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O60716

- CTND1_HUMAN

UniProt

O60716 - CTND1_HUMAN

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Protein

Catenin delta-1

Gene

CTNND1

Organism
Homo sapiens (Human)
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.By similarity2 Publications

Sites

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

GO - Molecular functioni

  1. cadherin binding Source: UniProtKB
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. brain development Source: Ensembl
  3. cell adhesion Source: ProtInc
  4. cell-cell junction organization Source: Reactome
  5. cell junction assembly Source: Reactome
  6. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  7. regulation of transcription, DNA-templated Source: UniProtKB-KW
  8. single organismal cell-cell adhesion Source: InterPro
  9. transcription, DNA-templated Source: UniProtKB-KW
  10. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Transcription, Transcription regulation, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_228016. VEGFR2 mediated vascular permeability.
SignaLinkiO60716.

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:KIAA0384
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:2515. CTNND1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: BHF-UCL
  4. dendritic spine Source: Ensembl
  5. extracellular vesicular exosome Source: UniProt
  6. growth cone Source: Ensembl
  7. lamellipodium Source: Ensembl
  8. midbody Source: UniProtKB
  9. nucleus Source: BHF-UCL
  10. plasma membrane Source: UniProtKB
  11. synapse Source: Ensembl
  12. zonula adherens Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi363 – 3631W → A: Severely disrupts cadherin interaction. 1 Publication
Mutagenesisi401 – 4011K → M: Complete loss of cadherin interaction. 1 Publication
Mutagenesisi444 – 4441K → M: Severely disrupts cadherin interaction. 1 Publication
Mutagenesisi477 – 4771W → A: Severely disrupts cadherin interaction. 1 Publication
Mutagenesisi478 – 4781N → A: Complete loss of cadherin interaction. 1 Publication

Organism-specific databases

PharmGKBiPA27016.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Catenin delta-1PRO_0000064296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei47 – 471Phosphoserine3 Publications
Modified residuei112 – 1121Phosphotyrosine; by FYN1 Publication
Modified residuei217 – 2171PhosphotyrosineBy similarity
Modified residuei221 – 2211PhosphotyrosineBy similarity
Modified residuei228 – 2281PhosphotyrosineBy similarity
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei252 – 2521PhosphoserineBy similarity
Modified residuei257 – 2571PhosphotyrosineBy similarity
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei269 – 2691Phosphoserine1 Publication
Modified residuei280 – 2801PhosphotyrosineBy similarity
Modified residuei288 – 2881Phosphoserine; by PAK7/PAK54 Publications
Modified residuei320 – 3201Phosphoserine1 Publication
Modified residuei349 – 3491Phosphoserine2 Publications
Modified residuei352 – 3521Phosphoserine1 Publication
Modified residuei811 – 8111Phosphoserine1 Publication
Modified residuei847 – 8471Phosphoserine1 Publication
Modified residuei857 – 8571Phosphoserine1 Publication
Modified residuei859 – 8591Phosphoserine1 Publication
Modified residuei864 – 8641Phosphoserine1 Publication
Modified residuei865 – 8651PhosphotyrosineBy similarity
Modified residuei879 – 8791Phosphoserine1 Publication
Modified residuei899 – 8991PhosphoserineBy similarity
Modified residuei904 – 9041PhosphotyrosineBy similarity
Modified residuei916 – 9161Phosphothreonine1 Publication
Modified residuei920 – 9201Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ.10 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO60716.
PaxDbiO60716.
PRIDEiO60716.

PTM databases

PhosphoSiteiO60716.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure.1 Publication

Gene expression databases

BgeeiO60716.
ExpressionAtlasiO60716. baseline and differential.
GenevestigatoriO60716.

Organism-specific databases

HPAiCAB003837.
HPA015955.

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. Interacts with ZBTB33. Interacts with GLIS2. Interacts with NANOS1 (via N-terminal region). Interacts with FER.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdh1P098033EBI-702059,EBI-984420From a different organism.
EGFRP005334EBI-701927,EBI-297353
FRMD5Q7Z6J63EBI-701927,EBI-727282
NANOS1Q8WY412EBI-9634525,EBI-9630165
PPAP2BO144959EBI-701927,EBI-766232
PTPRJQ129135EBI-701927,EBI-2264500

Protein-protein interaction databases

BioGridi107881. 39 interactions.
DIPiDIP-33850N.
IntActiO60716. 23 interactions.
MINTiMINT-4999228.

Structurei

Secondary structure

1
968
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi368 – 3747Combined sources
Helixi380 – 39415Combined sources
Helixi398 – 4069Combined sources
Helixi409 – 4157Combined sources
Helixi416 – 4183Combined sources
Helixi422 – 43514Combined sources
Beta strandi437 – 4393Combined sources
Helixi441 – 4499Combined sources
Helixi452 – 46211Combined sources
Helixi466 – 47914Combined sources
Helixi483 – 4853Combined sources
Helixi486 – 4927Combined sources
Helixi494 – 5007Combined sources
Helixi502 – 5065Combined sources
Helixi524 – 53714Combined sources
Helixi542 – 5509Combined sources
Helixi554 – 56714Combined sources
Helixi574 – 58714Combined sources
Helixi590 – 5934Combined sources
Helixi655 – 6606Combined sources
Helixi662 – 67413Combined sources
Helixi678 – 69215Combined sources
Helixi697 – 70610Combined sources
Helixi709 – 7179Combined sources
Helixi718 – 7203Combined sources
Helixi724 – 73815Combined sources
Helixi744 – 75714Combined sources
Beta strandi759 – 7635Combined sources
Helixi766 – 7683Combined sources
Helixi772 – 78615Combined sources
Helixi790 – 7989Combined sources
Helixi801 – 8099Combined sources
Beta strandi812 – 8143Combined sources
Helixi816 – 83015Combined sources
Helixi833 – 8408Combined sources
Turni841 – 8433Combined sources
Helixi846 – 8494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6XX-ray2.40A324-937[»]
3L6YX-ray3.00A/C/E324-937[»]
ProteinModelPortaliO60716.
SMRiO60716. Positions 358-852.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60716.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 4637Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi622 – 63413Nuclear localization signalBy similarityAdd
BLAST

Domaini

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.

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG276924.
GeneTreeiENSGT00760000119167.
HOVERGENiHBG004284.
InParanoidiO60716.
KOiK05690.
OMAiVLQTIWG.
OrthoDBiEOG7N37BV.
PhylomeDBiO60716.
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 (32)i

Sequence statusi: Complete.

This entry describes 32 isoformsi produced by alternative splicing and alternative initiation. Align

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) [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

        10         20         30         40         50
MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD
60 70 80 90 100
ANPLMANGTL TRRHQNGRFV GDADLERQKF SDLKLNGPQD HSHLLYSTIP
110 120 130 140 150
RMQEPGQIVE TYTEEDPEGA MSVVSVETSD DGTTRRTETT VKKVVKTVTT
160 170 180 190 200
RTVQPVAMGP DGLPVDASSV SNNYIQTLGR DFRKNGNGGP GPYVGQAGTA
210 220 230 240 250
TLPRNFHYPP DGYSRHYEDG YPGGSDNYGS LSRVTRIEER YRPSMEGYRA
260 270 280 290 300
PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
310 320 330 340 350
DYGTARRTGT PSDPRRRLRS YEDMIGEEVP SDQYYWAPLA QHERGSLASL
360 370 380 390 400
DSLRKGGPPP PNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV
410 420 430 440 450
KTDVRKLKGI PVLVGLLDHP KKEVHLGACG ALKNISFGRD QDNKIAIKNC
460 470 480 490 500
DGVPALVRLL RKARDMDLTE VITGTLWNLS SHDSIKMEIV DHALHALTDE
510 520 530 540 550
VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE RSEARRKLRE
560 570 580 590 600
CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
610 620 630 640 650
QEAAPNVANN TGPHAASCFG AKKGKDEWFS RGKKPIEDPA NDTVDFPKRT
660 670 680 690 700
SPARGYELLF QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR
710 720 730 740 750
YIRSALRQEK ALSAIADLLT NEHERVVKAA SGALRNLAVD ARNKELIGKH
760 770 780 790 800
AIPNLVKNLP GGQQNSSWNF SEDTVISILN TINEVIAENL EAAKKLRETQ
810 820 830 840 850
GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE KEGWKKSDFQ
860 870 880 890 900
VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIQM SNMGSNTKSL
910 920 930 940 950
DNNYSTPNER GDHNRTLDRS GDLGDMEPLK GTTPLMQDEG QESLEEELDV
960
LVLDDEGGQV SYPSMQKI
Length:968
Mass (Da):108,170
Last modified:August 1, 1998 - v1
Checksum:iD5C37489A891F292
GO
Isoform 1AB (identifier: O60716-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:962
Mass (Da):107,349
Checksum:i62C1AA58EC4ED712
GO
Isoform 1AC (identifier: O60716-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     937-965: Missing.

Note: Contains a phosphothreonine at position 916.

Show »
Length:939
Mass (Da):104,977
Checksum:iD436D996ECBEBDC7
GO
Isoform 1BC (identifier: O60716-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:947
Mass (Da):105,779
Checksum:i46867A61854BBEDF
GO
Isoform 1A (identifier: O60716-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:933
Mass (Da):104,156
Checksum:iA4E1ABA2FE3D6B54
GO
Isoform 1B (identifier: O60716-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:941
Mass (Da):104,958
Checksum:iA82D282A5DF1C4BE
GO
Isoform 1C (identifier: O60716-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:918
Mass (Da):102,586
Checksum:i17D678061E042572
GO
Isoform 1 (identifier: O60716-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:912
Mass (Da):101,765
Checksum:i879022D64712C805
GO
Isoform 2ABC (identifier: O60716-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.

Show »
Length:914
Mass (Da):102,063
Checksum:i57A26859239AA55A
GO
Isoform 2AB (identifier: O60716-10) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.

Show »
Length:908
Mass (Da):101,242
Checksum:i95094A101A1B6DB4
GO
Isoform 2AC (identifier: O60716-11) [UniParc]FASTAAdd to Basket

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.

Show »
Length:885
Mass (Da):98,870
Checksum:iDF4D8956D2827CAA
GO
Isoform 2BC (identifier: O60716-12) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     880-900: Missing.

Show »
Length:893
Mass (Da):99,673
Checksum:iD0985DD5A04D4B3F
GO
Isoform 2A (identifier: O60716-13) [UniParc]FASTAAdd to Basket

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.

Show »
Length:879
Mass (Da):98,049
Checksum:iF58CA78A7097EFEB
GO
Isoform 2B (identifier: O60716-14) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.
     880-900: Missing.

Show »
Length:887
Mass (Da):98,852
Checksum:i1DCDD3510D31FA82
GO
Isoform 2C (identifier: O60716-15) [UniParc]FASTAAdd to Basket

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.

Show »
Length:864
Mass (Da):96,479
Checksum:iE418647839C3B386
GO
Isoform 2 (identifier: O60716-16) [UniParc]FASTAAdd to Basket

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.

Show »
Length:858
Mass (Da):95,658
Checksum:iA16496DCF8B2F524
GO
Isoform 3ABC (identifier: O60716-17) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Show »
Length:867
Mass (Da):96,689
Checksum:i5F9E3A466CA81D74
GO
Isoform 3AB (identifier: O60716-18) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.

Show »
Length:861
Mass (Da):95,868
Checksum:i3D2744052161BD93
GO
Isoform 3AC (identifier: O60716-19) [UniParc]FASTAAdd to Basket

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.

Show »
Length:838
Mass (Da):93,496
Checksum:iF840912548316394
GO
Isoform 3BC (identifier: O60716-20) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     880-900: Missing.

Show »
Length:846
Mass (Da):94,299
Checksum:iD482BB16BD5A898A
GO
Isoform 3A (identifier: O60716-21) [UniParc]FASTAAdd to Basket

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.

Show »
Length:832
Mass (Da):92,675
Checksum:iFAB29A345A6AABBC
GO
Isoform 3B (identifier: O60716-22) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.
     880-900: Missing.

Show »
Length:840
Mass (Da):93,478
Checksum:i0F78D45C15426031
GO
Isoform 3C (identifier: O60716-23) [UniParc]FASTAAdd to Basket

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.

Show »
Length:817
Mass (Da):91,105
Checksum:i7308172E06E2AC56
GO
Isoform 3 (identifier: O60716-24) [UniParc]FASTAAdd to Basket

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.

Show »
Length:811
Mass (Da):90,284
Checksum:i3EB46C6A74AA396C
GO
Isoform 4ABC (identifier: O60716-25) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.

Show »
Length:645
Mass (Da):72,045
Checksum:iDD32175D2F59D40D
GO
Isoform 4AB (identifier: O60716-26) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.

Show »
Length:639
Mass (Da):71,225
Checksum:iF45EA4D758555CE3
GO
Isoform 4AC (identifier: O60716-27) [UniParc]FASTAAdd to Basket

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.

Show »
Length:616
Mass (Da):68,852
Checksum:iE1014C183DAFB90D
GO
Isoform 4BC (identifier: O60716-28) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     880-900: Missing.

Show »
Length:624
Mass (Da):69,655
Checksum:iEEDFAEC10BE108A5
GO
Isoform 4A (identifier: O60716-29) [UniParc]FASTAAdd to Basket

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.

Show »
Length:610
Mass (Da):68,031
Checksum:i402B89CAE47E6A8E
GO
Isoform 4B (identifier: O60716-30) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.
     880-900: Missing.

Show »
Length:618
Mass (Da):68,834
Checksum:iAE57FD1DC87F15AF
GO
Isoform 4C (identifier: O60716-31) [UniParc]FASTAAdd to Basket

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.

Show »
Length:595
Mass (Da):66,461
Checksum:iC93D22BB614EA62B
GO
Isoform 4 (identifier: O60716-32) [UniParc]FASTAAdd to Basket

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.

Show »
Length:589
Mass (Da):65,641
Checksum:i34C9A6E2B5944D2C
GO

Sequence cautioni

The sequence BAA20838.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191R → M in BAA20838. (PubMed:9205841)Curated
Sequence conflicti380 – 3801D → G in AAH75795. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711S → F.
Corresponds to variant rs11229133 [ dbSNP | Ensembl ].
VAR_038255
Natural varianti217 – 2171Y → C.1 Publication
Corresponds to variant rs11570194 [ dbSNP | Ensembl ].
VAR_020929
Natural varianti464 – 4641R → C.1 Publication
Corresponds to variant rs11570199 [ dbSNP | Ensembl ].
VAR_020930
Natural varianti915 – 9151R → K.1 Publication
Corresponds to variant rs11570222 [ dbSNP | Ensembl ].
VAR_020931

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 323323Missing in isoform 4ABC, isoform 4AB, isoform 4AC, isoform 4BC, isoform 4A, isoform 4B, isoform 4C and isoform 4. CuratedVSP_006742Add
BLAST
Alternative sequencei1 – 101101Missing in isoform 3ABC, isoform 3AB, isoform 3AC, isoform 3BC, isoform 3A, isoform 3B, isoform 3C and isoform 3. CuratedVSP_006741Add
BLAST
Alternative sequencei1 – 5454Missing in isoform 2ABC, isoform 2AB, isoform 2AC, isoform 2BC, isoform 2A, isoform 2B, isoform 2C and isoform 2. CuratedVSP_006740Add
BLAST
Alternative sequencei626 – 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. 1 PublicationVSP_006743
Alternative sequencei880 – 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. CuratedVSP_006744Add
BLAST
Alternative sequencei937 – 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. 3 PublicationsVSP_006745Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44604.1. [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]
CCDS73290.1. [O60716-3]
RefSeqiNP_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]
UniGeneiHs.166011.

Genome annotation databases

EnsembliENST00000358694; ENSP00000351527; ENSG00000198561. [O60716-5]
ENST00000361332; ENSP00000354823; ENSG00000198561. [O60716-2]
ENST00000361391; ENSP00000354785; ENSG00000198561. [O60716-6]
ENST00000361796; ENSP00000354907; ENSG00000198561. [O60716-3]
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]
GeneIDi1500.
KEGGihsa:1500.
UCSCiuc001nlf.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]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS44604.1. [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 ]
CCDS73290.1. [O60716-3 ]
RefSeqi NP_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 ]
UniGenei Hs.166011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L6X X-ray 2.40 A 324-937 [» ]
3L6Y X-ray 3.00 A/C/E 324-937 [» ]
ProteinModelPortali O60716.
SMRi O60716. Positions 358-852.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107881. 39 interactions.
DIPi DIP-33850N.
IntActi O60716. 23 interactions.
MINTi MINT-4999228.

PTM databases

PhosphoSitei O60716.

Proteomic databases

MaxQBi O60716.
PaxDbi O60716.
PRIDEi O60716.

Protocols and materials databases

DNASUi 1500.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358694 ; ENSP00000351527 ; ENSG00000198561 . [O60716-5 ]
ENST00000361332 ; ENSP00000354823 ; ENSG00000198561 . [O60716-2 ]
ENST00000361391 ; ENSP00000354785 ; ENSG00000198561 . [O60716-6 ]
ENST00000361796 ; ENSP00000354907 ; ENSG00000198561 . [O60716-3 ]
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 ]
GeneIDi 1500.
KEGGi hsa:1500.
UCSCi uc001nlf.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

CTDi 1500.
GeneCardsi GC11P057531.
HGNCi HGNC:2515. CTNND1.
HPAi CAB003837.
HPA015955.
MIMi 601045. gene.
neXtProti NX_O60716.
PharmGKBi PA27016.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG276924.
GeneTreei ENSGT00760000119167.
HOVERGENi HBG004284.
InParanoidi O60716.
KOi K05690.
OMAi VLQTIWG.
OrthoDBi EOG7N37BV.
PhylomeDBi O60716.
TreeFami TF321877.

Enzyme and pathway databases

Reactomei REACT_19195. Adherens junctions interactions.
REACT_228016. VEGFR2 mediated vascular permeability.
SignaLinki O60716.

Miscellaneous databases

ChiTaRSi CTNND1. human.
EvolutionaryTracei O60716.
GeneWikii CTNND1.
GenomeRNAii 1500.
NextBioi 6177.
PROi O60716.
SOURCEi Search...

Gene expression databases

Bgeei O60716.
ExpressionAtlasi O60716. baseline and differential.
Genevestigatori O60716.

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. "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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiCTND1_HUMAN
AccessioniPrimary (citable) accession number: O60716
Secondary accession number(s): A8K939
, O15088, O60713, O60714, O60715, O60935, Q6DHZ7, Q6RBX8, Q9UP71, Q9UP72, Q9UP73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3