CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001438
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-actinin-3 
Protein Synonyms/Alias
 Alpha-actinin skeletal muscle isoform 3; F-actin cross-linking protein 
Gene Name
 Actn3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
108HKIANVNKALDFIASubiquitination[1]
211IDYAKLRKDDPIGNLubiquitination[1]
277TAANRICKVLAVNQEubiquitination[1]
287AVNQENEKLMEEYEKubiquitination[1]
411RLQHLAEKFQQKASLubiquitination[1]
415LAEKFQQKASLHEAWubiquitination[1]
426HEAWTRGKEEMLNQHubiquitination[1]
616SSQDINNKWDTVRKLubiquitination[1]
622NKWDTVRKLVPSRDQubiquitination[1]
754QVLTRDAKGLSQEQLubiquitination[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
Functional Description
 F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). 
Sequence Annotation
 DOMAIN 1 260 Actin-binding.
 DOMAIN 44 148 CH 1.
 DOMAIN 157 260 CH 2.
 REPEAT 287 397 Spectrin 1.
 REPEAT 407 512 Spectrin 2.
 REPEAT 522 633 Spectrin 3.
 REPEAT 643 746 Spectrin 4.
 DOMAIN 759 794 EF-hand 1.
 DOMAIN 795 830 EF-hand 2.  
Keyword
 Actin-binding; Calcium; Complete proteome; Metal-binding; 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 SLVFDNKHTV 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:0005865; C:striated muscle thin filament; TAS:MGI.
 GO:0030018; C:Z disc; IDA:MGI.
 GO:0051015; F:actin filament binding; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030674; F:protein binding, bridging; TAS:MGI.
 GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
 GO:0051764; P:actin crosslink formation; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
 GO:0006936; P:muscle contraction; IDA:MGI. 
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