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P35221 (CTNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catenin alpha-1
Alternative name(s):
Alpha E-catenin
Cadherin-associated protein
Renal carcinoma antigen NY-REN-13
Gene names
Name:CTNNA1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherence junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.

Subunit structure

Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Binds MLLT4 and F-actin. Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interacts with ARHGAP21 and with AJUBA. Interacts with LIMA1 By similarity. Ref.10 Ref.11 Ref.13 Ref.16 Ref.21

Subcellular location

Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries.

Tissue specificity

Expressed ubiquitously in normal tissues.

Post-translational modification

Sumoylated. Ref.15

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35221-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P35221-2)

The sequence of this isoform differs from the canonical sequence as follows:
     811-811: G → GNCDTCGALQGLKGWPPPLCLATHW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 906905Catenin alpha-1
PRO_0000064261

Regions

Region2 – 228227Involved in homodimerization
Region97 – 14852Interaction with JUP and CTNNB1
Region325 – 39470Interaction with alpha-actinin

Amino acid modifications

Modified residue21N-acetylthreonine Ref.7
Modified residue1771Phosphotyrosine Ref.19
Modified residue1861N6-acetyllysine Ref.28
Modified residue6191Phosphotyrosine Ref.19
Modified residue6411Phosphoserine Ref.14 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Modified residue6451Phosphothreonine Ref.24
Modified residue6521Phosphoserine Ref.20 Ref.23 Ref.25 Ref.27
Modified residue6541Phosphothreonine Ref.25
Modified residue6551Phosphoserine Ref.23 Ref.25
Modified residue6581Phosphothreonine Ref.20 Ref.23 Ref.25

Natural variations

Alternative sequence8111G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2.
VSP_017494
Natural variant1791A → V. Ref.5
Corresponds to variant rs28363394 [ dbSNP | Ensembl ].
VAR_022303
Natural variant2191P → S. Ref.5
Corresponds to variant rs28363406 [ dbSNP | Ensembl ].
VAR_022304

Experimental info

Sequence conflict921A → V in AAA86430. Ref.3
Sequence conflict921A → V in AAA18949. Ref.3
Sequence conflict1291R → P in AAA18949. Ref.3
Sequence conflict1751I → N in AAA86430. Ref.3
Sequence conflict1751I → N in AAA18949. Ref.3
Sequence conflict2161K → S in AAA86430. Ref.3
Sequence conflict2161K → S in AAA18949. Ref.3
Sequence conflict3421Q → K in BAA03530. Ref.1
Sequence conflict344 – 3485LQDLL → CRTCV in AAA86430. Ref.3
Sequence conflict4601L → G in AAA86430. Ref.3
Sequence conflict4601L → G in AAA18949. Ref.3
Sequence conflict4691L → TW in AAA86430. Ref.3
Sequence conflict4691L → TW in AAA18949. Ref.3
Sequence conflict4731A → P in AAA86430. Ref.3
Sequence conflict4731A → P in AAA18949. Ref.3
Sequence conflict6531R → E in AAA86430. Ref.3
Sequence conflict6531R → E in AAA18949. Ref.3
Sequence conflict6851A → R in AAA86430. Ref.3
Sequence conflict6851A → R in AAA18949. Ref.3
Sequence conflict7641A → R in AAA86430. Ref.3
Sequence conflict7641A → R in AAA18949. Ref.3
Sequence conflict7891Q → H in BAA03530. Ref.1
Sequence conflict8591W → M in AAA86430. Ref.3
Sequence conflict8591W → M in AAA18949. Ref.3

Secondary structure

........................... 906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 7AAE6F5DDBAF5099

FASTA906100,071
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 6EDF38C221CA2FA0
Show »

FASTA930102,635

References

« Hide 'large scale' references
[1]"Structure, expression and chromosome assignment of the human catenin (cadherin-associated protein) alpha 1 gene (CTNNA1)."
Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T., Nakamura Y., Horii A.
Cytogenet. Cell Genet. 65:74-78(1994) [PubMed: 8404069] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line."
Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S., Hirohashi S.
Biochem. Biophys. Res. Commun. 193:897-904(1993) [PubMed: 8323564] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon and Lung.
[3]"Molecular cloning reveals alternative splice forms of human alpha(E)-catenin."
Rimm D.L., Kebriaei P., Morrow J.S.
Biochem. Biophys. Res. Commun. 203:1691-1699(1994) [PubMed: 7945318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Colon.
[4]"Genomic organization of the human alphaE-catenin gene (CTNNA1)."
Nollet F.H., Vanpoucke G.G., van Roy F.M.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-179 AND SER-219.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]Bienvenut W.V., Zebisch A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[8]"Assignment of the human alpha-catenin gene (CTNNA1) to chromosome 5q21-q22."
McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J., Nagafuchi A., Tsukita S., Isaacs W.B.
Genomics 19:188-190(1994) [PubMed: 8188230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
Tissue: Prostate.
[9]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed: 7982500] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[10]"Alpha-catenin can form asymmetric homodimeric complexes and/or heterodimeric complexes with beta-catenin."
Koslov E.R., Maupin P., Pradhan D., Morrow J.S., Rimm D.L.
J. Biol. Chem. 272:27301-27306(1997) [PubMed: 9341178] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH CTNNB1.
[11]"Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin."
Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R., Wheelock M.J.
J. Cell Sci. 110:1013-1022(1997) [PubMed: 9152027] [Abstract]
Cited for: INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
[12]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
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.
Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[13]"The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin."
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.
J. Biol. Chem. 278:1220-1228(2003) [PubMed: 12417594] [Abstract]
Cited for: INTERACTION WITH AJUBA.
[14]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed: 15561718] [Abstract]
Cited for: SUMOYLATION.
[16]"ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion."
Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.
Nat. Cell Biol. 7:954-960(2005) [PubMed: 16184169] [Abstract]
Cited for: INTERACTION WITH ARHGAP21.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[18]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
Tissue: Pituitary.
[19]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177 AND TYR-619, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[20]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652 AND THR-658, MASS SPECTROMETRY.
Tissue: Prostate cancer.
[21]"EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
Abe K., Takeichi M.
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed: 18093941] [Abstract]
Cited for: INTERACTION WITH LIMA1.
[22]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652; SER-655 AND THR-658, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, MASS SPECTROMETRY.
Tissue: Liver.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652; THR-654; SER-655 AND THR-658, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[26]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
[27]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[28]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186, MASS SPECTROMETRY.
[29]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion."
Yang J., Dokurno P., Tonks N.K., Barford D.
EMBO J. 20:3645-3656(2001) [PubMed: 11447106] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14705 mRNA. Translation: BAA03530.1.
D13866 mRNA. Translation: BAA02979.1.
L23805 mRNA. Translation: AAA86430.1.
U03100 mRNA. Translation: AAA18949.1.
AF102803 expand/collapse EMBL AC list , AF102787, AF102788, AF102789, AF102790, AF102791, AF102792, AF102793, AF102794, AF102795, AF102796, AF102797, AF102798, AF102799, AF102800, AF102801, AF102802 Genomic DNA. Translation: AAC99459.1.
AY884207 Genomic DNA. Translation: AAW56940.1.
BC000385 mRNA. Translation: AAH00385.1.
L22080 mRNA. Translation: AAA35502.1.
IPIIPI00215948.
IPI00473136.
PIRJC2542.
JN0607.
RefSeqNP_001894.2. NM_001903.2.
UniGeneHs.445981.
Hs.656653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6GX-ray2.20A/B377-632[»]
ProteinModelPortalP35221.
SMRP35221. Positions 57-261, 377-631.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29632N.
DIP-515N.
IntActP35221. 9 interactions.
MINTMINT-4998962.
STRINGP35221.

PTM databases

PhosphoSiteP35221.

Polymorphism databases

DMDM461853.

Proteomic databases

PeptideAtlasP35221.
PRIDEP35221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302763; ENSP00000304669; ENSG00000044115.
GeneID1495.
KEGGhsa:1495.
UCSCuc003ldh.1. human.

Organism-specific databases

CTD1495.
GeneCardsGC05P137947.
H-InvDBHIX0005216.
HGNCHGNC:2509. CTNNA1.
HPACAB021089.
MIM116805. gene.
neXtProtNX_P35221.
PharmGKBPA27008.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17774.
HOVERGENHBG000069.
OrthoDBEOG49W2G4.

Enzyme and pathway databases

Pathway_Interaction_DBarf6_traffickingpathway. Arf6 trafficking events.
ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP35221.
BgeeP35221.
CleanExHS_CTNNA1.
GenevestigatorP35221.
GermOnlineENSG00000044115. Homo sapiens.

Family and domain databases

InterProIPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
KOK05691.
PfamPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSPR00805. ALPHACATENIN.
SUPFAMSSF47220. Vinculin/catenin. 4 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio6145.
SOURCESearch...

Entry information

Entry nameCTNA1_HUMAN
AccessionPrimary (citable) accession number: P35221
Secondary accession number(s): Q12795
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 25, 2012
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families