CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009111
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-actinin-4 
Protein Synonyms/Alias
 F-actin cross-linking protein; Non-muscle alpha-actinin 4 
Gene Name
 Actn4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
126FIASKGVKLVSIGAEubiquitination[1]
215PELIEYDKLRKDDPVubiquitination[1]
218IEYDKLRKDDPVTNLubiquitination[1]
234NAFEVAEKYLDIPKMubiquitination[1]
256NTARPDEKAIMTYVSubiquitination[2]
332TIQEMQQKLEDFRDYubiquitination[1]
351KPPKVQEKCQLEINFubiquitination[1]
418RLDHLAEKFRQKASIubiquitination[1]
422LAEKFRQKASIHEAWubiquitination[1]
433HEAWTDGKEAMLKQRubiquitination[1]
451TATLSDIKALIRKHEubiquitination[1]
605IAESNHIKLSGSNPYacetylation[3]
605IAESNHIKLSGSNPYubiquitination[1]
623TPQIINSKWEKVQQLacetylation[3]
626IINSKWEKVQQLVPKacetylation[4, 5]
626IINSKWEKVQQLVPKsuccinylation[5]
633KVQQLVPKRDHALLEubiquitination[1]
761QILTRDAKGISQEQMubiquitination[1]
780ASFNHFDKDHGGALGacetylation[3, 4, 5]
860FKVLAGDKNFITAEEacetylation[5]
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]
 [2] Glomerular epithelial cell injury associated with mutant alpha-actinin-4.
 Cybulsky AV, Takano T, Papillon J, Bijian K, Guillemette J, Kennedy CR.
 Am J Physiol Renal Physiol. 2009 Oct;297(4):F987-95. [PMID: 19640905]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). 
Sequence Annotation
 DOMAIN 1 267 Actin-binding.
 DOMAIN 51 155 CH 1.
 DOMAIN 164 267 CH 2.
 REPEAT 294 404 Spectrin 1.
 REPEAT 414 519 Spectrin 2.
 REPEAT 529 640 Spectrin 3.
 REPEAT 650 753 Spectrin 4.
 DOMAIN 766 801 EF-hand 1.
 DOMAIN 807 842 EF-hand 2.
 REGION 178 193 Polyphosphoinositide (PIP2)-binding
 MOD_RES 115 115 N6-acetyllysine (By similarity).
 MOD_RES 593 593 N6-acetyllysine (By similarity).
 MOD_RES 626 626 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Actin-binding; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; Nucleus; Protein transport; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 912 AA 
Protein Sequence
MVDYHAANQA YQYGPNSGGG NGAGGGGSMG DYMAQEDDWD RDLLLDPAWE KQQRKTFTAW 60
CNSHLRKAGT QIENIDEDFR DGLKLMLLLE VISGERLPKP ERGKMRVHKI NNVNKALDFI 120
ASKGVKLVSI GAEEIVDGNA KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP 180
YKNVNVQNFH ISWKDGLAFN ALIHRHRPEL IEYDKLRKDD PVTNLNNAFE VAEKYLDIPK 240
MLDAEDIVNT ARPDEKAIMT YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEHLMEDYE 300
RLASDLLEWI RRTIPWLEDR VPQKTIQEMQ QKLEDFRDYR RVHKPPKVQE KCQLEINFNT 360
LQTKLRLSNR PAFMPSEGRM VSDINNGWQH LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR 420
QKASIHEAWT DGKEAMLKQR DYETATLSDI KALIRKHEAF ESDLAAHQDR VEQIAAIAQE 480
LNELDYYDSH NVNTRCQKIC DQWDNLGSLT HSRREALEKT EKQLETIDQL HLEYAKRAAP 540
FNNWMESAME DLQDMFIVHT IEEIEGLISA HDQFKSTLPD ADREREAILA IHKEAQRIAE 600
SNHIKLSGSN PYTTVTPQII NSKWEKVQQL VPKRDHALLE EQSKQQSNEH LRRQFASQAN 660
MVGPWIQTKM EEIGRISIEM NGTLEDQLSH LKQYERSIVD YKPSLDLLEQ QHQLIQEALI 720
FDNKHTNYTM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMQE FRASFNHFDK 780
DHGGALGPEE FKACLISLGY DVENDRQGDA EFNRIMSVVD PNHSGLVTFQ AFIDFMSRET 840
TDTDTADQVI ASFKVLAGDK NFITAEELRR ELPPDQAEYC IARMAPYQGP DAAPGALDYK 900
SFSTALYGES DL 912 
Gene Ontology
 GO:0030863; C:cortical cytoskeleton; IDA:MGI.
 GO:0070062; C:extracellular vesicular exosome; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0031143; C:pseudopodium; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0030018; C:Z disc; IDA:MGI.
 GO:0051015; F:actin filament binding; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0001882; F:nucleoside binding; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
 GO:0051764; P:actin crosslink formation; IEA:InterPro.
 GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
 GO:0051271; P:negative regulation of cellular component movement; IDA:UniProtKB.
 GO:0051272; P:positive regulation of cellular component movement; IDA:UniProtKB.
 GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara. 
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