Details for: CTNND1
Associated with
Other Information
Genular Protein ID: 203065753
Symbol: CTND1_HUMAN
Name: Catenin delta-1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9653641
Title: Molecular cloning of the human p120ctn catenin gene (CTNND1): expression of multiple alternatively spliced isoforms.
PubMed ID: 9653641
PubMed ID: 9205841
Title: 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.
PubMed ID: 9205841
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 16554811
Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.
PubMed ID: 16554811
DOI: 10.1038/nature04632
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 7623846
Title: The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors.
PubMed ID: 7623846
PubMed ID: 10207085
Title: The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor.
PubMed ID: 10207085
PubMed ID: 11896187
Title: Specific sequences in p120ctn determine subcellular distribution of its multiple isoforms involved in cellular adhesion of normal and malignant epithelial cells.
PubMed ID: 11896187
PubMed ID: 12370829
Title: The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn).
PubMed ID: 12370829
PubMed ID: 14610055
Title: A core function for p120-catenin in cadherin turnover.
PubMed ID: 14610055
PubMed ID: 14699141
Title: Laminar shear stress differentially modulates gene expression of p120 catenin, Kaiso transcription factor, and vascular endothelial cadherin in human coronary artery endothelial cells.
PubMed ID: 14699141
PubMed ID: 15240885
Title: A role for Galpha12/Galpha13 in p120ctn regulation.
PubMed ID: 15240885
PubMed ID: 17047063
Title: E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion.
PubMed ID: 17047063
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17115030
Title: The armadillo protein p0071 regulates Rho signalling during cytokinesis.
PubMed ID: 17115030
DOI: 10.1038/ncb1504
PubMed ID: 17487921
Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.
PubMed ID: 17487921
PubMed ID: 17344476
Title: The transcriptional repressor Glis2 is a novel binding partner for p120 catenin.
PubMed ID: 17344476
PubMed ID: 17194753
Title: Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA.
PubMed ID: 17194753
DOI: 10.1128/mcb.01974-06
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 20564219
Title: p120-catenin is a binding partner and substrate for Group B Pak kinases.
PubMed ID: 20564219
DOI: 10.1002/jcb.22639
PubMed ID: 20123964
Title: Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures.
PubMed ID: 20123964
DOI: 10.1128/mcb.00038-09
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25009281
Title: DIPA-family coiled-coils bind conserved isoform-specific head domain of p120-catenin family: potential roles in hydrocephalus and heterotopia.
PubMed ID: 25009281
PubMed ID: 28301459
Title: Blepharocheilodontic syndrome is a CDH1 pathway-related disorder due to mutations in CDH1 and CTNND1.
PubMed ID: 28301459
DOI: 10.1038/gim.2017.11
PubMed ID: 28051089
Title: Cadherin 26 is an alpha integrin-binding epithelial receptor regulated during allergic inflammation.
PubMed ID: 28051089
DOI: 10.1038/mi.2016.120
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 20371349
Title: Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.
PubMed ID: 20371349
Sequence Information:
- Length: 968
- Mass: 108170
- Checksum: D5C37489A891F292
- Sequence:
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANPLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HSHLLYSTIP RMQEPGQIVE TYTEEDPEGA MSVVSVETSD DGTTRRTETT VKKVVKTVTT RTVQPVAMGP DGLPVDASSV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYSRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS DYGTARRTGT PSDPRRRLRS YEDMIGEEVP SDQYYWAPLA QHERGSLASL DSLRKGGPPP PNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PVLVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY QEAAPNVANN TGPHAASCFG AKKGKDEWFS RGKKPIEDPA NDTVDFPKRT SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIADLLT NEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVISILN TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIQM SNMGSNTKSL DNNYSTPNER GDHNRTLDRS GDLGDMEPLK GTTPLMQDEG QESLEEELDV LVLDDEGGQV SYPSMQKI
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.