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UniProtKB/Swiss-Prot entry Q14289


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

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Entry information
Entry name FAK2_HUMAN
Primary accession number Q14289
Secondary accession numbers Q13475 Q14290 Q16709
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 15, 1998 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 111)
Name and origin of the protein
Protein name Protein tyrosine kinase 2 beta
Synonyms EC 2.7.10.2
Focal adhesion kinase 2
FADK 2
Proline-rich tyrosine kinase 2
Cell adhesion kinase beta
CAK beta
Calcium-dependent tyrosine kinase
CADTK
Related adhesion focal tyrosine kinase
RAFTK
Gene name
Name: PTK2B
Synonyms: FAK2, PYK2, RAFTK
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 1).
TISSUE=Brain;
DOI=10.1038/376737a0; PubMed=7544443 [NCBI, ExPASy, EBI, Israel, Japan]
Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.;
"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions.";
Nature 376:737-745(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
DOI=10.1006/geno.1996.0149; PubMed=8838818 [NCBI, ExPASy, EBI, Israel, Japan]
Herzog H., Nicholl J., Hort Y.J., Sutherland G.R., Shine J.;
"Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization.";
Genomics 32:484-486(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
DOI=10.1074/jbc.270.36.21206; PubMed=7673154 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki H., Nagura K., Ishino M., Tobioka H., Kotani K., Sasaki T.;
"Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily.";
J. Biol. Chem. 270:21206-21219(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1074/jbc.270.46.27742; PubMed=7499242 [NCBI, ExPASy, EBI, Israel, Japan]
Avraham S., London R., Fu Y., Ota S., Hiregowdara D., Li J., Jiang S., Pasztor L.M., White R.A., Groopman J.E., Avraham H.;
"Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain.";
J. Biol. Chem. 270:27742-27751(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Monocyte;
DOI=10.1074/jbc.273.16.9361; PubMed=9545257 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Hunter D., Morris J., Haskill J.S., Earp H.S.;
"A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal.";
J. Biol. Chem. 273:9361-9364(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04406; PubMed=16421571 [NCBI, ExPASy, EBI, Israel, Japan]
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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).
[8]
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).
[9]
INTERACTION WITH ASAP2.
PubMed=10022920 [NCBI, ExPASy, EBI, Israel, Japan]
Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G., Randazzo P.A., Schlessinger J.;
"Identification of a new Pyk2 target protein with Arf-GAP activity.";
Mol. Cell. Biol. 19:2338-2350(1999).
[10]
PHOSPHORYLATION AT TYR-402, MUTAGENESIS OF PRO-859, AND INTERACTION WITH NEPHROCYSTIN.
DOI=10.1073/pnas.171269898; PubMed=11493697 [NCBI, ExPASy, EBI, Israel, Japan]
Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
"Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2.";
Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
[11]
INTERACTION WITH SKAP2, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1074/jbc.M213217200; PubMed=12893833 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H., Avraham S., Yasuda M., Matsumoto M.;
"Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation.";
J. Biol. Chem. 278:42225-42233(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-579 AND TYR-580, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan]
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-579 AND TYR-580, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375 AND TYR-579, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-399; SER-758; SER-762; THR-765; SER-839 AND THR-842, 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).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[18]
VARIANTS [LARGE SCALE ANALYSIS] GLU-359; HIS-698; PRO-808; THR-838 AND LYS-970.
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: Involved in calcium induced regulation of ion channel and activation of the map kinase signaling pathway. May represent an important signaling intermediate between neuropeptide activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity. Interacts with the SH2 domain of Grb2. May phosphorylate the voltage-gated potassium channel protein Kv1.2. Its activation is highly correlated with the stimulation of c-Jun N-terminal kinase activity. Involved in osmotic stress-dependent SNCA 'Tyr-125' phosphorylation.
  • CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
  • SUBUNIT: Interacts with Crk-associated substrate (Cas), PTPNS1 and SH2D3C (By similarity). Interacts with nephrocystin, ASAP2, OPHN1L, SKAP2 and TGFB1I1.
  • INTERACTION:
    Q7L0Q8:RHOU; NbExp=4; IntAct=EBI-298640, EBI-1638043;
  • SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Interaction with nephrocystin induces the membrane-association of the kinase.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ14289-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ14289-2
    Features which should be applied to build the isoform sequence: VSP_004981.
  • TISSUE SPECIFICITY: Most abundant in the brain, with highest levels in amygdala and hippocampus. Low levels in kidney. Also expressed in spleen and lymphocytes.
  • PTM: Phosphorylated on tyrosine residues in response to various stimuli that elevate the intracellular calcium concentration, as well as by PKC activation. Recruitment by nephrocystin to cell matrix adhesions initiates Tyr-402 phosphorylation. In monocytes, adherence to substrata is required for tyrosine phosphorylation and kinase activation. Angiotensin II, thapsigargin and L-alpha-lysophosphatidic acid (LPA) also induce autophosphorylation and increase kinase activity (By similarity).
  • 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
U33284; AAC50203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L49207; AAB47217.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D45853; BAA08289.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U43522; AAC05330.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S80542; AAB35701.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC042599; AAH42599.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00029702; -.
IPI00216435; -.
PIR S60248; S60248.
RefSeq NP_004094.3; -.
NP_775266.1; -.
NP_775267.1; -.
NP_775268.1; -.
UniGene Hs.491322
3D structure databases
PDB
2FO6; Model; -; X=45-350.[ExPASy / RCSB / EBI]
3CC6; X-ray; 1.60 A; A=414-692.[ExPASy / RCSB / EBI]
3FZO; X-ray; 2.20 A; A=416-692.[ExPASy / RCSB / EBI]
3FZP; X-ray; 2.10 A; A=416-692.[ExPASy / RCSB / EBI]
3FZR; X-ray; 2.70 A; A=416-692.[ExPASy / RCSB / EBI]
3FZS; X-ray; 1.75 A; A=416-692.[ExPASy / RCSB / EBI]
3FZT; X-ray; 1.95 A; A=416-692.[ExPASy / RCSB / EBI]
3GM1; X-ray; 2.95 A; A/B=861-1009.[ExPASy / RCSB / EBI]
3GM2; X-ray; 2.71 A; A=861-1009.[ExPASy / RCSB / EBI]
3GM3; X-ray; 2.60 A; A=861-1009.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2FO6; -.
3CC6; -.
3FZO; -.
3FZP; -.
3FZR; -.
3FZS; -.
3FZT; -.
3GM1; -.
3GM2; -.
3GM3; -.
ModBase Q14289.
Protein-protein interaction databases
IntAct Q14289; 8.
PTM databases
PhosphoSite Q14289; -.
Enzyme and pathway databases
BRENDA 2.7.10.2; 247.
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
ar_pathway; Coregulation of Androgen receptor activity.
endothelinpathway; Endothelins.
fgf_pathway; FGF signaling pathway.
il2_1pathway; IL2-mediated signaling events.
avb3_integrin_pathway; Integrins in angiogenesis.
lysophospholipid_pathway; LPA receptor mediated events.
avb3_opn_pathway; Osteopontin-mediated events.
met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
Organism-specific databases
GeneCards GC08P027224; -.
H-InvDB HIX0025557; -.
HGNC HGNC:9612; PTK2B.
GenAtlas PTK2B.
HPA CAB003850; -.
MIM 601212; gene. [NCBI / EBI]
PharmGKB PA33956; -.
Gene expression databases
ArrayExpress Q14289; -.
Bgee Q14289; -.
CleanEx HS_PTK2B; -.
GermOnline ENSG00000120899; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005856; Cellular component: cytoskeleton (inferred from electronic annotation from InterPro).
GO:0005925; Cellular component: focal adhesion (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004715; Molecular function: non-membrane spanning protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004871; Molecular function: signal transducer activity (non-traceable author statement from ProtInc).
GO:0006915; Biological process: apoptosis (traceable author statement from ProtInc).
GO:0008284; Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0006950; Biological process: response to stress (traceable author statement from ProtInc).
GO:0007172; Biological process: signal complex assembly (traceable author statement from ProtInc).
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; FALSE_NEG.
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 Q14289; -.
Genome annotation databases
Ensembl ENSG00000120899; Homo sapiens. [Contig view]
GeneID 2185; -.
KEGG hsa:2185; -.
Phylogenomic databases
HOGENOM Q14289; -.
HOVERGEN Q14289; -.
OMA Q14289; VKTCKKD.
Other
NextBio 8821; -.
SOURCE PTK2B; Homo sapiens.
ProtoNet Q14289.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1009  1009     Protein tyrosine kinase 2 beta. PRO_0000088081
DOMAIN   39    359  321     FERM. 
DOMAIN   425    683  259     Protein kinase. 
NP_BIND   431    439  9     ATP (By similarity). 
REGION   801   1009  209     Interaction with TGFB1I1 (By similarity). 
REGION   868   1009  142     Focal adhesion targeting (FAT). 
COMPBIAS   702    767  66     Pro-rich. 
COMPBIAS   831    869  39     Pro-rich. 
ACT_SITE   549    549        Proton acceptor (By similarity). 
BINDING   457    457        ATP (By similarity). 
MOD_RES   375    375        Phosphoserine. 
MOD_RES   399    399        Phosphoserine. 
MOD_RES   402    402        Phosphotyrosine. 
MOD_RES   440    440        Phosphotyrosine (By similarity). 
MOD_RES   579    579        Phosphotyrosine; by autocatalysis. 
MOD_RES   580    580        Phosphotyrosine. 
MOD_RES   758    758        Phosphoserine. 
MOD_RES   762    762        Phosphoserine. 
MOD_RES   765    765        Phosphothreonine. 
MOD_RES   839    839        Phosphoserine. 
MOD_RES   842    842        Phosphothreonine. 
MOD_RES   881    881        Phosphotyrosine (By similarity). 
VAR_SEQ   739    780        Missing (in isoform 2). VSP_004981
VARIANT   359    359  1     Q -> E. VAR_041687 
VARIANT   698    698  1     R -> H. VAR_041688 
VARIANT   808    808  1     L -> P. VAR_041689 
VARIANT   838    838  1     K -> T (in dbSNP:rs751019 [NCBI]). VAR_020284 
VARIANT   970    970  1     E -> K. VAR_041690 
MUTAGEN   859    859        P->A: Loss of interaction with nephrocystin. 
CONFLICT   23     23        A -> G (in Ref. 3; BAA08289/AAC05330). 
CONFLICT   256    256        G -> P (in Ref. 2; AAB47217). 
CONFLICT   435    435        F -> L (in Ref. 3; AAC05330). 
CONFLICT   780    780        R -> G (in Ref. 2; AAB47217). 
HELIX   422    424  3      
STRAND   425    433  9      
STRAND   435    445  11      
STRAND   451    458  8      
HELIX   465    481  17      
STRAND   489    493  5      
STRAND   495    497  3      
STRAND   499    503  5      
HELIX   510    517  8      
TURN   518    520  3      
HELIX   523    542  20      
HELIX   552    554  3      
STRAND   555    559  5      
STRAND   562    565  4      
HELIX   570    572  3      
HELIX   589    591  3      
HELIX   594    599  6      
HELIX   604    619  16      
TURN   620    622  3      
TURN   625    628  4      
HELIX   631    633  3      
HELIX   634    640  7      
HELIX   652    661  10      
HELIX   666    668  3      
HELIX   672    691  20      
Sequence information
Length: 1009 AA [This is the length of the unprocessed precursor] Molecular weight: 115875 Da [This is the MW of the unprocessed precursor] CRC64: 420B21046274E7C2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGVSEPLSR VKLGTLRRPE GPAEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK 

        70         80         90        100        110        120 
CTVQTEIREI ITSILLSGRI GPNIRLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC 

       130        140        150        160        170        180 
LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC 

       190        200        210        220        230        240 
LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS 

       250        260        270        280        290        300 
LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDAKPTCLA 

       310        320        330        340        350        360 
EFKQIRSIRC LPLEEGQAVL QLGIEGAPQA LSIKTSSLAE AENMADLIDG YCRLQGEHQG 

       370        380        390        400        410        420 
SLIIHPRKDG EKRNSLPQIP MLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGI 

       430        440        450        460        470        480 
AREDVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTLDNKEK FMSEAVIMKN 

       490        500        510        520        530        540 
LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVLTLVLYS LQICKAMAYL 

       550        560        570        580        590        600 
ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR 

       610        620        630        640        650        660 
RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPDLC PPVLYTLMTR 

       670        680        690        700        710        720 
CWDYDPSDRP RFTELVCSLS DVYQMEKDIA MEQERNARYR TPKILEPTAF QEPPPKPSRP 

       730        740        750        760        770        780 
KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR 

       790        800        810        820        830        840 
EEDFIQPSSR EEAQQLWEAE KVKMRQILDK QQKQMVEDYQ WLRQEEKSLD PMVYMNDKSP 

       850        860        870        880        890        900 
LTPEKEVGYL EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YLNVMELVRA VLELKNELCQ 

       910        920        930        940        950        960 
LPPEGYVVVV KNVGLTLRKL IGSVDDLLPS LPSSSRTEIE GTQKLLNKDL AELINKMRLA 

       970        980        990       1000 
QQNAVTSLSE ECKRQMLTAS HTLAVDAKNL LDAVDQAKVL ANLAHPPAE 

Q14289 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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