P35221 (CTNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catenin alpha-1

Alternative name(s):
Alpha E-catenin
Cadherin-associated protein
Renal carcinoma antigen NY-REN-13

Gene names

Name:

CTNNA1

Organism

Homo sapiens (Human)

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. 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 adherence 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.
Subunit structure	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. Ref.10 Ref.11 Ref.13 Ref.16 Ref.21
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.15
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 Reference proteome
Gene Ontology (GO)
Biological process	adherens junction organization Traceable author statement. Source: Reactome apical junction assembly Non-traceable author statement. Source: UniProtKB cell adhesion Non-traceable author statement. Source: ProtInc cellular response to indole-3-methanol Inferred from direct assay. Source: UniProtKB muscle cell differentiation Traceable author statement. Source: Reactome positive regulation of muscle cell differentiation Traceable author statement. Source: Reactome
Cellular component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro catenin complex Inferred from direct assay. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome
Molecular function	beta-catenin binding Inferred from physical interaction. Source: BHF-UCL cadherin binding Inferred from physical interaction. Source: UniProtKB gamma-catenin binding Inferred from physical interaction. Source: BHF-UCL 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

Regions

Region

2 – 228

227

Involved in homodimerization

Region

97 – 148

52

Interaction with JUP and CTNNB1

Region

325 – 394

70

Interaction with alpha-actinin

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.7

Modified residue

177

1

Phosphotyrosine Ref.19

Modified residue

186

1

N6-acetyllysine Ref.28

Modified residue

619

1

Phosphotyrosine Ref.19

Modified residue

641

1

Phosphoserine Ref.14 Ref.17 Ref.18 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Modified residue

645

1

Phosphothreonine Ref.24

Modified residue

652

1

Phosphoserine Ref.20 Ref.23 Ref.25 Ref.27

Modified residue

654

1

Phosphothreonine Ref.25

Modified residue

655

1

Phosphoserine Ref.23 Ref.25

Modified residue

658

1

Phosphothreonine Ref.20 Ref.23 Ref.25

Natural variations

Alternative sequence

811

1

G → GNCDTCGALQGLKGWPPPLC LATHW in isoform 2.

VSP_017494

Natural variant

179

1

A → V. Ref.5
Corresponds to variant rs28363394 [ dbSNP | Ensembl ].

VAR_022303

Natural variant

219

1

P → S. Ref.5
Corresponds to variant rs28363406 [ dbSNP | Ensembl ].

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 [UniParc]. 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]	"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion." Butz S., Kemler R. FEBS Lett. 355:195-200(1994) [PubMed: 7982500] [Abstract] Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[10]	"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: 9341178] [Abstract] Cited for: SUBUNIT, INTERACTION WITH CTNNB1.
[11]	"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: 9152027] [Abstract] Cited for: INTERACTION WITH JUP; CTNNB1 AND ALPHA-ACTININ.
[12]	"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.
[13]	"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 AJUBA.
[14]	"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: Cervix carcinoma.
[15]	"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.
[16]	"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.
[17]	"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: Cervix carcinoma.
[18]	"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.
[19]	"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. Tissue: Lung carcinoma.
[20]	"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. Tissue: Prostate cancer.
[21]	"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: 18093941] [Abstract] Cited for: INTERACTION WITH LIMA1.
[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 SER-641, 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-641; SER-652; SER-655 AND THR-658, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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.
[25]	"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-641; SER-652; THR-654; SER-655 AND THR-658, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[26]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
[27]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"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.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"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

EMBL
GenBank
DDBJ

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. NM_001903.2.

UniGene

Hs.445981.
Hs.656653.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P35221.

SMR

P35221. Positions 57-261, 377-631.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29632N.
DIP-515N.

IntAct

P35221. 9 interactions.

MINT

MINT-4998962.

STRING

P35221.

PTM databases

PhosphoSite

P35221.

Polymorphism databases

DMDM

461853.

Proteomic databases

PeptideAtlas

P35221.

PRIDE

P35221.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302763; ENSP00000304669; ENSG00000044115.

GeneID

1495.

KEGG

hsa:1495.

UCSC

uc003ldh.1. human.

Organism-specific databases

CTD

1495.

GeneCards

GC05P137947.

H-InvDB

HIX0005216.

HGNC

HGNC:2509. CTNNA1.

HPA

CAB021089.

MIM

116805. gene.

neXtProt

NX_P35221.

PharmGKB

PA27008.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17774.

HOVERGEN

HBG000069.

OrthoDB

EOG49W2G4.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.

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]

KO

K05691.

Pfam

PF01044. Vinculin. 2 hits.
[Graphical view]

PRINTS

PR00805. ALPHACATENIN.

SUPFAM

SSF47220. Vinculin/catenin. 4 hits.

PROSITE

PS00663. VINCULIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

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:	January 25, 2012
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.