CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006324
UniProt Accession
Genbank Protein ID
 L05628; AF022853; AF022827; AF022828; AF022829; AF022831; AF022833; AF022835; AF022837; AF022839; AF022841; AF022850; AF022849; AF022848; AF022847; AF022846; AF022845; AF022844; AF022843; AF022842; AF022852; AF022851; AF022840; AF022838; AF022836; AF022834; AF022832; AF022826; AF022825; AF022824; AF022830; AF022853; AF022824; AF022825; AF022826; AF022828; AF022830; AF022832; AF022834; AF022836; AF022838; AF022848; AF022847; AF022846; AF022845; AF022844; AF022843; AF022842; AF022841; AF022839; AF022852; AF022851; AF022850; AF022849; AF022837; AF022835; AF022833; AF022831; AF022829; AF022827; AF022853; AF022824; AF022825; AF022826; AF022827; AF022829; AF022831; AF022833; AF022835; AF022837; AF022847; AF022846; AF022845; AF022844; AF022843; AF022842; AF022841; AF022840; AF022838; AF022852; AF022851; AF022850; AF022849; AF022848; AF022836; AF022834; AF022832; AF022830; AF022828; AF022853; AF022824; AF022825; AF022826; AF022827; AF022828; AF022829; AF022830; AF022831; AF022832; AF022833; AF022834; AF022835; AF022836; AF022837; AF022838; AF022839; AF022840; AF022841; AF022842; AF022843; AF022844; AF022845; AF022846; AF022847; AF022848; AF022849; AF022850; AF022851; EF419769; AC025778; AC130651; AC136624; AB209120; U91318; AC003026 
Genbank Nucleotide ID
 AAB46616.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83979.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83980.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83981.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; AAB83983.1; ABN79590.1; BAD92357.1; AAC15784.1; AAC05808.1 
Protein Name
 Multidrug resistance-associated protein 1 
Protein Synonyms/Alias
 ATP-binding cassette sub-family C member 1; Leukotriene C(4) transporter; LTC4 transporter 
Gene Name
 ABCC1 
Gene Synonyms/Alias
 MRP; MRP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
72IQMTPLNKTKTALGFubiquitination[1, 2]
246SDLWSLNKEDTSEQVubiquitination[1, 3]
259QVVPVLVKNWKKECAubiquitination[1]
280VKVVYSSKDPAQPKEubiquitination[1, 3]
290AQPKESSKVDANEEVubiquitination[1, 3]
303EVEALIVKSPQKEWNubiquitination[1, 4]
307LIVKSPQKEWNPSLFubiquitination[1, 4]
315EWNPSLFKVLYKTFGubiquitination[4]
396FVSGMRIKTAVIGAVubiquitination[1, 3]
406VIGAVYRKALVITNSubiquitination[3]
416VITNSARKSSTVGEIubiquitination[1]
488AVMAMKTKTYQVAHMubiquitination[1, 3]
496TYQVAHMKSKDNRIKubiquitination[1, 3]
498QVAHMKSKDNRIKLMacetylation[5]
498QVAHMKSKDNRIKLMubiquitination[3]
503KSKDNRIKLMNEILNacetylation[5]
503KSKDNRIKLMNEILNubiquitination[1, 3, 4, 6]
513NEILNGIKVLKLYAWubiquitination[1, 3, 4, 6]
525YAWELAFKDKVLAIRubiquitination[1]
636SIERRPVKDGGGTNSubiquitination[1, 3, 7]
773VNLSGGQKQRVSLARubiquitination[3]
804AVDAHVGKHIFENVIubiquitination[1]
814FENVIGPKGMLKNKTubiquitination[1, 3, 4, 6]
891TGVSGPGKEAKQMENubiquitination[1, 3, 8, 9]
894SGPGKEAKQMENGMLubiquitination[1, 3]
908LVTDSAGKQLQRQLSubiquitination[1, 3, 4, 7]
936NSTAELQKAEAKKEEubiquitination[1, 3, 7]
952WKLMEADKAQTGQVKubiquitination[1, 3]
1078NLVNRFSKELDTVDSubiquitination[1]
1181FIHQSDLKVDENQKAubiquitination[1, 3, 7]
1187LKVDENQKAYYPSIVubiquitination[1, 3]
1265IVAVERLKEYSETEKubiquitination[1, 3]
1272KEYSETEKEAPWQIQubiquitination[1, 3]
1322VTINGGEKVGIVGRTubiquitination[3]
1333VGRTGAGKSSLTLGLubiquitination[3]
1369GLHDLRFKITIIPQDubiquitination[1, 3]
1502TRVIVLDKGEIQEYGubiquitination[1, 3]
1526GLFYSMAKDAGLV**ubiquitination[1, 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] 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]
 [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] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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]
 [9] 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] 
Functional Description
 Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o- glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. 
Sequence Annotation
 DOMAIN 325 608 ABC transmembrane type-1 1.
 DOMAIN 644 868 ABC transporter 1.
 DOMAIN 975 1256 ABC transmembrane type-1 2.
 DOMAIN 1293 1527 ABC transporter 2.
 NP_BIND 678 685 ATP 1.
 NP_BIND 1327 1334 ATP 2 (Potential).
 BINDING 653 653 ATP 1.
 BINDING 713 713 ATP 1.
 MOD_RES 905 905 Phosphoserine.
 MOD_RES 915 915 Phosphoserine.
 MOD_RES 930 930 Phosphoserine.
 CARBOHYD 19 19 N-linked (GlcNAc...).
 CARBOHYD 23 23 N-linked (GlcNAc...).
 CARBOHYD 1006 1006 N-linked (GlcNAc...).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Glycoprotein; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1531 AA 
Protein Sequence
MALRGFCSAD GSDPLWDWNV TWNTSNPDFT KCFQNTVLVW VPCFYLWACF PFYFLYLSRH 60
DRGYIQMTPL NKTKTALGFL LWIVCWADLF YSFWERSRGI FLAPVFLVSP TLLGITMLLA 120
TFLIQLERRK GVQSSGIMLT FWLVALVCAL AILRSKIMTA LKEDAQVDLF RDITFYVYFS 180
LLLIQLVLSC FSDRSPLFSE TIHDPNPCPE SSASFLSRIT FWWITGLIVR GYRQPLEGSD 240
LWSLNKEDTS EQVVPVLVKN WKKECAKTRK QPVKVVYSSK DPAQPKESSK VDANEEVEAL 300
IVKSPQKEWN PSLFKVLYKT FGPYFLMSFF FKAIHDLMMF SGPQILKLLI KFVNDTKAPD 360
WQGYFYTVLL FVTACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNSARKSSTV 420
GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPVN 480
AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK 540
KSAYLSAVGT FTWVCTPFLV ALCTFAVYVT IDENNILDAQ TAFVSLALFN ILRFPLNILP 600
MVISSIVQAS VSLKRLRIFL SHEELEPDSI ERRPVKDGGG TNSITVRNAT FTWARSDPPT 660
LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVAIKGSVAY VPQQAWIQND 720
SLRENILFGC QLEEPYYRSV IQACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR 780
AVYSNADIYL FDDPLSAVDA HVGKHIFENV IGPKGMLKNK TRILVTHSMS YLPQVDVIIV 840
MSGGKISEMG SYQELLARDG AFAEFLRTYA STEQEQDAEE NGVTGVSGPG KEAKQMENGM 900
LVTDSAGKQL QRQLSSSSSY SGDISRHHNS TAELQKAEAK KEETWKLMEA DKAQTGQVKL 960
SVYWDYMKAI GLFISFLSIF LFMCNHVSAL ASNYWLSLWT DDPIVNGTQE HTKVRLSVYG 1020
ALGISQGIAV FGYSMAVSIG GILASRCLHV DLLHSILRSP MSFFERTPSG NLVNRFSKEL 1080
DTVDSMIPEV IKMFMGSLFN VIGACIVILL ATPIAAIIIP PLGLIYFFVQ RFYVASSRQL 1140
KRLESVSRSP VYSHFNETLL GVSVIRAFEE QERFIHQSDL KVDENQKAYY PSIVANRWLA 1200
VRLECVGNCI VLFAALFAVI SRHSLSAGLV GLSVSYSLQV TTYLNWLVRM SSEMETNIVA 1260
VERLKEYSET EKEAPWQIQE TAPPSSWPQV GRVEFRNYCL RYREDLDFVL RHINVTINGG 1320
EKVGIVGRTG AGKSSLTLGL FRINESAEGE IIIDGINIAK IGLHDLRFKI TIIPQDPVLF 1380
SGSLRMNLDP FSQYSDEEVW TSLELAHLKD FVSALPDKLD HECAEGGENL SVGQRQLVCL 1440
ARALLRKTKI LVLDEATAAV DLETDDLIQS TIRTQFEDCT VLTIAHRLNT IMDYTRVIVL 1500
DKGEIQEYGA PSDLLQQRGL FYSMAKDAGL V 1531 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; TAS:ProtInc.
 GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc.
 GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
 GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
 GO:0042493; P:response to drug; TAS:ProtInc. 
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.
 IPR005292; Multidrug-R_assoc.
 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