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Protein Page:
CTNNA1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CTNNA1 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. 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. Expressed ubiquitously in normal tissues. Belongs to the vinculin/alpha-catenin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Actin binding protein
Cellular Component: lamellipodium; plasma membrane; acrosome; catenin complex; zonula adherens; intercellular junction; cytosol; actin cytoskeleton
Molecular Function: actin filament binding; protein binding; cadherin binding; gamma-catenin binding; beta-catenin binding; structural molecule activity; vinculin binding
Biological Process: intercellular junction assembly and maintenance; apical junction assembly; gap junction assembly; axon regeneration; male gonad development; establishment and/or maintenance of cell polarity; odontogenesis of dentine-containing teeth; muscle cell differentiation; negative regulation of neuroblast proliferation; ovarian follicle development; response to estrogen stimulus; positive regulation of muscle cell differentiation; positive regulation of smoothened signaling pathway; cell adhesion; negative regulation of apoptosis; aging
Reference #:  P35221 (UniProtKB)
Alt. Names/Synonyms: Alpha E-catenin; alpha-catenin; alpha-E-catenin; alphaE-catenin; Cadherin-associated protein; cadherin-associated protein,102kDa; CAP102; catenin (cadherin-associated protein), alpha 1, 102kDa; Catenin alpha-1; CTNA1; CTNNA1; FLJ36832; FLJ52416; Renal carcinoma antigen NY-REN-13
Gene Symbols: CTNNA1
Molecular weight: 100,071 Da
Basal Isoelectric point: 5.95  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  Wnt/ß-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CTNNA1
Protein Structure Not Found.


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Sites Implicated In
carcinogenesis, induced: S641‑p
cell motility, altered: S641‑p
transcription, altered: S641‑p
molecular association, regulation: S641‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 2 K12-u HAGNINFkWDPkSLE
0 6 K16-u INFkWDPkSLEIRTL
0 1 T38-p PLVTQVTtLVNTNSk
0 7 K45-u tLVNTNSkGPSNkKR
0 2 K50-u NSkGPSNkKRGRSKK
0 1 K57 kKRGRSKKAHVLAAS
0 1 K75 ATENFLEKGDKIAkE
0 2 K81-u EKGDKIAkEsQFLKE
0 1 S83-p GDKIAkEsQFLKEEL
0 1 S118-p FADDPCSsVKRGNMV
0 1 Y148-p LADMADVyKLLVQLK
0 1 K163 VVEDGILKLRNAGNE
0 568 Y177-p EQDLGIQykALkPEV
0 4 K178-u QDLGIQykALkPEVD
0 1 K181-u GIQykALkPEVDkLN
0 1 K186-a ALkPEVDkLNIMAAk
0 8 K193-a kLNIMAAkRQQELKD
0 1 K193 kLNIMAAKRQQELKD
0 2 K216-u AARGILQkNVPILyt
0 15 Y222-p QkNVPILytASQACL
0 5 T223-p kNVPILytASQACLQ
0 1 S225 VPILytASQACLQHP
0 4 Y237-p QHPDVAAyKANRDLI
0 3 Y245-p KANRDLIyKQLQQAV
0 2 S268-p ATASDDAsQHQGGGG
0 49 Y280-p GGGGELAyALNNFDK
0 1 S323-p AALMADSsCTRDDRR
0 1 S361-p NAGRKERsDALNSAI
0 1 T372-p NSAIDKMtKKTRDLR
0 1 K414-u AAKNGNEkEVKEyAQ
0 52 Y419-p NEkEVKEyAQVFREH
0 1 K448-u SNNEEGVkLVRMSAs
0 3 S455-p kLVRMSAsQLEALCP
0 2 K478-u LAAKPQSkLAQENMD
0 1 T541-p DVDGLDRtAGAIRGR
0 2 Y563-p VTSEMDNyEPGVYTE
0 1 K571 EPGVYTEKVLEATkL
0 2 K577-u EKVLEATkLLSNTVM
0 39 Y619-p IDASRLVyDGIRDIR
0 21 T634-p KAVLMIRtPEELDDs
2 112 S641-p tPEELDDsDFEtEDF
0 8 T645-p LDDsDFEtEDFDVRs
0 23 S652-p tEDFDVRsRtsVQtE
0 22 T654-p DFDVRsRtsVQtEDD
0 37 S655-p FDVRsRtsVQtEDDQ
0 34 T658-p RsRtsVQtEDDQLIA
0 1 K681 AQLPQEQKAKIAEQV
0 1 K683 LPQEQKAKIAEQVAS
0 2 K695-u VASFQEEkSKLDAEV
0 1 K697 SFQEEkSKLDAEVSK
0 1 K704 KLDAEVSKWDDSGND
0 1 K737 TRGKGPLKNTSDVIs
0 1 S744-p KNTSDVIsAAkKIAE
0 1 K747-a SDVIsAAkKIAEAGS
0 1 K758-u EAGSRMDkLGRTIAD
0 5 K797-u LNICSKVkAEVQNLG
0 1 Y837-p VQTVKASyVASTKYQ
0 1 K845 VASTKYQKSQGMASL
0 1 K860 NLPAVSWKMKAPEKK
0 6 S886-p QTKIKRAsQKKHVNP
0 1 S898-p VNPVQALsEFkAMDS
0 1 K901-u VQALsEFkAMDSI__
  mouse

 
K12-u HAGNINFkWDPkSLE
K16-u INFkWDPkSLEIRTL
T38 PLVTQVTTLVNTNSk
K45-u TLVNTNSkGPSNkKR
K50-u NSkGPSNkKRGRSKk
K57-u kKRGRSKkAHVLAAS
K75-u ATENFLEkGDKIAkE
K81-u EkGDKIAkESQFLKE
S83 GDKIAkESQFLKEEL
S118 FADDPCSSVKRGNMV
Y148 LADMADVYKLLVQLK
K163-u VVEDGILkLRNAGNE
Y177-p EQDLGIQykALKPEV
K178-u QDLGIQykALKPEVD
K181 GIQykALKPEVDKLN
K186 ALKPEVDKLNIMAAk
K193 KLNIMAAKRQQELKD
K193-u KLNIMAAkRQQELKD
K216-u AARGILQkNVPILYT
Y222 QkNVPILYTAsQACL
T223 kNVPILYTAsQACLQ
S225-p VPILYTAsQACLQHP
Y237 QHPDVAAYKANRDLI
Y245 KANRDLIYKQLQQAV
A268 ATASDDAAQHQGGSG
Y280-p GSGGELAyALNNFDK
S323 AALMADSSCTRDDRR
S361 NAGRKERSDALNSAI
T372 NSAIDKMTKKTRDLR
K414 AAKNGNEKEVKEyAQ
Y419-p NEKEVKEyAQVFREH
K448 SNNEEGVKLVRMSAs
S455-p KLVRMSAsQLEALCP
K478-u LAAKPQSkLAQENMD
T541 DVDGLDRTAGAIRGR
Y563 VTSEMDNYEPGVYTE
K571-u EPGVYTEkVLEATkL
K577-u EkVLEATkLLSNTVM
Y619-p IDASRLVyDGIRDIR
T634-p KAVLMIRtPEELDDs
S641-p tPEELDDsDFEtEDF
T645-p LDDsDFEtEDFDVRs
S652-p tEDFDVRsRtsVQtE
T654-p DFDVRsRtsVQtEDD
S655-p FDVRsRtsVQtEDDQ
T658-p RsRtsVQtEDDQLIA
K681-u AQLPQEQkAkIAEQV
K683-u LPQEQkAkIAEQVAS
K695-u VASFQEEkSkLDAEV
K697-u SFQEEkSkLDAEVSk
K704-u kLDAEVSkWDDSGND
K737-u TRGKGPLkNTSDVIS
S744 kNTSDVISAAKKIAE
K747 SDVISAAKKIAEAGS
K758 EAGSRMDKLGRTIAD
K797-u LNICSKVkAEVQNLG
Y837 VQTVKASYVASTKYQ
K845-u VASTKYQkSQGMASL
K860-u NLPAVSWkMKAPEKK
S886 QTKIKRASQKKHVNP
S898-p VNPVQALsEFKAMDS
K901 VQALsEFKAMDSI__
  rat

 
K12 HTGNINFKWDPKSLE
K16 INFKWDPKSLEIRTL
T38 PLVTQVTTLVNTNSK
K45 TLVNTNSKGPSNKKR
K50 NSKGPSNKKRGRSKK
K57 KKRGRSKKAHVLAAS
K75 ATENFLEKGDKIAKE
K81 EKGDKIAKESQFLKE
S83 GDKIAKESQFLKEEL
S118 FADDPCSSVKRGNMV
Y148 LADMADVYKLLVQLK
K163 VVEDGILKLRNAGNE
Y177 EQDLGIQYRALKPEV
R178 QDLGIQYRALKPEVD
K181 GIQYRALKPEVDKLN
K186 ALKPEVDKLNIMAAK
K193 KLNIMAAKRQQELKD
K193 KLNIMAAKRQQELKD
K216 AARGILQKNVPILYT
Y222 QKNVPILYTASQACL
T223 KNVPILYTASQACLQ
S225 VPILYTASQACLQHP
Y237 QHPDVAAYKANRDLI
Y245 KANRDLIYKQLQQAV
S268 ATASDDASQQQGGGG
Y282 GGGGELAYALNNFDK
S325 AALMADSSCTRDDRR
S363 NAGRKERSDALNSAI
T374 NSAIDKMTKKTRDLR
K416 AAKNGNEKEVKEYAQ
Y421 NEKEVKEYAQVFREH
K450 SNNEEGVKLVRMSAS
S457 KLVRMSASQLEALCP
K480 LAAKPQSKLAQENMD
T543 DVDGLDRTAGAIRGR
Y565 VTSEMDNYEPGVYTE
K573 EPGVYTEKVLEATKL
K579 EKVLEATKLLSNTVM
Y621 IDASRLVYDGIRDIR
T636 KAVLMIRTPEELDDs
S643-p TPEELDDsDFETEDF
T647 LDDsDFETEDFDVRs
S654-p TEDFDVRsRtsVQtE
T656-p DFDVRsRtsVQtEDD
S657-p FDVRsRtsVQtEDDQ
T660-p RsRtsVQtEDDQLIA
K683 AQLPQEQKAKIAEQV
K685 LPQEQKAKIAEQVAS
K697 VASFQEEKSKLDAEV
K699 SFQEEKSKLDAEVSK
K706 KLDAEVSKWDDSGND
K739 TRGKGPLKNTSDVIS
S746 KNTSDVISAAKKIAE
K749 SDVISAAKKIAEAGS
K760 EAGSRMDKLGRTIAD
K799 LNICSKVKAEVQNLG
Y839 VQTVKASYVASTKYQ
K847 VASTKYQKSQGMASL
K862 NLPAVSWKMKAPEKK
S888 QTKIKRASQKKHVNP
S900 VNPVQALSEFKAMDS
K903 VQALSEFKAMDSI__
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