MRP6_HUMAN - dbPTM
MRP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRP6_HUMAN
UniProt AC O95255
Protein Name Multidrug resistance-associated protein 6
Gene Name ABCC6
Organism Homo sapiens (Human).
Sequence Length 1503
Subcellular Localization Isoform 1: Basolateral cell membrane
Multi-pass membrane protein .
Isoform 2: Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description Isoform 1: May participate directly in the active transport of drugs into subcellular organelles or influence drug distribution indirectly. Transports glutathione conjugates as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS).; Isoform 2: Inhibits TNF-alpha-mediated apoptosis through blocking one or more caspases..
Protein Sequence MAAPAEPCAGQGVWNQTEPEPAATSLLSLCFLRTAGVWVPPMYLWVLGPIYLLFIHHHGRGYLRMSPLFKAKMVLGFALIVLCTSSVAVALWKIQQGTPEAPEFLIHPTVWLTTMSFAVFLIHTERKKGVQSSGVLFGYWLLCFVLPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPPFFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKAIAFKRKGGSGMKAPETEPFLRQEGSQWRPLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQARQPGDRGEGETEPGTSTKDPRGTSAGRRPELRRERSIKSVPEKDRTTSEAQTEVPLDDPDRAGWPAGKDSIQYGRVKATVHLAYLRAVGTPLCLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGLV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
15N-linked_GlycosylationCAGQGVWNQTEPEPA
CCCCCCCCCCCCCHH		36.1712901863
238PhosphorylationLRPKDLWSLGRENSS
CCHHHHHHCCCCCCH		28.3924719451
254AcetylationELVSRLEKEWMRNRS
HHHHHHHHHHHHCHH		62.3612433359
278PhosphorylationAFKRKGGSGMKAPET
EEECCCCCCCCCCCC		44.3720166139
281AcetylationRKGGSGMKAPETEPF
CCCCCCCCCCCCCHH		65.4011793931
281UbiquitinationRKGGSGMKAPETEPF
CCCCCCCCCCCCCHH		65.40-
294PhosphorylationPFLRQEGSQWRPLLK
HHHCCCCCCHHHHHH		26.3122617229
372PhosphorylationLFEQQNMYRLKVLQM
HHHHHCHHHHHHHHH		21.97-
491PhosphorylationKDSRARLTSSILRNS
HHHHHHHHHHHHHCC		18.1868700241
492PhosphorylationDSRARLTSSILRNSK
HHHHHHHHHHHHCCC		21.7028857561
493PhosphorylationSRARLTSSILRNSKT
HHHHHHHHHHHCCCC		22.0224719451
652PhosphorylationCLHRINLTVPQGCLL
CCEEEEEEECCCCEE		26.1746156787
681PhosphorylationSALLGELSKVEGFVS
HHHHHHHHCCCCEEE		30.2872550289
762PhosphorylationGGQKQRLSLARAVYR
HHHHHHHHHHHHHHH		23.3624505115
833 (in isoform 3)Phosphorylation-37.6522210691
834 (in isoform 3)Phosphorylation-2.9822210691
878PhosphorylationTKDPRGTSAGRRPEL
CCCCCCCCCCCCHHH		31.3923532336
902PhosphorylationPEKDRTTSEAQTEVP
CCCCCCCCCCCCCCC		30.2672500023
1135PhosphorylationAETFQGSTVVRAFRT
HHHHCCCHHHHHHHC		29.8224719451
1224PhosphorylationQWVVRNWTDLENSIV
HHHHHCCCCCCCCEE		33.9729978859
1229PhosphorylationNWTDLENSIVSVERM
CCCCCCCCEEEEEEH		18.2629978859
1232PhosphorylationDLENSIVSVERMQDY
CCCCCEEEEEEHHHC		19.3224719451
1252PhosphorylationEAPWRLPTCAAQPPW
CCCCCCCCCCCCCCC		21.2624852491
1286PhosphorylationPLAVQGVSFKIHAGE
CEEEEEEEEEEECCC		27.8720034067
1310PhosphorylationAGKSSLASGLLRLQE
CCHHHHHHHHHHHHH		34.9546156781
1436PhosphorylationTAAVDPGTELQMQAM
CCCCCCCCHHHHHHH		38.6222210691
1446PhosphorylationQMQAMLGSWFAQCTV
HHHHHHHHHHHHHHH		18.3022210691
1480PhosphorylationDKGQVAESGSPAQLL
ECCCCCCCCCHHHHH		34.5368700759
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MRP6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRP6_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MRP6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD2_HUMANAK2physical
21988832
NR4A1_HUMANNR4A1physical
21988832
FURIN_HUMANFURINphysical
21988832
CRYL1_HUMANCRYL1physical
21988832
Drug and Disease Associations
Kegg Disease
H00560 Pseudoxanthoma elasticum, including: Pseudoxanthoma elasticum (PXE); Pseudoxanthoma elasticum-like d
OMIM Disease
264800Pseudoxanthoma elasticum (PXE)
614473Arterial calcification of infancy, generalized, 2 (GACI2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00515Cisplatin
DB00970Dactinomycin
DB00694Daunorubicin
DB00997Doxorubicin
DB00773Etoposide
DB00328Indomethacin
DB01032Probenecid
DB01138Sulfinpyrazone
DB00444Teniposide
DB00570Vinblastine
Regulatory Network of MRP6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681 AND SER-1310, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND MASSSPECTROMETRY.

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