CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004844
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-actinin-2 
Protein Synonyms/Alias
 Alpha-actinin skeletal muscle isoform 2; F-actin cross-linking protein 
Gene Name
 ACTN2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Gallus gallus (Chicken) 
NCBI Taxa ID
 9031 
Lysine Modification
Position
Peptide
Type
References
57WCNSHLRKAGTQIENubiquitination[1]
105HKIANVNKALDYIASubiquitination[1]
116YIASKGVKLVSIGAEubiquitination[1]
242EDIVNTPKPDERAIMubiquitination[1]
274TAANRICKVLAVNQEubiquitination[1]
314LENRTPEKTMQAMQKubiquitination[1]
322TMQAMQKKLEDFRDYubiquitination[1]
341KPPKVQEKCQLEINFubiquitination[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 1 257 Actin-binding.
 DOMAIN 41 145 CH 1.
 DOMAIN 154 257 CH 2.
 REPEAT 284 394 Spectrin 1.
 REPEAT 404 509 Spectrin 2.
 REPEAT 519 630 Spectrin 3.
 REPEAT 640 743 Spectrin 4.
 DOMAIN 756 791 EF-hand 1.
 DOMAIN 792 827 EF-hand 2.  
Keyword
 Actin-binding; Alternative splicing; Calcium; Complete proteome; Cytoplasm; Metal-binding; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 897 AA 
Protein Sequence
MNSMNQIETN MQYTYNYEED EYMTQEEEWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT 60
QIENIEEDFR NGLKLMLLLE VISGERLPKP DRGKMRFHKI ANVNKALDYI ASKGVKLVSI 120
GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YRNVNIQNFH 180
LSWKDGLGLC ALIHRHRPDL IDYSKLNKDD PIGNINLAME IAEKHLDIPK MLDAEDIVNT 240
PKPDERAIMT YVSCFYHAFA GAEQAETAAN RICKVLAVNQ ENERLMEEYE RLASELLEWI 300
RRTIPWLENR TPEKTMQAMQ KKLEDFRDYR RKHKPPKVQE KCQLEINFNT LQTKLRISNR 360
PAFMPSEGKM VSDIAGAWQR LEQAEKGYEE WLLNEIRRLE RLEHLAEKFR QKASTHEQWA 420
YGKEQILLQK DYESASLTEV RAMLRKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYHDAA 480
SVNDRCQKIC DQWDSLGTLT QKRREALERT EKLLETIDQL HLEFAKRAAP FNNWMEGAME 540
DLQDMFIVHS IEEIQSLISA HDQFKATLPE ADGERQAILS IQNEVEKVIQ SYSMRISASN 600
PYSTVTVEEI RTKWEKVKQL VPQRDQSLQE ELARQHANER LRRQFAAQAN VIGPWIQTKM 660
EEIARSSIEM TGPLEDQMNQ LKQYEQNIIN YKHNIDKLEG DHQLIQEALV FDNKHTNYTM 720
EHIRVGWELL LTTIARTINE VETQILTRDA KGITQEQMND FRASFNHFDR RKNGLMDHDD 780
FRACLISMGY DLGEAEFARI MSLVDPNGQG TVTFQSFIDF MTRETADTDT AEQVIASFRI 840
LASDKPYILA DELRRELPPE QAQYCIKRMP QYTGPGSVPG ALDYTSFSSA LYGESDL 897 
Gene Ontology
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0030018; C:Z disc; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030375; F:thyroid hormone receptor coactivator activity; IEA:Compara.
 GO:0051764; P:actin crosslink formation; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IEA:InterPro.
 GO:0048041; P:focal adhesion assembly; IEA:Compara.
 GO:0030035; P:microspike assembly; IDA:UniProtKB.
 GO:0006936; P:muscle contraction; IEA:Compara.
 GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IEA:Compara.
 GO:0043267; P:negative regulation of potassium ion transport; IEA:Compara.
 GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Compara.
 GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IEA:Compara.
 GO:0043268; P:positive regulation of potassium ion transport; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:Compara.
 GO:0042391; P:regulation of membrane potential; 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
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 
PRINTS