CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006442
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Catenin alpha-1 
Protein Synonyms/Alias
 Alpha E-catenin; Cadherin-associated protein; Renal carcinoma antigen NY-REN-13 
Gene Name
 CTNNA1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12HAGNINFKWDPKSLEubiquitination[1, 2]
16INFKWDPKSLEIRTLubiquitination[1, 2]
45TLVNTNSKGPSNKKRubiquitination[2, 3]
81EKGDKIAKESQFLKEubiquitination[1]
163VVEDGILKLRNAGNEubiquitination[1]
178QDLGIQYKALKPEVDubiquitination[1, 3]
181GIQYKALKPEVDKLNubiquitination[3]
478LAAKPQSKLAQENMDubiquitination[1, 3]
571EPGVYTEKVLEATKLubiquitination[3]
577EKVLEATKLLSNTVMubiquitination[1]
683LPQEQKAKIAEQVASubiquitination[3]
695VASFQEEKSKLDAEVubiquitination[3]
925VQALSEFKAMDSI**ubiquitination[3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
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 Annotation
 REGION 2 228 Involved in homodimerization.
 REGION 97 148 Interaction with JUP and CTNNB1.
 REGION 325 394 Interaction with alpha-actinin.
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 634 634 Phosphothreonine.
 MOD_RES 641 641 Phosphoserine.
 MOD_RES 645 645 Phosphothreonine.
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 654 654 Phosphothreonine (By similarity).
 MOD_RES 655 655 Phosphoserine (By similarity).
 MOD_RES 658 658 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 906 AA 
Protein Sequence
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 GNCDTCGALQ GLKGWPPPLC LATHWVDSAM 840
SLIQAAKNLM NAVVQTVKAS YVASTKYQKS QGMASLNLPA VSWKMKAPEK KPLVKREKQD 900
ETQTKIKRAS QKKHVNPVQA LSEFKAMDSI 930 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0016342; C:catenin complex; IDA:BHF-UCL.
 GO:0005911; C:cell-cell junction; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0014704; C:intercalated disc; IEA:Compara.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0005915; C:zonula adherens; IEA:Compara.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0034332; P:adherens junction organization; TAS:Reactome.
 GO:0007568; P:aging; IEA:Compara.
 GO:0043297; P:apical junction assembly; NAS:UniProtKB.
 GO:0031103; P:axon regeneration; IEA:Compara.
 GO:0007155; P:cell adhesion; NAS:ProtInc.
 GO:0071681; P:cellular response to indole-3-methanol; IDA:UniProtKB.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 GO:0016264; P:gap junction assembly; IEA:Compara.
 GO:0008584; P:male gonad development; IEA:Compara.
 GO:0042692; P:muscle cell differentiation; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Compara.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0001541; P:ovarian follicle development; IEA:Compara.
 GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
 GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Compara.
 GO:0051291; P:protein heterooligomerization; IEA:Compara.
 GO:0043627; P:response to estrogen stimulus; IEA:Compara. 
Interpro
 IPR001033; Alpha_catenin.
 IPR006077; Vinculin/catenin.
 IPR000633; Vinculin_CS. 
Pfam
 PF01044; Vinculin 
SMART
  
PROSITE
 PS00663; VINCULIN_1 
PRINTS
 PR00805; ALPHACATENIN.