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P30999 (CTND1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catenin delta-1
Alternative name(s):
Cadherin-associated Src substrate
Short name=CAS
p120 catenin
Short name=p120(ctn)
p120(cas)
Gene names
Name:Ctnnd1
Synonyms:Catns, Kiaa0384
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length938 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.13

Subunit structure

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. Ref.6 Ref.7 Ref.13

Subcellular location

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. Ref.8 Ref.13

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the beta-catenin family.

Contains 10 ARM repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Transcription
Transcription regulation
Wnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

brain development

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from mutant phenotype PubMed 14657280. Source: MGI

epithelial cell differentiation involved in salivary gland development

Inferred from mutant phenotype PubMed 16399075. Source: MGI

keratinocyte differentiation

Inferred from mutant phenotype PubMed 16510873. Source: MGI

morphogenesis of a polarized epithelium

Inferred from mutant phenotype PubMed 16399075PubMed 16510873. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 16399075. Source: MGI

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 16399075. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell-cell adherens junction

Inferred from direct assay PubMed 15775979. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from direct assay PubMed 14657280. Source: MGI

membrane

Inferred from direct assay PubMed 14657280. Source: MGI

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from mutant phenotype PubMed 16510873. Source: MGI

synapse

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from direct assay PubMed 17130295. Source: MGI

zonula adherens

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6PubMed 9670943. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 18794329. Source: MGI

protein phosphatase binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ptpn11P352353EBI-529924,EBI-397236
Zbtb33Q8BN783EBI-529924,EBI-1216314

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30999-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P30999-2)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
     880-900: Missing.
Isoform 3 (identifier: P30999-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 938938Catenin delta-1
PRO_0000064297

Regions

Repeat358 – 39538ARM 1
Repeat398 – 43740ARM 2
Repeat441 – 47535ARM 3
Repeat476 – 51641ARM 4
Repeat534 – 57340ARM 5
Repeat583 – 62442ARM 6
Repeat653 – 69341ARM 7
Repeat700 – 73940ARM 8
Repeat740 – 78041ARM 9
Repeat781 – 82646ARM 10
Coiled coil10 – 4637 Potential
Motif622 – 63514Nuclear localization signal Ref.8

Sites

Site4011Essential for interaction with cadherins By similarity
Site4781Essential for interaction with cadherins By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue41Phosphoserine By similarity
Modified residue471Phosphoserine By similarity
Modified residue1121Phosphotyrosine; by FYN By similarity
Modified residue2171Phosphotyrosine Ref.11
Modified residue2211Phosphotyrosine Ref.11
Modified residue2281Phosphotyrosine Ref.17
Modified residue2301Phosphoserine Ref.14
Modified residue2521Phosphoserine Ref.14
Modified residue2571Phosphotyrosine Ref.17
Modified residue2681Phosphoserine By similarity
Modified residue2691Phosphoserine By similarity
Modified residue2801Phosphotyrosine Ref.11
Modified residue2881Phosphoserine; alternate Ref.14
Modified residue2881Phosphoserine; by PAK7/PAK5; alternate By similarity
Modified residue3201Phosphoserine By similarity
Modified residue3491Phosphoserine Ref.14 Ref.15 Ref.17
Modified residue3521Phosphoserine Ref.17
Modified residue8111Phosphoserine By similarity
Modified residue8471Phosphoserine Ref.14
Modified residue8571Phosphoserine Ref.14
Modified residue8591Phosphoserine By similarity
Modified residue8641Phosphoserine By similarity
Modified residue8651Phosphotyrosine Ref.14
Modified residue8791Phosphoserine By similarity
Modified residue8991Phosphoserine Ref.14
Modified residue9041Phosphotyrosine Ref.12 Ref.17
Modified residue9161Phosphothreonine By similarity
Modified residue9201Phosphoserine By similarity

Natural variations

Alternative sequence626 – 6316Missing in isoform 2.
VSP_030567
Alternative sequence880 – 90021Missing in isoform 2 and isoform 3.
VSP_030568

Experimental info

Mutagenesis622 – 6232KK → AA: Abolishes nuclear localization. Ref.8
Sequence conflict4051R → A in CAA79078. Ref.1
Sequence conflict6761K → N in CAA79078. Ref.1
Sequence conflict7151I → R in CAA79078. Ref.1
Sequence conflict7521I → R in CAA79078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 2F13DB7350355832

FASTA938104,925
        10         20         30         40         50         60 
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL 

        70         80         90        100        110        120 
TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA 

       130        140        150        160        170        180 
MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR 

       190        200        210        220        230        240 
DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER 

       250        260        270        280        290        300 
YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 

       310        320        330        340        350        360 
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP 

       370        380        390        400        410        420 
SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP 

       430        440        450        460        470        480 
KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS 

       490        500        510        520        530        540 
SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE 

       550        560        570        580        590        600 
RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 

       610        620        630        640        650        660 
QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF 

       670        680        690        700        710        720 
QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT 

       730        740        750        760        770        780 
SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN 

       790        800        810        820        830        840 
TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE 

       850        860        870        880        890        900 
KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL 

       910        920        930 
DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI 

« Hide

Isoform 2 [UniParc].

Checksum: 8EBEA0D3FA88C843
Show »

FASTA911101,744
Isoform 3 [UniParc].

Checksum: 8FA40C72176733E8
Show »

FASTA917102,565

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16186.1. [P30999-1]
CCDS50622.1. [P30999-2]
CCDS50623.1. [P30999-3]
PIRS28498. I48701.
RefSeqNP_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]
UniGeneMm.35738.

3D structure databases

ProteinModelPortalP30999.
SMRP30999. Positions 358-852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198513. 15 interactions.
IntActP30999. 14 interactions.
MINTMINT-89877.

PTM databases

PhosphoSiteP30999.

Proteomic databases

MaxQBP30999.
PaxDbP30999.
PRIDEP30999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3]
ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2]
ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1]
ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1]
ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3]
GeneID12388.
KEGGmmu:12388.
UCSCuc008kio.1. mouse. [P30999-3]
uc008kip.1. mouse. [P30999-1]
uc008kit.1. mouse. [P30999-2]

Organism-specific databases

CTD1500.
MGIMGI:105100. Ctnnd1.
RougeSearch...

Phylogenomic databases

eggNOGNOG276924.
GeneTreeENSGT00690000101851.
HOGENOMHOG000231862.
HOVERGENHBG004284.
KOK05690.
PhylomeDBP30999.
TreeFamTF321877.

Gene expression databases

BgeeP30999.
CleanExMM_CTNND1.
GenevestigatorP30999.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR028439. Catenin_d1.
IPR028435. Plakophilin/d_Catenin.
[Graphical view]
PANTHERPTHR10372. PTHR10372. 1 hit.
PTHR10372:SF6. PTHR10372:SF6. 1 hit.
PfamPF00514. Arm. 3 hits.
[Graphical view]
SMARTSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS50176. ARM_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTNND1. mouse.
NextBio281110.
PROP30999.
SOURCESearch...

Entry information

Entry nameCTND1_MOUSE
AccessionPrimary (citable) accession number: P30999
Secondary accession number(s): Q3TSU9, Q80XQ4, Q8CHF8
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot