CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030795
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family B member 7, mitochondrial 
Protein Synonyms/Alias
 cDNA FLJ53391, highly similar to ATP-binding cassette sub-family B member 7, mitochondrial 
Gene Name
 ABCB7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
190VRNAVFGKVAQNSIRacetylation[1, 2]
190VRNAVFGKVAQNSIRubiquitination[3]
582QVGERGLKLSGGEKQubiquitination[4]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 702 AA 
Protein Sequence
MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQALQV 60
WPLIEKRTCW HGHAGGGLHT DPKEGLKDVD TRKIIKAMLS YVWPKDRPDL RARVAISLGF 120
LGGAKAMNIV VPFMFKYAVD SLNQMSGNML NLSDAPNTVA TMATAVLIGY GVSRAGAAFF 180
NEVRNAVFGK VAQNSIRRIA KNVFLHLHNL DLGFHLSRQT GALSKAIDRG TRGISFVLSA 240
LVFNLLPIMF EVMLVSGVLY YKCGAQFALV TLGTLGTYTA FTVAVTRWRT RFRIEMNKAD 300
NDAGNAAIDS LLNYETVKYF NNERYEAQRY DGFLKTYETA SLKSTSTLAM LNFGQSAIFS 360
VGLTAIMVLA SQGIVAGTLT VGDLVMVNGL LFQLSLPLNF LGTVYRETRQ ALIDMNTLFT 420
LLKVDTQIKD KVMASPLQIT PQTATVAFDN VHFEYIEGQK VLSGISFEVP AGKKVAIVGG 480
SGSGKSTIVR LLFRFYEPQK GSIYLAGQNI QDVSLESLRR AVGVVPQDAV LFHNTIYYNL 540
LYGNISASPE EVYAVAKLAG LHDAILRMPH GYDTQVGERG LKLSGGEKQR VAIARAILKD 600
PPVILYDEAT SSLDSITEET ILGAMKDVVK HRTSIFIAHR LSTVVDADEI IVLDQGKVAE 660
RGTHHGLLAN PHSIYSEMWH TQSSRVQNHD NPKWEAKKEN IS 702 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:InterPro.
 GO:0005739; C:mitochondrion; 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