CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-027597
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Actinin alpha 3, isoform CRA_a 
Protein Synonyms/Alias
 Protein Actn3; Skeletal muscle-specific alpha-actinin 3 
Gene Name
 Actn3 
Gene Synonyms/Alias
 rCG_48289 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
108HKIANVNKALDFIASacetylation[1]
208PDLIDYAKLRKDDPIacetylation[1]
211IDYAKLRKDDPIGNLacetylation[1]
227TAFEVAEKYLDIPKMacetylation[1]
245EDIVNTPKPDEKAIMacetylation[1]
287AVNQENEKLMEEYEKacetylation[1]
372AFMPSEGKLVSDIANacetylation[1]
411RLQHLAEKFQQKASLacetylation[1]
415LAEKFQQKASLHEAWacetylation[1]
426HEAWTRGKEEMLNQHacetylation[1]
505NLGTLTQKRRDALERacetylation[1]
590GIQGEIQKICQTYGLacetylation[1]
662IGPWIQGKVEEVGRLacetylation[1]
717EGLVFDNKHTVYSMEacetylation[1]
754QVLTRDAKGLSQEQLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
  
Keyword
 Actin-binding; Calcium; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 900 AA 
Protein Sequence
MMMVMQPEGL GAGEGPFSGG GGGEYMEQEE DWDRDLLLDP AWEKQQRKTF TAWCNSHLRK 60
AGTQIENIEE DFRNGLKLML LLEVISGERL PRPDKGKMRF HKIANVNKAL DFIASKGVKL 120
VSIGAEEIVD GNLKMTLGMI WTIILRFAIQ DISVEETSAK EGLLLWCQRK TAPYRNVNVQ 180
NFHTSWKDGL ALCALIHRHR PDLIDYAKLR KDDPIGNLNT AFEVAEKYLD IPKMLDAEDI 240
VNTPKPDEKA IMTYVSCFYH AFAGAEQAET AANRICKVLA VNQENEKLME EYEKLASELL 300
EWIRRTVPWL ENRVGEPSMS AMQRKLEDFR DYRRLHKPPR VQEKCQLEIN FNTLQTKLRL 360
SHRPAFMPSE GKLVSDIANA WRGLEQVEKG YEDWLLSEIR RLQRLQHLAE KFQQKASLHE 420
AWTRGKEEML NQHDYESASL QEVRALLRRH EAFESDLAAH QDRVEHIAAL AQELNELDYH 480
EAASVNSRCQ AICDQWDNLG TLTQKRRDAL ERMEKLLETI DQLQLEFARR AAPFNNWLDG 540
AIEDLQDVWL VHSVEETQSL LTAHEQFKAT LPEADRERGA ILGIQGEIQK ICQTYGLRPK 600
SGNPYITLSS QDINNKWDTV RKLVPSRDQT LQEELARQQV NERLRRQFAA QANAIGPWIQ 660
GKVEEVGRLA AGLAGSLEEQ MAGLRQQEQN IINYKSNIDR LEGDHQLLQE GLVFDNKHTV 720
YSMEHIRVGW EQLLTSIART INEVENQVLT RDAKGLSQEQ LNEFRASFNH FDRKRNGMME 780
PDDFRACLIS MGYDLGEVEF ARIMTMVDPN AAGVVTFQAF IDFMTRETAE TDTAEQVVAS 840
FKILAGDKNY ITPEELRREL PAEQAEYCIR RMAPYKGSGA PSGALDYVAF SSALYGESDL 900 
Gene Ontology
 GO:0030018; C:Z disc; IEA:Compara.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0051764; P:actin crosslink formation; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
 GO:0006936; P:muscle contraction; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR026921; Alpha-actinin.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR014837; EF-hand_Ca_insen.
 IPR002048; EF_hand_dom.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF08726; efhand_Ca_insen
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS50222; EF_HAND_2 
PRINTS