CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022170
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family F member 3 
Protein Synonyms/Alias
  
Gene Name
 ABCF3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
294ELAEIYAKLEEIEADubiquitination[1, 2]
319AGLGFTPKMQQQPTRubiquitination[3]
531VGENGAGKSTMLKLLubiquitination[3]
616ASLSGGQKSRVAFAQubiquitination[3]
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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] 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] 
Functional Description
 Displays an antiviral effect against flaviviruses such as west Nile virus (WNV) in the presence of OAS1B (By similarity). 
Sequence Annotation
 DOMAIN 178 424 ABC transporter 1.
 DOMAIN 492 707 ABC transporter 2.
 NP_BIND 210 217 ATP 1 (Potential).
 NP_BIND 525 532 ATP 2 (Potential).
 MOD_RES 283 283 Phosphoserine.  
Keyword
 Alternative splicing; Antiviral defense; ATP-binding; Complete proteome; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 709 AA 
Protein Sequence
MATCAEILRS EFPEIDGQVF DYVTGVLHSG SADFESVDDL VEAVGELLQE VSGDSKDDAG 60
IRAVCQRMYN TLRLAEPQSQ GNSQVLLDAP IQLSKITENY DCGTKLPGLL KREQSSTVNA 120
KKLEKAEARL KAKQEKRSEK DTLKTSNPLV LEEASASQAG SRKESRLESS GKNKSYDVRI 180
ENFDVSFGDR VLLAGADVNL AWGRRYGLVG RNGLGKTTLL KMLATRSLRV PAHISLLHVE 240
QEVAGDDTPA LQSVLESDSV REDLLRRERE LTAQIAAGRA EGSEAAELAE IYAKLEEIEA 300
DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV 360
RAILWLENYL QTWPSTILVV SHDRNFLNAI ATDIIHLHSQ RLDGYRGDFE TFIKSKQERL 420
LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVMKF 480
PDGFEKFSPP ILQLDEVDFY YDPKHVIFSR LSVSADLESR ICVVGENGAG KSTMLKLLLG 540
DLAPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGRPEEEY RHQLGRYGIS 600
GELAMRPLAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG RALNNFRGGV 660
ILVSHDERFI RLVCRELWVC EGGGVTRVEG GFDQYRALLQ EQFRREGFL 709 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS