CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Atlastin-2 
Protein Synonyms/Alias
 ADP-ribosylation factor-like protein 6-interacting protein 2; ARL-6-interacting protein 2; Aip-2 
Gene Name
 ATL2 
Gene Synonyms/Alias
 ARL6IP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
265GGKQFLEKRLQVKQNubiquitination[1]
270LEKRLQVKQNQHEELubiquitination[1, 2]
314PSFDGRLKDIDEDFKacetylation[3]
314PSFDGRLKDIDEDFKubiquitination[1, 2]
321KDIDEDFKRELRNLVacetylation[3]
321KDIDEDFKRELRNLVubiquitination[1, 2]
340APENLVEKEISGSKVubiquitination[1]
346EKEISGSKVTCRDLVubiquitination[1]
361EYFKAYIKIYQGEELubiquitination[1, 2, 4, 5]
372GEELPHPKSMLQATAubiquitination[1, 2]
396GARDTYCKSMEQVCGubiquitination[1]
422ERKHLDLKEVAIKQFubiquitination[2]
427DLKEVAIKQFRSVKKubiquitination[1]
461ETYANFIKHNDGKNIubiquitination[2]
567QSVTNSIKAGLTDQVubiquitination[1, 4, 5, 6]
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] 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]
 [4] 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]
 [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] 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
 GTPase tethering membranes through formation of trans- homooligomer and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. 
Sequence Annotation
 NP_BIND 101 108 GTP (Potential).
 NP_BIND 173 177 GTP (Potential).
 MOD_RES 24 24 Phosphoserine.  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 583 AA 
Protein Sequence
MAEGDEAARG QQPHQGLWRR RRTSDPSAAV NHVSSTTSLG ENYEDDDLVN SDEVMKKPCP 60
VQIVLAHEDD HNFELDEEAL EQILLQEHIR DLNIVVVSVA GAFRKGKSFL LDFMLRYMYN 120
KDSQSWIGGN NEPLTGFTWR GGCERETTGI QVWNEVFVID RPNGTKVAVL LMDTQGAFDS 180
QSTIKDCATV FALSTMTSSV QVYNLSQNIQ EDDLQHLQLF TEYGRLAMEE IYQKPFQTLM 240
FLIRDWSYPY EHSYGLEGGK QFLEKRLQVK QNQHEELQNV RKHIHNCFSN LGCFLLPHPG 300
LKVATNPSFD GRLKDIDEDF KRELRNLVPL LLAPENLVEK EISGSKVTCR DLVEYFKAYI 360
KIYQGEELPH PKSMLQATAE ANNLAAVAGA RDTYCKSMEQ VCGGDKPYIA PSDLERKHLD 420
LKEVAIKQFR SVKKMGGDEF CRRYQDQLEA EIEETYANFI KHNDGKNIFY AARTPATLFA 480
VMFAMYIISG LTGFIGLNSI AVLCNLVMGL ALIFLCTWAY VKYSGEFREI GTVIDQIAET 540
LWEQVLKPLG DNLMEENIRQ SVTNSIKAGL TDQVSHHARL KTD 583 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; NAS:UniProtKB.
 GO:0042802; F:identical protein binding; IDA:UniProtKB.
 GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
 GO:0007030; P:Golgi organization; IMP:UniProtKB.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB. 
Interpro
 IPR003191; Guanylate-bd_C.
 IPR015894; Guanylate-bd_N.
 IPR027417; P-loop_NTPase. 
Pfam
 PF02263; GBP
 PF02841; GBP_C 
SMART
  
PROSITE
  
PRINTS