CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014301
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family B member 7, mitochondrial 
Protein Synonyms/Alias
 ATP-binding cassette transporter 7; ABC transporter 7 protein 
Gene Name
 Abcb7 
Gene Synonyms/Alias
 Abc7 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
113TDPKEGLKDVDTRKIacetylation[1, 2]
216VRNAVFGKVAQNSIRacetylation[1, 2, 3, 4, 5]
216VRNAVFGKVAQNSIRsuccinylation[5]
251RQTGALSKAIDRGTRacetylation[2, 4]
350VKYFNNEKYEAQRYDacetylation[1, 2, 4, 5, 6]
350VKYFNNEKYEAQRYDsuccinylation[5]
350VKYFNNEKYEAQRYDubiquitination[7]
361QRYDGFLKTYETASLacetylation[1, 2, 4]
614LKLSGGEKQRVAIARacetylation[1]
656GAMRDVVKHRTSIFIacetylation[1]
723DSLGWDAKKESLSKEacetylation[1]
729AKKESLSKEEERKKLacetylation[1]
Reference
 [1] 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]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] 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] 
Functional Description
 Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins (By similarity). 
Sequence Annotation
 DOMAIN 140 436 ABC transmembrane type-1.
 DOMAIN 472 706 ABC transporter.
 NP_BIND 505 512 ATP (Potential).
 MOD_RES 216 216 N6-acetyllysine (By similarity).
 MOD_RES 251 251 N6-acetyllysine (By similarity).
 MOD_RES 336 336 Phosphoserine (By similarity).
 MOD_RES 340 340 Phosphotyrosine (By similarity).
 MOD_RES 342 342 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 752 AA 
Protein Sequence
MALLAIHSWR WAAAAVAFEK HKHSAVLTRA LVSMCGSGPR WSSSQRGASG SARLSQTTES 60
LRNTTQQRWG KDNSRQLLDA TKALQTWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI 120
IKAMLSYVWP EDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD 180
APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF 240
HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIVFEMML VSSVLYYKCG AQFALVTLGT 300
LGAYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNEK YEAQRYDGFL 360
KTYETASLKS TSTLAMLNFG QNAIFSVGLT AIMVLASQGI VAGALTVGDL VMVNGLLFQL 420
SLPLNFLGTV YRETRQALID MNTLFTLLKV DTRIKDKVMA PPLQITPQTA TVAFDNVHFE 480
YIEGQKVLNG VSFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNLQDVS 540
LESLRRAVGV VPQDAVLFHN TIYYNLLYGN INASPEEVYA VAKLAGLHDA ILRMPHGYDT 600
QVGERGLKLS GGEKQRVAIA RAILKNPPVI LYDEATSSLD SITEETILGA MRDVVKHRTS 660
IFIAHRLSTV VDADEIIVLS QGKVAERGTH YGLLANSSSI YSEMWHTQSN RVQNQDSLGW 720
DAKKESLSKE EERKKLQEEI VNSVKGCGNC SC 752 
Gene Ontology
 GO:0016021; C:integral to membrane; IBA:RefGenome.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:RefGenome.
 GO:0006879; P:cellular iron ion homeostasis; IMP:MGI. 
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