CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018335
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ataxin-2-like protein 
Protein Synonyms/Alias
 Ataxin-2 domain protein; Ataxin-2-related protein 
Gene Name
 ATXN2L 
Gene Synonyms/Alias
 A2D; A2LG; A2LP; A2RP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
106ARGQSTGKGPPQSPVubiquitination[1]
138VGSTCDVKVKNGTTYubiquitination[1]
140STCDVKVKNGTTYEGubiquitination[1]
150TTYEGIFKTLSSKFEubiquitination[1]
155IFKTLSSKFELAVDAubiquitination[1]
205VDFNYATKDKFTDSAubiquitination[1, 2]
207FNYATKDKFTDSAIAubiquitination[1, 3, 4]
218SAIAMNSKVNGEHKEubiquitination[1]
267NEENYGVKTTYDSSLubiquitination[2]
283SYTVPLEKDNSEEFRubiquitination[1]
348SLASREGKYIPLPQRacetylation[5]
348SLASREGKYIPLPQRubiquitination[1]
507SLAPTDVKELSTKEPubiquitination[3, 4]
529ELARIAGKVPGLQNEubiquitination[2]
553RKFGAQFKLQPSSSPubiquitination[1]
573PFPPRILKEEPKGKEubiquitination[1]
Reference
 [1] 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]
 [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] 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
Functional Description
  
Sequence Annotation
 REGION 98 121 Interaction with MPL.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 103 103 Phosphoserine.
 MOD_RES 111 111 Phosphoserine.
 MOD_RES 118 118 Phosphotyrosine.
 MOD_RES 238 238 Phosphoserine.
 MOD_RES 264 264 Phosphotyrosine.
 MOD_RES 309 309 Phosphotyrosine.
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 349 349 Phosphotyrosine.
 MOD_RES 409 409 Phosphoserine.
 MOD_RES 449 449 Phosphoserine.
 MOD_RES 493 493 Phosphoserine.
 MOD_RES 496 496 Phosphoserine.
 MOD_RES 558 558 Phosphoserine.
 MOD_RES 559 559 Phosphoserine.
 MOD_RES 594 594 Phosphoserine.
 MOD_RES 634 634 Phosphoserine.
 MOD_RES 684 684 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1075 AA 
Protein Sequence
MLKPQPLQQP SQPQQPPPTQ QAVARRPPGG TSPPNGGLPG PLATSAAPPG PPAAASPCLG 60
PVAAAGSGLR RGAEGILAPQ PPPPQQHQER PGAAAIGSAR GQSTGKGPPQ SPVFEGVYNN 120
SRMLHFLTAV VGSTCDVKVK NGTTYEGIFK TLSSKFELAV DAVHRKASEP AGGPRREDIV 180
DTMVFKPSDV MLVHFRNVDF NYATKDKFTD SAIAMNSKVN GEHKEKVLQR WEGGDSNSDD 240
YDLESDMSNG WDPNEMFKFN EENYGVKTTY DSSLSSYTVP LEKDNSEEFR QRELRAAQLA 300
REIESSPQYR LRIAMENDDG RTEEEKHSAV QRQGSGRESP SLASREGKYI PLPQRVREGP 360
RGGVRCSSSR GGRPGLSSLP PRGPHHLDNS SPGPGSEARG INGGPSRMSP KAQRPLRGAK 420
TLSSPSNRPS GETSVPPPPA VGRMYPPRSP KSAAPAPISA SCPEPPIGSA VPTSSASIPV 480
TSSVSDPGVG SISPASPKIS LAPTDVKELS TKEPGRTLEP QELARIAGKV PGLQNEQKRF 540
QLEELRKFGA QFKLQPSSSP ENSLDPFPPR ILKEEPKGKE KEVDGLLTSE PMGSPVSSKT 600
ESVSDKEDKP PLAPSGGTEG PEQPPPPCPS QTGSPPVGLI KGEDKDEGPV AEQVKKSTLN 660
PNAKEFNPTK PLLSVNKSTS TPTSPGPRTH STPSIPVLTA GQSGLYSPQY ISYIPQIHMG 720
PAVQAPQMYP YPVSNSVPGQ QGKYRGAKGS LPPQRSDQHQ PASAPPMMQA AAAAGPPLVA 780
ATPYSSYIPY NPQQFPGQPA MMQPMAHYPS QPVFAPMLQS NPRMLTSGSH PQAIVSSSTP 840
QYPSAEQPTP QALYATVHQS YPHHATQLHA HQPQPATTPT GSQPQSQHAA PSPVQHQAGQ 900
APHLGSGQPQ QNLYHPGALT GTPPSLPPGP SAQSPQSSFP QPAAVYAIHH QQLPHGFTNM 960
AHVTQAHVQT GITAAPPPHP GAPHPPQVML LHPPQSHGGP PQGAVPQSGV PALSASTPSP 1020
YPYIGHPQGE QPGQAPGFPG GADDRIREFS LAGGIWHGRA EGLQVGQDAR VLGGE 1075 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:MGI.
 GO:0016607; C:nuclear speck; IDA:UniProtKB.
 GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IDA:UniProtKB.
 GO:0034063; P:stress granule assembly; IMP:UniProtKB. 
Interpro
 IPR009818; Ataxin-2_C.
 IPR009604; LsmAD_domain.
 IPR025852; SM_dom_ATX. 
Pfam
 PF06741; LsmAD
 PF07145; PAM2
 PF14438; SM-ATX 
SMART
  
PROSITE
  
PRINTS