CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021672
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Band 4.1-like protein 5 
Protein Synonyms/Alias
  
Gene Name
 EPB41L5 
Gene Synonyms/Alias
 KIAA1548 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40IPAAGDSKSIITCRVubiquitination[1]
350SRFRYSGKTEYQTTKubiquitination[2]
503EVEYETLKDTSEKLKubiquitination[2, 3]
508TLKDTSEKLKQLEMEubiquitination[1, 2, 3, 4, 5]
510KDTSEKLKQLEMENSubiquitination[1, 2, 3, 4, 5, 6]
542EVVKLTEKCLNNVIEubiquitination[2]
563MRVPPDFKSNILKAQubiquitination[1]
579EAVHKVTKEDSLLSHubiquitination[2, 3]
587EDSLLSHKNANVQDAubiquitination[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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] 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]
 [6] 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] 
Functional Description
 May contribute to the correct positioning of tight junctions during the establishment of polarity in epithelial cells. 
Sequence Annotation
 DOMAIN 43 327 FERM.
 MOD_RES 436 436 Phosphoserine.  
Keyword
 Alternative splicing; Cell junction; Complete proteome; Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 733 AA 
Protein Sequence
MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP 60
KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV 120
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLDCPFDTAV QLAAYNLQAE LGDYDLAEHS 180
PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR 240
DGNDYSLGLT PTGVLVFEGD TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV 300
FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK 360
ARRSTSFERR PSKRYSRRTL QMKACATKPE ELSVHNNVST QSNGSQQAWG MRSALPVSPS 420
ISSAPVPVEI ENLPQSPGTD QHDRKCIPLN IDLLNSPDLL EATIGDVIGA SDTMETSQAL 480
NDVNVATRLP GLGEPEVEYE TLKDTSEKLK QLEMENSPLL SPRSNIDVNI NSQEEVVKLT 540
EKCLNNVIES PGLNVMRVPP DFKSNILKAQ VEAVHKVTKE DSLLSHKNAN VQDAATNSAV 600
LNENNVPLPK ESLETLMLIT PADSGSVLKE ATDELDALLA SLTENLIDHT VAPQVSSTSM 660
ITPRWIVPQS GAMSNGLAGC EMLLTGKEGH GNKDGISLIS PPAPFLVDAV TSSGPILAEE 720
AVLKQKCLLT TEL 733 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:InterPro.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0031032; P:actomyosin structure organization; IEA:Compara.
 GO:0003383; P:apical constriction; IEA:Compara.
 GO:0048319; P:axial mesoderm morphogenesis; IEA:Compara.
 GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Compara.
 GO:0007398; P:ectoderm development; IEA:Compara.
 GO:0048617; P:embryonic foregut morphogenesis; IEA:Compara.
 GO:0007492; P:endoderm development; IEA:Compara.
 GO:0001837; P:epithelial to mesenchymal transition; IEA:Compara.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0070986; P:left/right axis specification; IEA:Compara.
 GO:0007509; P:mesoderm migration involved in gastrulation; IEA:Compara.
 GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Compara.
 GO:0032091; P:negative regulation of protein binding; IEA:Compara.
 GO:0001839; P:neural plate morphogenesis; IEA:Compara.
 GO:0048339; P:paraxial mesoderm development; IEA:Compara.
 GO:0010634; P:positive regulation of epithelial cell migration; IEA:Compara.
 GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Compara.
 GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Compara.
 GO:0032092; P:positive regulation of protein binding; IEA:Compara.
 GO:0010608; P:posttranscriptional regulation of gene expression; IEA:Compara.
 GO:0070201; P:regulation of establishment of protein localization; IEA:Compara.
 GO:0032525; P:somite rostral/caudal axis specification; IEA:Compara.
 GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; IEA:Compara.
 GO:0009826; P:unidimensional cell growth; IEA:Compara. 
Interpro
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 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. 
Pfam
 PF08736; FA
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.