDSVREKFLQ EALTMRQFDH 

       490        500        510        520        530        540 
PHIVKLIGVI TENPVWIIME LCTLGELRSF LQVRKYSLDL ASLILYAYQL STALAYLESK 

       550        560        570        580        590        600 
RFVHRDIAAR NVLVSSNDCV KLGDFGLSRY MEDSTYYKAS KGKLPIKWMA PESINFRRFT 

       610        620        630        640        650        660 
SASDVWMFGV CMWEILMHGV KPFQGVKNND VIGRIENGER LPMPPNCPPT LYSLMTKCWA 

       670        680        690        700        710        720 
YDPSRRPRFT ELKAQLSTIL EEEKAQQEER MRMESRRQAT VSWDSGGSDE APPKPSRPGY 

       730        740        750        760        770        780 
PSPRSSEGFY PSPQHMVQTN HYQVSGYPGS HGITAMAGSI YPGQASLLDQ TDSWNHRPQE 

       790        800        810        820        830        840 
IAMWQPNVED STVLDLRGIG QVLPTHLMEE RLIRQQQEME EDQRWLEKEE RFLKPDVRLS 

       850        860        870        880        890        900 
RGSIDREDGS LQGPIGNQHI YQPVGKPDPA APPKKPPRPG APGHLGSLAS LSSPADSYNE 

       910        920        930        940        950        960 
GVKLQPQEIS PPPTANLDRS NDKVYENVTG LVKAVIEMSS KIQPAPPEEY VPMVKEVGLA 

       970        980        990       1000       1010       1020 
LRTLLATVDE TIPLLPASTH REIEMAQKLL NSDLGELINK MKLAQQYVMT SLQQEYKKQM 

      1030       1040       1050 
LTAAHALAVD AKNLLDVIDQ ARLKMLGQTR PH

Q05397 in FASTA format

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