CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001054
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Band 4.1-like protein 2 
Protein Synonyms/Alias
 Generally expressed protein 4.1; 4.1G 
Gene Name
 Epb41l2 
Gene Synonyms/Alias
 Epb4.1l2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
196EVQTSELKAEVASQKubiquitination[1]
229EYSCDLEKRAKGQVLacetylation[2]
263FQDHPEQKNWLDPAKubiquitination[1]
367HTKELEEKVSELHKTubiquitination[1]
392SQFLENAKRLSMYGVubiquitination[1]
405GVDLHHAKDSEGVDIubiquitination[1]
507KFLTLGSKFRYSGRTacetylation[2, 3]
507KFLTLGSKFRYSGRTubiquitination[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]
 [2] 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]
 [3] 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
  
Sequence Annotation
 DOMAIN 211 492 FERM.
 REGION 495 651 Hydrophilic.
 REGION 652 837 Spectrin--actin-binding.
 REGION 838 988 C-terminal (CTD).
 MOD_RES 2 2 N-acetylthreonine (By similarity).
 MOD_RES 38 38 Phosphoserine.
 MOD_RES 86 86 Phosphoserine.
 MOD_RES 379 379 Phosphoserine (By similarity).
 MOD_RES 492 492 Phosphoserine (By similarity).
 MOD_RES 543 543 Phosphoserine (By similarity).
 MOD_RES 582 582 Phosphoserine.
 MOD_RES 606 606 Phosphotyrosine.
 MOD_RES 610 610 Phosphoserine.
 MOD_RES 630 630 Phosphoserine.
 MOD_RES 698 698 Phosphoserine.
 MOD_RES 745 745 Phosphothreonine.  
Keyword
 Acetylation; Actin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 988 AA 
Protein Sequence
MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP PVERQSTPRL 60
RKRGKDPSEN RGISRFIPPW LKKQRSYNLV VAKDGGDKKE PTQADVEDQI LGKEESLPEE 120
ESRAKGDAEE MAQRKHLEVQ VEVREAKPAL KSSVETQPAE EVRKDKEETI QDTQEEKLEG 180
GAAKRETKEV QTSELKAEVA SQKATKKTKT VLAKVTLLDG TEYSCDLEKR AKGQVLFDRV 240
CEHLNLLEKD YFGLLFQDHP EQKNWLDPAK EIKRQLKNLP WLFTFNVKFY PPDPSQLTED 300
ITRYFLCLQL RQDIASGRLP CSFVTHALLG SYTLQAEHGD YDPEEYDSID LGDFQFAPAH 360
TKELEEKVSE LHKTHRGLSP AQADSQFLEN AKRLSMYGVD LHHAKDSEGV DIKLGVCANG 420
LLIYKDRLRI NRFAWPKILK ISYKRSNFYI KVRPAELEQF ESTIGFKLPN HRAAKRLWKV 480
CVEHHTFYRL VSPEQPPKTK FLTLGSKFRY SGRTQAQTRE ASTLIDRPAP QFERASSKRV 540
SRSLDGAPIG VVDQSPPGEG SVPGPGVISY TTIQDGRRDS KSPTKATPLP AEGKKNTLRV 600
DGDNIYVRHS NLMLEDLDKA QEAILKHQAS ISELKRNFMA STPEPRPSEW EKRRVTPLPF 660
QPQASSHETL NVVEEKKRAE VGKDESVITE EMNGKEMSPG HGPGETRKVE PVAHKDSTSL 720
SSESSSSSSE SEEDVGEYQP HHRVTEGTIR EEQEECDEEL EEEPGQGAKV VEREAAVPDA 780
VPDRQAGASV LPVETEAQEH VVAQKLPGEK GAHGGTAEQD PREEAEEDPH RVNGEVPHLD 840
LDGLPEIICC SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG 900
DSGVLLTAQT ITSESASTTT TTHITKTVKG GISETRIEKR IVITGDAALD HDQALAQAIR 960
EAREQHPDMS VTRVVVHKET ELAEEGEE 988 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; ISS:MGI.
 GO:0030054; C:cell junction; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0008180; C:signalosome; IEA:Compara.
 GO:0003779; F:actin binding; ISS:MGI.
 GO:0042731; F:PH domain binding; IDA:MGI.
 GO:0030507; F:spectrin binding; IDA:MGI.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0030036; P:actin cytoskeleton organization; ISS:MGI.
 GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
 GO:0008360; P:regulation of cell shape; ISS:MGI. 
Interpro
 IPR008379; Band_4.1_C.
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 IPR021187; Band_41_protein.
 IPR000798; Ez/rad/moesin_like.
 IPR014847; FERM-adjacent.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR019747; FERM_CS.
 IPR000299; FERM_domain.
 IPR018979; FERM_N.
 IPR018980; FERM_PH-like_C.
 IPR011993; PH_like_dom.
 IPR007477; SAB_dom. 
Pfam
 PF05902; 4_1_CTD
 PF08736; FA
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N
 PF04382; SAB 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.