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Overview

Uniprot IDP35221
Protein NameCatenin alpha-1
Gene NameCTNNA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
120 DDPCSSVKRGNMVRA
493 LFKEQWEKQVRVLTD
683 LPQEQKAKIAEQVAS
695 VASFQEEKSKLDAEV
747 SDVISAAKKIAEAGS
842 ASYVASTKYQKSQGM
889 IKRASQKKHVNPVQA

Function

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 (PubMed:40983751). 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. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May play a crucial role in cell differentiation

Protein Sequence

10 MTAVHAGNIN 20 FKWDPKSLEI 30 RTLAVERLLE 40 PLVTQVTTLV 50 NTNSKGPSNK 60 KRGRSKKAHV 70 LAASVEQATE 80 NFLEKGDKIA 90 KESQFLKEEL 100 VAAVEDVRKQ 110 GDLMKAAAGE 120 FADDPCSSVK 130 RGNMVRAARA 140 LLSAVTRLLI 150 LADMADVYKL 160 LVQLKVVEDG 170 ILKLRNAGNE 180 QDLGIQYKAL 190 KPEVDKLNIM 200 AAKRQQELKD 210 VGHRDQMAAA 220 RGILQKNVPI 230 LYTASQACLQ 240 HPDVAAYKAN 250 RDLIYKQLQQ 260 AVTGISNAAQ 270 ATASDDASQH 280 QGGGGGELAY 290 ALNNFDKQII 300 VDPLSFSEER 310 FRPSLEERLE 320 SIISGAALMA 330 DSSCTRDDRR 340 ERIVAECNAV 350 RQALQDLLSE 360 YMGNAGRKER 370 SDALNSAIDK 380 MTKKTRDLRR 390 QLRKAVMDHV 400 SDSFLETNVP 410 LLVLIEAAKN 420 GNEKEVKEYA 430 QVFREHANKL 440 IEVANLACSI 450 SNNEEGVKLV 460 RMSASQLEAL 470 CPQVINAALA 480 LAAKPQSKLA 490 QENMDLFKEQ 500 WEKQVRVLTD 510 AVDDITSIDD 520 FLAVSENHIL 530 EDVNKCVIAL 540 QEKDVDGLDR 550 TAGAIRGRAA 560 RVIHVVTSEM 570 DNYEPGVYTE 580 KVLEATKLLS 590 NTVMPRFTEQ 600 VEAAVEALSS 610 DPAQPMDENE 620 FIDASRLVYD 630 GIRDIRKAVL 640 MIRTPEELDD 650 SDFETEDFDV 660 RSRTSVQTED 670 DQLIAGQSAR 680 AIMAQLPQEQ 690 KAKIAEQVAS 700 FQEEKSKLDA 710 EVSKWDDSGN 720 DIIVLAKQMC 730 MIMMEMTDFT 740 RGKGPLKNTS 750 DVISAAKKIA 760 EAGSRMDKLG 770 RTIADHCPDS 780 ACKQDLLAYL 790 QRIALYCHQL 800 NICSKVKAEV 810 QNLGGELVVS 820 GVDSAMSLIQ 830 AAKNLMNAVV 840 QTVKASYVAS 850 TKYQKSQGMA 860 SLNLPAVSWK 870 MKAPEKKPLV 880 KREKQDETQT 890 KIKRASQKKH 900 VNPVQALSEF KAMDSI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0001669 acrosomal vesicle
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005912 adherens junction
Cellular Component GO:0016342 catenin complex
Cellular Component GO:0030054 cell junction
Cellular Component GO:0005911 cell-cell junction
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016600 flotillin complex
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0014704 intercalated disc
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0005915 zonula adherens
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0008013 beta-catenin binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0045295 gamma-catenin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0005198 structural molecule activity
Molecular Function GO:0017166 vinculin binding
Biological Process GO:0043297 apical junction assembly
Biological Process GO:0031103 axon regeneration
Biological Process GO:0007155 cell adhesion
Biological Process GO:0016477 cell migration
Biological Process GO:0098609 cell-cell adhesion
Biological Process GO:0071681 cellular response to indole-3-methanol
Biological Process GO:0016264 gap junction assembly
Biological Process GO:0008584 male gonad development
Biological Process GO:1900181 negative regulation of protein localization to nucleus
Biological Process GO:0042475 odontogenesis of dentin-containing tooth
Biological Process GO:0001541 ovarian follicle development
Biological Process GO:0043627 response to estrogen

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.