P35221

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession CTNA1_HUMAN; P35221;
Entrez ID 1495
GenBank Protein ID NM_001290307.2; NM_001290309.2; NM_001290310.2; NM_001290312.1; NM_001323982.1; NM_001323983.1; NM_001323984.1; NM_001323987.1; NM_001323988.1; NM_001323989.1; NM_001323990.1; NM_001323991.1; NM_001323992.1; NM_001323993.1; NM_001323994.1; NM_001323995.1; NM_001323996.1; NM_001323997.1; NM_001323998.1; NM_001323999.1; NM_001324000.1; NM_001903.4;
GenBank Nucleotide ID NP_001277236.1; NP_001277238.1; NP_001277239.1; NP_001277241.1; NP_001310911.1; NP_001310912.1; NP_001310913.1; NP_001310916.1; NP_001310917.1; NP_001310918.1; NP_001310919.1; NP_001310920.1; NP_001310921.1; NP_001310922.1; NP_001310923.1; NP_001310924.1; NP_001310925.1; NP_001310926.1; NP_001310927.1; NP_001310928.1; NP_001310929.1; NP_001894.2;
Protein Name Catenin alpha-1 (Alpha E-catenin) (Cadherin-associated protein) (Renal carcinoma antigen NY-REN-13)
Gene Name CTNNA1
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionAssociates 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.
Sequence
(Fasta)
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV 60
LAASVEQATE NFLEKGDKIA KESQFLKEEL VAAVEDVRKQ GDLMKAAAGE FADDPCSSVK 120
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 180
KPEVDKLNIM AAKRQQELKD VGHRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 240
RDLIYKQLQQ AVTGISNAAQ ATASDDASQH QGGGGGELAY ALNNFDKQII VDPLSFSEER 300
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER 360
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA 420
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA 480
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR 540
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS 600
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED 660
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC 720
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL 780
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS 840
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF 900
KAMDSI 907

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationGlioblastomaDS64119941816
[Reference]: We demonstrate here that EGFR activation results in disruption of the complex of beta-catenin and alpha-catenin, thereby abrogating the inhibitory effect of alpha-catenin on beta-catenin transactivation via CK2alpha-dependent phosphorylation of alpha-catenin at S641.?

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 4)
MESH:D046152 ; Gastrointestinal Stromal Tumors
MESH:D015470 ; Leukemia, Myeloid, Acute
MESH:D009190 ; Myelodysplastic Syndromes
MESH:C536309 ; Patterned dystrophy of retinal pigment epithelium
DisGeNet (Curated)
(count: 6)
C0023467; Leukemia, Myelocytic, Acute
C1708349; Hereditary Diffuse Gastric Cancer
C1837029; Macular Dystrophy, Butterfly-Shaped Pigmentary, 2
C1864690; Microphthalmia, Syndromic 5
C1868569; Patterned dystrophy of retinal pigment epithelium
C3463824; MYELODYSPLASTIC SYNDROME
GWASdb
(count: 3)
rs3804204; HDL cholesterol; cholesterol ester storage disease|cholesterol embolism|coronary artery disease
rs10515503; Fibrinogen; cardiovascular system disease
rs10515503; Coronary artery calcification; coronary artery disease

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 47)
(view all)
117       EFADDPCSSVKRGNM     dbPAF
118       FADDPCSSVKRGNMV     dbPAF
148       LADMADVYKLLVQLK     dbPAF
177       EQDLGIQYKALKPEV     dbPAF
222       QKNVPILYTASQACL     dbPAF
223       KNVPILYTASQACLQ     dbPAF
Acetylation
(count: 6)
120       DDPCSSVKRGNMVRA     PLMD
155       YKLLVQLKVVEDGIL     PLMD
181       GIQYKALKPEVDKLN     PLMD
186       ALKPEVDKLNIMAAK     PLMD
193       KLNIMAAKRQQELKD     PLMD
842       ASYVASTKYQKSQGM     PLMD
Ubiquitination
(count: 31)
(view all)
12        HAGNINFKWDPKSLE     PLMD
120       DDPCSSVKRGNMVRA     PLMD
16        INFKWDPKSLEIRTL     PLMD
163       VVEDGILKLRNAGNE     PLMD
178       QDLGIQYKALKPEVD     PLMD
181       GIQYKALKPEVDKLN     PLMD
Glycation
(count: 1)
704       KLDAEVSKWDDSGND     PLMD
Malonylation
(count: 2)
181       GIQYKALKPEVDKLN     PLMD
747       SDVISAAKKIAEAGS     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource