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Protein
Submitted name:

Catenin (Cadherin associated protein), alpha 1

Gene

Ctnna1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_280475. VEGFR2 mediated vascular permeability.
REACT_287155. CDO in myogenesis.
REACT_312354. Adherens junctions interactions.
REACT_362399. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Submitted name:
Catenin (Cadherin associated protein), alpha 1Imported
Submitted name:
Catenin (Cadherin-associated protein), alpha 1, isoform CRA_bImported
Submitted name:
Protein Ctnna1Imported
Gene namesi
Name:Ctnna1Imported
Synonyms:Catna1Imported
ORF Names:rCG_49560Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi1359485. Ctnna1.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • actin cytoskeleton Source: InterPro
  • catenin complex Source: Ensembl
  • cell-cell adherens junction Source: RGD
  • cell-cell junction Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: InterPro
  • focal adhesion Source: Ensembl
  • intercalated disc Source: Ensembl
  • lamellipodium Source: Ensembl
  • plasma membrane Source: RGD
  • zonula adherens Source: Ensembl
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008041.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG240050.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
KOiK05691.
OMAiPPLCATH.
OrthoDBiEOG7HQN7B.
TreeFamiTF313686.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030047. CTNNA1.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF24. PTHR18914:SF24. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5U302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAVHTGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK
60 70 80 90 100
KRGRSKKAHV LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVDDVRKQ
110 120 130 140 150
GDLMKSAAGE FADDPCSSVK RGNMVRAARA LLSAVTRLLI LADMADVYKL
160 170 180 190 200
LVQLKVVEDG ILKLRNAGNE QDLGIQYRAL KPEVDKLNIM AAKRQQELKD
210 220 230 240 250
VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ
260 270 280 290 300
AVTGISNAAQ ATASDDASQQ QGGGGGGGEL AYALNNFDKQ IIVDPLSFSE
310 320 330 340 350
ERFRPSLEER LESIISGAAL MADSSCTRDD RRERIVAECN AVRQALQDLL
360 370 380 390 400
SEYMGNAGRK ERSDALNSAI DKMTKKTRDL RRQLRKAVMD HVSDSFLETN
410 420 430 440 450
VPLLVLIEAA KNGNEKEVKE YAQVFREHAN KLIEVANLAC SISNNEEGVK
460 470 480 490 500
LVRMSASQLE ALCPQVINAA LALAAKPQSK LAQENMDLFK EQWEKQVRVL
510 520 530 540 550
TDAVDDITSI DDFLAVSENH ILEDVNKCVI ALQEKDVDGL DRTAGAIRGR
560 570 580 590 600
AARVIHVVTS EMDNYEPGVY TEKVLEATKL LSNTVMPRFT EQVEAAVEAL
610 620 630 640 650
SSDPAQPMDE NEFIDASRLV YDGIRDIRKA VLMIRTPEEL DDSDFETEDF
660 670 680 690 700
DVRSRTSVQT EDDQLIAGQS ARAIMAQLPQ EQKAKIAEQV ASFQEEKSKL
710 720 730 740 750
DAEVSKWDDS GNDIIVLAKQ MCMIMMEMTD FTRGKGPLKN TSDVISAAKK
760 770 780 790 800
IAEAGSRMDK LGRTIADHCP DSACKQDLLA YLQRIALYCH QLNICSKVKA
810 820 830 840 850
EVQNLGGELV VSGVDSAMSL IQAAKNLMNA VVQTVKASYV ASTKYQKSQG
860 870 880 890 900
MASLNLPAVS WKMKAPEKKP LVKREKQDET QTKIKRASQK KHVNPVQALS

EFKAMDSI
Length:908
Mass (Da):100,236
Last modified:December 7, 2004 - v1
Checksum:i247F212CF5C620C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072580 Genomic DNA. No translation available.
AC126530 Genomic DNA. No translation available.
BC085789 mRNA. Translation: AAH85789.1.
CH473974 Genomic DNA. Translation: EDL76253.1.
RefSeqiNP_001007146.1. NM_001007145.1.
UniGeneiRn.103790.

Genome annotation databases

EnsembliENSRNOT00000008041; ENSRNOP00000008041; ENSRNOG00000005796.
GeneIDi307505.
KEGGirno:307505.
UCSCiRGD:1359485. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07072580 Genomic DNA. No translation available.
AC126530 Genomic DNA. No translation available.
BC085789 mRNA. Translation: AAH85789.1.
CH473974 Genomic DNA. Translation: EDL76253.1.
RefSeqiNP_001007146.1. NM_001007145.1.
UniGeneiRn.103790.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008041; ENSRNOP00000008041; ENSRNOG00000005796.
GeneIDi307505.
KEGGirno:307505.
UCSCiRGD:1359485. rat.

Organism-specific databases

CTDi1495.
RGDi1359485. Ctnna1.

Phylogenomic databases

eggNOGiNOG240050.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
KOiK05691.
OMAiPPLCATH.
OrthoDBiEOG7HQN7B.
TreeFamiTF313686.

Enzyme and pathway databases

ReactomeiREACT_280475. VEGFR2 mediated vascular permeability.
REACT_287155. CDO in myogenesis.
REACT_312354. Adherens junctions interactions.
REACT_362399. RHO GTPases activate IQGAPs.

Miscellaneous databases

NextBioi657513.

Family and domain databases

InterProiIPR001033. Alpha_catenin.
IPR030047. CTNNA1.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PTHR18914:SF24. PTHR18914:SF24. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00805. ALPHACATENIN.
SUPFAMiSSF47220. SSF47220. 4 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: KidneyImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ5U302_RAT
AccessioniPrimary (citable) accession number: Q5U302
Entry historyi
Integrated into UniProtKB/TrEMBL: December 7, 2004
Last sequence update: December 7, 2004
Last modified: July 22, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

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 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.