CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005488
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Catenin alpha-1 
Protein Synonyms/Alias
 102 kDa cadherin-associated protein; Alpha E-catenin; CAP102 
Gene Name
 Ctnna1 
Gene Synonyms/Alias
 Catna1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
12HAGNINFKWDPKSLEubiquitination[1]
16INFKWDPKSLEIRTLubiquitination[1]
45TLVNTNSKGPSNKKRubiquitination[1]
57KKRGRSKKAHVLAASubiquitination[1]
75ATENFLEKGDKIAKEubiquitination[1]
81EKGDKIAKESQFLKEubiquitination[1]
163VVEDGILKLRNAGNEubiquitination[1]
178QDLGIQYKALKPEVDubiquitination[1]
181GIQYKALKPEVDKLNubiquitination[1]
186ALKPEVDKLNIMAAKacetylation[2, 3, 4]
193KLNIMAAKRQQELKDacetylation[3]
193KLNIMAAKRQQELKDubiquitination[1]
216AARGILQKNVPILYTubiquitination[1]
417NGNEKEVKEYAQVFRubiquitination[1]
478LAAKPQSKLAQENMDubiquitination[1]
571EPGVYTEKVLEATKLubiquitination[1]
577EKVLEATKLLSNTVMubiquitination[1]
681AQLPQEQKAKIAEQVubiquitination[1]
683LPQEQKAKIAEQVASubiquitination[1]
695VASFQEEKSKLDAEVacetylation[3]
695VASFQEEKSKLDAEVubiquitination[1]
697SFQEEKSKLDAEVSKubiquitination[1]
704KLDAEVSKWDDSGNDubiquitination[1]
737TRGKGPLKNTSDVISubiquitination[1]
797LNICSKVKAEVQNLGubiquitination[1]
842ASYVASTKYQKSQGMubiquitination[1]
845VASTKYQKSQGMASLubiquitination[1]
860NLPAVSWKMKAPEKKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
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 (By
 REGION 97 148 Interaction with JUP and CTNNB1 (By
 REGION 325 394 Interaction with alpha-actinin (By
 MOD_RES 2 2 N-acetylthreonine (By similarity).
 MOD_RES 634 634 Phosphothreonine (By similarity).
 MOD_RES 641 641 Phosphoserine.
 MOD_RES 645 645 Phosphothreonine (By similarity).
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 654 654 Phosphothreonine.
 MOD_RES 655 655 Phosphoserine.
 MOD_RES 658 658 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; 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 VVAVEDVRKQ GDLMKSAAGE FADDPCSSVK 120
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL 180
KPEVDKLNIM AAKRQQELKD VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN 240
RDLIYKQLQQ AVTGISNAAQ ATASDDAAQH QGGSGGELAY 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 906 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IEA:Compara.
 GO:0015629; C:actin cytoskeleton; IEA:InterPro.
 GO:0016342; C:catenin complex; IEA:Compara.
 GO:0014704; C:intercalated disc; IDA:MGI.
 GO:0030027; C:lamellipodium; IDA:MGI.
 GO:0005886; C:plasma membrane; IDA:MGI.
 GO:0005915; C:zonula adherens; IDA:MGI.
 GO:0051015; F:actin filament binding; IDA:MGI.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0007568; P:aging; IEA:Compara.
 GO:0043297; P:apical junction assembly; IMP:MGI.
 GO:0031103; P:axon regeneration; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0071681; P:cellular response to indole-3-methanol; IEA:Compara.
 GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
 GO:0016264; P:gap junction assembly; IEA:Compara.
 GO:0008584; P:male gonad development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
 GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0001541; P:ovarian follicle development; IEA:Compara.
 GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:MGI.
 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.