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
2Phosphoserine------MSSSNVEVF
------CCCCCEEEE
42.3420068231
50PhosphoserineCYRVKLKSGFLPCRK
HHHHCCCCCCCCCCC
45.2650558679
65PhosphoserinePVEKEILSNINGIMK
CCHHHHHHHCCCCCC
41.1320068231
100PhosphoserineLAARKDPSGLSGDVL
HHHCCCCCCCCCCEE
63.6036012623
103PhosphoserineRKDPSGLSGDVLING
CCCCCCCCCCEEECC
36.1536012629
143PhosphoserineVRENLQFSAALRLAT
HHHHHHHHHHHHHHH
10.3246156969
153PhosphothreonineLRLATTMTNHEKNER
HHHHHHCCHHHHHHH
31.1921081558
172N6-acetyllysineIQELGLDKVADSKVG
HHHHCCHHHCCCCCC
44.3526051181
187PhosphoserineTQFIRGVSGGERKRT
HHHHCCCCCCCCCCC
43.867919223
194PhosphothreonineSGGERKRTSIGMELI
CCCCCCCCCCCCEEC
27.9418433525
195PhosphoserineGGERKRTSIGMELIT
CCCCCCCCCCCEECC
22.607919233
353PhosphoserineKAELHQLSGGEKKKK
HHHHHHHCCCCCCCC
37.8872267159
362PhosphothreonineGEKKKKITVFKEISY
CCCCCCEEEEEEEEE
28.863636023
464PhosphotyrosineHEYISGYYRVSSYFL
HHHHHHCHHHHHHHH
14.2069213047
596N-linked (GlcNAc)QNFCPGLNATGNNPC
CCCCCCCCCCCCCCC
41.1815807535

Disease-associated PTM Sites based on nsSNP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP 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.
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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