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Protein

DE-cadherin

Gene

shg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins (PubMed:7958432). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (PubMed:7958432). N-cadherin may be involved in neuronal recognition mechanism (PubMed:7958432). May function in cell intercalation in the lateral epidermis during germband extension (PubMed:24681004).2 Publications

GO - Molecular functioni

  • beta-catenin binding Source: FlyBase
  • calcium ion binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase
  • myosin binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • receptor activity Source: FlyBase

GO - Biological processi

  • apical protein localization Source: FlyBase
  • asymmetric cell division Source: FlyBase
  • asymmetric protein localization Source: FlyBase
  • axon guidance Source: FlyBase
  • axonogenesis Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • brain development Source: FlyBase
  • branch fusion, open tracheal system Source: FlyBase
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • cell adhesion Source: FlyBase
  • cell-cell adhesion mediated by cadherin Source: FlyBase
  • cell competition in a multicellular organism Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cell projection assembly Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • defense response to fungus Source: FlyBase
  • determination of digestive tract left/right asymmetry Source: FlyBase
  • establishment or maintenance of cell polarity Source: FlyBase
  • female germ-line stem cell population maintenance Source: FlyBase
  • gastrulation involving germ band extension Source: FlyBase
  • germarium-derived female germ-line cyst encapsulation Source: FlyBase
  • germ cell development Source: FlyBase
  • germ cell migration Source: FlyBase
  • germ-line stem cell division Source: FlyBase
  • gonadal mesoderm development Source: FlyBase
  • gonad development Source: FlyBase
  • gonad morphogenesis Source: FlyBase
  • head involution Source: FlyBase
  • heart development Source: FlyBase
  • hemocyte migration Source: FlyBase
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: FlyBase
  • maintenance of epithelial integrity, open tracheal system Source: FlyBase
  • male germline stem cell symmetric division Source: FlyBase
  • morphogenesis of an epithelium Source: FlyBase
  • morphogenesis of a polarized epithelium Source: FlyBase
  • nervous system development Source: FlyBase
  • ommatidial rotation Source: FlyBase
  • oocyte anterior/posterior axis specification Source: FlyBase
  • oocyte localization involved in germarium-derived egg chamber formation Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • optic lobe placode development Source: FlyBase
  • outflow tract morphogenesis Source: FlyBase
  • ovarian follicle cell migration Source: FlyBase
  • pole cell migration Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • segment specification Source: FlyBase
  • single organismal cell-cell adhesion Source: FlyBase
  • somatic stem cell division Source: FlyBase
  • somatic stem cell population maintenance Source: FlyBase
  • ventral furrow formation Source: FlyBase
  • wound healing Source: FlyBase
  • zonula adherens assembly Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DE-cadherin
Alternative name(s):
Protein shotgun
Gene namesi
Name:shgImported
Synonyms:E-cadherinImported
ORF Names:CG3722Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003391. shg.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini262 – 13281067ExtracellularSequence analysisAdd
BLAST
Transmembranei1329 – 134921HelicalSequence analysisAdd
BLAST
Topological domaini1350 – 1507158CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • adherens junction Source: FlyBase
  • apical junction complex Source: FlyBase
  • catenin complex Source: FlyBase
  • cell-cell adherens junction Source: FlyBase
  • cell cortex Source: FlyBase
  • filopodium Source: FlyBase
  • integral component of membrane Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
  • plasma membrane Source: UniProtKB
  • recycling endosome Source: FlyBase
  • spot adherens junction Source: FlyBase
  • zonula adherens Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 6969Sequence analysisAdd
BLAST
Propeptidei70 – 261192Sequence analysisPRO_0000003879Add
BLAST
Chaini262 – 15071246DE-cadherinPRO_0000003880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence analysis
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence analysis
Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence analysis
Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence analysis
Glycosylationi983 – 9831N-linked (GlcNAc...)Sequence analysis
Glycosylationi999 – 9991N-linked (GlcNAc...)Sequence analysis
Glycosylationi1073 – 10731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1098 ↔ 1112By similarity
Disulfide bondi1114 ↔ 1123Sequence analysis
Glycosylationi1145 – 11451N-linked (GlcNAc...)Sequence analysis
Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1287 ↔ 1313By similarity
Glycosylationi1290 – 12901N-linked (GlcNAc...)Sequence analysis
Modified residuei1493 – 14931Phosphoserine1 Publication

Post-translational modificationi

N-glycosylation is important for biosynthesis and function.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ24298.

PTM databases

iPTMnetiQ24298.

Expressioni

Tissue specificityi

In the embryo, expressed in the leading edge cells of the dorsal epidermis (at protein level) (PubMed:16831834). Stage 10 embryos exhibit intense expression in epithelial cells (PubMed:7958432). Stage 14 embryos show expression in the hindgut (at the apical poles of cell-cell boundaries), at the apical junctions of tracheal cells and in the dorsal longitudinal trunk (PubMed:7958432). In stage 16 embryos the glial midline cells of the central nervous system show strong expression (PubMed:7958432).2 Publications

Gene expression databases

BgeeiQ24298.
ExpressionAtlasiQ24298. differential.
GenevisibleiQ24298. DM.

Interactioni

Subunit structurei

Interacts (via cytoplasmic region) with Inx2 (via cytoplasmic loop).1 Publication

GO - Molecular functioni

  • beta-catenin binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase
  • myosin binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase

Protein-protein interaction databases

BioGridi63025. 10 interactions.
DIPiDIP-22198N.
IntActiQ24298. 3 interactions.
MINTiMINT-1608719.
STRINGi7227.FBpp0071475.

Structurei

3D structure databases

DisProtiDP00269.
ProteinModelPortaliQ24298.
SMRiQ24298. Positions 81-854, 1171-1300, 1413-1489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 19599Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini204 – 30198Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini311 – 412102Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini420 – 522103Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini532 – 633102Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini631 – 733103Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini741 – 83595Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 112340EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini1125 – 1313189Laminin G-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1350 – 1507158Interaction with Inx2Add
BLAST

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Sequence similaritiesi

Contains 7 cadherin domains.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00840000129706.
InParanoidiQ24298.
OMAiDFYNVKV.
OrthoDBiEOG718KB7.
PhylomeDBiQ24298.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
2.60.40.60. 7 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
IPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 7 hits.
SM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 8 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS00232. CADHERIN_1. 5 hits.
PS50268. CADHERIN_2. 7 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q24298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSVQRMSR SYHCINMSAT PQAGHLNPAQ QQTHQQHKRK CRDLGRRLIP
60 70 80 90 100
ARLLLGVIVA ISLLSPALAL HSPPDKNFSG DNRKPAFKNC AGYAPKVKEE
110 120 130 140 150
QPENTYVLTV EAVDPDPDQV IRYSIVQSPF ERPKFFINPS TGVIFTTHTF
160 170 180 190 200
DRDEPIHEKF VFVTVQATDN GLPPLDDVCT FNVTIEDIND NAPAFNKARY
210 220 230 240 250
DESMSENAQP DAVVMTISAS DFDDGNNSLV EYEILRERDF QYFKIDKESG
260 270 280 290 300
IIYLKRPIDK RPGQSYAIIV RAYNVVPDPP QDAQIEVRIR VVESSIKPPS
310 320 330 340 350
FVNPIDTPIY LKENLKNFTH PIATLRAVSN MPDKPEVIFE LNTGRTEQTN
360 370 380 390 400
SKNTFVFNQI GNEVTISLGK TLDYEAITDY TLTMIVRNTH ELGTEHQIKI
410 420 430 440 450
QVEDVNDNIP YYTEVKSGTI LENEPPGTPV MQVRAFDMDG TSANNIVSFE
460 470 480 490 500
LADNREYFTI DPNTGNITAL TTFDREERDF YNVKVIASDN SPSSLFDNGE
510 520 530 540 550
PNRGHQVFRI SIGDKNDHKP HFQQDKYLAE RLLEDANTNT EVIEVKAEDE
560 570 580 590 600
DNASQILYSI ESGNVGDAFK IGLKTGKITV NQKLDYETIT EYELKVRAFD
610 620 630 640 650
GIYDDYTTVV IKIEDVNDNP PVFKQDYSVT ILEETTYDDC ILTVEAYDPD
660 670 680 690 700
IKDRNADQHI VYSIHQNDGN RWTIDNSGCL RLVKTLDRDP PNGHKNWQVL
710 720 730 740 750
IKANDEDGVG TTVSTVKEVT VTLKDINDNA PFLINEMPVY WQENRNPGHV
760 770 780 790 800
VQLQANDYDD TPGAGNFTFG IDSEATPDIK TKFSMDGDYL HANVQFDREA
810 820 830 840 850
QKEYFIPIRI SDSGVPRQSA VSILHLVIGD VNDNAMSEGS SRIFIYNYKG
860 870 880 890 900
EAPETDIGRV FVDDLDDWDL EDKYFEWKDL PHDQFRLNPS TGMITMLVHT
910 920 930 940 950
AEGEYDLSFV VTEDSMFVPR HSVDAYVTVV VRELPEEAVD KSGSIRFINV
960 970 980 990 1000
TKEEFISVPR DFQSPDALSL KDRLQLSLAK LFNTSVSNVD VFTVLQNENH
1010 1020 1030 1040 1050
TLDVRFSAHG SPYYAPEKLN GIVAQNQQRL ENELDLQMLM VNIDECLIEK
1060 1070 1080 1090 1100
FKCEESCTNE LHKSSVPYMI YSNTTSFVGV NAFVQAQCVC EAPLMRRCLN
1110 1120 1130 1140 1150
GGSPRYGEND VCDCIDGFTG PHCELVSVAF YGSGYAFYEP IAACNNTKIS
1160 1170 1180 1190 1200
LEITPQIDQG LIMYLGPLNF NPLLAISDFL ALELDNGYPV LTVDYGSGAI
1210 1220 1230 1240 1250
RIRHQHIKMV ADRTYQLDII LQRTSIEMTV DNCRLSTCQT LGAPIGPNEF
1260 1270 1280 1290 1300
LNVNAPLQLG GTPVDLEQLG RQLNWTHVPN QKGFFGCIRN LTINEQTYNL
1310 1320 1330 1340 1350
GMPSVFRNID SGCQQSVAVA FSFGIDRNFI IAIIVCLALL LIILLAVVVQ
1360 1370 1380 1390 1400
KKQKNGWHEK DIDDIRETII NYEDEGGGER DTDYDLNVLR TQPFYEEKLY
1410 1420 1430 1440 1450
KDPHALQGNM RDPNDIPDIA DFLGDKKENC DRDVGATTVD DVRHYAYEGD
1460 1470 1480 1490 1500
GNSDGSLSSL ASCTDDGDLN FDYLSNFGPR FRKLADMYGE EPSDTDSNVD

DDQGWRI
Length:1,507
Mass (Da):169,821
Last modified:June 1, 2000 - v2
Checksum:iDF2B5CAAA29D8EE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti974 – 9741L → F in BAA05942 (PubMed:7958432).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28749 mRNA. Translation: BAA05942.1.
AE013599 Genomic DNA. Translation: AAF46659.1.
RefSeqiNP_476722.1. NM_057374.3.

Genome annotation databases

EnsemblMetazoaiFBtr0071546; FBpp0071475; FBgn0003391.
GeneIDi37386.
KEGGidme:Dmel_CG3722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28749 mRNA. Translation: BAA05942.1.
AE013599 Genomic DNA. Translation: AAF46659.1.
RefSeqiNP_476722.1. NM_057374.3.

3D structure databases

DisProtiDP00269.
ProteinModelPortaliQ24298.
SMRiQ24298. Positions 81-854, 1171-1300, 1413-1489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63025. 10 interactions.
DIPiDIP-22198N.
IntActiQ24298. 3 interactions.
MINTiMINT-1608719.
STRINGi7227.FBpp0071475.

PTM databases

iPTMnetiQ24298.

Proteomic databases

PaxDbiQ24298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071546; FBpp0071475; FBgn0003391.
GeneIDi37386.
KEGGidme:Dmel_CG3722.

Organism-specific databases

CTDi37386.
FlyBaseiFBgn0003391. shg.

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00840000129706.
InParanoidiQ24298.
OMAiDFYNVKV.
OrthoDBiEOG718KB7.
PhylomeDBiQ24298.

Miscellaneous databases

GenomeRNAii37386.
NextBioi803387.
PROiQ24298.

Gene expression databases

BgeeiQ24298.
ExpressionAtlasiQ24298. differential.
GenevisibleiQ24298. DM.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
2.60.40.60. 7 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
IPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 7 hits.
SM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 8 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS00232. CADHERIN_1. 5 hits.
PS50268. CADHERIN_2. 7 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A Drosophila homolog of cadherin associated with armadillo and essential for embryonic cell-cell adhesion."
    Oda H., Uemura T., Harada Y., Iwai Y., Takeichi M.
    Dev. Biol. 165:716-726(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  5. "Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo."
    Bauer R., Lehmann C., Martini J., Eckardt F., Hoch M.
    Mol. Biol. Cell 15:2992-3004(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INX2.
  6. "The Fes/Fer non-receptor tyrosine kinase cooperates with Src42A to regulate dorsal closure in Drosophila."
    Murray M.J., Davidson C.M., Hayward N.M., Brand A.H.
    Development 133:3063-3073(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "The glucosyltransferase Xiantuan of the endoplasmic reticulum specifically affects E-Cadherin expression and is required for gastrulation movements in Drosophila."
    Zhang Y., Kong D., Reichl L., Vogt N., Wolf F., Grosshans J.
    Dev. Biol. 390:208-220(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION.

Entry informationi

Entry nameiCADE_DROME
AccessioniPrimary (citable) accession number: Q24298
Secondary accession number(s): Q9W2N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: May 11, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.