CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018569
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
315EKEINGSKVTCRGLLubiquitination[1]
341GEDLPHPKSMLQATAubiquitination[1]
391EEKHLEFKQLALDHFubiquitination[1]
399QLALDHFKKIKKMGGacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
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 (By similarity). 
Sequence Annotation
 NP_BIND 67 74 GTP (Potential).
 NP_BIND 142 146 GTP (Potential).
 MOD_RES 391 391 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 541 AA 
Protein Sequence
MLSPQRTAAV ASRGAGDAME NGKPGPVQVV LVHKEQHSFE LEERALASVL LQDHIRDLDV 60
VVVSVAGAFR KGKSFILDFM LRYLYSQKEG GHSDWLGDPE EPLTGFSWRG GSDPETTGIQ 120
IWSEVFTVKK PCGKKVAVVL MDTQGAFDSQ STVKDCATIF ALSTMTSSVQ IYNLSQNIQE 180
DDLQQLQLFT EYGRLAMDEI FQKPFQTLMF LIRDWSFPYE YNYGLQGGMA FLDKRLHVKE 240
HQHEEIQNVR NHIHSCFSDV TCFLLPHPGL QVATSPNFDG KLKDIASEFK EQLQALIPYV 300
LNPSKLMEKE INGSKVTCRG LLEYFKAYIK IYQGEDLPHP KSMLQATAEA NNLAAAASAK 360
DIYYNNMEEI CGGEKPYLSP DILEEKHLEF KQLALDHFKK IKKMGGKDFS FRYQQELEEE 420
IKELYENFCK HNGSKNVFST FRTPAVLFTG IAALYIASGF TGFIGLEVVA QLFNCMVGLL 480
LIALLTWGYI RYSGQYRELG GAIDSGAAYV LEQASSHIGN STQAAVRDAV VGRPPADKKS 540
Q 541 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; ISS:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0042802; F:identical protein binding; ISS:UniProtKB.
 GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
 GO:0007030; P:Golgi organization; ISS:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0051260; P:protein homooligomerization; ISS:UniProtKB. 
Interpro
 IPR003191; Guanylate-bd_C.
 IPR015894; Guanylate-bd_N.
 IPR027417; P-loop_NTPase. 
Pfam
 PF02263; GBP
 PF02841; GBP_C 
SMART
  
PROSITE
  
PRINTS