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 Description | 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. |
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 |
|
Database | Annotation |
---|---|
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 | 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 |
Network | Interaction | ||
---|---|---|---|
A | B | Source | |