CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014886
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Atlastin-3 
Protein Synonyms/Alias
  
Gene Name
 ATL3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23DDAMESSKPGPVQVVubiquitination[1, 2]
239LDKRLQVKEHQHEEIubiquitination[1, 2, 3, 4]
283PDFDGKLKDIAGEFKubiquitination[1]
309NPSKLMEKEINGSKVubiquitination[2]
315EKEINGSKVTCRGLLubiquitination[2]
326RGLLEYFKAYIKIYQubiquitination[2]
330EYFKAYIKIYQGEDLubiquitination[2]
341GEDLPHPKSMLQATAubiquitination[1]
391EEKHCEFKQLALDHFacetylation[5]
391EEKHCEFKQLALDHFubiquitination[2, 6, 7, 8]
407KTKKMGGKDFSFRYQubiquitination[2, 7]
538VGRPSMDKKAQ****ubiquitination[2]
539GRPSMDKKAQ*****ubiquitination[2]
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] 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]
 [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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] 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]
 [7] 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]
 [8] 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] 
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 67 74 GTP (Potential).
 NP_BIND 142 146 GTP (Potential).
 MOD_RES 391 391 N6-acetyllysine.
 MOD_RES 535 535 Phosphoserine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 541 AA 
Protein Sequence
MLSPQRVAAA ASRGADDAME SSKPGPVQVV LVQKDQHSFE LDEKALASIL LQDHIRDLDV 60
VVVSVAGAFR KGKSFILDFM LRYLYSQKES GHSNWLGDPE EPLTGFSWRG GSDPETTGIQ 120
IWSEVFTVEK PGGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE 180
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LVRDWSFPYE YSYGLQGGMA FLDKRLQVKE 240
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPDFDG KLKDIAGEFK EQLQALIPYV 300
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK 360
DIYYNNMEEV CGGEKPYLSP DILEEKHCEF KQLALDHFKK TKKMGGKDFS FRYQQELEEE 420
IKELYENFCK HNGSKNVFST FRTPAVLFTG IVALYIASGL TGFIGLEVVA QLFNCMVGLL 480
LIALLTWGYI RYSGQYRELG GAIDFGAAYV LEQASSHIGN STQATVRDAV VGRPSMDKKA 540
Q 541 
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