P30999 (CTND1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin delta-1

Alternative name(s):
Cadherin-associated Src substrate
Short name=CAS
p120 catenin
Short name=p120(ctn)
p120(cas)

Gene names

Name:	Ctnnd1
Synonyms:	Catns, Kiaa0384

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	938 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway By similarity. Associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage. Ref.8 Ref.10 Ref.13
Subunit structure	Belongs to a multiprotein cell-cell adhesion complex that also contains E-cadherin, alpha-catenin, beta-catenin, and gamma-catenin. Binds to the C-terminal fragment of PSEN1 and mutually competes for E-cadherin By similarity. Interacts with ZBTB33. Interacts with GLIS2 and FER. Interacts with NANOS1 (via N-terminal region) By similarity. Ref.6 Ref.7 Ref.13
Subcellular location	Cytoplasm. Nucleus. Cell membrane. Note: Interaction with GLIS2 promotes nuclear translocation. Detected at cell-cell contacts. NANOS1 induces its translocation from sites of cell-cell contact to the cytoplasm By similarity. Ref.8 Ref.13
Domain	ARM repeats 1 to 5 mediate interaction with cadherins By similarity.
Post-translational modification	Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ By similarity.
Sequence similarities	Belongs to the beta-catenin family. Contains 10 ARM repeats.
Sequence caution	The sequence BAC41421.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell adhesion Transcription Transcription regulation Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW brain development Inferred from electronic annotation. Source: Ensembl cell adhesion Inferred from mutant phenotype PubMed 14657280. Source: MGI epithelial cell differentiation involved in salivary gland development Inferred from mutant phenotype PubMed 16399075. Source: MGI keratinocyte differentiation Inferred from mutant phenotype PubMed 16510873. Source: MGI morphogenesis of a polarized epithelium Inferred from mutant phenotype PubMed 16399075PubMed 16510873. Source: MGI negative regulation of canonical Wnt signaling pathway Inferred from electronic annotation. Source: Ensembl regulation of transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW salivary gland morphogenesis Inferred from mutant phenotype PubMed 16399075. Source: MGI single organismal cell-cell adhesion Inferred from mutant phenotype PubMed 16399075. Source: MGI transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell-cell adherens junction Inferred from direct assay PubMed 15775979. Source: MGI cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Ensembl dendritic spine Inferred from electronic annotation. Source: Ensembl growth cone Inferred from electronic annotation. Source: Ensembl lamellipodium Inferred from direct assay PubMed 14657280. Source: MGI membrane Inferred from direct assay PubMed 14657280. Source: MGI midbody Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from mutant phenotype PubMed 16510873. Source: MGI synapse Inferred from electronic annotation. Source: Ensembl tight junction Inferred from direct assay PubMed 17130295. Source: MGI zonula adherens Inferred from electronic annotation. Source: Ensembl
Molecular_function	protein binding Inferred from physical interaction Ref.6PubMed 9670943. Source: IntAct protein domain specific binding Inferred from physical interaction PubMed 18794329. Source: MGI protein phosphatase binding Inferred from physical interaction PubMed 16973135. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ptpn11	P35235	3	EBI-529924,EBI-397236
Zbtb33	Q8BN78	3	EBI-529924,EBI-1216314

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P30999-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P30999-2)

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

Isoform 3 (identifier: P30999-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 938	938	Catenin delta-1		PRO_0000064297
Regions
	Repeat	358 – 395	38	ARM 1
	Repeat	398 – 437	40	ARM 2
	Repeat	441 – 475	35	ARM 3
	Repeat	476 – 516	41	ARM 4
	Repeat	534 – 573	40	ARM 5
	Repeat	583 – 624	42	ARM 6
	Repeat	653 – 693	41	ARM 7
	Repeat	700 – 739	40	ARM 8
	Repeat	740 – 780	41	ARM 9
	Repeat	781 – 826	46	ARM 10
	Coiled coil	10 – 46	37	Potential
	Motif	622 – 635	14	Nuclear localization signal Ref.8
Sites
	Site	401	1	Essential for interaction with cadherins By similarity
	Site	478	1	Essential for interaction with cadherins By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	4	1	Phosphoserine By similarity
	Modified residue	47	1	Phosphoserine By similarity
	Modified residue	112	1	Phosphotyrosine; by FYN By similarity
	Modified residue	217	1	Phosphotyrosine Ref.11
	Modified residue	221	1	Phosphotyrosine Ref.11
	Modified residue	228	1	Phosphotyrosine Ref.17
	Modified residue	230	1	Phosphoserine Ref.14
	Modified residue	252	1	Phosphoserine Ref.14
	Modified residue	257	1	Phosphotyrosine Ref.17
	Modified residue	268	1	Phosphoserine By similarity
	Modified residue	269	1	Phosphoserine By similarity
	Modified residue	280	1	Phosphotyrosine Ref.11
	Modified residue	288	1	Phosphoserine; alternate Ref.14
	Modified residue	288	1	Phosphoserine; by PAK7/PAK5; alternate By similarity
	Modified residue	320	1	Phosphoserine By similarity
	Modified residue	349	1	Phosphoserine Ref.14 Ref.15 Ref.17
	Modified residue	352	1	Phosphoserine Ref.17
	Modified residue	811	1	Phosphoserine By similarity
	Modified residue	847	1	Phosphoserine Ref.14
	Modified residue	857	1	Phosphoserine Ref.14
	Modified residue	859	1	Phosphoserine By similarity
	Modified residue	864	1	Phosphoserine By similarity
	Modified residue	865	1	Phosphotyrosine Ref.14
	Modified residue	879	1	Phosphoserine By similarity
	Modified residue	899	1	Phosphoserine Ref.14
	Modified residue	904	1	Phosphotyrosine Ref.12 Ref.17
	Modified residue	916	1	Phosphothreonine By similarity
	Modified residue	920	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	626 – 631	6	Missing in isoform 2.		VSP_030567
	Alternative sequence	880 – 900	21	Missing in isoform 2 and isoform 3.		VSP_030568
Experimental info
	Mutagenesis	622 – 623	2	KK → AA: Abolishes nuclear localization. Ref.8
	Sequence conflict	405	1	R → A in CAA79078. Ref.1
	Sequence conflict	676	1	K → N in CAA79078. Ref.1
	Sequence conflict	715	1	I → R in CAA79078. Ref.1
	Sequence conflict	752	1	I → R in CAA79078. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 2F13DB7350355832	FASTA	938	104,925
	10 20 30 40 50 60 MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL 70 80 90 100 110 120 TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA 130 140 150 160 170 180 MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR 190 200 210 220 230 240 DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER 250 260 270 280 290 300 YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 310 320 330 340 350 360 DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP 370 380 390 400 410 420 SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP 430 440 450 460 470 480 KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS 490 500 510 520 530 540 SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE 550 560 570 580 590 600 RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 610 620 630 640 650 660 QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF 670 680 690 700 710 720 QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT 730 740 750 760 770 780 SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN 790 800 810 820 830 840 TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE 850 860 870 880 890 900 KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL 910 920 930 DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI
	Isoform 2 [UniParc]. Checksum: 8EBEA0D3FA88C843	FASTA	911	101,744
	10 20 30 40 50 60 MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL 70 80 90 100 110 120 TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA 130 140 150 160 170 180 MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR 190 200 210 220 230 240 DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER 250 260 270 280 290 300 YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 310 320 330 340 350 360 DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP 370 380 390 400 410 420 SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP 430 440 450 460 470 480 KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS 490 500 510 520 530 540 SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE 550 560 570 580 590 600 RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 610 620 630 640 650 660 QEALPTVANS TGPHAASCFG AKKGKGKKPT EDPANDTVDF PKRTSPARGY ELLFQPEVVR 670 680 690 700 710 720 IYISLLKESK TPAILEASAG AIQNLCAGRW TYGRYIRSAL RQEKALSAIA ELLTSEHERV 730 740 750 760 770 780 VKAASGALRN LAVDARNKEL IGKHAIPNLV KNLPGGQQNS SWNFSEDTVV SILNTINEVI 790 800 810 820 830 840 AENLEAAKKL RETQGIEKLV LINKSGNRSE KEVRAAALVL QTIWGYKELR KPLEKEGWKK 850 860 870 880 890 900 SDFQVNLNNA SRSQSSHSYD DSTLPLIDRN QKSDNNYSTL NERGDHNRTL DRSGDLGDME 910 PLKGAPLMQK I
	Isoform 3 [UniParc]. Checksum: 8FA40C72176733E8	FASTA	917	102,565
	10 20 30 40 50 60 MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL 70 80 90 100 110 120 TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA 130 140 150 160 170 180 MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR 190 200 210 220 230 240 DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER 250 260 270 280 290 300 YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS 310 320 330 340 350 360 DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP 370 380 390 400 410 420 SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP 430 440 450 460 470 480 KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS 490 500 510 520 530 540 SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE 550 560 570 580 590 600 RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY 610 620 630 640 650 660 QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF 670 680 690 700 710 720 QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT 730 740 750 760 770 780 SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN 790 800 810 820 830 840 TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE 850 860 870 880 890 900 KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD NNYSTLNERG DHNRTLDRSG 910 DLGDMEPLKG APLMQKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors beta-catenin, plakoglobin and armadillo." Reynolds A.B., Herbert L., Cleveland J.L., Berg S.T., Gaut J.R. Oncogene 7:2439-2445(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: Swiss.
[2]	Reynolds A.B. Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H. DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Brain.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Strain: C57BL/6J. Tissue: Testis.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[6]	"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor." Daniel J.M., Reynolds A.B. Mol. Cell. Biol. 19:3614-3623(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZBTB33.
[7]	"The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides." Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A. Nucleic Acids Res. 30:2911-2919(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZBTB33.
[8]	"NLS-dependent nuclear localization of p120ctn is necessary to relieve Kaiso-mediated transcriptional repression." Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M. J. Cell Sci. 117:2675-2686(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 622-LYS-LYS-623.
[9]	Erratum Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M. J. Cell Sci. 117:3405-3405(2004)
[10]	"The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin." Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C., Daniel J.M. Exp. Cell Res. 305:253-265(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217; TYR-221 AND TYR-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Mast cell.
[13]	"The transcriptional repressor Glis2 is a novel binding partner for p120 catenin." Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A., Gevaert K., Birchmeier W., Briscoe J., Fujita Y. Mol. Biol. Cell 18:1918-1927(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
[14]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-288; SER-349; SER-847; SER-857; TYR-865 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[15]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[16]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349; SER-352 AND TYR-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z17804 mRNA. Translation: CAA79078.1. AB093237 mRNA. Translation: BAC41421.1. Different initiation. AK133193 mRNA. Translation: BAE21551.1. AK161790 mRNA. Translation: BAE36576.1. BC043108 mRNA. Translation: AAH43108.1. BC054544 mRNA. Translation: AAH54544.1.
CCDS	CCDS16186.1. [P30999-1] CCDS50622.1. [P30999-2] CCDS50623.1. [P30999-3]
PIR	S28498. I48701.
RefSeq	NP_001078917.1. NM_001085448.1. [P30999-3] NP_001078918.1. NM_001085449.1. NP_001078919.1. NM_001085450.1. [P30999-1] NP_001078922.1. NM_001085453.1. [P30999-2] NP_031641.2. NM_007615.4. [P30999-1] XP_006498698.1. XM_006498635.1. [P30999-1] XP_006498700.1. XM_006498637.1. [P30999-3]
UniGene	Mm.35738.
3D structure databases
ProteinModelPortal	P30999.
SMR	P30999. Positions 358-852.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	198513. 15 interactions.
IntAct	P30999. 14 interactions.
MINT	MINT-89877.
PTM databases
PhosphoSite	P30999.
Proteomic databases
MaxQB	P30999.
PaxDb	P30999.
PRIDE	P30999.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000036811; ENSMUSP00000042543; ENSMUSG00000034101. [P30999-3] ENSMUST00000066177; ENSMUSP00000065252; ENSMUSG00000034101. [P30999-2] ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101. [P30999-1] ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101. [P30999-1] ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101. [P30999-3]
GeneID	12388.
KEGG	mmu:12388.
UCSC	uc008kio.1. mouse. [P30999-3] uc008kip.1. mouse. [P30999-1] uc008kit.1. mouse. [P30999-2]
Organism-specific databases
CTD	1500.
MGI	MGI:105100. Ctnnd1.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG276924.
GeneTree	ENSGT00690000101851.
HOGENOM	HOG000231862.
HOVERGEN	HBG004284.
KO	K05690.
PhylomeDB	P30999.
TreeFam	TF321877.
Gene expression databases
Bgee	P30999.
CleanEx	MM_CTNND1.
Genevestigator	P30999.
Family and domain databases
Gene3D	1.25.10.10. 1 hit.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. IPR028439. Catenin_d1. IPR028435. Plakophilin/d_Catenin. [Graphical view]
PANTHER	PTHR10372. PTHR10372. 1 hit. PTHR10372:SF6. PTHR10372:SF6. 1 hit.
Pfam	PF00514. Arm. 3 hits. [Graphical view]
SMART	SM00185. ARM. 6 hits. [Graphical view]
SUPFAM	SSF48371. SSF48371. 2 hits.
PROSITE	PS50176. ARM_REPEAT. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CTNND1. mouse.
NextBio	281110.
PRO	P30999.
SOURCE	Search...

Entry information

Entry name

CTND1_MOUSE

Accession

Primary (citable) accession number: P30999
Secondary accession number(s): Q3TSU9, Q80XQ4, Q8CHF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 15, 2008
Last modified:	July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program