CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021749
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
239EDIVNTPKPDERAIMubiquitination[1]
271TAANRICKVLAVNQEubiquitination[1]
311LENRTPEKTMQAMQKubiquitination[1]
405RLEHLAEKFRQKASTubiquitination[1]
409LAEKFRQKASTHETWubiquitination[1]
420HETWAYGKEQILLQKubiquitination[1]
427KEQILLQKDYESASLubiquitination[1]
748QILTRDAKGITQEQMubiquitination[1]
842FRILASDKPYILAEEubiquitination[1]
864DQAQYCIKRMPPYSGubiquitination[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 1 254 Actin-binding.
 DOMAIN 38 142 CH 1.
 DOMAIN 151 254 CH 2.
 REPEAT 281 391 Spectrin 1.
 REPEAT 401 506 Spectrin 2.
 REPEAT 516 627 Spectrin 3.
 REPEAT 637 740 Spectrin 4.
 DOMAIN 753 788 EF-hand 1.
 DOMAIN 789 824 EF-hand 2.
 MOD_RES 237 237 Phosphothreonine.  
Keyword
 Actin-binding; Calcium; Complete proteome; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 894 AA 
Protein Sequence
MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE 60
NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDYIASK GVKLVSIGAE 120
EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW 180
KDGLGLCALI HRHRPDLIDY SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP 240
DERAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT 300
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF 360
MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE HLAEKFRQKA STHETWAYGK 420
EQILLQKDYE SASLTEVRAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN 480
DRCQKICDQW DRLGTLTQKR REALERTEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ 540
DMFIVHSIEE IQSLITAHEQ FKATLPEADG ERQSILAIQN EVEKVIQSYS IRISSSNPYS 600
TVTMDELRNK WDKVKQLVPV RDQSLQEELA RQHANERLRR QFAAQANAIG PWIQNKMEEI 660
ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ LIQEALVFDN KHTNYTMEHI 720
RVGWELLLTT IARTINEVET QILTRDAKGI TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA 780
CLISMGYDLG EAEFARIMTL VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS 840
DKPYILAEEL RRELPPDQAQ YCIKRMPPYS GPGSVPGALD YTAFSSALYG ESDL 894 
Gene Ontology
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0005865; C:striated muscle thin filament; TAS:MGI.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 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:0030375; F:thyroid hormone receptor coactivator activity; IDA:MGI.
 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; IEA:Compara.
 GO:0006936; P:muscle contraction; IDA:MGI.
 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
 PS50222; EF_HAND_2 
PRINTS