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UniProtKB/Swiss-Prot entry P35221


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

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Entry information
Entry name CTNA1_HUMAN
Primary accession number P35221
Secondary accession number Q12795
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 98)
Name and origin of the protein
Protein name Catenin alpha-1
Synonyms Cadherin-associated protein
Alpha E-catenin
NY-REN-13 antigen
Gene name
Name: CTNNA1
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;
PubMed=8404069 [NCBI, ExPASy, EBI, Israel, Japan]
Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T., Nakamura Y., Horii A.;
"Structure, expression and chromosome assignment of the human catenin (cadherin-associated protein) alpha 1 gene (CTNNA1).";
Cytogenet. Cell Genet. 65:74-78(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon, and Lung;
DOI=10.1006/bbrc.1993.1710; PubMed=8323564 [NCBI, ExPASy, EBI, Israel, Japan]
Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S., Hirohashi S.;
"Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line.";
Biochem. Biophys. Res. Commun. 193:897-904(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon;
DOI=10.1006/bbrc.1994.2381; PubMed=7945318 [NCBI, ExPASy, EBI, Israel, Japan]
Rimm D.L., Kebriaei P., Morrow J.S.;
"Molecular cloning reveals alternative splice forms of human alpha(E)-catenin.";
Biochem. Biophys. Res. Commun. 203:1691-1699(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nollet F.H., Vanpoucke G.G., van Roy F.M.;
"Genomic organization of the human alphaE-catenin gene (CTNNA1).";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-179 AND SER-219.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[7]
PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
TISSUE=Prostate;
DOI=10.1006/geno.1994.1042; PubMed=8188230 [NCBI, ExPASy, EBI, Israel, Japan]
McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J., Nagafuchi A., Tsukita S., Isaacs W.B.;
"Assignment of the human alpha-catenin gene (CTNNA1) to chromosome 5q21-q22.";
Genomics 19:188-190(1994).
[9]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[10]
COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1.
DOI=10.1016/S1097-2765(00)80219-1; PubMed=10635315 [NCBI, ExPASy, EBI, Israel, Japan]
Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K.;
"Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts.";
Mol. Cell 4:893-902(1999).
[11]
INTERACTION WITH JUB.
DOI=10.1074/jbc.M205391200; PubMed=12417594 [NCBI, ExPASy, EBI, Israel, Japan]
Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L., Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.;
"The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin.";
J. Biol. Chem. 278:1220-1228(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, 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).
[13]
SUMOYLATION.
DOI=10.1074/jbc.M411718200; PubMed=15561718 [NCBI, ExPASy, EBI, Israel, Japan]
Gocke C.B., Yu H., Kang J.;
"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates.";
J. Biol. Chem. 280:5004-5012(2005).
[14]
INTERACTION WITH ARHGAP21.
DOI=10.1038/ncb1308; PubMed=16184169 [NCBI, ExPASy, EBI, Israel, Japan]
Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.;
"ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion.";
Nat. Cell Biol. 7:954-960(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS SPECTROMETRY.
TISSUE=Pituitary;
DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan]
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177 AND TYR-619, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652 AND THR-658, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.";
Electrophoresis 28:2027-2034(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652; SER-655 AND THR-658, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan]
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.";
Proteomics 8:1346-1361(2008).
[22]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. May play a crucial role in cell differentiation.
  • SUBUNIT: Binds MLLT4 and F-actin (By similarity). Interacts directly with PSEN1 and CTNNB1 to form part of the PSEN1/cadherin/catenin adhesion complex. Interacts with ARHGAP21 and with JUB.
  • SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDP35221-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDP35221-2
    Features which should be applied to build the isoform sequence: VSP_017494.
  • TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
  • PTM: Sumoylated.
  • DISEASE: Abnormalities of alpha-catenin are involved in the process of cancer invasion and metastasis.
  • SIMILARITY: Belongs to the vinculin/alpha-catenin family.
  • WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ctnna1/";.
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
D14705; BAA03530.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D13866; BAA02979.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L23805; AAA86430.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U03100; AAA18949.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102803; AAC99459.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102787; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102788; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102789; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102790; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102791; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102792; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102793; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102794; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102795; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102796; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102797; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102798; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102799; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102800; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102801; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102802; AAC99459.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY884207; AAW56940.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000385; AAH00385.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L22080; AAA35502.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00215948; -.
IPI00473136; -.
PIR JC2542; JC2542.
JN0607; JN0607.
RefSeq NP_001894.2; -.
UniGene Hs.534797
3D structure databases
PDB
1H6G; X-ray; 2.20 A; A/B=377-632.[ExPASy / RCSB / EBI]
1L7C; X-ray; 2.50 A; A/B/C=385-651.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H6G; -.
1L7C; -.
SMR P35221; 57-261.
ModBase P35221.
Protein-protein interaction databases
DIP DIP:515N; -.
PTM databases
PhosphoSite P35221; -.
Enzyme and pathway databases
Pathway_Interaction_DB arf6_traffickingpathway; Arf6 trafficking events.
Organism-specific databases
GeneCards GC05P138117; -.
H-InvDB HIX0005216; -.
HGNC HGNC:2509; CTNNA1.
GenAtlas CTNNA1.
MIM 116805; gene. [NCBI / EBI]
PharmGKB PA27008; -.
Gene expression databases
ArrayExpress P35221; -.
Bgee P35221; -.
CleanEx HS_CTNNA1; -.
GermOnline ENSG00000044115; Homo sapiens.
Ontologies
GO
GO:0015629; Cellular component: actin cytoskeleton (inferred from electronic annotation from InterPro).
GO:0005912; Cellular component: adherens junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0045296; Molecular function: cadherin binding (inferred from physical interaction from UniProtKB).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0017166; Molecular function: vinculin binding (inferred from physical interaction from UniProtKB).
GO:0043297; Biological process: apical junction assembly (non-traceable author statement from UniProtKB).
GO:0007155; Biological process: cell adhesion (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001033; Alpha_catenin.
IPR006077; Vinculin/catenin.
IPR000633; Vinculin_CS.
Graphical view of domain structure.
Pfam PF01044; Vinculin; 1.
Pfam graphical view of domain structure.
PRINTS PR00805; ALPHACATENIN.
PROSITE PS00663; VINCULIN_1; 1.
Proteomic databases
PeptideAtlas P35221; -.
PRIDE P35221; -.
Genome annotation databases
Ensembl ENSG00000044115; Homo sapiens. [Contig view]
GeneID 1495; -.
KEGG hsa:1495; -.
Phylogenomic databases
HOVERGEN P35221; -.
Other
NextBio 6145; -.
SOURCE CTNNA1; Homo sapiens.
ProtoNet P35221.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   906  905     Catenin alpha-1. PRO_0000064261
MOD_RES   2     2        N-acetylthreonine. 
MOD_RES   177   177        Phosphotyrosine. 
MOD_RES   619   619        Phosphotyrosine. 
MOD_RES   641   641        Phosphoserine. 
MOD_RES   645   645        Phosphothreonine. 
MOD_RES   652   652        Phosphoserine. 
MOD_RES   654   654        Phosphothreonine (By similarity). 
MOD_RES   655   655        Phosphoserine. 
MOD_RES   658   658        Phosphothreonine. 
VAR_SEQ   811   811        G -> GNCDTCGALQGLKGWPPPLCLATHW (in isoform 2). VSP_017494
VARIANT   179   179  1     A -> V. VAR_022303 [3D]
VARIANT   219   219  1     P -> S (in dbSNP:rs28363406 [NCBI]). VAR_022304 [3D]
CONFLICT   92    92        A -> V (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   129   129        R -> P (in Ref. 3; AAA18949). 
CONFLICT   175   175        I -> N (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   216   216        K -> S (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   342   342        Q -> K (in Ref. 1; BAA03530). 
CONFLICT   344   348        LQDLL -> CRTCV (in Ref. 3; AAA86430). 
CONFLICT   460   460        L -> G (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   469   469        L -> TW (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   473   473        A -> P (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   653   653        R -> E (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   685   685        A -> R (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   764   764        A -> R (in Ref. 3; AAA86430/AAA18949). 
CONFLICT   789   789        Q -> H (in Ref. 1; BAA03530). 
CONFLICT   859   859        W -> M (in Ref. 3; AAA86430/AAA18949). 
HELIX   378   386  9      
HELIX   387   389  3      
TURN   393   395  3      
HELIX   398   409  12      
HELIX   413   438  26      
HELIX   444   473  30      
HELIX   478   506  29      
HELIX   509   531  23      
HELIX   535   559  25      
TURN   560   562  3      
HELIX   567   581  15      
HELIX   583   598  16      
STRAND   600   602  3      
HELIX   608   630  23      
Sequence information
Length: 906 AA [This is the length of the unprocessed precursor] Molecular weight: 100071 Da [This is the MW of the unprocessed precursor] CRC64: 7AAE6F5DDBAF5099 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 

        70         80         90        100        110        120 
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK 

       130        140        150        160        170        180 
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 

       190        200        210        220        230        240 
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 

       250        260        270        280        290        300 
RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 

       310        320        330        340        350        360 
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 

       370        380        390        400        410        420 
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 

       430        440        450        460        470        480 
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 

       490        500        510        520        530        540 
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 

       550        560        570        580        590        600 
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 

       610        620        630        640        650        660 
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 

       670        680        690        700        710        720 
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 

       730        740        750        760        770        780 
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 

       790        800        810        820        830        840 
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS 

       850        860        870        880        890        900 
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 


KAMDSI 

P35221 in FASTA format

View entry in raw text format (no links)
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