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P35221

- CTNA1_HUMAN

UniProt

P35221 - CTNA1_HUMAN

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Protein

Catenin alpha-1

Gene
CTNNA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.

GO - Molecular functioni

  1. beta-catenin binding Source: BHF-UCL
  2. cadherin binding Source: UniProtKB
  3. gamma-catenin binding Source: BHF-UCL
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: HGNC
  6. structural molecule activity Source: InterPro
  7. vinculin binding Source: UniProtKB

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. aging Source: Ensembl
  3. apical junction assembly Source: UniProtKB
  4. axon regeneration Source: Ensembl
  5. cell adhesion Source: ProtInc
  6. cell-cell junction organization Source: Reactome
  7. cell junction assembly Source: Reactome
  8. cellular protein localization Source: Ensembl
  9. cellular response to indole-3-methanol Source: UniProtKB
  10. epithelial cell-cell adhesion Source: Ensembl
  11. establishment or maintenance of cell polarity Source: Ensembl
  12. gap junction assembly Source: Ensembl
  13. male gonad development Source: Ensembl
  14. muscle cell differentiation Source: Reactome
  15. negative regulation of apoptotic process Source: Ensembl
  16. negative regulation of cell motility Source: Ensembl
  17. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  18. negative regulation of integrin-mediated signaling pathway Source: Ensembl
  19. negative regulation of neuroblast proliferation Source: Ensembl
  20. odontogenesis of dentin-containing tooth Source: Ensembl
  21. ovarian follicle development Source: Ensembl
  22. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  23. positive regulation of muscle cell differentiation Source: Reactome
  24. positive regulation of smoothened signaling pathway Source: Ensembl
  25. protein heterooligomerization Source: Ensembl
  26. response to estrogen Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.
REACT_21402. CDO in myogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Catenin alpha-1
Alternative name(s):
Alpha E-catenin
Cadherin-associated protein
Renal carcinoma antigen NY-REN-13
Gene namesi
Name:CTNNA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:2509. CTNNA1.

Subcellular locationi

Isoform 1 : Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction
Note: Found at cell-cell boundaries and probably at cell-matrix boundaries.1 Publication
Isoform 3 : Cell membrane; Peripheral membrane protein; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. actin cytoskeleton Source: InterPro
  3. catenin complex Source: BHF-UCL
  4. cell-cell junction Source: UniProtKB
  5. cytosol Source: Reactome
  6. intercalated disc Source: Ensembl
  7. lamellipodium Source: Ensembl
  8. plasma membrane Source: Reactome
  9. zonula adherens Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27008.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 906905Catenin alpha-1PRO_0000064261Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei634 – 6341Phosphothreonine1 Publication
Modified residuei641 – 6411Phosphoserine9 Publications
Modified residuei645 – 6451Phosphothreonine2 Publications
Modified residuei652 – 6521Phosphoserine3 Publications

Post-translational modificationi

Sumoylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP35221.
PaxDbiP35221.
PeptideAtlasiP35221.
PRIDEiP35221.

PTM databases

PhosphoSiteiP35221.

Expressioni

Tissue specificityi

Expressed ubiquitously in normal tissues.

Gene expression databases

ArrayExpressiP35221.
BgeeiP35221.
CleanExiHS_CTNNA1.
GenevestigatoriP35221.

Organism-specific databases

HPAiCAB021089.
HPA046119.

Interactioni

Subunit structurei

Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Binds MLLT4 and F-actin. Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interacts with ARHGAP21 and with AJUBA. Interacts with LIMA1 By similarity.6 Publications

Protein-protein interaction databases

BioGridi107876. 49 interactions.
DIPiDIP-515N.
IntActiP35221. 18 interactions.
MINTiMINT-4998962.
STRINGi9606.ENSP00000304669.

Structurei

Secondary structure

1
906
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi293 – 2997
Beta strandi300 – 3023
Helixi305 – 31612
Helixi325 – 3273
Helixi328 – 35225
Helixi353 – 3553
Helixi378 – 3869
Helixi387 – 3893
Turni393 – 3953
Helixi398 – 40912
Helixi413 – 43826
Helixi444 – 47330
Helixi478 – 50629
Helixi509 – 53123
Helixi535 – 55925
Turni560 – 5623
Helixi567 – 58115
Helixi583 – 59816
Beta strandi600 – 6023
Helixi608 – 63023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6GX-ray2.20A/B377-632[»]
4EHPX-ray2.66B277-382[»]
4IGGX-ray3.66A/B82-906[»]
ProteinModelPortaliP35221.
SMRiP35221. Positions 22-878.

Miscellaneous databases

EvolutionaryTraceiP35221.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 228227Involved in homodimerizationAdd
BLAST
Regioni97 – 14852Interaction with JUP and CTNNB1Add
BLAST
Regioni325 – 39470Interaction with alpha-actininAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG240050.
HOGENOMiHOG000280724.
HOVERGENiHBG000069.
KOiK05691.
OMAiWERQVRV.
OrthoDBiEOG7HQN7B.
PhylomeDBiP35221.
TreeFamiTF313686.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35221-1) [UniParc]FASTAAdd to Basket

Also known as: CTNNA1a

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

« Hide

MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK    50
KRGRSKKAHV LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ 100
GDLMKAAAGE FADDPCSSVK RGNMVRAARA LLSAVTRLLI LADMADVYKL 150
LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL KPEVDKLNIM AAKRQQELKD 200
VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN RDLIYKQLQQ 250
AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 300
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE 350
YMGNAGRKER SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP 400
LLVLIEAAKN GNEKEVKEYA QVFREHANKL IEVANLACSI SNNEEGVKLV 450
RMSASQLEAL CPQVINAALA LAAKPQSKLA QENMDLFKEQ WEKQVRVLTD 500
AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR TAGAIRGRAA 550
RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 600
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV 650
RSRTSVQTED DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA 700
EVSKWDDSGN DIIVLAKQMC MIMMEMTDFT RGKGPLKNTS DVISAAKKIA 750
EAGSRMDKLG RTIADHCPDS ACKQDLLAYL QRIALYCHQL NICSKVKAEV 800
QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS TKYQKSQGMA 850
SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 900
KAMDSI 906
Length:906
Mass (Da):100,071
Last modified:February 1, 1994 - v1
Checksum:i7AAE6F5DDBAF5099
GO
Isoform 2 (identifier: P35221-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     811-811: G → GNCDTCGALQGLKGWPPPLCLATHW

Show »
Length:930
Mass (Da):102,635
Checksum:i6EDF38C221CA2FA0
GO
Isoform 3 (identifier: P35221-3) [UniParc]FASTAAdd to Basket

Also known as: CTNNA1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-370: Missing.

Note: Expressed at high levels in the nervous system. Lacks the beta-catenin interaction domain.

Show »
Length:536
Mass (Da):59,550
Checksum:i887A39433621F5DB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791A → V.1 Publication
Corresponds to variant rs28363394 [ dbSNP | Ensembl ].
VAR_022303
Natural varianti219 – 2191P → S.1 Publication
Corresponds to variant rs28363406 [ dbSNP | Ensembl ].
VAR_022304

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 370370Missing in isoform 3. VSP_047810Add
BLAST
Alternative sequencei811 – 8111G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2. VSP_017494

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921A → V in AAA86430. 1 Publication
Sequence conflicti92 – 921A → V in AAA18949. 1 Publication
Sequence conflicti129 – 1291R → P in AAA18949. 1 Publication
Sequence conflicti175 – 1751I → N in AAA86430. 1 Publication
Sequence conflicti175 – 1751I → N in AAA18949. 1 Publication
Sequence conflicti216 – 2161K → S in AAA86430. 1 Publication
Sequence conflicti216 – 2161K → S in AAA18949. 1 Publication
Sequence conflicti342 – 3421Q → K in BAA03530. 1 Publication
Sequence conflicti344 – 3485LQDLL → CRTCV in AAA86430. 1 Publication
Sequence conflicti460 – 4601L → G in AAA86430. 1 Publication
Sequence conflicti460 – 4601L → G in AAA18949. 1 Publication
Sequence conflicti469 – 4691L → TW in AAA86430. 1 Publication
Sequence conflicti469 – 4691L → TW in AAA18949. 1 Publication
Sequence conflicti473 – 4731A → P in AAA86430. 1 Publication
Sequence conflicti473 – 4731A → P in AAA18949. 1 Publication
Sequence conflicti653 – 6531R → E in AAA86430. 1 Publication
Sequence conflicti653 – 6531R → E in AAA18949. 1 Publication
Sequence conflicti685 – 6851A → R in AAA86430. 1 Publication
Sequence conflicti685 – 6851A → R in AAA18949. 1 Publication
Sequence conflicti764 – 7641A → R in AAA86430. 1 Publication
Sequence conflicti764 – 7641A → R in AAA18949. 1 Publication
Sequence conflicti789 – 7891Q → H in BAA03530. 1 Publication
Sequence conflicti859 – 8591W → M in AAA86430. 1 Publication
Sequence conflicti859 – 8591W → M in AAA18949. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14705 mRNA. Translation: BAA03530.1.
D13866 mRNA. Translation: BAA02979.1.
L23805 mRNA. Translation: AAA86430.1.
U03100 mRNA. Translation: AAA18949.1.
HQ589335 mRNA. Translation: AEF32483.1.
AF102803
, AF102787, AF102788, AF102789, AF102790, AF102791, AF102792, AF102793, AF102794, AF102795, AF102796, AF102797, AF102798, AF102799, AF102800, AF102801, AF102802 Genomic DNA. Translation: AAC99459.1.
AY884207 Genomic DNA. Translation: AAW56940.1.
AC010453 Genomic DNA. No translation available.
AC011405 Genomic DNA. No translation available.
AC034243 Genomic DNA. No translation available.
AC113340 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62124.1.
BC000385 mRNA. Translation: AAH00385.1.
BC031262 mRNA. Translation: AAH31262.1.
L22080 mRNA. Translation: AAA35502.1.
CCDSiCCDS34243.1. [P35221-1]
PIRiJC2542.
JN0607.
RefSeqiNP_001277236.1. NM_001290307.1.
NP_001277238.1. NM_001290309.1.
NP_001277239.1. NM_001290310.1.
NP_001277241.1. NM_001290312.1. [P35221-3]
NP_001894.2. NM_001903.3. [P35221-1]
XP_005271956.1. XM_005271899.1. [P35221-3]
XP_006714599.1. XM_006714536.1. [P35221-1]
UniGeneiHs.445981.

Genome annotation databases

EnsembliENST00000302763; ENSP00000304669; ENSG00000044115. [P35221-1]
ENST00000540387; ENSP00000438476; ENSG00000044115. [P35221-3]
GeneIDi1495.
KEGGihsa:1495.
UCSCiuc003ldh.3. human. [P35221-1]

Polymorphism databases

DMDMi461853.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14705 mRNA. Translation: BAA03530.1 .
D13866 mRNA. Translation: BAA02979.1 .
L23805 mRNA. Translation: AAA86430.1 .
U03100 mRNA. Translation: AAA18949.1 .
HQ589335 mRNA. Translation: AEF32483.1 .
AF102803
, AF102787 , AF102788 , AF102789 , AF102790 , AF102791 , AF102792 , AF102793 , AF102794 , AF102795 , AF102796 , AF102797 , AF102798 , AF102799 , AF102800 , AF102801 , AF102802 Genomic DNA. Translation: AAC99459.1 .
AY884207 Genomic DNA. Translation: AAW56940.1 .
AC010453 Genomic DNA. No translation available.
AC011405 Genomic DNA. No translation available.
AC034243 Genomic DNA. No translation available.
AC113340 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62124.1 .
BC000385 mRNA. Translation: AAH00385.1 .
BC031262 mRNA. Translation: AAH31262.1 .
L22080 mRNA. Translation: AAA35502.1 .
CCDSi CCDS34243.1. [P35221-1 ]
PIRi JC2542.
JN0607.
RefSeqi NP_001277236.1. NM_001290307.1.
NP_001277238.1. NM_001290309.1.
NP_001277239.1. NM_001290310.1.
NP_001277241.1. NM_001290312.1. [P35221-3 ]
NP_001894.2. NM_001903.3. [P35221-1 ]
XP_005271956.1. XM_005271899.1. [P35221-3 ]
XP_006714599.1. XM_006714536.1. [P35221-1 ]
UniGenei Hs.445981.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H6G X-ray 2.20 A/B 377-632 [» ]
4EHP X-ray 2.66 B 277-382 [» ]
4IGG X-ray 3.66 A/B 82-906 [» ]
ProteinModelPortali P35221.
SMRi P35221. Positions 22-878.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107876. 49 interactions.
DIPi DIP-515N.
IntActi P35221. 18 interactions.
MINTi MINT-4998962.
STRINGi 9606.ENSP00000304669.

PTM databases

PhosphoSitei P35221.

Polymorphism databases

DMDMi 461853.

Proteomic databases

MaxQBi P35221.
PaxDbi P35221.
PeptideAtlasi P35221.
PRIDEi P35221.

Protocols and materials databases

DNASUi 1495.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302763 ; ENSP00000304669 ; ENSG00000044115 . [P35221-1 ]
ENST00000540387 ; ENSP00000438476 ; ENSG00000044115 . [P35221-3 ]
GeneIDi 1495.
KEGGi hsa:1495.
UCSCi uc003ldh.3. human. [P35221-1 ]

Organism-specific databases

CTDi 1495.
GeneCardsi GC05P137947.
HGNCi HGNC:2509. CTNNA1.
HPAi CAB021089.
HPA046119.
MIMi 116805. gene.
neXtProti NX_P35221.
PharmGKBi PA27008.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240050.
HOGENOMi HOG000280724.
HOVERGENi HBG000069.
KOi K05691.
OMAi WERQVRV.
OrthoDBi EOG7HQN7B.
PhylomeDBi P35221.
TreeFami TF313686.

Enzyme and pathway databases

Reactomei REACT_19195. Adherens junctions interactions.
REACT_21402. CDO in myogenesis.

Miscellaneous databases

ChiTaRSi CTNNA1. human.
EvolutionaryTracei P35221.
GeneWikii Catenin_(cadherin-associated_protein),_alpha_1.
GenomeRNAii 1495.
NextBioi 6145.
PROi P35221.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35221.
Bgeei P35221.
CleanExi HS_CTNNA1.
Genevestigatori P35221.

Family and domain databases

InterProi IPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view ]
PANTHERi PTHR18914. PTHR18914. 1 hit.
Pfami PF01044. Vinculin. 2 hits.
[Graphical view ]
PRINTSi PR00805. ALPHACATENIN.
SUPFAMi SSF47220. SSF47220. 4 hits.
PROSITEi PS00663. VINCULIN_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, expression and chromosome assignment of the human catenin (cadherin-associated protein) alpha 1 gene (CTNNA1)."
    Furukawa Y., Nakatsuru S., Nagafuchi A., Tsukita S., Muto T., Nakamura Y., Horii A.
    Cytogenet. Cell Genet. 65:74-78(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Cloning of the human alpha-catenin cDNA and its aberrant mRNA in a human cancer cell line."
    Oda T., Kanai Y., Shimoyama Y., Nagafuchi A., Tsukita S., Hirohashi S.
    Biochem. Biophys. Res. Commun. 193:897-904(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon and Lung.
  3. "Molecular cloning reveals alternative splice forms of human alpha(E)-catenin."
    Rimm D.L., Kebriaei P., Morrow J.S.
    Biochem. Biophys. Res. Commun. 203:1691-1699(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Colon.
  4. "Bidirectional transcription from human LRRTM2/CTNNA1 and LRRTM1/CTNNA2 gene loci leads to expression of N-terminally truncated CTNNA1 and CTNNA2 isoforms."
    Kask M., Pruunsild P., Timmusk T.
    Biochem. Biophys. Res. Commun. 411:56-61(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORM 3).
    Tissue: Hippocampus.
  5. "Genomic organization of the human alphaE-catenin gene (CTNNA1)."
    Nollet F.H., Vanpoucke G.G., van Roy F.M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. NIEHS SNPs program
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-179 AND SER-219.
  7. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Lung.
  10. Bienvenut W.V., Zebisch A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 166-178 AND 617-623, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  11. "Assignment of the human alpha-catenin gene (CTNNA1) to chromosome 5q21-q22."
    McPherson J.D., Morton R.A., Ewing C.M., Wasmuth J.J., Overhauser J., Nagafuchi A., Tsukita S., Isaacs W.B.
    Genomics 19:188-190(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 159-250.
    Tissue: Prostate.
  12. "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
    Butz S., Kemler R.
    FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
  13. "Alpha-catenin can form asymmetric homodimeric complexes and/or heterodimeric complexes with beta-catenin."
    Koslov E.R., Maupin P., Pradhan D., Morrow J.S., Rimm D.L.
    J. Biol. Chem. 272:27301-27306(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CTNNB1.
  14. "Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin."
    Nieset J.E., Redfield A.R., Jin F., Knudsen K.A., Johnson K.R., Wheelock M.J.
    J. Cell Sci. 110:1013-1022(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
  15. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  16. "The LIM protein Ajuba is recruited to cadherin-dependent cell junctions through an association with alpha-catenin."
    Marie H., Pratt S.J., Betson M., Epple H., Kittler J.T., Meek L., Moss S.J., Troyanovsky S., Attwell D., Longmore G.D., Braga V.M.
    J. Biol. Chem. 278:1220-1228(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AJUBA.
  17. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  18. "ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions and for Listeria invasion."
    Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M., Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.
    Nat. Cell Biol. 7:954-960(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP21.
  19. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  22. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-645 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  23. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
    Abe K., Takeichi M.
    Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIMA1.
  26. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion."
    Yang J., Dokurno P., Tonks N.K., Barford D.
    EMBO J. 20:3645-3656(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCTNA1_HUMAN
AccessioniPrimary (citable) accession number: P35221
Secondary accession number(s): Q12795, Q8N1C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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