CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-actinin-1 
Protein Synonyms/Alias
 Alpha-actinin cytoskeletal isoform; F-actin cross-linking protein; Non-muscle alpha-actinin-1 
Gene Name
 ACTN1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35AWEKQQRKTFTAWCNubiquitination[1, 2]
95HKISNVNKALDFIASacetylation[3]
162QRKTAPYKNVNIQNFubiquitination[2]
195PELIDYGKLRKDDPLacetylation[3]
195PELIDYGKLRKDDPLubiquitination[2]
198IDYGKLRKDDPLTNLubiquitination[2]
214TAFDVAEKYLDIPKMubiquitination[2]
220EKYLDIPKMLDAEDIubiquitination[2]
331KPPKVQEKCQLEINFubiquitination[2, 4]
398RLDHLAEKFRQKASIubiquitination[1, 2]
402LAEKFRQKASIHEAWubiquitination[2, 4]
633QHNERLRKQFGAQANubiquitination[1, 2]
676SHLRQYEKSIVNYKPacetylation[3]
676SHLRQYEKSIVNYKPubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] 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]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. 
Sequence Annotation
 DOMAIN 1 247 Actin-binding.
 DOMAIN 31 135 CH 1.
 DOMAIN 144 247 CH 2.
 REPEAT 274 384 Spectrin 1.
 REPEAT 394 499 Spectrin 2.
 REPEAT 509 620 Spectrin 3.
 REPEAT 630 733 Spectrin 4.
 DOMAIN 746 781 EF-hand 1.
 DOMAIN 787 822 EF-hand 2.
 REGION 274 733 Interaction with DDN.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 6 6 Phosphoserine.
 MOD_RES 12 12 Phosphotyrosine; by FAK1.
 MOD_RES 95 95 N6-acetyllysine.
 MOD_RES 195 195 N6-acetyllysine.
 MOD_RES 676 676 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 892 AA 
Protein Sequence
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR 60
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV 120
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC 180
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT 240
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR 300
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM 360
VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK 420
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC 480
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT 540
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI 600
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM 660
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL 720
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY 780
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK 840
NYITMDELRR ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL 892 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043197; C:dendritic spine; IEA:Compara.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005916; C:fascia adherens; IEA:Compara.
 GO:0005925; C:focal adhesion; IMP:UniProtKB.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
 GO:0031143; C:pseudopodium; TAS:UniProtKB.
 GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
 GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005178; F:integrin binding; IDA:UniProtKB.
 GO:0051764; P:actin crosslink formation; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IEA:Compara.
 GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
 GO:0051271; P:negative regulation of cellular component movement; IMP:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR026921; Alpha-actinin.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR014837; EF-hand_Ca_insen.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF13405; EF_hand_4
 PF08726; efhand_Ca_insen
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS