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P35221

- CTNA1_HUMAN

UniProt

P35221 - CTNA1_HUMAN

Protein

Catenin alpha-1

Gene

CTNNA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. beta-catenin binding Source: BHF-UCL
    2. cadherin binding Source: UniProtKB
    3. gamma-catenin binding Source: BHF-UCL
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: HGNC
    6. structural molecule activity Source: InterPro
    7. vinculin binding Source: UniProtKB

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. aging Source: Ensembl
    3. apical junction assembly Source: UniProtKB
    4. axon regeneration Source: Ensembl
    5. cell adhesion Source: ProtInc
    6. cell-cell junction organization Source: Reactome
    7. cell junction assembly Source: Reactome
    8. cellular protein localization Source: Ensembl
    9. cellular response to indole-3-methanol Source: UniProtKB
    10. epithelial cell-cell adhesion Source: Ensembl
    11. establishment or maintenance of cell polarity Source: Ensembl
    12. gap junction assembly Source: Ensembl
    13. male gonad development Source: Ensembl
    14. muscle cell differentiation Source: Reactome
    15. negative regulation of apoptotic process Source: Ensembl
    16. negative regulation of cell motility Source: Ensembl
    17. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    18. negative regulation of integrin-mediated signaling pathway Source: Ensembl
    19. negative regulation of neuroblast proliferation Source: Ensembl
    20. odontogenesis of dentin-containing tooth Source: Ensembl
    21. ovarian follicle development Source: Ensembl
    22. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    23. positive regulation of muscle cell differentiation Source: Reactome
    24. positive regulation of smoothened signaling pathway Source: Ensembl
    25. protein heterooligomerization Source: Ensembl
    26. response to estrogen Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.
    REACT_21402. CDO in myogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catenin alpha-1
    Alternative name(s):
    Alpha E-catenin
    Cadherin-associated protein
    Renal carcinoma antigen NY-REN-13
    Gene namesi
    Name:CTNNA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2509. CTNNA1.

    Subcellular locationi

    Isoform 1 : 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.
    Isoform 3 : Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. actin cytoskeleton Source: InterPro
    3. catenin complex Source: BHF-UCL
    4. cell-cell junction Source: UniProtKB
    5. cytosol Source: Reactome
    6. intercalated disc Source: Ensembl
    7. lamellipodium Source: Ensembl
    8. plasma membrane Source: Reactome
    9. zonula adherens Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27008.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 906905Catenin alpha-1PRO_0000064261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei634 – 6341Phosphothreonine1 Publication
    Modified residuei641 – 6411Phosphoserine9 Publications
    Modified residuei645 – 6451Phosphothreonine2 Publications
    Modified residuei652 – 6521Phosphoserine3 Publications

    Post-translational modificationi

    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP35221.
    PaxDbiP35221.
    PeptideAtlasiP35221.
    PRIDEiP35221.

    PTM databases

    PhosphoSiteiP35221.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously in normal tissues.

    Gene expression databases

    ArrayExpressiP35221.
    BgeeiP35221.
    CleanExiHS_CTNNA1.
    GenevestigatoriP35221.

    Organism-specific databases

    HPAiCAB021089.
    HPA046119.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APCP250542EBI-701918,EBI-727707
    ARRB2P321213EBI-701918,EBI-714559
    EGFRP005334EBI-701918,EBI-297353
    JUPP149232EBI-701918,EBI-702484

    Protein-protein interaction databases

    BioGridi107876. 49 interactions.
    DIPiDIP-515N.
    IntActiP35221. 19 interactions.
    MINTiMINT-4998962.
    STRINGi9606.ENSP00000304669.

    Structurei

    Secondary structure

    1
    906
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi293 – 2997
    Beta strandi300 – 3023
    Helixi305 – 31612
    Helixi325 – 3273
    Helixi328 – 35225
    Helixi353 – 3553
    Helixi378 – 3869
    Helixi387 – 3893
    Turni393 – 3953
    Helixi398 – 40912
    Helixi413 – 43826
    Helixi444 – 47330
    Helixi478 – 50629
    Helixi509 – 53123
    Helixi535 – 55925
    Turni560 – 5623
    Helixi567 – 58115
    Helixi583 – 59816
    Beta strandi600 – 6023
    Helixi608 – 63023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H6GX-ray2.20A/B377-632[»]
    4EHPX-ray2.66B277-382[»]
    4IGGX-ray3.66A/B82-906[»]
    ProteinModelPortaliP35221.
    SMRiP35221. Positions 22-878.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35221.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 228227Involved in homodimerizationAdd
    BLAST
    Regioni97 – 14852Interaction with JUP and CTNNB1Add
    BLAST
    Regioni325 – 39470Interaction with alpha-actininAdd
    BLAST

    Sequence similaritiesi

    Belongs to the vinculin/alpha-catenin family.Curated

    Phylogenomic databases

    eggNOGiNOG240050.
    HOGENOMiHOG000280724.
    HOVERGENiHBG000069.
    KOiK05691.
    OMAiWERQVRV.
    OrthoDBiEOG7HQN7B.
    PhylomeDBiP35221.
    TreeFamiTF313686.

    Family and domain databases

    InterProiIPR001033. Alpha_catenin.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view]
    PANTHERiPTHR18914. PTHR18914. 1 hit.
    PfamiPF01044. Vinculin. 2 hits.
    [Graphical view]
    PRINTSiPR00805. ALPHACATENIN.
    SUPFAMiSSF47220. SSF47220. 4 hits.
    PROSITEiPS00663. VINCULIN_1. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35221-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK    50
    KRGRSKKAHV LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ 100
    GDLMKAAAGE FADDPCSSVK RGNMVRAARA LLSAVTRLLI LADMADVYKL 150
    LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL KPEVDKLNIM AAKRQQELKD 200
    VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ 250
    AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 300
    FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE 350
    YMGNAGRKER SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP 400
    LLVLIEAAKN GNEKEVKEYA QVFREHANKL IEVANLACSI SNNEEGVKLV 450
    RMSASQLEAL CPQVINAALA LAAKPQSKLA QENMDLFKEQ WEKQVRVLTD 500
    AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR TAGAIRGRAA 550
    RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 600
    DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV 650
    RSRTSVQTED DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA 700
    EVSKWDDSGN DIIVLAKQMC MIMMEMTDFT RGKGPLKNTS DVISAAKKIA 750
    EAGSRMDKLG RTIADHCPDS ACKQDLLAYL QRIALYCHQL NICSKVKAEV 800
    QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS TKYQKSQGMA 850
    SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 900
    KAMDSI 906
    Length:906
    Mass (Da):100,071
    Last modified:February 1, 1994 - v1
    Checksum:i7AAE6F5DDBAF5099
    GO
    Isoform 2 (identifier: P35221-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:930
    Mass (Da):102,635
    Checksum:i6EDF38C221CA2FA0
    GO
    Isoform 3 (identifier: P35221-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:536
    Mass (Da):59,550
    Checksum:i887A39433621F5DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921A → V in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti92 – 921A → V in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti129 – 1291R → P in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti175 – 1751I → N in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti175 – 1751I → N in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti216 – 2161K → S in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti216 – 2161K → S in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti342 – 3421Q → K in BAA03530. (PubMed:8404069)Curated
    Sequence conflicti344 – 3485LQDLL → CRTCV in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti460 – 4601L → G in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti460 – 4601L → G in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti469 – 4691L → TW in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti469 – 4691L → TW in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti473 – 4731A → P in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti473 – 4731A → P in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti653 – 6531R → E in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti653 – 6531R → E in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti685 – 6851A → R in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti685 – 6851A → R in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti764 – 7641A → R in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti764 – 7641A → R in AAA18949. (PubMed:7945318)Curated
    Sequence conflicti789 – 7891Q → H in BAA03530. (PubMed:8404069)Curated
    Sequence conflicti859 – 8591W → M in AAA86430. (PubMed:7945318)Curated
    Sequence conflicti859 – 8591W → M in AAA18949. (PubMed:7945318)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti179 – 1791A → V.1 Publication
    Corresponds to variant rs28363394 [ dbSNP | Ensembl ].
    VAR_022303
    Natural varianti219 – 2191P → S.1 Publication
    Corresponds to variant rs28363406 [ dbSNP | Ensembl ].
    VAR_022304

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 370370Missing in isoform 3. 2 PublicationsVSP_047810Add
    BLAST
    Alternative sequencei811 – 8111G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2. 1 PublicationVSP_017494

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS34243.1. [P35221-1]
    PIRiJC2542.
    JN0607.
    RefSeqiNP_001277236.1. NM_001290307.1.
    NP_001277238.1. NM_001290309.1.
    NP_001277239.1. NM_001290310.1.
    NP_001277241.1. NM_001290312.1. [P35221-3]
    NP_001894.2. NM_001903.3. [P35221-1]
    XP_005271956.1. XM_005271899.1. [P35221-3]
    XP_006714599.1. XM_006714536.1. [P35221-1]
    UniGeneiHs.445981.

    Genome annotation databases

    EnsembliENST00000302763; ENSP00000304669; ENSG00000044115. [P35221-1]
    ENST00000540387; ENSP00000438476; ENSG00000044115. [P35221-3]
    GeneIDi1495.
    KEGGihsa:1495.
    UCSCiuc003ldh.3. human. [P35221-1]

    Polymorphism databases

    DMDMi461853.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS34243.1. [P35221-1 ]
    PIRi JC2542.
    JN0607.
    RefSeqi NP_001277236.1. NM_001290307.1.
    NP_001277238.1. NM_001290309.1.
    NP_001277239.1. NM_001290310.1.
    NP_001277241.1. NM_001290312.1. [P35221-3 ]
    NP_001894.2. NM_001903.3. [P35221-1 ]
    XP_005271956.1. XM_005271899.1. [P35221-3 ]
    XP_006714599.1. XM_006714536.1. [P35221-1 ]
    UniGenei Hs.445981.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H6G X-ray 2.20 A/B 377-632 [» ]
    4EHP X-ray 2.66 B 277-382 [» ]
    4IGG X-ray 3.66 A/B 82-906 [» ]
    ProteinModelPortali P35221.
    SMRi P35221. Positions 22-878.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107876. 49 interactions.
    DIPi DIP-515N.
    IntActi P35221. 19 interactions.
    MINTi MINT-4998962.
    STRINGi 9606.ENSP00000304669.

    PTM databases

    PhosphoSitei P35221.

    Polymorphism databases

    DMDMi 461853.

    Proteomic databases

    MaxQBi P35221.
    PaxDbi P35221.
    PeptideAtlasi P35221.
    PRIDEi P35221.

    Protocols and materials databases

    DNASUi 1495.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302763 ; ENSP00000304669 ; ENSG00000044115 . [P35221-1 ]
    ENST00000540387 ; ENSP00000438476 ; ENSG00000044115 . [P35221-3 ]
    GeneIDi 1495.
    KEGGi hsa:1495.
    UCSCi uc003ldh.3. human. [P35221-1 ]

    Organism-specific databases

    CTDi 1495.
    GeneCardsi GC05P137947.
    HGNCi HGNC:2509. CTNNA1.
    HPAi CAB021089.
    HPA046119.
    MIMi 116805. gene.
    neXtProti NX_P35221.
    PharmGKBi PA27008.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240050.
    HOGENOMi HOG000280724.
    HOVERGENi HBG000069.
    KOi K05691.
    OMAi WERQVRV.
    OrthoDBi EOG7HQN7B.
    PhylomeDBi P35221.
    TreeFami TF313686.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.
    REACT_21402. CDO in myogenesis.

    Miscellaneous databases

    ChiTaRSi CTNNA1. human.
    EvolutionaryTracei P35221.
    GeneWikii Catenin_(cadherin-associated_protein),_alpha_1.
    GenomeRNAii 1495.
    NextBioi 6145.
    PROi P35221.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35221.
    Bgeei P35221.
    CleanExi HS_CTNNA1.
    Genevestigatori P35221.

    Family and domain databases

    InterProi IPR001033. Alpha_catenin.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view ]
    PANTHERi PTHR18914. PTHR18914. 1 hit.
    Pfami PF01044. Vinculin. 2 hits.
    [Graphical view ]
    PRINTSi PR00805. ALPHACATENIN.
    SUPFAMi SSF47220. SSF47220. 4 hits.
    PROSITEi PS00663. VINCULIN_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiCTNA1_HUMAN
    AccessioniPrimary (citable) accession number: P35221
    Secondary accession number(s): Q12795, Q8N1C0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3