Reviewed, UniProtKB/Swiss-Prot P35221 (CTNA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Catenin alpha-1
Alternative name(s):
    Cadherin-associated protein
    Alpha E-catenin
    NY-REN-13 antigen

Gene names

Name:

CTNNA1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. May play a crucial role in cell differentiation.
Subunit structure	Binds MLLT4 and F-actin By similarity. Interacts directly with PSEN1 and CTNNB1 to form part of the PSEN1/cadherin/catenin adhesion complex. Interacts with ARHGAP21 and with JUB.
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries.
Tissue specificity	Expressed ubiquitously in normal tissues.
Post-translational modification	Sumoylated. Ref.13
Involvement in disease	Abnormalities of alpha-catenin are involved in the process of cancer invasion and metastasis.
Sequence similarities	Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	apical junction assembly Non-traceable author statement. Source: UniProtKB cell adhesion Ref.2 Non-traceable author statement. Source: ProtInc
Cellular component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro adherens junction Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cadherin binding Inferred from physical interaction. Source: UniProtKB structural molecule activity Inferred from electronic annotation. Source: InterPro vinculin binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35221-1)

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

Isoform 2 (identifier: P35221-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 906

905

Catenin alpha-1

PRO_0000064261

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.7

Modified residue

177

1

Phosphotyrosine Ref.17

Modified residue

186

1

N6-acetyllysine Ref.23

Modified residue

619

1

Phosphotyrosine Ref.17

Modified residue

641

1

Phosphoserine Ref.12 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21

Modified residue

645

1

Phosphothreonine Ref.21

Modified residue

652

1

Phosphoserine Ref.18 Ref.20

Modified residue

654

1

Phosphothreonine By similarity

Modified residue

655

1

Phosphoserine Ref.20

Modified residue

658

1

Phosphothreonine Ref.18 Ref.20

Natural variations

Alternative sequence

811

1

G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2.

VSP_017494

Natural variant

179

1

A → V

VAR_022303

Natural variant

219

1

P → S: dbSNP rs28363406. Ref.5

VAR_022304

Experimental info

Sequence conflict

92

1

A → V in AAA86430. Ref.3

Sequence conflict

92

1

A → V in AAA18949. Ref.3

Sequence conflict

129

1

R → P in AAA18949. Ref.3

Sequence conflict

175

1

I → N in AAA86430. Ref.3

Sequence conflict

175

1

I → N in AAA18949. Ref.3

Sequence conflict

216

1

K → S in AAA86430. Ref.3

Sequence conflict

216

1

K → S in AAA18949. Ref.3

Sequence conflict

342

1

Q → K in BAA03530. Ref.1

Sequence conflict

344 – 348

5

LQDLL → CRTCV in AAA86430. Ref.3

Sequence conflict

460

1

L → G in AAA86430. Ref.3

Sequence conflict

460

1

L → G in AAA18949. Ref.3

Sequence conflict

469

1

L → TW in AAA86430. Ref.3

Sequence conflict

469

1

L → TW in AAA18949. Ref.3

Sequence conflict

473

1

A → P in AAA86430. Ref.3

Sequence conflict

473

1

A → P in AAA18949. Ref.3

Sequence conflict

653

1

R → E in AAA86430. Ref.3

Sequence conflict

653

1

R → E in AAA18949. Ref.3

Sequence conflict

685

1

A → R in AAA86430. Ref.3

Sequence conflict

685

1

A → R in AAA18949. Ref.3

Sequence conflict

764

1

A → R in AAA86430. Ref.3

Sequence conflict

764

1

A → R in AAA18949. Ref.3

Sequence conflict

789

1

Q → H in BAA03530. Ref.1

Sequence conflict

859

1

W → M in AAA86430. Ref.3

Sequence conflict

859

1

W → M in AAA18949. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

906

Helix Strand Turn

Details...

Helix

378 – 386

9

Helix

387 – 389

3

Turn

393 – 395

3

Helix

398 – 409

12

Helix

413 – 438

26

Helix

444 – 473

30

Helix

478 – 506

29

Helix

509 – 531

23

Helix

535 – 559

25

Turn

560 – 562

3

Helix

567 – 581

15

Helix

583 – 598

16

Beta strand

600 – 602

3

Helix

608 – 630

23

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 7AAE6F5DDBAF5099	FASTA	906	100,071
	10 20 30 40 50 60 MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 70 80 90 100 110 120 LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK 130 140 150 160 170 180 RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 190 200 210 220 230 240 KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 250 260 270 280 290 300 RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 310 320 330 340 350 360 FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 370 380 390 400 410 420 SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 430 440 450 460 470 480 QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 490 500 510 520 530 540 QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 550 560 570 580 590 600 TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 610 620 630 640 650 660 DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 670 680 690 700 710 720 DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 730 740 750 760 770 780 MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 790 800 810 820 830 840 QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS 850 860 870 880 890 900 TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF KAMDSI
	Isoform 2. Checksum: 6EDF38C221CA2FA0	FASTA	930	102,635
	10 20 30 40 50 60 MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 70 80 90 100 110 120 LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK 130 140 150 160 170 180 RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 190 200 210 220 230 240 KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 250 260 270 280 290 300 RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 310 320 330 340 350 360 FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 370 380 390 400 410 420 SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 430 440 450 460 470 480 QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 490 500 510 520 530 540 QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 550 560 570 580 590 600 TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 610 620 630 640 650 660 DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 670 680 690 700 710 720 DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 730 740 750 760 770 780 MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 790 800 810 820 830 840 QRIALYCHQL NICSKVKAEV QNLGGELVVS GNCDTCGALQ GLKGWPPPLC LATHWVDSAM 850 860 870 880 890 900 SLIQAAKNLM NAVVQTVKAS YVASTKYQKS QGMASLNLPA VSWKMKAPEK KPLVKREKQD 910 920 930 ETQTKIKRAS QKKHVNPVQA LSEFKAMDSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8404069] [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: 8323564] [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: 7945318] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Colon.
[4]	"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].
[5]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-179 AND SER-219.
[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]. Tissue: Lung.
[7]	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, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[8]	"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: 8188230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 159-250. Tissue: Prostate.
[9]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J. Int. J. Cancer 83:456-464(1999) [PubMed: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[10]	"Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts." Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K. Mol. Cell 4:893-902(1999) [PubMed: 10635315] [Abstract] Cited for: COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1.
[11]	"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: 12417594] [Abstract] Cited for: INTERACTION WITH JUB.
[12]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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: 15561718] [Abstract] Cited for: SUMOYLATION.
[14]	"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: 16184169] [Abstract] Cited for: INTERACTION WITH ARHGAP21.
[15]	"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-641, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Pituitary.
[17]	"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. , 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-177 AND TYR-619, MASS SPECTROMETRY.
[18]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-652 AND THR-658, MASS SPECTROMETRY.
[19]	"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 SER-641, MASS SPECTROMETRY.
[20]	"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-641; SER-652; SER-655 AND THR-658, MASS SPECTROMETRY.
[21]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND THR-645, MASS SPECTROMETRY. Tissue: Liver.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-186, MASS SPECTROMETRY.
[24]	"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: 11447106] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 377-632, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

D14705 mRNA. Translation: BAA03530.1.
D13866 mRNA. Translation: BAA02979.1.
L23805 mRNA. Translation: AAA86430.1.
U03100 mRNA. Translation: AAA18949.1.
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.
BC000385 mRNA. Translation: AAH00385.1.
L22080 mRNA. Translation: AAA35502.1.

IPI

IPI00215948.
IPI00473136.

PIR

JC2542.
JN0607.

RefSeq

NP_001894.2.

UniGene

Hs.534797

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H6G	X-ray	2.20	A/B	377-632	[»]

SMR

P35221. Positions 57-261.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:515N.

STRING

P35221.

PTM databases

PhosphoSite

P35221.

Proteomic databases

PeptideAtlas

P35221.

PRIDE

P35221.

Genome annotation databases

Ensembl

ENST00000302763; ENSP00000304669; ENSG00000044115; Homo sapiens. [Genome view]
ENST00000355078; ENSP00000347190; ENSG00000044115; Homo sapiens. [Genome view]

GeneID

1495.

KEGG

hsa:1495.

UCSC

uc003ldh.1. human.

Organism-specific databases

CTD

1495.

GeneCards

GC05P138117.

H-InvDB

HIX0005216.

HGNC

HGNC:2509. CTNNA1.

HPA

CAB021089.

MIM

116805. gene.

PharmGKB

PA27008.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P35221.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_19331. Cell-cell adhesion systems.

Gene expression databases

ArrayExpress

P35221.

Bgee

P35221.

CleanEx

HS_CTNNA1.

Genevestigator

P35221.

GermOnline

ENSG00000044115. Homo sapiens.

Family and domain databases

InterPro

IPR001033. Alpha_catenin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]

Pfam

PF01044. Vinculin. 1 hit.
[Graphical view]

PRINTS

PR00805. ALPHACATENIN.

PROSITE

PS00663. VINCULIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

6145.

SOURCE

Search...

Entry information

Entry name

CTNA1_HUMAN

Accession

Primary (citable) accession number: P35221
Secondary accession number(s): Q12795

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.