CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023547
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Band 4.1-like protein 3 
Protein Synonyms/Alias
 4.1B; Differentially expressed in adenocarcinoma of the lung protein 1; DAL-1; DAL1P; mDAL-1; Band 4.1-like protein 3, N-terminally processed 
Gene Name
 Epb41l3 
Gene Synonyms/Alias
 Dal1; Epb4.1l3; Kiaa0987 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
94YQQFEDDKLSQRSSSubiquitination[1]
136EYGCDVDKRSRGQVLubiquitination[1]
146RGQVLFDKVCEHLNLacetylation[2]
146RGQVLFDKVCEHLNLubiquitination[1]
156EHLNLLEKDYFGLTYubiquitination[1]
170YRDAENQKNWLDPAKubiquitination[1, 3]
269RFAPNHTKELEDKVIubiquitination[1]
274HTKELEDKVIELHKSacetylation[4]
274HTKELEDKVIELHKSubiquitination[1, 3]
405LLPEAPPKKFLTLGSubiquitination[1]
498ITTVTPEKKAEEERVubiquitination[1]
578QTNISELKRTFLETSubiquitination[1]
630TKQSSGEKLMDGSEIubiquitination[1]
646SLLESARKPTEFIGGubiquitination[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] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [4] 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
Functional Description
 Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N- methyltransferases, including PRMT3 and PRMT5 (By similarity). 
Sequence Annotation
 DOMAIN 118 399 FERM.
 REGION 402 528 Hydrophilic.
 REGION 559 602 Spectrin--actin-binding.
 REGION 777 929 C-terminal (CTD).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 2 2 N-acetylthreonine; in Band 4.1-like
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 428 428 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 470 470 Phosphoserine.
 MOD_RES 486 486 Phosphoserine.
 MOD_RES 488 488 Phosphothreonine.
 MOD_RES 495 495 Phosphothreonine.
 MOD_RES 542 542 Phosphothreonine.
 MOD_RES 543 543 Phosphoserine.
 MOD_RES 547 547 Phosphoserine.
 MOD_RES 599 599 Phosphoserine.
 MOD_RES 623 623 Phosphothreonine.
 MOD_RES 626 626 Phosphoserine.
 MOD_RES 627 627 Phosphoserine.
 MOD_RES 797 797 Phosphoserine.
 MOD_RES 798 798 Phosphothreonine.
 MOD_RES 804 804 Phosphoserine.
 MOD_RES 923 923 Phosphothreonine.  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Apoptosis; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 929 AA 
Protein Sequence
MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA 60
AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC 120
KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK 180
KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT 240
VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK 300
LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR 360
PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT 420
QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA 480
TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG 540
ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST 600
SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEILSL LESARKPTEF IGGVSSTTQS 660
WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD 720
AAESTPTDRR HTGKGKEGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE 780
GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL 840
EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK 900
EAKEQHPDMS VTKVVVHKET EITPEDGED 929 
Gene Ontology
 GO:0005911; C:cell-cell junction; ISS:HGNC.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
 GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL.
 GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
 GO:0030865; P:cortical cytoskeleton organization; TAS:BHF-UCL.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; TAS:BHF-UCL.
 GO:0043217; P:myelin maintenance; IMP:BHF-UCL.
 GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
 GO:0030913; P:paranodal junction assembly; IMP:BHF-UCL.
 GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:BHF-UCL.
 GO:0002175; P:protein localization to paranode region of axon; IMP:BHF-UCL.
 GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
 GO:0008360; P:regulation of cell shape; IMP:BHF-UCL. 
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.