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O60716 (CTND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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:KIAA0384
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length968 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.17 Ref.28

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. Interacts with ZBTB33. Interacts with GLIS2. Interacts with NANOS1 (via N-terminal region). Interacts with FER. Ref.7 Ref.8 Ref.12 Ref.17 Ref.28

Subcellular location

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. Ref.9 Ref.12 Ref.15

Isoform 1A: Nucleus Ref.9 Ref.12 Ref.15.

Isoform 2A: Nucleus Ref.9 Ref.12 Ref.15.

Isoform 3A: Nucleus Ref.9 Ref.12 Ref.15.

Tissue specificity

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. Ref.9 Ref.11

Induction

Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure. Ref.11

Domain

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.

Post-translational modification

Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ. Ref.7 Ref.10 Ref.18 Ref.22

Sequence similarities

Belongs to the beta-catenin family.

Contains 10 ARM repeats.

Sequence caution

The sequence BAA20838.2 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 initiation
Alternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

adherens junction organization

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Non-traceable author statement PubMed 8808291. Source: ProtInc

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

epithelial cell differentiation involved in salivary gland development

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

morphogenesis of a polarized epithelium

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell-cell junction

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Inferred from mutant phenotype PubMed 20123964. Source: BHF-UCL

dendritic spine

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 20123964. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.15PubMed 19615783. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: Ensembl

zonula adherens

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncadherin binding

Inferred from physical interaction PubMed 12734196. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.28. Source: IntAct

receptor binding

Inferred from physical interaction PubMed 19332538. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdh1P098033EBI-702059,EBI-984420From a different organism.
FRMD5Q7Z6J63EBI-701927,EBI-727282
PPAP2BO144959EBI-701927,EBI-766232
PTPRJQ129135EBI-701927,EBI-2264500

Alternative products

This entry describes 32 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

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)

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 1AB (identifier: O60716-2)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
Isoform 1AC (identifier: O60716-3)

The sequence of this isoform differs from the canonical sequence as follows:
     937-965: Missing.
Note: Contains a phosphothreonine at position 916.
Isoform 1BC (identifier: O60716-4)

The sequence of this isoform differs from the canonical sequence as follows:
     880-900: Missing.
Isoform 1A (identifier: O60716-5)

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.
Isoform 1B (identifier: O60716-6)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
     880-900: Missing.
Isoform 1C (identifier: O60716-7)

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.
Isoform 1 (identifier: O60716-8)

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.
Isoform 2ABC (identifier: O60716-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
Isoform 2AB (identifier: O60716-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.
Isoform 2AC (identifier: O60716-11)

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.
Isoform 2BC (identifier: O60716-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     880-900: Missing.
Isoform 2A (identifier: O60716-13)

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.
Isoform 2B (identifier: O60716-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.
     880-900: Missing.
Isoform 2C (identifier: O60716-15)

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.
Isoform 2 (identifier: O60716-16)

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.
Isoform 3ABC (identifier: O60716-17)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
Isoform 3AB (identifier: O60716-18)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.
Isoform 3AC (identifier: O60716-19)

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.
Isoform 3BC (identifier: O60716-20)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     880-900: Missing.
Isoform 3A (identifier: O60716-21)

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.
Isoform 3B (identifier: O60716-22)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.
     880-900: Missing.
Isoform 3C (identifier: O60716-23)

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.
Isoform 3 (identifier: O60716-24)

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.
Isoform 4ABC (identifier: O60716-25)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
Isoform 4AB (identifier: O60716-26)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.
Isoform 4AC (identifier: O60716-27)

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.
Isoform 4BC (identifier: O60716-28)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     880-900: Missing.
Isoform 4A (identifier: O60716-29)

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.
Isoform 4B (identifier: O60716-30)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.
     880-900: Missing.
Isoform 4C (identifier: O60716-31)

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.
Isoform 4 (identifier: O60716-32)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 968968Catenin delta-1
PRO_0000064296

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 – 63413Nuclear localization signal By similarity

Sites

Site4011Essential for interaction with cadherins
Site4781Essential for interaction with cadherins

Amino acid modifications

Modified residue11N-acetylmethionine Ref.23 Ref.26 Ref.27
Modified residue41Phosphoserine Ref.23
Modified residue471Phosphoserine Ref.13 Ref.20 Ref.23
Modified residue1121Phosphotyrosine; by FYN Ref.18
Modified residue2171Phosphotyrosine By similarity
Modified residue2211Phosphotyrosine By similarity
Modified residue2281Phosphotyrosine By similarity
Modified residue2301Phosphoserine Ref.20 Ref.25
Modified residue2521Phosphoserine By similarity
Modified residue2571Phosphotyrosine By similarity
Modified residue2681Phosphoserine Ref.13
Modified residue2691Phosphoserine Ref.13
Modified residue2801Phosphotyrosine By similarity
Modified residue2881Phosphoserine; by PAK7/PAK5 Ref.16 Ref.19 Ref.20 Ref.22
Modified residue3201Phosphoserine Ref.25
Modified residue3491Phosphoserine Ref.13 Ref.25
Modified residue3521Phosphoserine Ref.13
Modified residue8111Phosphoserine Ref.23
Modified residue8471Phosphoserine Ref.25
Modified residue8571Phosphoserine Ref.25
Modified residue8591Phosphoserine Ref.25
Modified residue8641Phosphoserine Ref.25
Modified residue8651Phosphotyrosine By similarity
Modified residue8791Phosphoserine Ref.25
Modified residue8991Phosphoserine By similarity
Modified residue9041Phosphotyrosine By similarity
Modified residue9161Phosphothreonine Ref.20 Ref.23
Modified residue9201Phosphoserine Ref.23 Ref.25

Natural variations

Alternative sequence1 – 323323Missing in isoform 4ABC, isoform 4AB, isoform 4AC, isoform 4BC, isoform 4A, isoform 4B, isoform 4C and isoform 4.
VSP_006742
Alternative sequence1 – 101101Missing in isoform 3ABC, isoform 3AB, isoform 3AC, isoform 3BC, isoform 3A, isoform 3B, isoform 3C and isoform 3.
VSP_006741
Alternative sequence1 – 5454Missing in isoform 2ABC, isoform 2AB, isoform 2AC, isoform 2BC, isoform 2A, isoform 2B, isoform 2C and isoform 2.
VSP_006740
Alternative sequence626 – 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.
VSP_006743
Alternative sequence880 – 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.
VSP_006744
Alternative sequence937 – 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.
VSP_006745
Natural variant1711S → F.
Corresponds to variant rs11229133 [ dbSNP | Ensembl ].
VAR_038255
Natural variant2171Y → C. Ref.4
Corresponds to variant rs11570194 [ dbSNP | Ensembl ].
VAR_020929
Natural variant4641R → C. Ref.4
Corresponds to variant rs11570199 [ dbSNP | Ensembl ].
VAR_020930
Natural variant9151R → K. Ref.4
Corresponds to variant rs11570222 [ dbSNP | Ensembl ].
VAR_020931

Experimental info

Mutagenesis3631W → A: Severely disrupts cadherin interaction. Ref.28
Mutagenesis4011K → M: Complete loss of cadherin interaction. Ref.28
Mutagenesis4441K → M: Severely disrupts cadherin interaction. Ref.28
Mutagenesis4771W → A: Severely disrupts cadherin interaction. Ref.28
Mutagenesis4781N → A: Complete loss of cadherin interaction. Ref.28
Sequence conflict3191R → M in BAA20838. Ref.2
Sequence conflict3801D → G in AAH75795. Ref.6

Secondary structure

....................................................................... 968
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: D5C37489A891F292

FASTA968108,170
        10         20         30         40         50         60 
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANPLMANGTL 

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

       130        140        150        160        170        180 
MSVVSVETSD DGTTRRTETT VKKVVKTVTT RTVQPVAMGP DGLPVDASSV SNNYIQTLGR 

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

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

       310        320        330        340        350        360 
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP SDQYYWAPLA QHERGSLASL DSLRKGGPPP 

       370        380        390        400        410        420 
PNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PVLVGLLDHP 

       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 
QEAAPNVANN TGPHAASCFG AKKGKDEWFS RGKKPIEDPA NDTVDFPKRT SPARGYELLF 

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

       730        740        750        760        770        780 
NEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVISILN 

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

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

       910        920        930        940        950        960 
DNNYSTPNER GDHNRTLDRS GDLGDMEPLK GTTPLMQDEG QESLEEELDV LVLDDEGGQV 


SYPSMQKI 

« Hide

Isoform 1AB [UniParc].

Checksum: 62C1AA58EC4ED712
Show »

FASTA962107,349
Isoform 1AC [UniParc].

Checksum: D436D996ECBEBDC7
Show »

FASTA939104,977
Isoform 1BC [UniParc].

Checksum: 46867A61854BBEDF
Show »

FASTA947105,779
Isoform 1A [UniParc].

Checksum: A4E1ABA2FE3D6B54
Show »

FASTA933104,156
Isoform 1B [UniParc].

Checksum: A82D282A5DF1C4BE
Show »

FASTA941104,958
Isoform 1C [UniParc].

Checksum: 17D678061E042572
Show »

FASTA918102,586
Isoform 1 [UniParc].

Checksum: 879022D64712C805
Show »

FASTA912101,765
Isoform 2ABC [UniParc].

Checksum: 57A26859239AA55A
Show »

FASTA914102,063
Isoform 2AB [UniParc].

Checksum: 95094A101A1B6DB4
Show »

FASTA908101,242
Isoform 2AC [UniParc].

Checksum: DF4D8956D2827CAA
Show »

FASTA88598,870
Isoform 2BC [UniParc].

Checksum: D0985DD5A04D4B3F
Show »

FASTA89399,673
Isoform 2A [UniParc].

Checksum: F58CA78A7097EFEB
Show »

FASTA87998,049
Isoform 2B [UniParc].

Checksum: 1DCDD3510D31FA82
Show »

FASTA88798,852
Isoform 2C [UniParc].

Checksum: E418647839C3B386
Show »

FASTA86496,479
Isoform 2 [UniParc].

Checksum: A16496DCF8B2F524
Show »

FASTA85895,658
Isoform 3ABC [UniParc].

Checksum: 5F9E3A466CA81D74
Show »

FASTA86796,689
Isoform 3AB [UniParc].

Checksum: 3D2744052161BD93
Show »

FASTA86195,868
Isoform 3AC [UniParc].

Checksum: F840912548316394
Show »

FASTA83893,496
Isoform 3BC [UniParc].

Checksum: D482BB16BD5A898A
Show »

FASTA84694,299
Isoform 3A [UniParc].

Checksum: FAB29A345A6AABBC
Show »

FASTA83292,675
Isoform 3B [UniParc].

Checksum: 0F78D45C15426031
Show »

FASTA84093,478
Isoform 3C [UniParc].

Checksum: 7308172E06E2AC56
Show »

FASTA81791,105
Isoform 3 [UniParc].

Checksum: 3EB46C6A74AA396C
Show »

FASTA81190,284
Isoform 4ABC [UniParc].

Checksum: DD32175D2F59D40D
Show »

FASTA64572,045
Isoform 4AB [UniParc].

Checksum: F45EA4D758555CE3
Show »

FASTA63971,225
Isoform 4AC [UniParc].

Checksum: E1014C183DAFB90D
Show »

FASTA61668,852
Isoform 4BC [UniParc].

Checksum: EEDFAEC10BE108A5
Show »

FASTA62469,655
Isoform 4A [UniParc].

Checksum: 402B89CAE47E6A8E
Show »

FASTA61068,031
Isoform 4B [UniParc].

Checksum: AE57FD1DC87F15AF
Show »

FASTA61868,834
Isoform 4C [UniParc].

Checksum: C93D22BB614EA62B
Show »

FASTA59566,461
Isoform 4 [UniParc].

Checksum: 34C9A6E2B5944D2C
Show »

FASTA58965,641

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44604.1. [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]
RefSeqNP_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]
UniGeneHs.166011.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6XX-ray2.40A324-937[»]
3L6YX-ray3.00A/C/E324-937[»]
ProteinModelPortalO60716.
SMRO60716. Positions 358-852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107881. 37 interactions.
IntActO60716. 22 interactions.
MINTMINT-4999228.

PTM databases

PhosphoSiteO60716.

Proteomic databases

MaxQBO60716.
PaxDbO60716.
PRIDEO60716.

Protocols and materials databases

DNASU1500.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358694; ENSP00000351527; ENSG00000198561. [O60716-5]
ENST00000360682; ENSP00000353902; ENSG00000198561. [O60716-4]
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]
GeneID1500.
KEGGhsa:1500.
UCSCuc001nlf.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

CTD1500.
GeneCardsGC11P057531.
HGNCHGNC:2515. CTNND1.
HPACAB003837.
HPA015955.
MIM601045. gene.
neXtProtNX_O60716.
PharmGKBPA27016.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276924.
HOVERGENHBG004284.
InParanoidO60716.
KOK05690.
OMAVLQTIWG.
OrthoDBEOG7N37BV.
PhylomeDBO60716.
TreeFamTF321877.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
SignaLinkO60716.

Gene expression databases

ArrayExpressO60716.
BgeeO60716.
GenevestigatorO60716.

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. human.
EvolutionaryTraceO60716.
GeneWikiCTNND1.
GenomeRNAi1500.
NextBio6177.
PROO60716.
SOURCESearch...

Entry information

Entry nameCTND1_HUMAN
AccessionPrimary (citable) accession number: O60716
Secondary accession number(s): A8K939 expand/collapse secondary AC list , O15088, O60713, O60714, O60715, O60935, Q6DHZ7, Q6RBX8, Q9UP71, Q9UP72, Q9UP73
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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