CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029028
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ABCB8 protein 
Protein Synonyms/Alias
 ATP-binding cassette sub-family B member 8, mitochondrial 
Gene Name
 ABCB8 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
230ITFFDANKTGQLVSRubiquitination[1, 2, 3, 4]
246TTDVQEFKSSFKLVIubiquitination[1, 3, 4]
448SGGCCVPKEQLRGSVubiquitination[3]
496VGQSGGGKTTVASLLubiquitination[1, 3]
556MENIRFGKLEASDEEubiquitination[1, 3, 4]
611AIARALIKQPTVLILubiquitination[1, 3, 4]
657THEELLKKGGLYAELubiquitination[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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 693 AA 
Protein Sequence
MLVHLFRVGI RGGPFPGRLL PPLRFQTFSA VRYSDGYRSS SLLRAVAHLR SQLWAHLPRA 60
PLAPRWSPSA WCWVGGALLG PMVLSKHPHL CLVALCEAEE APPASSTPHV VGSRFNWKLF 120
WQFLHPHLLV LGVAVVLALG AALVNVQIPL LLGQLVEVVA KYTRDHVGSF MTESQNLSTH 180
LLILYGVQGL LTFGYLVLLS HVGERMAVDM RRALFSSLLR QDITFFDANK TGQLVSRLTT 240
DVQEFKSSFK LVISQGLRSC TQVAGCLVSL SMLSTRLTLL LMVATPALMG VGTLMGSGLR 300
KLSRQCQEQI ARAMGVADEA LGNVRTVRAF AMEQREEERY GAELEACRCR AEELGRGIAL 360
FQGLSNIAFN CMVLGTLFIG GSLVAGQQLT GGDLMSFLVA SQTVQRSMAN LSVLFGQVVR 420
GLSAGARVFE YMALNPCIPL SGGCCVPKEQ LRGSVTFQNV CFSYPCRPGF EVLKDFTLTL 480
PPGKIVALVG QSGGGKTTVA SLLERFYDPT AGVVMLDGRD LRTLDPSWLR GQVVGFISQE 540
PVLFGTTIME NIRFGKLEAS DEEVYTAARE ANAHEFITSF PEGYNTVVGE RGTTLSGGQK 600
QRLAIARALI KQPTVLILDE ATSALDAESE RVVQEALDRA SAGRTVLAGT HEELLKKGGL 660
YAELIRRQAL DAPRTAAPPP KKPEGPRSHQ HKS 693 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR017940; ABC_transporter_type1.
 IPR001140; ABC_transptr_TM_dom.
 IPR011527; ABC_transptrTM_dom_typ1.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00664; ABC_membrane
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS50929; ABC_TM1F
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS