CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015413
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase LRSAM1 
Protein Synonyms/Alias
 Leucine-rich repeat and sterile alpha motif-containing protein 1; Tsg101-associated ligase; hTAL 
Gene Name
 LRSAM1 
Gene Synonyms/Alias
 TAL; UNQ6496/PRO21356 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
491QLTQLELKRKSLDTEubiquitination[1, 2, 3, 4, 5, 6, 7]
493TQLELKRKSLDTESLubiquitination[2, 4]
520SLLQQLLKEKQQREEubiquitination[2, 3, 5]
522LQQLLKEKQQREEELubiquitination[4]
564NQKPLSLKLQEEGMEubiquitination[1, 6]
640ARIQPELKPPMGEVVubiquitination[5]
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] 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]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos. 
Sequence Annotation
 REPEAT 30 51 LRR 1.
 REPEAT 56 77 LRR 2.
 REPEAT 82 103 LRR 3.
 REPEAT 105 127 LRR 4.
 REPEAT 128 149 LRR 5.
 REPEAT 151 172 LRR 6.
 DOMAIN 569 632 SAM.
 ZN_FING 675 710 RING-type.
 MOTIF 649 652 PTAP motif 1.
 MOTIF 661 664 PTAP motif 2.
 MOD_RES 234 234 Phosphoserine.
 MOD_RES 604 604 Phosphoserine.  
Keyword
 Alternative splicing; Charcot-Marie-Tooth disease; Coiled coil; Complete proteome; Cytoplasm; Leucine-rich repeat; Ligase; Metal-binding; Neuropathy; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Transport; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 723 AA 
Protein Sequence
MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL 60
IVHTNHLTSL LPKSCSLLSL ATIKVLDLHD NQLTALPDDL GQLTALQVLN VERNQLMQLP 120
RSIGNLTQLQ TLNVKDNKLK ELPDTVGELR SLRTLNISGN EIQRLPQMLA HVRTLEMLSL 180
DASAMVYPPR EVCGAGTAAI LQFLCKESGL EYYPPSQYLL PILEQDGIEN SRDSPDGPTD 240
RFSREELEWQ NRFSDYEKRK EQKMLEKLEF ERRLELGQRE HTQLLQQSSS QKDEILQTVK 300
EEQSRLEQGL SEHQRHLNAE RQRLQEQLKQ TEQNISSRIQ KLLQDNQRQK KSSEILKSLE 360
NERIRMEQLM SITQEETESL RRRDVASAMQ QMLTESCKNR LIQMAYESQR QNLVQQACSS 420
MAEMDERFQQ ILSWQQMDQN KAISQILQES AMQKAAFEAL QVKKDLMHRQ IRSQIKLIET 480
ELLQLTQLEL KRKSLDTESL QEMISEQRWA LSSLLQQLLK EKQQREEELR EILTELEAKS 540
ETRQENYWLI QYQRLLNQKP LSLKLQEEGM ERQLVALLEE LSAEHYLPIF AHHRLSLDLL 600
SQMSPGDLAK VGVSEAGLQH EILRRVQELL DAARIQPELK PPMGEVVTPT APQEPPESVR 660
PSAPPAELEV QASECVVCLE REAQMIFLNC GHVCCCQQCC QPLRTCPLCR QDIAQRLRIY 720
HSS 723 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005576; C:extracellular region; IEA:InterPro.
 GO:0044425; C:membrane part; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045806; P:negative regulation of endocytosis; IMP:UniProtKB.
 GO:0046755; P:non-lytic virus budding; IMP:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
 GO:0030163; P:protein catabolic process; IMP:UniProtKB.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0070086; P:ubiquitin-dependent endocytosis; IDA:UniProtKB. 
Interpro
 IPR016179; Insulin-like.
 IPR001611; Leu-rich_rpt.
 IPR025875; Leu-rich_rpt_4.
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR011510; SAM_2.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12799; LRR_4
 PF07647; SAM_2 
SMART
 SM00078; IlGF
 SM00184; RING
 SM00454; SAM 
PROSITE
 PS51450; LRR
 PS50105; SAM_DOMAIN
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS