ABCG2_HUMAN - dbPTM
ABCG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCG2_HUMAN
UniProt AC Q9UNQ0
Protein Name ATP-binding cassette sub-family G member 2
Gene Name ABCG2
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Cell membrane
Multi-pass membrane protein . Mitochondrion membrane
Multi-pass membrane protein .
Protein Description High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin..
Protein Sequence MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS
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
2Phosphorylation------MSSSNVEVF
------CCCCCEEEE		42.3420068231
3Phosphorylation-----MSSSNVEVFI
-----CCCCCEEEEE		25.3220068231
4Phosphorylation----MSSSNVEVFIP
----CCCCCEEEEEE		37.2720068231
13PhosphorylationVEVFIPVSQGNTNGF
EEEEEECCCCCCCCC		27.3220068231
17PhosphorylationIPVSQGNTNGFPATA
EECCCCCCCCCCCCC		43.4720068231
23PhosphorylationNTNGFPATASNDLKA
CCCCCCCCCCHHHHH		30.7520068231
25PhosphorylationNGFPATASNDLKAFT
CCCCCCCCHHHHHHH		26.9020068231
50PhosphorylationCYRVKLKSGFLPCRK
HHHHCCCCCCCCCCC		45.2650558679
65PhosphorylationPVEKEILSNINGIMK
CCHHHHHHHCCCCCC		41.1320068231
82PhosphorylationLNAILGPTGGGKSSL
CCEECCCCCCCHHHH		46.8120068231
100PhosphorylationLAARKDPSGLSGDVL
HHHCCCCCCCCCCEE		63.6020068231
103PhosphorylationRKDPSGLSGDVLING
CCCCCCCCCCEEECC		36.1520068231
143PhosphorylationVRENLQFSAALRLAT
HHHHHHHHHHHHHHH		10.3246156969
153PhosphorylationLRLATTMTNHEKNER
HHHHHHCCHHHHHHH		31.1920068231
172AcetylationIQELGLDKVADSKVG
HHHHCCHHHCCCCCC		44.3526051181
172UbiquitinationIQELGLDKVADSKVG
HHHHCCHHHCCCCCC		44.35-
1772-HydroxyisobutyrylationLDKVADSKVGTQFIR
CHHHCCCCCCHHHHC		45.27-
177UbiquitinationLDKVADSKVGTQFIR
CHHHCCCCCCHHHHC		45.27-
187PhosphorylationTQFIRGVSGGERKRT
HHHHCCCCCCCCCCC		43.867919223
194PhosphorylationSGGERKRTSIGMELI
CCCCCCCCCCCCEEC		27.9418433525
195PhosphorylationGGERKRTSIGMELIT
CCCCCCCCCCCEECC		22.607919233
247PhosphorylationFSIHQPRYSIFKLFD
EEECCCCCHHHHHHH		16.8922210691
248PhosphorylationSIHQPRYSIFKLFDS
EECCCCCHHHHHHHH		23.8724719451
261PhosphorylationDSLTLLASGRLMFHG
HHHHHHHCCCEEEEC		25.1522210691
314UbiquitinationLNREEDFKATEIIEP
CCCHHHCCCCEEECC		67.72-
323UbiquitinationTEIIEPSKQDKPLIE
CEEECCCCCCCCHHH		73.55-
343UbiquitinationYVNSSFYKETKAELH
HHCCHHHHHHHHHHH		57.82-
346UbiquitinationSSFYKETKAELHQLS
CHHHHHHHHHHHHHC		40.74-
353PhosphorylationKAELHQLSGGEKKKK
HHHHHHHCCCCCCCC		37.8825159151
357UbiquitinationHQLSGGEKKKKITVF
HHHCCCCCCCCEEEE		73.50-
362PhosphorylationGEKKKKITVFKEISY
CCCCCCEEEEEEEEE		28.863636023
365UbiquitinationKKKITVFKEISYTTS
CCCEEEEEEEEECHH		50.21-
464PhosphorylationHEYISGYYRVSSYFL
HHHHHHCHHHHHHHH		14.2069213047
592 (in isoform 2)Phosphorylation-3.2425332170
596N-linked_GlycosylationQNFCPGLNATGNNPC
CCCCCCCCCCCCCCC		41.1828554189
596N-linked_GlycosylationQNFCPGLNATGNNPC
CCCCCCCCCCCCCCC		41.1815807535
597 (in isoform 2)Phosphorylation-23.1725332170
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
362TPhosphorylationKinasePIM1P11309
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
362TPhosphorylation

18056989
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 ABCG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ABCG2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00067 Estrone (JAN/USP/INN); Estrone (TN)
D00142 Methotrexate (JP16/USP/INN); Mexate (TN)
D00184 Ciclosporin (JP16); Cyclosporine (USP); Gengraf (TN); Neoral (TN); Restasis (TN); Sandimmune (TN)
D00359 Lovastatin (USP/INN); MK-803; ML-530B; Mevacor (TN)
D00448 Salazosulfapyridine (JP16); Sulfasalazine (USP/INN); Azulfidine (TN)
D01061 Irinotecan hydrochloride hydrate (JAN); Irinotecan hydrochloride (USAN); CPT 11; CPT-11; Campto (TN)
D01441 Imatinib mesilate (JAN); Imatinib mesylate (USAN); Gleevec (TN); Glivec (TN)
D01915 Rosuvastatin calcium (JAN/USAN); ZD 4522; Crestor (TN)
D01977 Gefitinib (JAN/USAN/INN); Iressa (TN)
D02115 Methotrexate sodium; Trexall (TN)
D02166 Mitoxantrone hydrochloride (JAN/USP); Novantron (TN)
D02168 Nogitecan hydrochloride (JAN); Topotecan hydrochloride (USAN); Hycamtin (TN)
D03213 Apixaban (JAN/USAN/INN); Eliquis (TN)
D03968 Elacridar hydrochloride (USAN)
D03978 Eltrombopag olamine (JAN/USAN); Promacta (TN)
D04024 Lapatinib tosilate hydrate (JAN); Lapatinib ditosylate (USAN); Tykerb (TN)
D08066 Imatinib (INN); Glamox (TN)
D08086 Irinotecan (INN); Biotecan (TN)
D08108 Lapatinib (INN)
D08224 Mitoxantrone (INN); Misostol (TN)
D08492 Rosuvastatin (INN); Creston (TN)
D08618 Topotecan (BAN); Hycamtin (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCG2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"N-linked glycosylation of the human ABC transporter ABCG2 onasparagine 596 is not essential for expression, transport activity, ortrafficking to the plasma membrane.";
Diop N.K., Hrycyna C.A.;
Biochemistry 44:5420-5429(2005).
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-596, AND MUTAGENESIS OFASN-418; ASN-557 AND ASN-596.

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