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O60716 (CTND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. 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)
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. May associate with and regulate the cell adhesion properties of both C- and E-cadherins. 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.19

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.15 Ref.19

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. Ref.15 Ref.17

Tissue specificity

Expressed in vascular endothelium. Ref.10

Induction

Induced in vascular endothelium by wounding. This effect is potentiated by prior laminar shear stress, which enhances wound closure. Ref.10

Domain

A possible nuclear localization signal exists in all isoforms where Asp-626--631-Arg are deleted.

Post-translational modification

Phosphorylated by FER and other protein-tyrosine kinases. Phosphorylated at Ser-288 by PAK7/PAK5. Dephosphorylated by PTPRJ. Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdh1P098033EBI-702059,EBI-984420From a different organism.

Alternative products

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

Note: Experimental confirmation may be lacking for some isoforms.
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.
Isoform 1BC (identifier: O60716-4)

The sequence of this isoform differs from the canonical sequence as follows:
     881-900: Missing.
Isoform 1A (identifier: O60716-5)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
     937-965: Missing.
Isoform 1B (identifier: O60716-6)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
     881-900: Missing.
Isoform 1C (identifier: O60716-7)

The sequence of this isoform differs from the canonical sequence as follows:
     881-900: Missing.
     937-965: Missing.
Isoform 1 (identifier: O60716-8)

The sequence of this isoform differs from the canonical sequence as follows:
     626-631: Missing.
     881-900: Missing.
     937-965: Missing.
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.
Isoform 2BC (identifier: O60716-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     881-900: 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.
Isoform 2B (identifier: O60716-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.
     881-900: Missing.
Isoform 2C (identifier: O60716-15)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     881-900: Missing.
     937-965: Missing.
Isoform 2 (identifier: O60716-16)

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.
     626-631: Missing.
     881-900: Missing.
     937-965: Missing.
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.
Isoform 3BC (identifier: O60716-20)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     881-900: 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.
Isoform 3B (identifier: O60716-22)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.
     881-900: Missing.
Isoform 3C (identifier: O60716-23)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     881-900: Missing.
     937-965: Missing.
Isoform 3 (identifier: O60716-24)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     626-631: Missing.
     881-900: Missing.
     937-965: Missing.
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.
Isoform 4BC (identifier: O60716-28)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     881-900: 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.
Isoform 4B (identifier: O60716-30)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.
     881-900: Missing.
Isoform 4C (identifier: O60716-31)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     881-900: Missing.
     937-965: Missing.
Isoform 4 (identifier: O60716-32)

The sequence of this isoform differs from the canonical sequence as follows:
     1-323: Missing.
     626-631: Missing.
     881-900: Missing.
     937-965: Missing.

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

Amino acid modifications

Modified residue471Phosphoserine Ref.16 Ref.23
Modified residue961Phosphotyrosine Ref.12 Ref.18 Ref.25
Modified residue1121Phosphotyrosine; by FYN Ref.20
Modified residue1741Phosphotyrosine Ref.12 Ref.21 Ref.25
Modified residue1931Phosphotyrosine Ref.25
Modified residue2081Phosphotyrosine Ref.21
Modified residue2131Phosphotyrosine Ref.21 Ref.25
Modified residue2171Phosphotyrosine Ref.12 Ref.14 Ref.21
Modified residue2281Phosphotyrosine Ref.12 Ref.14 Ref.16 Ref.21 Ref.22 Ref.25
Modified residue2301Phosphoserine Ref.22 Ref.23
Modified residue2321Phosphoserine Ref.22
Modified residue2441Phosphoserine Ref.22
Modified residue2481Phosphotyrosine Ref.25
Modified residue2521Phosphoserine By similarity
Modified residue2571Phosphotyrosine Ref.12 Ref.14 Ref.18 Ref.21 Ref.25
Modified residue2681Phosphoserine Ref.16 Ref.24
Modified residue2691Phosphoserine Ref.16 Ref.24
Modified residue2801Phosphotyrosine Ref.14 Ref.21 Ref.25
Modified residue2881Phosphoserine; by PAK7/PAK5 Ref.22 Ref.23 Ref.26
Modified residue2911Phosphotyrosine By similarity
Modified residue3021Phosphotyrosine Ref.12
Modified residue3101Phosphothreonine Ref.16
Modified residue3201Phosphoserine By similarity
Modified residue3211Phosphotyrosine Ref.13 Ref.16
Modified residue3341Phosphotyrosine Ref.13
Modified residue3461Phosphoserine By similarity
Modified residue3491Phosphoserine Ref.11 Ref.16 Ref.24
Modified residue3521Phosphoserine Ref.11 Ref.16 Ref.24
Modified residue8571Phosphoserine By similarity
Modified residue8591Phosphoserine By similarity
Modified residue8641Phosphoserine By similarity
Modified residue8651Phosphotyrosine Ref.12
Modified residue8691Phosphothreonine Ref.22
Modified residue9041Phosphotyrosine Ref.18 Ref.25
Modified residue9161Phosphothreonine Ref.16
Modified residue9201Phosphoserine By similarity

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 sequence881 – 90020Missing 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

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: 8C4C0C4B6F742833
Show »

FASTA948105,894
Isoform 1A [UniParc].

Checksum: A4E1ABA2FE3D6B54
Show »

FASTA933104,156
Isoform 1B [UniParc].

Checksum: D712A71924AC9249
Show »

FASTA942105,074
Isoform 1C [UniParc].

Checksum: 3064281A404F0742
Show »

FASTA919102,701
Isoform 1 [UniParc].

Checksum: 75E46E40901611AF
Show »

FASTA913101,880
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: 0EDA126CDB512EC6
Show »

FASTA89499,788
Isoform 2A [UniParc].

Checksum: F58CA78A7097EFEB
Show »

FASTA87998,049
Isoform 2B [UniParc].

Checksum: F1E747E25FFC5277
Show »

FASTA88898,967
Isoform 2C [UniParc].

Checksum: AF57E6063E68C0D4
Show »

FASTA86596,594
Isoform 2 [UniParc].

Checksum: 42729AF49AA9B192
Show »

FASTA85995,774
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: FCAE088A184C3904
Show »

FASTA84794,414
Isoform 3A [UniParc].

Checksum: FAB29A345A6AABBC
Show »

FASTA83292,675
Isoform 3B [UniParc].

Checksum: 0625F2E552E421ED
Show »

FASTA84193,593
Isoform 3C [UniParc].

Checksum: 00C0F6756857E1CB
Show »

FASTA81891,220
Isoform 3 [UniParc].

Checksum: 236D4A0E2C25A95E
Show »

FASTA81290,400
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: C304559FCFFA8285
Show »

FASTA62569,770
Isoform 4A [UniParc].

Checksum: 402B89CAE47E6A8E
Show »

FASTA61068,031
Isoform 4B [UniParc].

Checksum: CDA4DDCC13391C98
Show »

FASTA61968,949
Isoform 4C [UniParc].

Checksum: 4B8AC340FD304DC1
Show »

FASTA59666,577
Isoform 4 [UniParc].

Checksum: 4F6737C4A4E4972A
Show »

FASTA59065,756

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: 9653641] [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: 9205841] [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: 14702039] [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: 16554811] [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: 15489334] [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: 7623846] [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: 10207085] [Abstract]
Cited for: INTERACTION WITH ZBTB33.
[9]"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: 12370829] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ.
[10]"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: 14699141] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[11]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-352, MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[12]"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)."
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.
J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-96; TYR-174; TYR-217; TYR-228; TYR-257; TYR-302 AND TYR-865, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321 AND TYR-334, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[14]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-217; TYR-228; TYR-257 AND TYR-280, MASS SPECTROMETRY.
[15]"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: 17047063] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NANOS1.
[16]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; TYR-228; SER-268; SER-269; THR-310; TYR-321; SER-349; SER-352 AND THR-916, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[17]"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: 17115030] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-96; TYR-257 AND TYR-904, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[19]"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: 17344476] [Abstract]
Cited for: INTERACTION WITH GLIS2, FUNCTION.
[20]"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: 17194753] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-112 BY FYN.
[21]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-174; TYR-208; TYR-213; TYR-217; TYR-228; TYR-257 AND TYR-280, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[22]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; SER-230; SER-232; SER-244; SER-288 AND THR-869, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[23]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-230 AND SER-288, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-269; SER-349 AND SER-352, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[25]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-96; TYR-174; TYR-193; TYR-213; TYR-228; TYR-248; TYR-257; TYR-280 AND TYR-904, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[26]"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: 20564219] [Abstract]
Cited for: PHOSPHORYLATION AT SER-288 BY PAK7/PAK5.
+Additional computationally mapped references.

Web resources

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.
IPIIPI00182469.
IPI00182540.
IPI00219725.
IPI00219726.
IPI00219727.
IPI00219728.
IPI00219730.
IPI00219731.
IPI00219732.
IPI00219733.
IPI00219734.
IPI00219735.
IPI00219737.
IPI00219738.
IPI00219739.
IPI00219741.
IPI00219742.
IPI00219743.
IPI00219744.
IPI00219745.
IPI00219746.
IPI00219747.
IPI00219748.
IPI00219749.
IPI00219750.
IPI00219869.
IPI00219870.
IPI00219872.
IPI00219873.
IPI00219875.
IPI00845519.
IPI00942869.
RefSeqNP_001078927.1. NM_001085458.1.
NP_001078928.1. NM_001085459.1.
NP_001078929.1. NM_001085460.1.
NP_001078930.1. NM_001085461.1.
NP_001078931.1. NM_001085462.1.
NP_001078932.1. NM_001085463.1.
NP_001078933.1. NM_001085464.1.
NP_001078934.1. NM_001085465.1.
NP_001078935.1. NM_001085466.1.
NP_001078936.1. NM_001085467.1.
NP_001078937.1. NM_001085468.1.
NP_001078938.1. NM_001085469.1.
NP_001193812.1. NM_001206883.1.
NP_001193813.1. NM_001206884.1.
NP_001193814.1. NM_001206885.1.
NP_001193815.1. NM_001206886.1.
NP_001193816.1. NM_001206887.1.
NP_001193817.1. NM_001206888.1.
NP_001193818.1. NM_001206889.1.
NP_001193819.1. NM_001206890.1.
NP_001193820.1. NM_001206891.1.
NP_001322.1. NM_001331.2.
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...

Protein-protein interaction databases

IntActO60716. 14 interactions.
STRINGO60716.

PTM databases

PhosphoSiteO60716.

Proteomic databases

PRIDEO60716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399050; ENSP00000382004; ENSG00000198561.
GeneID1500.
KEGGhsa:1500.
UCSCuc001nlh.1. human.
uc001nli.2. human.
uc001nlj.2. human.
uc001nll.2. human.
uc001nlw.2. human.
uc001nlx.2. human.
uc001nly.2. human.
uc001nlz.2. human.
uc001nma.2. human.
uc001nmc.2. human.
uc001nmd.2. human.

Organism-specific databases

CTD1500.
GeneCardsGC11P057531.
H-InvDBHIX0009643.
HGNCHGNC:2515. CTNND1.
HPACAB003837.
HPA015955.
MIM601045. gene.
neXtProtNX_O60716.
PharmGKBPA27016.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12799.
HOVERGENHBG004284.
InParanoidO60716.
OMAEVHLGAC.
PhylomeDBO60716.

Enzyme and pathway databases

Pathway_Interaction_DBarf6_traffickingpathway. Arf6 trafficking events.
fgf_pathway. FGF signaling pathway.
ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressO60716.
BgeeO60716.
GenevestigatorO60716.
GermOnlineENSG00000198561. Homo sapiens.

Family and domain databases

InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 2 hits.
KOK05690.
PfamPF00514. Arm. 3 hits.
[Graphical view]
SMARTSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
PROSITEPS50176. ARM_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio6177.
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: January 25, 2012
This is version 116 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.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families