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P30999

- CTND1_MOUSE

UniProt

P30999 - CTND1_MOUSE

Protein

Catenin delta-1

Gene

Ctnnd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      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 similarity3 Publications

    Sites

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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein domain specific binding Source: MGI
    3. protein phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cell adhesion Source: MGI
    3. epithelial cell differentiation involved in salivary gland development Source: MGI
    4. keratinocyte differentiation Source: MGI
    5. morphogenesis of a polarized epithelium Source: MGI
    6. negative regulation of canonical Wnt signaling pathway Source: Ensembl
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. salivary gland morphogenesis Source: MGI
    9. single organismal cell-cell adhesion Source: MGI
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

    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:Catns, Kiaa0384
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:105100. Ctnnd1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell membrane
    Note: Interaction with GLIS2 promotes nuclear translocation. Detected at cell-cell contacts. NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm By similarity.By similarity

    GO - Cellular componenti

    1. cell-cell adherens junction Source: MGI
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Ensembl
    4. dendritic spine Source: Ensembl
    5. growth cone Source: Ensembl
    6. lamellipodium Source: MGI
    7. membrane Source: MGI
    8. midbody Source: UniProtKB
    9. nucleus Source: UniProtKB-SubCell
    10. plasma membrane Source: MGI
    11. synapse Source: Ensembl
    12. tight junction Source: MGI
    13. zonula adherens Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi622 – 6232KK → AA: Abolishes nuclear localization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 938938Catenin delta-1PRO_0000064297Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei4 – 41PhosphoserineBy similarity
    Modified residuei47 – 471PhosphoserineBy similarity
    Modified residuei112 – 1121Phosphotyrosine; by FYNBy similarity
    Modified residuei217 – 2171Phosphotyrosine1 Publication
    Modified residuei221 – 2211Phosphotyrosine1 Publication
    Modified residuei228 – 2281Phosphotyrosine1 Publication
    Modified residuei230 – 2301Phosphoserine1 Publication
    Modified residuei252 – 2521Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphotyrosine1 Publication
    Modified residuei268 – 2681PhosphoserineBy similarity
    Modified residuei269 – 2691PhosphoserineBy similarity
    Modified residuei280 – 2801Phosphotyrosine1 Publication
    Modified residuei288 – 2881Phosphoserine; alternate1 Publication
    Modified residuei288 – 2881Phosphoserine; by PAK7/PAK5; alternateBy similarity
    Modified residuei320 – 3201PhosphoserineBy similarity
    Modified residuei349 – 3491Phosphoserine3 Publications
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei811 – 8111PhosphoserineBy similarity
    Modified residuei847 – 8471Phosphoserine1 Publication
    Modified residuei857 – 8571Phosphoserine1 Publication
    Modified residuei859 – 8591PhosphoserineBy similarity
    Modified residuei864 – 8641PhosphoserineBy similarity
    Modified residuei865 – 8651Phosphotyrosine1 Publication
    Modified residuei879 – 8791PhosphoserineBy similarity
    Modified residuei899 – 8991Phosphoserine1 Publication
    Modified residuei904 – 9041Phosphotyrosine2 Publications
    Modified residuei916 – 9161PhosphothreonineBy similarity
    Modified residuei920 – 9201PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP30999.
    PaxDbiP30999.
    PRIDEiP30999.

    PTM databases

    PhosphoSiteiP30999.

    Expressioni

    Gene expression databases

    BgeeiP30999.
    CleanExiMM_CTNND1.
    GenevestigatoriP30999.

    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 By similarity. Interacts with ZBTB33. Interacts with GLIS2 and FER. Interacts with NANOS1 (via N-terminal region) By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ptpn11P352353EBI-529924,EBI-397236
    Zbtb33Q8BN783EBI-529924,EBI-1216314

    Protein-protein interaction databases

    BioGridi198513. 15 interactions.
    DIPiDIP-31972N.
    IntActiP30999. 14 interactions.
    MINTiMINT-89877.

    Structurei

    3D structure databases

    ProteinModelPortaliP30999.
    SMRiP30999. Positions 358-852.
    ModBaseiSearch...
    MobiDBiSearch...

    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 – 63514Nuclear localization signal1 PublicationAdd
    BLAST

    Domaini

    ARM repeats 1 to 5 mediate interaction with cadherins.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG276924.
    GeneTreeiENSGT00690000101851.
    HOGENOMiHOG000231862.
    HOVERGENiHBG004284.
    KOiK05690.
    PhylomeDBiP30999.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30999-1) [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
    ANSLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP 100
    RMQEPGQIVE TYTEEDPEGA MSVVSVETTD DGTTRRTETT VKKVVKTMTT 150
    RTVQPVPMGP DGLPVDASAV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA 200
    TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA 250
    PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 300
    DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL 350
    DSLRKGMPPP SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV 400
    KTDVRKLKGI PILVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC 450
    DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE 500
    VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE 550
    CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 600
    QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT 650
    SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR 700
    YIRSALRQEK ALSAIAELLT SEHERVVKAA SGALRNLAVD ARNKELIGKH 750
    AIPNLVKNLP GGQQNSSWNF SEDTVVSILN TINEVIAENL EAAKKLRETQ 800
    GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ 850
    VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL 900
    DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI 938
    Length:938
    Mass (Da):104,925
    Last modified:January 15, 2008 - v2
    Checksum:i2F13DB7350355832
    GO
    Isoform 2 (identifier: P30999-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:911
    Mass (Da):101,744
    Checksum:i8EBEA0D3FA88C843
    GO
    Isoform 3 (identifier: P30999-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:917
    Mass (Da):102,565
    Checksum:i8FA40C72176733E8
    GO

    Sequence cautioni

    The sequence BAC41421.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti405 – 4051R → A in CAA79078. (PubMed:1334250)Curated
    Sequence conflicti676 – 6761K → N in CAA79078. (PubMed:1334250)Curated
    Sequence conflicti715 – 7151I → R in CAA79078. (PubMed:1334250)Curated
    Sequence conflicti752 – 7521I → R in CAA79078. (PubMed:1334250)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei626 – 6316Missing in isoform 2. 1 PublicationVSP_030567
    Alternative sequencei880 – 90021Missing in isoform 2 and isoform 3. 3 PublicationsVSP_030568Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17804 mRNA. Translation: CAA79078.1.
    AB093237 mRNA. Translation: BAC41421.1. Different initiation.
    AK133193 mRNA. Translation: BAE21551.1.
    AK161790 mRNA. Translation: BAE36576.1.
    BC043108 mRNA. Translation: AAH43108.1.
    BC054544 mRNA. Translation: AAH54544.1.
    CCDSiCCDS16186.1. [P30999-1]
    CCDS50622.1. [P30999-2]
    CCDS50623.1. [P30999-3]
    PIRiI48701. S28498.
    RefSeqiNP_001078917.1. NM_001085448.1. [P30999-3]
    NP_001078918.1. NM_001085449.1.
    NP_001078919.1. NM_001085450.1. [P30999-1]
    NP_001078922.1. NM_001085453.1. [P30999-2]
    NP_031641.2. NM_007615.4. [P30999-1]
    XP_006498698.1. XM_006498635.1. [P30999-1]
    XP_006498700.1. XM_006498637.1. [P30999-3]
    UniGeneiMm.35738.

    Genome annotation databases

    EnsembliENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3]
    ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2]
    ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1]
    ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1]
    ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3]
    GeneIDi12388.
    KEGGimmu:12388.
    UCSCiuc008kio.1. mouse. [P30999-3]
    uc008kip.1. mouse. [P30999-1]
    uc008kit.1. mouse. [P30999-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z17804 mRNA. Translation: CAA79078.1 .
    AB093237 mRNA. Translation: BAC41421.1 . Different initiation.
    AK133193 mRNA. Translation: BAE21551.1 .
    AK161790 mRNA. Translation: BAE36576.1 .
    BC043108 mRNA. Translation: AAH43108.1 .
    BC054544 mRNA. Translation: AAH54544.1 .
    CCDSi CCDS16186.1. [P30999-1 ]
    CCDS50622.1. [P30999-2 ]
    CCDS50623.1. [P30999-3 ]
    PIRi I48701. S28498.
    RefSeqi NP_001078917.1. NM_001085448.1. [P30999-3 ]
    NP_001078918.1. NM_001085449.1.
    NP_001078919.1. NM_001085450.1. [P30999-1 ]
    NP_001078922.1. NM_001085453.1. [P30999-2 ]
    NP_031641.2. NM_007615.4. [P30999-1 ]
    XP_006498698.1. XM_006498635.1. [P30999-1 ]
    XP_006498700.1. XM_006498637.1. [P30999-3 ]
    UniGenei Mm.35738.

    3D structure databases

    ProteinModelPortali P30999.
    SMRi P30999. Positions 358-852.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198513. 15 interactions.
    DIPi DIP-31972N.
    IntActi P30999. 14 interactions.
    MINTi MINT-89877.

    PTM databases

    PhosphoSitei P30999.

    Proteomic databases

    MaxQBi P30999.
    PaxDbi P30999.
    PRIDEi P30999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036811 ; ENSMUSP00000042543 ; ENSMUSG00000034101 . [P30999-3 ]
    ENSMUST00000066177 ; ENSMUSP00000065252 ; ENSMUSG00000034101 . [P30999-2 ]
    ENSMUST00000067232 ; ENSMUSP00000064518 ; ENSMUSG00000034101 . [P30999-1 ]
    ENSMUST00000111691 ; ENSMUSP00000107320 ; ENSMUSG00000034101 . [P30999-1 ]
    ENSMUST00000111697 ; ENSMUSP00000107326 ; ENSMUSG00000034101 . [P30999-3 ]
    GeneIDi 12388.
    KEGGi mmu:12388.
    UCSCi uc008kio.1. mouse. [P30999-3 ]
    uc008kip.1. mouse. [P30999-1 ]
    uc008kit.1. mouse. [P30999-2 ]

    Organism-specific databases

    CTDi 1500.
    MGIi MGI:105100. Ctnnd1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG276924.
    GeneTreei ENSGT00690000101851.
    HOGENOMi HOG000231862.
    HOVERGENi HBG004284.
    KOi K05690.
    PhylomeDBi P30999.
    TreeFami TF321877.

    Miscellaneous databases

    ChiTaRSi CTNND1. mouse.
    NextBioi 281110.
    PROi P30999.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30999.
    CleanExi MM_CTNND1.
    Genevestigatori P30999.

    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. "p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors beta-catenin, plakoglobin and armadillo."
      Reynolds A.B., Herbert L., Cleveland J.L., Berg S.T., Gaut J.R.
      Oncogene 7:2439-2445(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: Swiss.
    2. Reynolds A.B.
      Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
      DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Testis.
    5. "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 1).
      Strain: C57BL/6.
      Tissue: Brain.
    6. "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.
    7. "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides."
      Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.
      Nucleic Acids Res. 30:2911-2919(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZBTB33.
    8. "NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression."
      Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
      J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623.
    9. Erratum
      Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.
      J. Cell Sci. 117:3405-3405(2004)
    10. "The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin."
      Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M.
      Exp. Cell Res. 305:253-265(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217; TYR-221 AND TYR-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    13. "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, SUBCELLULAR LOCATION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-288; SER-349; SER-847; SER-857; TYR-865 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349; SER-352 AND TYR-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCTND1_MOUSE
    AccessioniPrimary (citable) accession number: P30999
    Secondary accession number(s): Q3TSU9, Q80XQ4, Q8CHF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3