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P30999

- CTND1_MOUSE

UniProt

P30999 - CTND1_MOUSE

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Protein
Catenin delta-1
Gene
Ctnnd1, Catns, Kiaa0384
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei401 – 4011Essential for interaction with cadherins By similarity
Sitei478 – 4781Essential for interaction with cadherins By 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. Wnt signaling pathway Source: UniProtKB-KW
  2. brain development Source: Ensembl
  3. cell adhesion Source: MGI
  4. epithelial cell differentiation involved in salivary gland development Source: MGI
  5. keratinocyte differentiation Source: MGI
  6. morphogenesis of a polarized epithelium Source: MGI
  7. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  8. regulation of transcription, DNA-templated Source: UniProtKB-KW
  9. salivary gland morphogenesis Source: MGI
  10. single organismal cell-cell adhesion Source: MGI
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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-1
PRO_0000064297Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei4 – 41Phosphoserine By similarity
Modified residuei47 – 471Phosphoserine By similarity
Modified residuei112 – 1121Phosphotyrosine; by FYN By 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 – 2681Phosphoserine By similarity
Modified residuei269 – 2691Phosphoserine By similarity
Modified residuei280 – 2801Phosphotyrosine1 Publication
Modified residuei288 – 2881Phosphoserine; alternate1 Publication
Modified residuei288 – 2881Phosphoserine; by PAK7/PAK5; alternate By similarity
Modified residuei320 – 3201Phosphoserine By similarity
Modified residuei349 – 3491Phosphoserine3 Publications
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei811 – 8111Phosphoserine By similarity
Modified residuei847 – 8471Phosphoserine1 Publication
Modified residuei857 – 8571Phosphoserine1 Publication
Modified residuei859 – 8591Phosphoserine By similarity
Modified residuei864 – 8641Phosphoserine By similarity
Modified residuei865 – 8651Phosphotyrosine1 Publication
Modified residuei879 – 8791Phosphoserine By similarity
Modified residuei899 – 8991Phosphoserine1 Publication
Modified residuei904 – 9041Phosphotyrosine2 Publications
Modified residuei916 – 9161Phosphothreonine By similarity
Modified residuei920 – 9201Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ 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.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi198513. 15 interactions.
IntActiP30999. 14 interactions.
MINTiMINT-89877.

Structurei

3D structure databases

ProteinModelPortaliP30999.
SMRiP30999. Positions 358-852.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 4637 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi622 – 63514Nuclear localization signal1 Publication
Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the beta-catenin family.
Contains 10 ARM repeats.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei626 – 6316Missing in isoform 2.
VSP_030567
Alternative sequencei880 – 90021Missing in isoform 2 and isoform 3.
VSP_030568Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti405 – 4051R → A in CAA79078. 1 Publication
Sequence conflicti676 – 6761K → N in CAA79078. 1 Publication
Sequence conflicti715 – 7151I → R in CAA79078. 1 Publication
Sequence conflicti752 – 7521I → R in CAA79078. 1 Publication

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.
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 128 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

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