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P35221 (CTNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. 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) [Reference proteome]
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 adherens 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.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.25

Subcellular location

Isoform 1: Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.4. Cell junction. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries. Ref.4

Isoform 3: Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.4.

Tissue specificity

Expressed ubiquitously in normal tissues.

Post-translational modification

Sumoylated. Ref.17

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction organization

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

apical junction assembly

Non-traceable author statement PubMed 9700171. Source: UniProtKB

axon regeneration

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Non-traceable author statement Ref.2. Source: ProtInc

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

cellular protein localization

Inferred from electronic annotation. Source: Ensembl

cellular response to indole-3-methanol

Inferred from direct assay PubMed 10868478. Source: UniProtKB

epithelial cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

gap junction assembly

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell motility

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

ovarian follicle development

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from electronic annotation. Source: InterPro

catenin complex

Inferred from direct assay PubMed 7650039. Source: BHF-UCL

cell-cell junction

Inferred from direct assay PubMed 10460003. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intercalated disc

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

zonula adherens

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 7650039PubMed 7890674. Source: BHF-UCL

cadherin binding

Inferred from physical interaction PubMed 12734196. Source: UniProtKB

gamma-catenin binding

Inferred from physical interaction PubMed 7650039PubMed 7890674. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

structural molecule activity

Inferred from electronic annotation. Source: InterPro

vinculin binding

Inferred from physical interaction PubMed 9700171. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35221-1)

Also known as: CTNNA1a;

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
Isoform 3 (identifier: P35221-3)

Also known as: CTNNA1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-370: Missing.
Note: Expressed at high levels in the nervous system. Lacks the beta-catenin interaction domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
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.10
Modified residue6341Phosphothreonine Ref.32
Modified residue6411Phosphoserine Ref.19 Ref.21 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.32
Modified residue6451Phosphothreonine Ref.22 Ref.26
Modified residue6521Phosphoserine Ref.22 Ref.24 Ref.32

Natural variations

Alternative sequence1 – 370370Missing in isoform 3.
VSP_047810
Alternative sequence8111G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2.
VSP_017494
Natural variant1791A → V. Ref.6
Corresponds to variant rs28363394 [ dbSNP | Ensembl ].
VAR_022303
Natural variant2191P → S. Ref.6
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 (CTNNA1a) [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
Isoform 3 (CTNNA1b) [UniParc].

Checksum: 887A39433621F5DB
Show »

FASTA53659,550

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Colon.
[4]"Bidirectional transcription from human LRRTM2/CTNNA1 and LRRTM1/CTNNA2 gene loci leads to expression of N-terminally truncated CTNNA1 and CTNNA2 isoforms."
Kask M., Pruunsild P., Timmusk T.
Biochem. Biophys. Res. Commun. 411:56-61(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORM 3).
Tissue: Hippocampus.
[5]"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].
[6]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-179 AND SER-219.
[7]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Brain and Lung.
[10]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
Tissue: Prostate.
[12]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[13]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH CTNNB1.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AJUBA.
[17]"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] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP21.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[22]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-645 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMA1.
[26]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[27]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY 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.
HQ589335 mRNA. Translation: AEF32483.1.
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.
AC010453 Genomic DNA. No translation available.
AC011405 Genomic DNA. No translation available.
AC034243 Genomic DNA. No translation available.
AC113340 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62124.1.
BC000385 mRNA. Translation: AAH00385.1.
BC031262 mRNA. Translation: AAH31262.1.
L22080 mRNA. Translation: AAA35502.1.
PIRJC2542.
JN0607.
RefSeqNP_001894.2. NM_001903.2.
XP_005271955.1. XM_005271898.1.
XP_005271956.1. XM_005271899.1.
UniGeneHs.445981.
Hs.656653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6GX-ray2.20A/B377-632[»]
4EHPX-ray2.66B277-382[»]
4IGGX-ray3.66A/B82-906[»]
ProteinModelPortalP35221.
SMRP35221. Positions 22-878.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107876. 48 interactions.
DIPDIP-515N.
IntActP35221. 18 interactions.
MINTMINT-4998962.
STRING9606.ENSP00000304669.

PTM databases

PhosphoSiteP35221.

Polymorphism databases

DMDM461853.

Proteomic databases

PaxDbP35221.
PeptideAtlasP35221.
PRIDEP35221.

Protocols and materials databases

DNASU1495.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302763; ENSP00000304669; ENSG00000044115. [P35221-1]
ENST00000540387; ENSP00000438476; ENSG00000044115. [P35221-3]
GeneID1495.
KEGGhsa:1495.
UCSCuc003ldh.3. human. [P35221-1]

Organism-specific databases

CTD1495.
GeneCardsGC05P137947.
HGNCHGNC:2509. CTNNA1.
HPACAB021089.
HPA046119.
MIM116805. gene.
neXtProtNX_P35221.
PharmGKBPA27008.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240050.
HOGENOMHOG000280724.
HOVERGENHBG000069.
KOK05691.
OMAVLQRNIP.
OrthoDBEOG7HQN7B.
PhylomeDBP35221.
TreeFamTF313686.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP35221.
BgeeP35221.
CleanExHS_CTNNA1.
GenevestigatorP35221.

Family and domain databases

InterProIPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERPTHR18914. PTHR18914. 1 hit.
PfamPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSPR00805. ALPHACATENIN.
SUPFAMSSF47220. SSF47220. 4 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTNNA1. human.
EvolutionaryTraceP35221.
GeneWikiCatenin_(cadherin-associated_protein),_alpha_1.
GenomeRNAi1495.
NextBio6145.
PROP35221.
SOURCESearch...

Entry information

Entry nameCTNA1_HUMAN
AccessionPrimary (citable) accession number: P35221
Secondary accession number(s): Q12795, Q8N1C0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 148 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

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