CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023662
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; Band 4.1-like protein 3, N-terminally processed 
Gene Name
 EPB41L3 
Gene Synonyms/Alias
 DAL1; KIAA0987 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
75EFAARAAKQLEYQQLubiquitination[1]
138RGQVLFDKVCEHLNLubiquitination[2, 3]
162YRDAENQKNWLDPAKubiquitination[1]
266HTKELEDKVIELHKSubiquitination[1]
336INRFAWPKVLKISYKubiquitination[1, 2]
397LLPEAPPKKFLTLGSubiquitination[1]
398LPEAPPKKFLTLGSKubiquitination[1]
405KFLTLGSKFRYSGRTubiquitination[1, 2, 3, 4]
1027THITKTVKGGISETRubiquitination[2, 3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Tumor suppressor that inhibits cell proliferation and promotes apoptosis. Modulates the activity of protein arginine N- methyltransferases, including PRMT3 and PRMT5. 
Sequence Annotation
 DOMAIN 110 391 FERM.
 REGION 394 513 Hydrophilic.
 REGION 514 860 Spectrin--actin-binding (Potential).
 REGION 861 1083 C-terminal (CTD).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 2 2 N-acetylthreonine; in Band 4.1-like
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 420 420 Phosphoserine (By similarity).
 MOD_RES 443 443 Phosphoserine (By similarity).
 MOD_RES 460 460 Phosphoserine.
 MOD_RES 462 462 Phosphothreonine (By similarity).
 MOD_RES 469 469 Phosphothreonine.
 MOD_RES 703 703 Phosphothreonine (By similarity).
 MOD_RES 708 708 Phosphoserine (By similarity).
 MOD_RES 760 760 Phosphoserine (By similarity).
 MOD_RES 784 784 Phosphothreonine (By similarity).
 MOD_RES 787 787 Phosphoserine (By similarity).
 MOD_RES 788 788 Phosphoserine (By similarity).
 MOD_RES 962 962 Phosphoserine.
 MOD_RES 1081 1081 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Apoptosis; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1087 AA 
Protein Sequence
MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR 60
EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS 120
EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW 180
HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY 240
DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL 300
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE 360
STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS 420
ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE 480
EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP 540
GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL 600
DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL 660
ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE 720
LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV 780
PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT 840
VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG 900
AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS 960
VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT 1020
HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI 1080
TPEDGED 1087 
Gene Ontology
 GO:0005911; C:cell-cell junction; IDA: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; ISS:BHF-UCL.
 GO:0033270; C:paranode region of axon; ISS:BHF-UCL.
 GO:0005886; C:plasma membrane; NAS:UniProtKB.
 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; ISS:BHF-UCL.
 GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
 GO:0030913; P:paranodal junction assembly; ISS:BHF-UCL.
 GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
 GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL.
 GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
 GO:0008360; P:regulation of cell shape; ISS: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.