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UniProtKB/Swiss-Prot entry Q12830


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

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Entry information
Entry name BPTF_HUMAN
Primary accession number Q12830
Secondary accession numbers Q6NX67 Q7Z7D6 Q9UIG2
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on November 25, 2008 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 84)
Name and origin of the protein
Protein name Nucleosome-remodeling factor subunit BPTF
Synonyms Bromodomain and PHD finger-containing transcription factor
Fetal Alzheimer antigen
Fetal Alz-50 clone 1 protein
Gene name
Name: BPTF
Synonyms: FAC1, FALZ
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 2), AND TISSUE SPECIFICITY.
DOI=10.1006/geno.1999.6070; PubMed=10662542 [NCBI, ExPASy, EBI, Israel, Japan]
Jones M.H., Hamana N., Shimane M.;
"Identification and characterization of BPTF, a novel bromodomain transcription factor.";
Genomics 63:35-39(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04689; PubMed=16625196 [NCBI, ExPASy, EBI, Israel, Japan]
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 134-992 (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=7621746 [NCBI, ExPASy, EBI, Israel, Japan]
Bowser R., Giambrone A., Davies P.;
"FAC1, a novel gene identified with the monoclonal antibody Alz50, is developmentally regulated in human brain.";
Dev. Neurosci. 17:20-37(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 140-3046 (ISOFORM 4), IDENTIFICATION IN THE NURF COMPLEX, AND MASS SPECTROMETRY.
DOI=10.1093/emboj/cdg582; PubMed=14609955 [NCBI, ExPASy, EBI, Israel, Japan]
Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R.;
"Isolation of human NURF: a regulator of Engrailed gene expression.";
EMBO J. 22:6089-6100(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2876-3046 (ISOFORM 1).
TISSUE=Kidney;
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).
[6]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
DOI=10.1006/exnr.1997.6508; PubMed=9225734 [NCBI, ExPASy, EBI, Israel, Japan]
Mu X., Springer J.E., Bowser R.;
"FAC1 expression and localization in motor neurons of developing, adult, and amyotrophic lateral sclerosis spinal cord.";
Exp. Neurol. 146:17-24(1997).
[7]
DNA-BINDING, AND PHOSPHORYLATION.
DOI=10.1006/bbrc.1999.0986; PubMed=10403843 [NCBI, ExPASy, EBI, Israel, Japan]
Jordan-Sciutto K.L., Dragich J.M., Bowser R.;
"DNA binding activity of the fetal Alz-50 clone 1 (FAC1) protein is enhanced by phosphorylation.";
Biochem. Biophys. Res. Commun. 260:785-789(1999).
[8]
DNA-BINDING.
DOI=10.1074/jbc.274.49.35262; PubMed=10575013 [NCBI, ExPASy, EBI, Israel, Japan]
Jordan-Sciutto K.L., Dragich J.M., Rhodes J.L., Bowser R.;
"Fetal Alz-50 clone 1, a novel zinc finger protein, binds a specific DNA sequence and acts as a transcriptional regulator.";
J. Biol. Chem. 274:35262-35268(1999).
[9]
INTERACTION WITH MAZ, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
DOI=10.1021/bi992211q; PubMed=10727212 [NCBI, ExPASy, EBI, Israel, Japan]
Jordan-Sciutto K.L., Dragich J.M., Caltagarone J., Hall D.J., Bowser R.;
"Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-associated zinc finger protein (ZF87/MAZ) and alters its transcriptional activity.";
Biochemistry 39:3206-3215(2000).
[10]
INTERACTION WITH KEAP1, AND SUBCELLULAR LOCATION.
DOI=10.1021/bi0494166; PubMed=15379550 [NCBI, ExPASy, EBI, Israel, Japan]
Strachan G.D., Morgan K.L., Otis L.L., Caltagarone J., Gittis A., Bowser R., Jordan-Sciutto K.L.;
"Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated protein.";
Biochemistry 43:12113-12122(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-572; THR-1064; SER-1827 AND SER-1833, 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).
[13]
INTERACTION WITH HISTONE H3-K4ME3, MUTAGENESIS OF TRP-2891, AND MASS SPECTROMETRY.
DOI=10.1038/nature04815; PubMed=16728976 [NCBI, ExPASy, EBI, Israel, Japan]
Wysocka J., Swigut T., Xiao H., Milne T.A., Kwon S.Y., Landry J., Kauer M., Tackett A.J., Chait B.T., Badenhorst P., Wu C., Allis C.D.;
"A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling.";
Nature 442:86-90(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-839, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-763; SER-1300 AND SER-2098, 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).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2865-3033, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME3, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2865-3033 IN COMPLEX WITH H3(1-154)K4ME2, STRUCTURE BY NMR OF 2865-2922, STRUCTURE BY NMR OF 2865-2922 IN COMPLEX WITH H3(1-154)K4ME3, AND MUTAGENESIS OF TYR-2869; TYR-2876; TYR-2882; GLY-2884; ASP-2886; GLN-2889 AND TRP-2891.
DOI=10.1038/nature04802; PubMed=16728978 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Ilin S., Wang W., Duncan E.M., Wysocka J., Allis C.D., Patel D.J.;
"Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF.";
Nature 442:91-95(2006).
Comments
  • FUNCTION: Histone-binding component of NURF (nucleosome-remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin. Specifically recognizes H3 tails trimethylated on 'Lys-4' (H3-K4Me3), which mark transcription start sites of virtually all active genes. May also regulate transcription through direct binding to DNA or transcription factors.
  • SUBUNIT: Interacts with MAZ. Interacts with KEAP1. Part of the nucleosome-remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with histone H3-K4Me3 and to a lesser extent with histone H3-K4Me2.
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In brains of Alzheimer disease patients, present in a subset of amyloid-containing plaques.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ12830-1
    Note: No experimental confirmation exists.
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ12830-2
    Features which should be applied to build the isoform sequence: VSP_020402.
    Name4
    Isoform IDQ12830-4
    Features which should be applied to build the isoform sequence: VSP_020405.
  • TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in testis. Present in kidney, liver and brain. In the brain, highest levels are found in motor cortex (at protein level).
  • DEVELOPMENTAL STAGE: Abundantly expressed in the fetal brain. Present throughout the gray and white matter of the developing spinal cord at 18-22 gestational weeks. Expressed at low levels in adult brain and spinal cord and reexpressed in neurodegenerative diseases (at protein level).
  • DOMAIN: The second PHD-type zinc finger mediates binding to histone H3-K4Me3.
  • PTM: Phosphorylation enhances DNA-binding. Phosphorylated upon DNA damage, probably by ATM or ATR.
  • MISCELLANEOUS: Highly susceptible to proteolysis.
  • SIMILARITY: Belongs to the PBTF family.
  • SIMILARITY: Contains 1 bromo domain.
  • SIMILARITY: Contains 1 DDT domain.
  • SIMILARITY: Contains 2 PHD-type zinc fingers.
  • SEQUENCE CAUTION:
    • Sequence=AAA97522.1; Type=Frameshift; Positions=136, 915;
    • Sequence=AAA97522.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors
    • Sequence=BAA89208.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors in the N-terminal part
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
AB032251; BAA89208.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006534; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC107377; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC134407; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
U05237; AAA97522.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY282495; AAP22284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067234; AAH67234.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00254408; -.
IPI00376404; -.
IPI00785110; -.
PIR G01252; G01252.
RefSeq NP_004450.3; -.
NP_872579.2; -.
UniGene Hs.444200
3D structure databases
PDB
2F6J; X-ray; 2.00 A; A/B/C=2865-3033.[ExPASy / RCSB / EBI]
2F6N; X-ray; 2.00 A; A/B=2865-3033.[ExPASy / RCSB / EBI]
2FSA; X-ray; 1.90 A; A/B/C=2865-3033.[ExPASy / RCSB / EBI]
2FUI; NMR; -; A=2865-2921.[ExPASy / RCSB / EBI]
2FUU; NMR; -; A=2865-2921.[ExPASy / RCSB / EBI]
2RI7; X-ray; 1.45 A; A=2865-3033.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2F6J; -.
2F6N; -.
2FSA; -.
2FUI; -.
2FUU; -.
2RI7; -.
ModBase Q12830.
PTM databases
PhosphoSite Q12830; -.
Organism-specific databases
GeneCards GC17P063253; -.
H-InvDB HIX0020770; -.
HGNC HGNC:3581; BPTF.
GenAtlas BPTF.
MIM 601819; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress Q12830; -.
Bgee Q12830; -.
CleanEx HS_BPTF; -.
GermOnline ENSG00000171634; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HGNC).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from direct assay from HGNC).
GO:0008134; Molecular function: transcription factor binding (inferred from direct assay from MGI).
GO:0030528; Molecular function: transcription regulator activity (inferred from mutant phenotype from HGNC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007420; Biological process: brain development (inferred from mutant phenotype from HGNC).
GO:0006338; Biological process: chromatin remodeling (inferred from direct assay from HGNC).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0043193; Biological process: positive regulation of gene-specific transcription (inferred from mutant phenotype from HGNC).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001487; Bromodomain.
IPR012644; CHP_FYDLN_acid.
IPR004022; DDT_family.
IPR018501; DDT_superfamily.
IPR019787; Znf_PHD-finger.
Graphical view of domain structure.
Pfam PF00439; Bromodomain; 1.
PF02791; DDT; 1.
PF09538; FYDLN_acid; 1.
PF00628; PHD; 2.
Pfam graphical view of domain structure.
PROSITE PS00633; BROMODOMAIN_1; 1.
PS50014; BROMODOMAIN_2; 1.
PS50827; DDT; 1.
PS01359; ZF_PHD_1; 2.
PS50016; ZF_PHD_2; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000171634; Homo sapiens. [Contig view]
GeneID 2186; -.
KEGG hsa:2186; -.
Phylogenomic databases
HOVERGEN Q12830; -.
OMA Q12830; FHLRTSY.
Other
NextBio 8831; -.
SOURCE BPTF; Homo sapiens.
ProtoNet Q12830.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Bromodomain; Chromatin regulator; Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   3046  3046     Nucleosome-remodeling factor subunit BPTF. PRO_0000087176
DOMAIN   240    300  61     DDT. 
DOMAIN   2944   3014  71     Bromo. 
ZN_FING   390    437  48     PHD-type 1. 
ZN_FING   2867   2918  52     PHD-type 2. 
REGION   640    749  110     Interaction with KEAP1. 
REGION   839    921  83     Interaction with MAZ. 
COILED   574    604  31     Potential. 
COILED   978   1007  30     Potential. 
COILED   2022   2050  29     Potential. 
COILED   2706   2732  27     Potential. 
COMPBIAS   143    180  38     Glu-rich. 
COMPBIAS   149    185  37     Asp-rich. 
COMPBIAS   1709   1803  95     Thr-rich. 
COMPBIAS   2338   2361  24     Thr-rich. 
COMPBIAS   2795   2817  23     Pro-rich. 
COMPBIAS   2848   2853  6     Poly-Lys. 
BINDING   2869   2869        Histone H3-K4Me3. 
BINDING   2876   2876        Histone H3-K4Me3. 
BINDING   2882   2882        Histone H3-K4Me3. 
BINDING   2891   2891        Histone H3-K4Me3. 
MOD_RES   216    216        Phosphoserine. 
MOD_RES   572    572        Phosphoserine. 
MOD_RES   763    763        Phosphoserine. 
MOD_RES   817    817        Phosphoserine. 
MOD_RES   839    839        Phosphotyrosine. 
MOD_RES   1064   1064        Phosphothreonine. 
MOD_RES   1300   1300        Phosphoserine. 
MOD_RES   1827   1827        Phosphoserine. 
MOD_RES   1833   1833        Phosphoserine. 
MOD_RES   2098   2098        Phosphoserine. 
VAR_SEQ   622    747        Missing (in isoform 2). VSP_020402
VAR_SEQ   2522   2664        Missing (in isoform 4). VSP_020405
MUTAGEN   2869   2869        Y->T: Abolishes binding to histone H3-K4Me3. 
MUTAGEN   2876   2876        Y->T: Strongly reduces binding to histone H3-K4Me3. 
MUTAGEN   2882   2882        Y->S: Abolishes binding to histone H3-K4Me3. 
MUTAGEN   2884   2884        G->E,L: Strongly reduces binding to histone H3-K4Me3. 
MUTAGEN   2886   2886        D->N,A: Abolishes binding to histone H3-K4Me3. 
MUTAGEN   2889   2889        Q->K: Strongly reduces binding to histone H3-K4Me3. 
MUTAGEN   2891   2891        W->E,F: Abolishes binding to histone H3-K4Me3. 
CONFLICT   752    752        K -> T (in Ref. 3; AAA97522). 
CONFLICT   757    757        N -> T (in Ref. 3; AAA97522). 
CONFLICT   969    969        S -> F (in Ref. 1; BAA89208). 
CONFLICT   1268   1268        E -> Q (in Ref. 1; BAA89208). 
CONFLICT   1330   1330        S -> T (in Ref. 1; BAA89208). 
CONFLICT   1842   1842        S -> T (in Ref. 1; BAA89208 and 4; AAP22284). 
CONFLICT   1926   1926        A -> V (in Ref. 1; BAA89208 and 4; AAP22284). 
CONFLICT   1932   1932        T -> S (in Ref. 1; BAA89208 and 4; AAP22284). 
CONFLICT   1960   1960        S -> F (in Ref. 1; BAA89208). 
CONFLICT   2393   2393        E -> K (in Ref. 1; BAA89208). 
CONFLICT   2404   2404        Q -> R (in Ref. 1; BAA89208). 
CONFLICT   2540   2540        T -> S (in Ref. 1; BAA89208). 
CONFLICT   2802   2803        AP -> VL (in Ref. 1; BAA89208). 
CONFLICT   2818   2818        A -> G (in Ref. 1; BAA89208). 
CONFLICT   2832   2832        A -> V (in Ref. 1; BAA89208). 
CONFLICT   2876   2876        Y -> G (in Ref. 5; AAH67234). 
CONFLICT   2880   2880        K -> Q (in Ref. 5; AAH67234). 
TURN   2870   2873  4      
STRAND   2882   2884  3      
TURN   2886   2888  3      
STRAND   2891   2893  3      
HELIX   2895   2897  3      
HELIX   2901   2905  5      
HELIX   2913   2922  10      
TURN   2923   2925  3      
HELIX   2930   2945  16      
HELIX   2947   2952  6      
TURN   2958   2960  3      
HELIX   2964   2967  4      
HELIX   2974   2982  9      
HELIX   2989   3006  18      
HELIX   3012   3028  17      
Sequence information
Length: 3046 AA [This is the length of the unprocessed precursor] Molecular weight: 338262 Da [This is the MW of the unprocessed precursor] CRC64: 37D7206977A8DB09 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRGRRGRPPK QPAAPAAERC APAPPPPPPP PTSGPIGGLR SRHRGSSRGR WAAAQAEVAP 

        70         80         90        100        110        120 
KTRLSSPRGG SSSRRKPPPP PPAPPSTSAP GRGGRGGGGG RTGGGGGGGH LARTTAARRA 

       130        140        150        160        170        180 
VNKVVYDDHE SEEEEEEEDM VSEEEEEEDG DAEETQDSED DEEDEMEEDD DDSDYPEEME 

       190        200        210        220        230        240 
DDDDDASYCT ESSFRSHSTY SSTPGRRKPR VHRPRSPILE EKDIPPLEFP KSSEDLMVPN 

       250        260        270        280        290        300 
EHIMNVIAIY EVLRNFGTVL RLSPFRFEDF CAALVSQEQC TLMAEMHVVL LKAVLREEDT 

       310        320        330        340        350        360 
SNTTFGPADL KDSVNSTLYF IDGMTWPEVL RVYCESDKEY HHVLPYQEAE DYPYGPVENK 

       370        380        390        400        410        420 
IKVLQFLVDQ FLTTNIAREE LMSEGVIQYD DHCRVCHKLG DLLCCETCSA VYHLECVKPP 

       430        440        450        460        470        480 
LEEVPEDEWQ CEVCVAHKVP GVTDCVAEIQ KNKPYIRHEP IGYDRSRRKY WFLNRRLIIE 

       490        500        510        520        530        540 
EDTENENEKK IWYYSTKVQL AELIDCLDKD YWEAELCKIL EEMREEIHRH MDITEDLTNK 

       550        560        570        580        590        600 
ARGSNKSFLA AANEEILESI RAKKGDIDNV KSPEETEKDK NETENDSKDA EKNREEFEDQ 

       610        620        630        640        650        660 
SLEKDSDDKT PDDDPEQGKS EEPTEVGDKG NSVSANLGDN TTNATSEETS PSEGRSPVGC 

       670        680        690        700        710        720 
LSETPDSSNM AEKKVASELP QDVPEEPNKT CESSNTSATT TSIQPNLENS NSSSELNSSQ 

       730        740        750        760        770        780 
SESAKAADDP ENGERESHTP VSIQEEIVGD FKSEKSNGEL SESPGAGKGA SGSTRIITRL 

       790        800        810        820        830        840 
RNPDSKLSQL KSQQVAAAAH EANKLFKEGK EVLVVNSQGE ISRLSTKKEV IMKGNINNYF 

       850        860        870        880        890        900 
KLGQEGKYRV YHNQYSTNSF ALNKHQHRED HDKRRHLAHK FCLTPAGEFK WNGSVHGSKV 

       910        920        930        940        950        960 
LTISTLRLTI TQLENNIPSS FLHPNWASHR ANWIKAVQMC SKPREFALAL AILECAVKPV 

       970        980        990       1000       1010       1020 
VMLPIWRESL GHTRLHRMTS IEREEKEKVK KKEKKQEEEE TMQQATWVKY TFPVKHQVWK 

      1030       1040       1050       1060       1070       1080 
QKGEEYRVTG YGGWSWISKT HVYRFVPKLP GNTNVNYRKS LEGTKNNMDE NMDESDKRKC 

      1090       1100       1110       1120       1130       1140 
SRSPKKIKIE PDSEKDEVKG SDAAKGADQN EMDISKITEK KDQDVKELLD SDSDKPCKEE 

      1150       1160       1170       1180       1190       1200 
PMEVDDDMKT ESHVNCQESS QVDVVNVSEG FHLRTSYKKK TKSSKLDGLL ERRIKQFTLE 

      1210       1220       1230       1240       1250       1260 
EKQRLEKIKL EGGIKGIGKT STNSSKNLSE SPVITKAKEG CQSDSMRQEQ SPNANNDQPE 

      1270       1280       1290       1300       1310       1320 
DLIQGCSESD SSVLRMSDPS HTTNKLYPKD RVLDDVSIRS PETKCPKQNS IENDIEEKVS 

      1330       1340       1350       1360       1370       1380 
DLASRGQEPS KSKTKGNDFF IDDSKLASAD DIGTLICKNK KPLIQEESDT IVSSSKSALH 

      1390       1400       1410       1420       1430       1440 
SSVPKSTNDR DATPLSRAMD FEGKLGCDSE SNSTLENSSD TVSIQDSSEE DMIVQNSNES 

      1450       1460       1470       1480       1490       1500 
ISEQFRTREQ DVEVLEPLKC ELVSGESTGN CEDRLPVKGT EANGKKPSQQ KKLEERPVNK 

      1510       1520       1530       1540       1550       1560 
CSDQIKLKNT TDKKNNENRE SEKKGQRTST FQINGKDNKP KIYLKGECLK EISESRVVSG 

      1570       1580       1590       1600       1610       1620 
NVEPKVNNIN KIIPENDIKS LTVKESAIRP FINGDVIMED FNERNSSETK SHLLSSSDAE 

      1630       1640       1650       1660       1670       1680 
GNYRDSLETL PSTKESDSTQ TTTPSASCPE SNSVNQVEDM EIETSEVKKV TSSPITSEEE 

      1690       1700       1710       1720       1730       1740 
SNLSNDFIDE NGLPINKNEN VNGESKRKTV ITEVTTMTST VATESKTVIK VEKGDKQTVV 

      1750       1760       1770       1780       1790       1800 
SSTENCAKST VTTTTTTVTK LSTPSTGGSV DIISVKEQSK TVVTTTVTDS LTTTGGTLVT 

      1810       1820       1830       1840       1850       1860 
SMTVSKEYST RDKVKLMKFS RPKKTRSGTA LPSYRKFVTK SSKKSIFVLP NDDLKKLARK 

      1870       1880       1890       1900       1910       1920 
GGIREVPYFN YNAKPALDIW PYPSPRPTFG ITWRYRLQTV KSLAGVSLML RLLWASLRWD 

      1930       1940       1950       1960       1970       1980 
DMAAKAPPGG GTTRTETSET EITTTEIIKR RDVGPYGIRS EYCIRKIICP IGVPETPKET 

      1990       2000       2010       2020       2030       2040 
PTPQRKGLRS SALRPKRPET PKQTGPVIIE TWVAEEELEL WEIRAFAERV EKEKAQAVEQ 

      2050       2060       2070       2080       2090       2100 
QAKKRLEQQK PTVIATSTTS PTSSTTSTIS PAQKVMVAPI SGSVTTGTKM VLTTKVGSPA 

      2110       2120       2130       2140       2150       2160 
TVTFQQNKNF HQTFATWVKQ GQSNSGVVQV QQKVLGIIPS STGTSQQTFT SFQPRTATVT 

      2170       2180       2190       2200       2210       2220 
IRPNTSGSGG TTSNSQVITG PQIRPGMTVI RTPLQQSTLG KAIIRTPVMV QPGAPQQVMT 

      2230       2240       2250       2260       2270       2280 
QIIRGQPVST AVSAPNTVSS TPGQKSLTSA TSTSNIQSSA SQPPRPQQGQ VKLTMAQLTQ 

      2290       2300       2310       2320       2330       2340 
LTQGHGGNQG LTVVIQGQGQ TTGQLQLIPQ GVTVLPGPGQ QLMQAAMPNG TVQRFLFTPL 

      2350       2360       2370       2380       2390       2400 
ATTATTASTT TTTVSTTAAG TGEQRQSKLS PQMQVHQDKT LPPAQSSSVG PAEAQPQTAQ 

      2410       2420       2430       2440       2450       2460 
PSAQPQPQTQ PQSPAQPEVQ TQPEVQTQTT VSSHVPSEAQ PTHAQSSKPQ VAAQSQPQSN 

      2470       2480       2490       2500       2510       2520 
VQGQSPVRVQ SPSQTRIRPS TPSQLSPGQQ SQVQTTTSQP IPIQPHTSLQ IPSQGQPQSQ 

      2530       2540       2550       2560       2570       2580 
PQVQSSTQTL SSGQTLNQVT VSSPSRPQLQ IQQPQPQVIA VPQLQQQVQV LSQIQSQVVA 

      2590       2600       2610       2620       2630       2640 
QIQAQQSGVP QQIKLQLPIQ IQQSSAVQTH QIQNVVTVQA ASVQEQLQRV QQLRDQQQKK 

      2650       2660       2670       2680       2690       2700 
KQQQIEIKRE HTLQASNQSE IIQKQVVMKH NAVIEHLKQK KSMTPAEREE NQRMIVCNQV 

      2710       2720       2730       2740       2750       2760 
MKYILDKIDK EEKQAAKKRK REESVEQKRS KQNATKLSAL LFKHKEQLRA EILKKRALLD 

      2770       2780       2790       2800       2810       2820 
KDLQIEVQEE LKRDLKIKKE KDLMQLAQAT AVAAPCPPVT PAPPAPPAPP PSPPPPPAVQ 

      2830       2840       2850       2860       2870       2880 
HTGLLSTPTL PAASQKRKRE EEKDSSSKSK KKKMISTTSK ETKKDTKLYC ICKTPYDESK 

      2890       2900       2910       2920       2930       2940 
FYIGCDRCQN WYHGRCVGIL QSEAELIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL 

      2950       2960       2970       2980       2990       3000 
RSLQAHKMAW PFLEPVDPND APDYYGVIKE PMDLATMEER VQRRYYEKLT EFVADMTKIF 

      3010       3020       3030       3040 
DNCRYYNPSD SPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAS 

Q12830 in FASTA format

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