CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008330
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipopolysaccharide-responsive and beige-like anchor protein 
Protein Synonyms/Alias
 Beige-like protein; CDC4-like protein 
Gene Name
 LRBA 
Gene Synonyms/Alias
 BGL; CDC4L; LBA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
820IQNPQILKVIATLLRubiquitination[1]
1243SSEQKIAKLDVSNVAubiquitination[1]
1259DTERLELKASPNVEAubiquitination[1, 2]
1473TRGDKALKPMHSLIPubiquitination[3, 4]
1487PLGKSAAKSPVDIVTubiquitination[1]
1665RGNDLDTKATPSVSVubiquitination[1]
1776GSRSSNAKLPSVPTVubiquitination[1]
1806RLEHALEKAAPLLREubiquitination[1, 3, 4]
1889RLLSQTMKDHLVRVAubiquitination[3, 4]
2116DEEDPNFKKIDPKILacetylation[5]
2117EEDPNFKKIDPKILAacetylation[5]
2271TNFRDLSKPIGALNPubiquitination[1, 3, 4]
2279PIGALNPKRAAFFAEubiquitination[1]
2742EGPENCLKPKLIQASubiquitination[6]
2744PENCLKPKLIQASREubiquitination[6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] 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]
 [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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] 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
Functional Description
 May be involved in coupling signal transduction and vesicle trafficking to enable polarized secretion and/or membrane deposition of immune effector molecules (By similarity). 
Sequence Annotation
 REPEAT 1301 1343 WD 1.
 DOMAIN 2200 2489 BEACH.
 REPEAT 2591 2633 WD 2.
 REPEAT 2636 2679 WD 3.
 REPEAT 2695 2735 WD 4.
 REPEAT 2777 2816 WD 5.
 REPEAT 2819 2858 WD 6.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 904 904 Phosphotyrosine (By similarity).
 MOD_RES 979 979 Phosphoserine.
 MOD_RES 1005 1005 Phosphoserine (By similarity).
 MOD_RES 1100 1100 Phosphoserine.
 MOD_RES 1139 1139 Phosphoserine.
 MOD_RES 1488 1488 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell membrane; Coiled coil; Complete proteome; Disease mutation; Endoplasmic reticulum; Golgi apparatus; Lysosome; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2863 AA 
Protein Sequence
MASEDNRVPS PPPTGDDGGG GGREETPTEG GALSLKPGLP IRGIRMKFAV LTGLVEVGEV 60
SNRDIVETVF NLLVGGQFDL EMNFIIQEGE SINCMVDLLE KCDITCQAEV WSMFTAILKK 120
SIRNLQVCTE VGLVEKVLGK IEKVDNMIAD LLVDMLGVLA SYNLTVRELK LFFSKLQGDK 180
GRWPPHAGKL LSVLKHMPQK YGPDAFFNFP GKSAAAIALP PIAKWPYQNG FTFHTWLRMD 240
PVNNINVDKD KPYLYCFRTS KGLGYSAHFV GGCLIVTSIK SKGKGFQHCV KFDFKPQKWY 300
MVTIVHIYNR WKNSELRCYV NGELASYGEI TWFVNTSDTF DKCFLGSSET ADANRVFCGQ 360
MTAVYLFSEA LNAAQIFAIY QLGLGYKGTF KFKAESDLFL AEHHKLLLYD GKLSSAIAFT 420
YNPRATDAQL CLESSPKDNP SIFVHSPHAL MLQDVKAVLT HSIQSAMHSI GGVQVLFPLF 480
AQLDYRQYLS DEIDLTICST LLAFIMELLK NSIAMQEQML ACKGFLVIGY SLEKSSKSHV 540
SRAVLELCLA FSKYLSNLQN GMPLLKQLCD HVLLNPAIWI HTPAKVQLML YTYLSTEFIG 600
TVNIYNTIRR VGTVLLIMHT LKYYYWAVNP QDRSGITPKG LDGPRPNQKE MLSLRAFLLM 660
FIKQLVMKDS GVKEDELQAI LNYLLTMHED DNLMDVLQLL VALMSEHPNS MIPAFDQRNG 720
LRVIYKLLAS KSEGIRVQAL KAMGYFLKHL APKRKAEVML GHGLFSLLAE RLMLQTNLIT 780
MTTYNVLFEI LIEQIGTQVI HKQHPDPDSS VKIQNPQILK VIATLLRNSP QCPESMEVRR 840
AFLSDMIKLF NNSRENRRSL LQCSVWQEWM LSLCYFNPKN SDEQKITEMV YAIFRILLYH 900
AVKYEWGGWR VWVDTLSITH SKVTFEIHKE NLANIFREQQ GKVDEEIGLC SSTSVQAASG 960
IRRDINVSVG SQQPDTKDSP VCPHFTTNGN ENSSIEKTSS LESASNIELQ TTNTSYEEMK 1020
AEQENQELPD EGTLEETLTN ETRNADDLEV SSDIIEAVAI SSNSFITTGK DSMTVSEVTA 1080
SISSPSEEDA SEMPEFLDKS IVEEEEDDDY VELKVEGSPT EEANLPTELQ DNSLSPAASE 1140
AGEKLDMFGN DDKLIFQEGK PVTEKQTDTE TQDSKDSGIQ TMTASGSSAM SPETTVSQIA 1200
VESDLGQMLE EGKKATNLTR ETKLINDCHG SVSEASSEQK IAKLDVSNVA TDTERLELKA 1260
SPNVEAPQPH RHVLEISRQH EQPGQGIAPD AVNGQRRDSR STVFRIPEFN WSQMHQRLLT 1320
DLLFSIETDI QMWRSHSTKT VMDFVNSSDN VIFVHNTIHL ISQVMDNMVM ACGGILPLLS 1380
AATSATHELE NIEPTQGLSI EASVTFLQRL ISLVDVLIFA SSLGFTEIEA EKSMSSGGIL 1440
RQCLRLVCAV AVRNCLECQQ HSQLKTRGDK ALKPMHSLIP LGKSAAKSPV DIVTGGISPV 1500
RDLDRLLQDM DINRLRAVVF RDIEDSKQAQ FLALAVVYFI SVLMVSKYRD ILEPQNERHS 1560
QSCTETGSEN ENVSLSEITP AAFSTLTTAS VEESESTSSA RRRDSGIGEE TATGLGSHVE 1620
VTPHTAPPGV SAGPDAISEV LSTLSLEVNK SPETKNDRGN DLDTKATPSV SVSKNVNVKD 1680
ILRSLVNIPA DGVTVDPALL PPACLGALGD LSVEQPVQFR SFDRSVIVAA KKSAVSPSTF 1740
NTSIPTNAVS VVSSVDSAQA SDMGGESPGS RSSNAKLPSV PTVDSVSQDP VSNMSITERL 1800
EHALEKAAPL LREIFVDFAP FLSRTLLGSH GQELLIEGTS LVCMKSSSSV VELVMLLCSQ 1860
EWQNSIQKNA GLAFIELVNE GRLLSQTMKD HLVRVANEAE FILSRQRAED IHRHAEFESL 1920
CAQYSADKRE DEKMCDHLIR AAKYRDHVTA TQLIQKIINI LTDKHGAWGN SAVSRPLEFW 1980
RLDYWEDDLR RRRRFVRNPL GSTHPEATLK TAVEHVCIFK LRENSKATDE DILAKGKQSI 2040
RSQALGNQNS ENEILLEGDD DTLSSVDEKD LENLAGPVSL STPAQLVAPS VVVKGTLSVT 2100
SSELYFEVDE EDPNFKKIDP KILAYTEGLH GKWLFTEIRS IFSRRYLLQN TALEIFMANR 2160
VAVMFNFPDP ATVKKVVNYL PRVGVGTSFG LPQTRRISLA SPRQLFKASN MTQRWQHREI 2220
SNFEYLMFLN TIAGRSYNDL NQYPVFPWVI TNYESEELDL TLPTNFRDLS KPIGALNPKR 2280
AAFFAERYES WEDDQVPKFH YGTHYSTASF VLAWLLRIEP FTTYFLNLQG GKFDHADRTF 2340
SSISRAWRNS QRDTSDIKEL IPEFYYLPEM FVNFNNYNLG VMDDGTVVSD VELPPWAKTS 2400
EEFVHINRLA LESEFVSCQL HQWIDLIFGY KQQGPEAVRA LNVFYYLTYE GAVNLNSITD 2460
PVLREAVEAQ IRSFGQTPSQ LLIEPHPPRG SAMQVSPLMF TDKAQQDVIM VLKFPSNSPV 2520
THVAANTQPG LATPAVITVT ANRLFAVNKW HNLPAHQGAV QDQPYQLPVE IDPLIASNTG 2580
MHRRQITDLL DQSIQVHSQC FVITSDNRYI LVCGFWDKSF RVYSTDTGRL IQVVFGHWDV 2640
VTCLARSESY IGGNCYILSG SRDATLLLWY WNGKCSGIGD NPGSETAAPR AILTGHDYEV 2700
TCAAVCAELG LVLSGSQEGP CLIHSMNGDL LRTLEGPENC LKPKLIQASR EGHCVIFYEN 2760
GLFCTFSVNG KLQATMETDD NIRAIQLSRD GQYLLTGGDR GVVVVRQVSD LKQLFAYPGC 2820
DAGIRAMALS YDQRCIISGM ASGSIVLFYN DFNRWHHEYQ TRY 2863 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Compara.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 
Interpro
 IPR016024; ARM-type_fold.
 IPR000409; BEACH_dom.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR010508; DUF1088.
 IPR023362; PH-BEACH_dom.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF02138; Beach
 PF06469; DUF1088
 PF00400; WD40 
SMART
 SM01026; Beach
 SM00320; WD40 
PROSITE
 PS50197; BEACH
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS