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O60716

- CTND1_HUMAN

UniProt

O60716 - CTND1_HUMAN

Protein

Catenin delta-1

Gene

CTNND1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway By similarity. Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei401 – 4011Essential for interaction with cadherins
    Sitei478 – 4781Essential for interaction with cadherins

    GO - Molecular functioni

    1. cadherin binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. receptor binding Source: UniProtKB

    GO - Biological processi

    1. adherens junction organization Source: Reactome
    2. brain development Source: Ensembl
    3. cell adhesion Source: ProtInc
    4. cell-cell junction organization Source: Reactome
    5. cell junction assembly Source: Reactome
    6. epithelial cell differentiation involved in salivary gland development Source: Ensembl
    7. keratinocyte differentiation Source: Ensembl
    8. morphogenesis of a polarized epithelium Source: Ensembl
    9. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    10. regulation of transcription, DNA-templated Source: UniProtKB-KW
    11. salivary gland morphogenesis Source: Ensembl
    12. single organismal cell-cell adhesion Source: Ensembl
    13. transcription, DNA-templated Source: UniProtKB-KW
    14. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_19195. Adherens junctions interactions.
    SignaLinkiO60716.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catenin delta-1
    Alternative name(s):
    Cadherin-associated Src substrate
    Short name:
    CAS
    p120 catenin
    Short name:
    p120(ctn)
    p120(cas)
    Gene namesi
    Name:CTNND1
    Synonyms:KIAA0384
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2515. CTNND1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane
    Note: Interaction with GLIS2 promotes nuclear translocation By similarity. Detected at cell-cell contacts. NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm. Isoforms 4A and 1AB are excluded from the nucleus.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: BHF-UCL
    4. dendritic spine Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. growth cone Source: Ensembl
    7. lamellipodium Source: Ensembl
    8. midbody Source: UniProtKB
    9. nucleus Source: BHF-UCL
    10. plasma membrane Source: UniProtKB
    11. synapse Source: Ensembl
    12. zonula adherens Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi363 – 3631W → A: Severely disrupts cadherin interaction. 1 Publication
    Mutagenesisi401 – 4011K → M: Complete loss of cadherin interaction. 1 Publication
    Mutagenesisi444 – 4441K → M: Severely disrupts cadherin interaction. 1 Publication
    Mutagenesisi477 – 4771W → A: Severely disrupts cadherin interaction. 1 Publication
    Mutagenesisi478 – 4781N → A: Complete loss of cadherin interaction. 1 Publication

    Organism-specific databases

    PharmGKBiPA27016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 968968Catenin delta-1PRO_0000064296Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei4 – 41Phosphoserine1 Publication
    Modified residuei47 – 471Phosphoserine3 Publications
    Modified residuei112 – 1121Phosphotyrosine; by FYN1 Publication
    Modified residuei217 – 2171PhosphotyrosineBy similarity
    Modified residuei221 – 2211PhosphotyrosineBy similarity
    Modified residuei228 – 2281PhosphotyrosineBy similarity
    Modified residuei230 – 2301Phosphoserine2 Publications
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei257 – 2571PhosphotyrosineBy similarity
    Modified residuei268 – 2681Phosphoserine1 Publication
    Modified residuei269 – 2691Phosphoserine1 Publication
    Modified residuei280 – 2801PhosphotyrosineBy similarity
    Modified residuei288 – 2881Phosphoserine; by PAK7/PAK54 Publications
    Modified residuei320 – 3201Phosphoserine1 Publication
    Modified residuei349 – 3491Phosphoserine2 Publications
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei811 – 8111Phosphoserine1 Publication
    Modified residuei847 – 8471Phosphoserine1 Publication
    Modified residuei857 – 8571Phosphoserine1 Publication
    Modified residuei859 – 8591Phosphoserine1 Publication
    Modified residuei864 – 8641Phosphoserine1 Publication
    Modified residuei865 – 8651PhosphotyrosineBy similarity
    Modified residuei879 – 8791Phosphoserine1 Publication
    Modified residuei899 – 8991PhosphoserineBy similarity
    Modified residuei904 – 9041PhosphotyrosineBy similarity
    Modified residuei916 – 9161Phosphothreonine1 Publication
    Modified residuei920 – 9201Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ.10 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60716.
    PaxDbiO60716.
    PRIDEiO60716.

    PTM databases

    PhosphoSiteiO60716.

    Expressioni

    Tissue specificityi

    Expressed in vascular endothelium. Melanocytes and melanoma cells primarily express the long isoform 1A, whereas keratinocytes express shorter isoforms, especially 3A. The shortest isoform 4A, is detected in normal keratinocytes and melanocytes, and generally lost from cells derived from squamous cell carcinomas or melanomas. The C-terminal alternatively spliced exon B is present in the p120ctn transcripts in the colon, intestine and prostate, but lost in several tumor tissues derived from these organs.2 Publications

    Inductioni

    Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure.1 Publication

    Gene expression databases

    ArrayExpressiO60716.
    BgeeiO60716.
    GenevestigatoriO60716.

    Organism-specific databases

    HPAiCAB003837.
    HPA015955.

    Interactioni

    Subunit structurei

    Belongs to a multiprotein cell-cell adhesion complex that also contains E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin. Binds to the C-terminal fragment of PSEN1 and mutually competes for E-cadherin. Interacts with ZBTB33. Interacts with GLIS2. Interacts with NANOS1 (via N-terminal region). Interacts with FER.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cdh1P098033EBI-702059,EBI-984420From a different organism.
    FRMD5Q7Z6J63EBI-701927,EBI-727282
    NANOS1Q8WY412EBI-9634525,EBI-9630165
    PPAP2BO144959EBI-701927,EBI-766232
    PTPRJQ129135EBI-701927,EBI-2264500

    Protein-protein interaction databases

    BioGridi107881. 38 interactions.
    DIPiDIP-33850N.
    IntActiO60716. 23 interactions.
    MINTiMINT-4999228.

    Structurei

    Secondary structure

    1
    968
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi368 – 3747
    Helixi380 – 39415
    Helixi398 – 4069
    Helixi409 – 4157
    Helixi416 – 4183
    Helixi422 – 43514
    Beta strandi437 – 4393
    Helixi441 – 4499
    Helixi452 – 46211
    Helixi466 – 47914
    Helixi483 – 4853
    Helixi486 – 4927
    Helixi494 – 5007
    Helixi502 – 5065
    Helixi524 – 53714
    Helixi542 – 5509
    Helixi554 – 56714
    Helixi574 – 58714
    Helixi590 – 5934
    Helixi655 – 6606
    Helixi662 – 67413
    Helixi678 – 69215
    Helixi697 – 70610
    Helixi709 – 7179
    Helixi718 – 7203
    Helixi724 – 73815
    Helixi744 – 75714
    Beta strandi759 – 7635
    Helixi766 – 7683
    Helixi772 – 78615
    Helixi790 – 7989
    Helixi801 – 8099
    Beta strandi812 – 8143
    Helixi816 – 83015
    Helixi833 – 8408
    Turni841 – 8433
    Helixi846 – 8494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L6XX-ray2.40A324-937[»]
    3L6YX-ray3.00A/C/E324-937[»]
    ProteinModelPortaliO60716.
    SMRiO60716. Positions 358-852.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60716.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati358 – 39538ARM 1Add
    BLAST
    Repeati398 – 43740ARM 2Add
    BLAST
    Repeati441 – 47535ARM 3Add
    BLAST
    Repeati476 – 51641ARM 4Add
    BLAST
    Repeati534 – 57340ARM 5Add
    BLAST
    Repeati583 – 62442ARM 6Add
    BLAST
    Repeati653 – 69341ARM 7Add
    BLAST
    Repeati700 – 73940ARM 8Add
    BLAST
    Repeati740 – 78041ARM 9Add
    BLAST
    Repeati781 – 82646ARM 10Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili10 – 4637Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi622 – 63413Nuclear localization signalBy similarityAdd
    BLAST

    Domaini

    A possible nuclear localization signal exists in all isoforms where Asp-626--631-Arg are deleted.
    ARM repeats 1 to 5 mediate interaction with cadherins.

    Sequence similaritiesi

    Belongs to the beta-catenin family.Curated
    Contains 10 ARM repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG276924.
    HOVERGENiHBG004284.
    InParanoidiO60716.
    KOiK05690.
    OMAiVLQTIWG.
    OrthoDBiEOG7N37BV.
    PhylomeDBiO60716.
    TreeFamiTF321877.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR028439. Catenin_d1.
    IPR028435. Plakophilin/d_Catenin.
    [Graphical view]
    PANTHERiPTHR10372. PTHR10372. 1 hit.
    PTHR10372:SF6. PTHR10372:SF6. 1 hit.
    PfamiPF00514. Arm. 3 hits.
    [Graphical view]
    SMARTiSM00185. ARM. 6 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    PROSITEiPS50176. ARM_REPEAT. 3 hits.
    [Graphical view]

    Sequences (32)i

    Sequence statusi: Complete.

    This entry describes 32 isoformsi produced by alternative splicing and alternative initiation. Align

    Note: Isoforms result of a combination of four transcription start sites and three alternatively spliced exons(A, B and C).

    Isoform 1ABC (identifier: O60716-1) [UniParc]FASTAAdd to Basket

    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

    MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD    50
    ANPLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HSHLLYSTIP 100
    RMQEPGQIVE TYTEEDPEGA MSVVSVETSD DGTTRRTETT VKKVVKTVTT 150
    RTVQPVAMGP DGLPVDASSV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA 200
    TLPRNFHYPP DGYSRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA 250
    PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 300
    DYGTARRTGT PSDPRRRLRS YEDMIGEEVP SDQYYWAPLA QHERGSLASL 350
    DSLRKGGPPP PNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV 400
    KTDVRKLKGI PVLVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC 450
    DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE 500
    VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE 550
    CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 600
    QEAAPNVANN TGPHAASCFG AKKGKDEWFS RGKKPIEDPA NDTVDFPKRT 650
    SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR 700
    YIRSALRQEK ALSAIADLLT NEHERVVKAA SGALRNLAVD ARNKELIGKH 750
    AIPNLVKNLP GGQQNSSWNF SEDTVISILN TINEVIAENL EAAKKLRETQ 800
    GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ 850
    VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIQM SNMGSNTKSL 900
    DNNYSTPNER GDHNRTLDRS GDLGDMEPLK GTTPLMQDEG QESLEEELDV 950
    LVLDDEGGQV SYPSMQKI 968
    Length:968
    Mass (Da):108,170
    Last modified:August 1, 1998 - v1
    Checksum:iD5C37489A891F292
    GO
    Isoform 1AB (identifier: O60716-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         626-631: Missing.

    Show »
    Length:962
    Mass (Da):107,349
    Checksum:i62C1AA58EC4ED712
    GO
    Isoform 1AC (identifier: O60716-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         937-965: Missing.

    Note: Contains a phosphothreonine at position 916.

    Show »
    Length:939
    Mass (Da):104,977
    Checksum:iD436D996ECBEBDC7
    GO
    Isoform 1BC (identifier: O60716-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         880-900: Missing.

    Show »
    Length:947
    Mass (Da):105,779
    Checksum:i46867A61854BBEDF
    GO
    Isoform 1A (identifier: O60716-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         626-631: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 910.

    Show »
    Length:933
    Mass (Da):104,156
    Checksum:iA4E1ABA2FE3D6B54
    GO
    Isoform 1B (identifier: O60716-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         626-631: Missing.
         880-900: Missing.

    Show »
    Length:941
    Mass (Da):104,958
    Checksum:iA82D282A5DF1C4BE
    GO
    Isoform 1C (identifier: O60716-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 895.

    Show »
    Length:918
    Mass (Da):102,586
    Checksum:i17D678061E042572
    GO
    Isoform 1 (identifier: O60716-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         626-631: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 889.

    Show »
    Length:912
    Mass (Da):101,765
    Checksum:i879022D64712C805
    GO
    Isoform 2ABC (identifier: O60716-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.

    Show »
    Length:914
    Mass (Da):102,063
    Checksum:i57A26859239AA55A
    GO
    Isoform 2AB (identifier: O60716-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         626-631: Missing.

    Show »
    Length:908
    Mass (Da):101,242
    Checksum:i95094A101A1B6DB4
    GO
    Isoform 2AC (identifier: O60716-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 862.

    Show »
    Length:885
    Mass (Da):98,870
    Checksum:iDF4D8956D2827CAA
    GO
    Isoform 2BC (identifier: O60716-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         880-900: Missing.

    Show »
    Length:893
    Mass (Da):99,673
    Checksum:iD0985DD5A04D4B3F
    GO
    Isoform 2A (identifier: O60716-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         626-631: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 856.

    Show »
    Length:879
    Mass (Da):98,049
    Checksum:iF58CA78A7097EFEB
    GO
    Isoform 2B (identifier: O60716-14) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         626-631: Missing.
         880-900: Missing.

    Show »
    Length:887
    Mass (Da):98,852
    Checksum:i1DCDD3510D31FA82
    GO
    Isoform 2C (identifier: O60716-15) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 841.

    Show »
    Length:864
    Mass (Da):96,479
    Checksum:iE418647839C3B386
    GO
    Isoform 2 (identifier: O60716-16) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: Missing.
         626-631: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 835.

    Show »
    Length:858
    Mass (Da):95,658
    Checksum:iA16496DCF8B2F524
    GO
    Isoform 3ABC (identifier: O60716-17) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.

    Show »
    Length:867
    Mass (Da):96,689
    Checksum:i5F9E3A466CA81D74
    GO
    Isoform 3AB (identifier: O60716-18) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         626-631: Missing.

    Show »
    Length:861
    Mass (Da):95,868
    Checksum:i3D2744052161BD93
    GO
    Isoform 3AC (identifier: O60716-19) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 815.

    Show »
    Length:838
    Mass (Da):93,496
    Checksum:iF840912548316394
    GO
    Isoform 3BC (identifier: O60716-20) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         880-900: Missing.

    Show »
    Length:846
    Mass (Da):94,299
    Checksum:iD482BB16BD5A898A
    GO
    Isoform 3A (identifier: O60716-21) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         626-631: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 809.

    Show »
    Length:832
    Mass (Da):92,675
    Checksum:iFAB29A345A6AABBC
    GO
    Isoform 3B (identifier: O60716-22) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         626-631: Missing.
         880-900: Missing.

    Show »
    Length:840
    Mass (Da):93,478
    Checksum:i0F78D45C15426031
    GO
    Isoform 3C (identifier: O60716-23) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 794.

    Show »
    Length:817
    Mass (Da):91,105
    Checksum:i7308172E06E2AC56
    GO
    Isoform 3 (identifier: O60716-24) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: Missing.
         626-631: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 788.

    Show »
    Length:811
    Mass (Da):90,284
    Checksum:i3EB46C6A74AA396C
    GO
    Isoform 4ABC (identifier: O60716-25) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.

    Show »
    Length:645
    Mass (Da):72,045
    Checksum:iDD32175D2F59D40D
    GO
    Isoform 4AB (identifier: O60716-26) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         626-631: Missing.

    Show »
    Length:639
    Mass (Da):71,225
    Checksum:iF45EA4D758555CE3
    GO
    Isoform 4AC (identifier: O60716-27) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 593.

    Show »
    Length:616
    Mass (Da):68,852
    Checksum:iE1014C183DAFB90D
    GO
    Isoform 4BC (identifier: O60716-28) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         880-900: Missing.

    Show »
    Length:624
    Mass (Da):69,655
    Checksum:iEEDFAEC10BE108A5
    GO
    Isoform 4A (identifier: O60716-29) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         626-631: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 587.

    Show »
    Length:610
    Mass (Da):68,031
    Checksum:i402B89CAE47E6A8E
    GO
    Isoform 4B (identifier: O60716-30) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         626-631: Missing.
         880-900: Missing.

    Show »
    Length:618
    Mass (Da):68,834
    Checksum:iAE57FD1DC87F15AF
    GO
    Isoform 4C (identifier: O60716-31) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 572.

    Show »
    Length:595
    Mass (Da):66,461
    Checksum:iC93D22BB614EA62B
    GO
    Isoform 4 (identifier: O60716-32) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-323: Missing.
         626-631: Missing.
         880-900: Missing.
         937-965: Missing.

    Note: Contains a phosphothreonine at position 566.

    Show »
    Length:589
    Mass (Da):65,641
    Checksum:i34C9A6E2B5944D2C
    GO

    Sequence cautioni

    The sequence BAA20838.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti319 – 3191R → M in BAA20838. (PubMed:9205841)Curated
    Sequence conflicti380 – 3801D → G in AAH75795. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711S → F.
    Corresponds to variant rs11229133 [ dbSNP | Ensembl ].
    VAR_038255
    Natural varianti217 – 2171Y → C.1 Publication
    Corresponds to variant rs11570194 [ dbSNP | Ensembl ].
    VAR_020929
    Natural varianti464 – 4641R → C.1 Publication
    Corresponds to variant rs11570199 [ dbSNP | Ensembl ].
    VAR_020930
    Natural varianti915 – 9151R → K.1 Publication
    Corresponds to variant rs11570222 [ dbSNP | Ensembl ].
    VAR_020931

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 323323Missing in isoform 4ABC, isoform 4AB, isoform 4AC, isoform 4BC, isoform 4A, isoform 4B, isoform 4C and isoform 4. CuratedVSP_006742Add
    BLAST
    Alternative sequencei1 – 101101Missing in isoform 3ABC, isoform 3AB, isoform 3AC, isoform 3BC, isoform 3A, isoform 3B, isoform 3C and isoform 3. CuratedVSP_006741Add
    BLAST
    Alternative sequencei1 – 5454Missing in isoform 2ABC, isoform 2AB, isoform 2AC, isoform 2BC, isoform 2A, isoform 2B, isoform 2C and isoform 2. CuratedVSP_006740Add
    BLAST
    Alternative sequencei626 – 6316Missing in isoform 1AB, isoform 1A, isoform 1B, isoform 1, isoform 2AB, isoform 2A, isoform 2B, isoform 2, isoform 3AB, isoform 3A, isoform 3B, isoform 3, isoform 4AB, isoform 4A, isoform 4B and isoform 4. 1 PublicationVSP_006743
    Alternative sequencei880 – 90021Missing in isoform 1BC, isoform 1B, isoform 1C, isoform 1, isoform 2BC, isoform 2B, isoform 2C, isoform 2, isoform 3BC, isoform 3B, isoform 3C, isoform 3, isoform 4BC, isoform 4B, isoform 4C and isoform 4. CuratedVSP_006744Add
    BLAST
    Alternative sequencei937 – 96529Missing in isoform 1AC, isoform 1A, isoform 1C, isoform 1, isoform 2AC, isoform 2A, isoform 2C, isoform 2, isoform 3AC, isoform 3A, isoform 3C, isoform 3, isoform 4AC, isoform 4A, isoform 4C and isoform 4. 3 PublicationsVSP_006745Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF062319 mRNA. Translation: AAC39804.1.
    AF062323 mRNA. Translation: AAC39808.1.
    AF062341 mRNA. Translation: AAC39826.1.
    AF062342 mRNA. Translation: AAC39827.1.
    AF062322 mRNA. Translation: AAC39807.1.
    AF062326 mRNA. Translation: AAC39811.1.
    AF062328 mRNA. Translation: AAC39813.1.
    AF062338 mRNA. Translation: AAC39823.1.
    AF062324 mRNA. Translation: AAC39809.1.
    AF062327 mRNA. Translation: AAC39812.1.
    AF062329 mRNA. Translation: AAC39814.1.
    AF062330 mRNA. Translation: AAC39815.1.
    AF062331 mRNA. Translation: AAC39816.1.
    AF062333 mRNA. Translation: AAC39818.1.
    AF062334 mRNA. Translation: AAC39819.1.
    AF062335 mRNA. Translation: AAC39820.1.
    AF062336 mRNA. Translation: AAC39821.1.
    AF062339 mRNA. Translation: AAC39824.1.
    AF062340 mRNA. Translation: AAC39825.1.
    AF062343 mRNA. Translation: AAC39828.1.
    AF062317 mRNA. Translation: AAC39802.1.
    AF062325 mRNA. Translation: AAC39810.1.
    AF062332 mRNA. Translation: AAC39817.1.
    AF062344 mRNA. Translation: AAC39829.1.
    AF062321 mRNA. Translation: AAC39806.1.
    AF062320 mRNA. Translation: AAC39805.1.
    AF062337 mRNA. Translation: AAC39822.1.
    AF062318 mRNA. Translation: AAC39803.1.
    AB002382 mRNA. Translation: BAA20838.2. Different initiation.
    AK292554 mRNA. Translation: BAF85243.1.
    AY505564 Genomic DNA. Translation: AAR84236.1.
    AP001931 Genomic DNA. No translation available.
    BC075795 mRNA. Translation: AAH75795.1.
    CCDSiCCDS44604.1. [O60716-1]
    CCDS44605.1. [O60716-2]
    CCDS44606.1. [O60716-5]
    CCDS44607.1. [O60716-6]
    CCDS44608.1. [O60716-17]
    CCDS44609.1. [O60716-21]
    CCDS53632.1. [O60716-19]
    CCDS53633.1. [O60716-18]
    CCDS53634.1. [O60716-22]
    CCDS55763.1. [O60716-9]
    CCDS55764.1. [O60716-11]
    CCDS55765.1. [O60716-10]
    CCDS55766.1. [O60716-13]
    CCDS55767.1. [O60716-14]
    RefSeqiNP_001078927.1. NM_001085458.1. [O60716-1]
    NP_001078928.1. NM_001085459.1. [O60716-2]
    NP_001078929.1. NM_001085460.1. [O60716-5]
    NP_001078930.1. NM_001085461.1. [O60716-5]
    NP_001078931.1. NM_001085462.1. [O60716-5]
    NP_001078932.1. NM_001085463.1. [O60716-17]
    NP_001078933.1. NM_001085464.1. [O60716-18]
    NP_001078934.1. NM_001085465.1. [O60716-22]
    NP_001078935.1. NM_001085466.1. [O60716-19]
    NP_001078936.1. NM_001085467.1. [O60716-21]
    NP_001078937.1. NM_001085468.1. [O60716-21]
    NP_001078938.1. NM_001085469.1. [O60716-21]
    NP_001193812.1. NM_001206883.1. [O60716-9]
    NP_001193813.1. NM_001206884.1. [O60716-11]
    NP_001193814.1. NM_001206885.1. [O60716-3]
    NP_001193815.1. NM_001206886.1. [O60716-10]
    NP_001193816.1. NM_001206887.1. [O60716-14]
    NP_001193817.1. NM_001206888.1. [O60716-13]
    NP_001193818.1. NM_001206889.1. [O60716-13]
    NP_001193819.1. NM_001206890.1. [O60716-21]
    NP_001193820.1. NM_001206891.1. [O60716-13]
    NP_001322.1. NM_001331.2. [O60716-6]
    UniGeneiHs.166011.

    Genome annotation databases

    EnsembliENST00000358694; ENSP00000351527; ENSG00000198561. [O60716-5]
    ENST00000361332; ENSP00000354823; ENSG00000198561. [O60716-2]
    ENST00000361391; ENSP00000354785; ENSG00000198561. [O60716-6]
    ENST00000361796; ENSP00000354907; ENSG00000198561. [O60716-5]
    ENST00000399050; ENSP00000382004; ENSG00000198561. [O60716-1]
    ENST00000415361; ENSP00000403518; ENSG00000198561. [O60716-17]
    ENST00000426142; ENSP00000409930; ENSG00000198561. [O60716-21]
    ENST00000428599; ENSP00000413586; ENSG00000198561. [O60716-5]
    ENST00000524630; ENSP00000436543; ENSG00000198561. [O60716-5]
    ENST00000525902; ENSP00000434672; ENSG00000198561. [O60716-27]
    ENST00000526357; ENSP00000433334; ENSG00000198561. [O60716-10]
    ENST00000526772; ENSP00000433158; ENSG00000198561. [O60716-29]
    ENST00000526938; ENSP00000432041; ENSG00000198561. [O60716-7]
    ENST00000527467; ENSP00000434900; ENSG00000198561. [O60716-25]
    ENST00000528232; ENSP00000435266; ENSG00000198561. [O60716-19]
    ENST00000528621; ENSP00000432243; ENSG00000198561. [O60716-13]
    ENST00000529526; ENSP00000436323; ENSG00000198561. [O60716-13]
    ENST00000529873; ENSP00000435494; ENSG00000198561. [O60716-14]
    ENST00000529986; ENSP00000437156; ENSG00000198561. [O60716-21]
    ENST00000530094; ENSP00000437327; ENSG00000198561. [O60716-18]
    ENST00000530748; ENSP00000436744; ENSG00000198561. [O60716-11]
    ENST00000531014; ENSP00000432623; ENSG00000198561. [O60716-26]
    ENST00000532245; ENSP00000434017; ENSG00000198561. [O60716-21]
    ENST00000532463; ENSP00000432075; ENSG00000198561. [O60716-21]
    ENST00000532649; ENSP00000435379; ENSG00000198561. [O60716-13]
    ENST00000532787; ENSP00000434949; ENSG00000198561. [O60716-22]
    ENST00000532844; ENSP00000433276; ENSG00000198561. [O60716-9]
    ENST00000533667; ENSP00000437051; ENSG00000198561. [O60716-30]
    ENST00000534579; ENSP00000435789; ENSG00000198561. [O60716-13]
    GeneIDi1500.
    KEGGihsa:1500.
    UCSCiuc001nlf.2. human. [O60716-3]
    uc001nli.4. human. [O60716-6]
    uc001nlj.4. human. [O60716-10]
    uc001nlk.4. human. [O60716-11]
    uc001nll.4. human. [O60716-13]
    uc001nlm.4. human. [O60716-5]
    uc001nlo.4. human. [O60716-18]
    uc001nlp.4. human. [O60716-14]
    uc001nlq.4. human. [O60716-19]
    uc001nls.4. human. [O60716-22]
    uc001nlt.4. human. [O60716-21]
    uc001nlx.4. human. [O60716-1]
    uc001nly.4. human. [O60716-26]
    uc001nlz.4. human. [O60716-27]
    uc001nma.4. human. [O60716-30]
    uc001nmb.4. human. [O60716-29]
    uc001nme.4. human. [O60716-2]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF062319 mRNA. Translation: AAC39804.1 .
    AF062323 mRNA. Translation: AAC39808.1 .
    AF062341 mRNA. Translation: AAC39826.1 .
    AF062342 mRNA. Translation: AAC39827.1 .
    AF062322 mRNA. Translation: AAC39807.1 .
    AF062326 mRNA. Translation: AAC39811.1 .
    AF062328 mRNA. Translation: AAC39813.1 .
    AF062338 mRNA. Translation: AAC39823.1 .
    AF062324 mRNA. Translation: AAC39809.1 .
    AF062327 mRNA. Translation: AAC39812.1 .
    AF062329 mRNA. Translation: AAC39814.1 .
    AF062330 mRNA. Translation: AAC39815.1 .
    AF062331 mRNA. Translation: AAC39816.1 .
    AF062333 mRNA. Translation: AAC39818.1 .
    AF062334 mRNA. Translation: AAC39819.1 .
    AF062335 mRNA. Translation: AAC39820.1 .
    AF062336 mRNA. Translation: AAC39821.1 .
    AF062339 mRNA. Translation: AAC39824.1 .
    AF062340 mRNA. Translation: AAC39825.1 .
    AF062343 mRNA. Translation: AAC39828.1 .
    AF062317 mRNA. Translation: AAC39802.1 .
    AF062325 mRNA. Translation: AAC39810.1 .
    AF062332 mRNA. Translation: AAC39817.1 .
    AF062344 mRNA. Translation: AAC39829.1 .
    AF062321 mRNA. Translation: AAC39806.1 .
    AF062320 mRNA. Translation: AAC39805.1 .
    AF062337 mRNA. Translation: AAC39822.1 .
    AF062318 mRNA. Translation: AAC39803.1 .
    AB002382 mRNA. Translation: BAA20838.2 . Different initiation.
    AK292554 mRNA. Translation: BAF85243.1 .
    AY505564 Genomic DNA. Translation: AAR84236.1 .
    AP001931 Genomic DNA. No translation available.
    BC075795 mRNA. Translation: AAH75795.1 .
    CCDSi CCDS44604.1. [O60716-1 ]
    CCDS44605.1. [O60716-2 ]
    CCDS44606.1. [O60716-5 ]
    CCDS44607.1. [O60716-6 ]
    CCDS44608.1. [O60716-17 ]
    CCDS44609.1. [O60716-21 ]
    CCDS53632.1. [O60716-19 ]
    CCDS53633.1. [O60716-18 ]
    CCDS53634.1. [O60716-22 ]
    CCDS55763.1. [O60716-9 ]
    CCDS55764.1. [O60716-11 ]
    CCDS55765.1. [O60716-10 ]
    CCDS55766.1. [O60716-13 ]
    CCDS55767.1. [O60716-14 ]
    RefSeqi NP_001078927.1. NM_001085458.1. [O60716-1 ]
    NP_001078928.1. NM_001085459.1. [O60716-2 ]
    NP_001078929.1. NM_001085460.1. [O60716-5 ]
    NP_001078930.1. NM_001085461.1. [O60716-5 ]
    NP_001078931.1. NM_001085462.1. [O60716-5 ]
    NP_001078932.1. NM_001085463.1. [O60716-17 ]
    NP_001078933.1. NM_001085464.1. [O60716-18 ]
    NP_001078934.1. NM_001085465.1. [O60716-22 ]
    NP_001078935.1. NM_001085466.1. [O60716-19 ]
    NP_001078936.1. NM_001085467.1. [O60716-21 ]
    NP_001078937.1. NM_001085468.1. [O60716-21 ]
    NP_001078938.1. NM_001085469.1. [O60716-21 ]
    NP_001193812.1. NM_001206883.1. [O60716-9 ]
    NP_001193813.1. NM_001206884.1. [O60716-11 ]
    NP_001193814.1. NM_001206885.1. [O60716-3 ]
    NP_001193815.1. NM_001206886.1. [O60716-10 ]
    NP_001193816.1. NM_001206887.1. [O60716-14 ]
    NP_001193817.1. NM_001206888.1. [O60716-13 ]
    NP_001193818.1. NM_001206889.1. [O60716-13 ]
    NP_001193819.1. NM_001206890.1. [O60716-21 ]
    NP_001193820.1. NM_001206891.1. [O60716-13 ]
    NP_001322.1. NM_001331.2. [O60716-6 ]
    UniGenei Hs.166011.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L6X X-ray 2.40 A 324-937 [» ]
    3L6Y X-ray 3.00 A/C/E 324-937 [» ]
    ProteinModelPortali O60716.
    SMRi O60716. Positions 358-852.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107881. 38 interactions.
    DIPi DIP-33850N.
    IntActi O60716. 23 interactions.
    MINTi MINT-4999228.

    PTM databases

    PhosphoSitei O60716.

    Proteomic databases

    MaxQBi O60716.
    PaxDbi O60716.
    PRIDEi O60716.

    Protocols and materials databases

    DNASUi 1500.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358694 ; ENSP00000351527 ; ENSG00000198561 . [O60716-5 ]
    ENST00000361332 ; ENSP00000354823 ; ENSG00000198561 . [O60716-2 ]
    ENST00000361391 ; ENSP00000354785 ; ENSG00000198561 . [O60716-6 ]
    ENST00000361796 ; ENSP00000354907 ; ENSG00000198561 . [O60716-5 ]
    ENST00000399050 ; ENSP00000382004 ; ENSG00000198561 . [O60716-1 ]
    ENST00000415361 ; ENSP00000403518 ; ENSG00000198561 . [O60716-17 ]
    ENST00000426142 ; ENSP00000409930 ; ENSG00000198561 . [O60716-21 ]
    ENST00000428599 ; ENSP00000413586 ; ENSG00000198561 . [O60716-5 ]
    ENST00000524630 ; ENSP00000436543 ; ENSG00000198561 . [O60716-5 ]
    ENST00000525902 ; ENSP00000434672 ; ENSG00000198561 . [O60716-27 ]
    ENST00000526357 ; ENSP00000433334 ; ENSG00000198561 . [O60716-10 ]
    ENST00000526772 ; ENSP00000433158 ; ENSG00000198561 . [O60716-29 ]
    ENST00000526938 ; ENSP00000432041 ; ENSG00000198561 . [O60716-7 ]
    ENST00000527467 ; ENSP00000434900 ; ENSG00000198561 . [O60716-25 ]
    ENST00000528232 ; ENSP00000435266 ; ENSG00000198561 . [O60716-19 ]
    ENST00000528621 ; ENSP00000432243 ; ENSG00000198561 . [O60716-13 ]
    ENST00000529526 ; ENSP00000436323 ; ENSG00000198561 . [O60716-13 ]
    ENST00000529873 ; ENSP00000435494 ; ENSG00000198561 . [O60716-14 ]
    ENST00000529986 ; ENSP00000437156 ; ENSG00000198561 . [O60716-21 ]
    ENST00000530094 ; ENSP00000437327 ; ENSG00000198561 . [O60716-18 ]
    ENST00000530748 ; ENSP00000436744 ; ENSG00000198561 . [O60716-11 ]
    ENST00000531014 ; ENSP00000432623 ; ENSG00000198561 . [O60716-26 ]
    ENST00000532245 ; ENSP00000434017 ; ENSG00000198561 . [O60716-21 ]
    ENST00000532463 ; ENSP00000432075 ; ENSG00000198561 . [O60716-21 ]
    ENST00000532649 ; ENSP00000435379 ; ENSG00000198561 . [O60716-13 ]
    ENST00000532787 ; ENSP00000434949 ; ENSG00000198561 . [O60716-22 ]
    ENST00000532844 ; ENSP00000433276 ; ENSG00000198561 . [O60716-9 ]
    ENST00000533667 ; ENSP00000437051 ; ENSG00000198561 . [O60716-30 ]
    ENST00000534579 ; ENSP00000435789 ; ENSG00000198561 . [O60716-13 ]
    GeneIDi 1500.
    KEGGi hsa:1500.
    UCSCi uc001nlf.2. human. [O60716-3 ]
    uc001nli.4. human. [O60716-6 ]
    uc001nlj.4. human. [O60716-10 ]
    uc001nlk.4. human. [O60716-11 ]
    uc001nll.4. human. [O60716-13 ]
    uc001nlm.4. human. [O60716-5 ]
    uc001nlo.4. human. [O60716-18 ]
    uc001nlp.4. human. [O60716-14 ]
    uc001nlq.4. human. [O60716-19 ]
    uc001nls.4. human. [O60716-22 ]
    uc001nlt.4. human. [O60716-21 ]
    uc001nlx.4. human. [O60716-1 ]
    uc001nly.4. human. [O60716-26 ]
    uc001nlz.4. human. [O60716-27 ]
    uc001nma.4. human. [O60716-30 ]
    uc001nmb.4. human. [O60716-29 ]
    uc001nme.4. human. [O60716-2 ]

    Organism-specific databases

    CTDi 1500.
    GeneCardsi GC11P057531.
    HGNCi HGNC:2515. CTNND1.
    HPAi CAB003837.
    HPA015955.
    MIMi 601045. gene.
    neXtProti NX_O60716.
    PharmGKBi PA27016.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG276924.
    HOVERGENi HBG004284.
    InParanoidi O60716.
    KOi K05690.
    OMAi VLQTIWG.
    OrthoDBi EOG7N37BV.
    PhylomeDBi O60716.
    TreeFami TF321877.

    Enzyme and pathway databases

    Reactomei REACT_19195. Adherens junctions interactions.
    SignaLinki O60716.

    Miscellaneous databases

    ChiTaRSi CTNND1. human.
    EvolutionaryTracei O60716.
    GeneWikii CTNND1.
    GenomeRNAii 1500.
    NextBioi 6177.
    PROi O60716.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60716.
    Bgeei O60716.
    Genevestigatori O60716.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR028439. Catenin_d1.
    IPR028435. Plakophilin/d_Catenin.
    [Graphical view ]
    PANTHERi PTHR10372. PTHR10372. 1 hit.
    PTHR10372:SF6. PTHR10372:SF6. 1 hit.
    Pfami PF00514. Arm. 3 hits.
    [Graphical view ]
    SMARTi SM00185. ARM. 6 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    PROSITEi PS50176. ARM_REPEAT. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the human p120ctn catenin gene (CTNND1): expression of multiple alternatively spliced isoforms."
      Keirsebilck A., Bonne S., Staes K., van Hengel J., Nollet F., Reynolds A., van Roy F.
      Genomics 50:129-146(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Fetal kidney.
    2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1AC).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1AC).
      Tissue: Testis.
    4. NIEHS SNPs program
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-217; CYS-464 AND LYS-915.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
      Tissue: Testis.
    7. "The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors."
      Kim L., Wong T.W.
      Mol. Cell. Biol. 15:4553-4561(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY FER, INTERACTION WITH FER.
    8. "The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor."
      Daniel J.M., Reynolds A.B.
      Mol. Cell. Biol. 19:3614-3623(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZBTB33.
    9. "Specific sequences in p120ctn determine subcellular distribution of its multiple isoforms involved in cellular adhesion of normal and malignant epithelial cells."
      Aho S., Levansuo L., Montonen O., Kari C., Rodeck U., Uitto J.
      J. Cell Sci. 115:1391-1402(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)."
      Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.
      Oncogene 21:7067-7076(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
    11. "Laminar shear stress differentially modulates gene expression of p120 catenin, Kaiso transcription factor, and vascular endothelial cadherin in human coronary artery endothelial cells."
      Kondapalli J., Flozak A.S., Albuquerque M.L.C.
      J. Biol. Chem. 279:11417-11424(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    12. "E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion."
      Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F.
      Cancer Res. 66:10007-10015(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS1.
    13. "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-47; SER-268; SER-269; SER-349 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. "The armadillo protein p0071 regulates Rho signalling during cytokinesis."
      Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M., Huttelmaier S., Hatzfeld M.
      Nat. Cell Biol. 8:1432-1440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "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 SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    17. "The transcriptional repressor Glis2 is a novel binding partner for p120 catenin."
      Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y.
      Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GLIS2, FUNCTION.
    18. "Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA."
      Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P., Bustelo X.R., Garcia de Herreros A., Dunach M.
      Mol. Cell. Biol. 27:1745-1757(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-112 BY FYN.
    19. "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-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-230 AND SER-288, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-889 (ISOFORM 1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-910 (ISOFORM 1A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916 (ISOFORM 1AC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-895 (ISOFORM 1C), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-835 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-856 (ISOFORM 2A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-862 (ISOFORM 2AC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-841 (ISOFORM 2C), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-788 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-809 (ISOFORM 3A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-815 (ISOFORM 3AC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-794 (ISOFORM 3C), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-566 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587 (ISOFORM 4A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-593 (ISOFORM 4AC), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-572 (ISOFORM 4C), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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].
    22. "p120-catenin is a binding partner and substrate for Group B Pak kinases."
      Wong L.E., Reynolds A.B., Dissanayaka N.T., Minden A.
      J. Cell. Biochem. 110:1244-1254(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-288 BY PAK7/PAK5.
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-47; SER-811; THR-916 AND SER-920, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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 SER-230; SER-320; SER-349; SER-847; SER-857; SER-859; SER-864; SER-879 AND SER-920, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion."
      Ishiyama N., Lee S.H., Liu S., Li G.Y., Smith M.J., Reichardt L.F., Ikura M.
      Cell 141:117-128(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 324-937 IN COMPLEX WITH CDH1, FUNCTION, SUBUNIT, MUTAGENESIS OF TRP-363; LYS-401; LYS-444; TRP-477 AND ASN-478.

    Entry informationi

    Entry nameiCTND1_HUMAN
    AccessioniPrimary (citable) accession number: O60716
    Secondary accession number(s): A8K939
    , O15088, O60713, O60714, O60715, O60935, Q6DHZ7, Q6RBX8, Q9UP71, Q9UP72, Q9UP73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2001
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 143 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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