MRP2_HUMAN - dbPTM
MRP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRP2_HUMAN
UniProt AC Q92887
Protein Name Canalicular multispecific organic anion transporter 1
Gene Name ABCC2
Organism Homo sapiens (Human).
Sequence Length 1545
Subcellular Localization Apical cell membrane
Multi-pass membrane protein .
Protein Description Mediates hepatobiliary excretion of numerous organic anions. May function as a cellular cisplatin transporter..
Protein Sequence MLEKFCNSTFWNSSFLDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAAIELALVLTEDSGQATVPAVRYTNPSLYLGTWLLVLLIQYSRQWCVQKNSWFLSLFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFFISYGFQILILIFSAFSENNESSNNPSSIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARRALQRRQEKSSQQNSGARLPGLNKNQSQSQDALVLEDVEKKKKKSGTKKDVPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLISSVEEIPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTKF
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
7N-linked_Glycosylation-MLEKFCNSTFWNSS
-CHHHHHCCCCCCCH		47.41UniProtKB CARBOHYD
12N-linked_GlycosylationFCNSTFWNSSFLDSP
HHCCCCCCCHHCCCC		24.47UniProtKB CARBOHYD
46UbiquitinationYLWLLAPWQLLHVYK
HHHHHHHHHHHHHHH		8.8822817900
60PhosphorylationKSRTKRSSTTKLYLA
HCCCCCCCCCHHHHH		44.0927251275
62UbiquitinationRTKRSSTTKLYLAKQ
CCCCCCCCHHHHHHH		22.4722817900
63UbiquitinationTKRSSTTKLYLAKQV
CCCCCCCHHHHHHHH		34.9122817900
64UbiquitinationKRSSTTKLYLAKQVF
CCCCCCHHHHHHHHH		3.8822817900
65PhosphorylationRSSTTKLYLAKQVFV
CCCCCHHHHHHHHHH		13.23101544799
65UbiquitinationRSSTTKLYLAKQVFV
CCCCCHHHHHHHHHH		13.2322817900
66UbiquitinationSSTTKLYLAKQVFVG
CCCCHHHHHHHHHHH		7.5122817900
68UbiquitinationTTKLYLAKQVFVGFL
CCHHHHHHHHHHHHH		44.3822817900
171UbiquitinationYSCLFFISYGFQILI
HHHHHHHHHHHHHHH		17.6627667366
181UbiquitinationFQILILIFSAFSENN
HHHHHHHHHHHCCCC		3.7522817900
236AcetylationVDEEMKTKTLVSKFE
CCHHHHHHHHHHHHH		34.058082941
236UbiquitinationVDEEMKTKTLVSKFE
CCHHHHHHHHHHHHH		34.0533845483
237PhosphorylationDEEMKTKTLVSKFET
CHHHHHHHHHHHHHH		37.31-
241UbiquitinationKTKTLVSKFETHMKR
HHHHHHHHHHHHHHH		39.4829967540
247UbiquitinationSKFETHMKRELQKAR
HHHHHHHHHHHHHHH		34.8129901268
253UbiquitinationMKRELQKARRALQRR
HHHHHHHHHHHHHHH		8.0127667366
278UbiquitinationARLPGLNKNQSQSQD
CCCCCCCCCCCCCCC		62.5021906983
281PhosphorylationPGLNKNQSQSQDALV
CCCCCCCCCCCCCCH		40.9925159151
281UbiquitinationPGLNKNQSQSQDALV
CCCCCCCCCCCCCCH		40.9922817900
283PhosphorylationLNKNQSQSQDALVLE
CCCCCCCCCCCCHHH		34.9626055452
294UbiquitinationLVLEDVEKKKKKSGT
CHHHHHHHHHCCCCC		70.5121906983
295UbiquitinationVLEDVEKKKKKSGTK
HHHHHHHHHCCCCCC		57.2122817900
296UbiquitinationLEDVEKKKKKSGTKK
HHHHHHHHCCCCCCC		76.2122817900
297UbiquitinationEDVEKKKKKSGTKKD
HHHHHHHCCCCCCCC		62.1422817900
298AcetylationDVEKKKKKSGTKKDV
HHHHHHCCCCCCCCC		64.1011794067
298UbiquitinationDVEKKKKKSGTKKDV
HHHHHHCCCCCCCCC		64.1022817900
302AcetylationKKKKSGTKKDVPKSW
HHCCCCCCCCCCHHH		50.9611794077
307AcetylationGTKKDVPKSWLMKAL
CCCCCCCHHHHHHHH		54.8611794087
325PhosphorylationFYMVLLKSFLLKLVN
HHHHHHHHHHHHHHH		22.5422210691
336PhosphorylationKLVNDIFTFVSPQLL
HHHHHHHHHCCHHHH		24.3822210691
383UbiquitinationFCLQCYFQLCFKLGV
HHHHHHHHHHHHHCH		15.7322817900
403UbiquitinationIMASVYKKALTLSNL
HHHHHHHHHHHHHHH		30.8227667366
413UbiquitinationTLSNLARKEYTVGET
HHHHHHCCCCCCCCC		49.8421906983
481PhosphorylationIPINAILSTKSKTIQ
EEHHHHHCCCCCCEE		27.8924719451
485UbiquitinationAILSTKSKTIQVKNM
HHHCCCCCCEEEEEC		51.7230230243
490UbiquitinationKSKTIQVKNMKNKDK
CCCCEEEEECCCHHH		34.6433845483
493UbiquitinationTIQVKNMKNKDKRLK
CEEEEECCCHHHHHH		70.9533845483
496UbiquitinationVKNMKNKDKRLKIMN
EEECCCHHHHHHHHH		51.1822817900
500UbiquitinationKNKDKRLKIMNEILS
CCHHHHHHHHHHHHH		43.9029967540
507PhosphorylationKIMNEILSGIKILKY
HHHHHHHHHHHHHHH		44.1023898821
510UbiquitinationNEILSGIKILKYFAW
HHHHHHHHHHHHHHC		45.5721906983
513UbiquitinationLSGIKILKYFAWEPS
HHHHHHHHHHHCCCC		41.6222817900
602PhosphorylationMLPMMISSMLQASVS
HHHHHHHHHHHHHCC		16.76113136043
609PhosphorylationSMLQASVSTERLEKY
HHHHHHCCHHHHHHH		23.27113136051
615UbiquitinationVSTERLEKYLGGDDL
CCHHHHHHHHCCCCC		50.8221906983
616PhosphorylationSTERLEKYLGGDDLD
CHHHHHHHHCCCCCC		10.9519664994
628UbiquitinationDLDTSAIRHDCNFDK
CCCHHHHHCCCCHHH		21.2227667366
708UbiquitinationTAYVPQQSWIQNGTI
EEECCCCHHEECCCC		22.3922817900
715UbiquitinationSWIQNGTIKDNILFG
HHEECCCCCCCEEEC		5.8222817900
716UbiquitinationWIQNGTIKDNILFGT
HEECCCCCCCEEECC		44.5629967540
718UbiquitinationQNGTIKDNILFGTEF
ECCCCCCCEEECCCC		28.0622817900
721UbiquitinationTIKDNILFGTEFNEK
CCCCCEEECCCCCHH		11.4423503661
723PhosphorylationKDNILFGTEFNEKRY
CCCEEECCCCCHHHH		30.0320068231
728UbiquitinationFGTEFNEKRYQQVLE
ECCCCCHHHHHHHHH		58.4721906983
811UbiquitinationLGPNGLLKGKTRLLV
HCCCCCCCCCCEEEE		64.5033845483
844PhosphorylationGTIVEKGSYSALLAK
CEEEECCCHHHHHHH		27.2924275569
851UbiquitinationSYSALLAKKGEFAKN
CHHHHHHHCCHHHHH		62.3733845483
852AcetylationYSALLAKKGEFAKNL
HHHHHHHCCHHHHHH		59.05158675
857AcetylationAKKGEFAKNLKTFLR
HHCCHHHHHHHHHHH		69.04158679
857UbiquitinationAKKGEFAKNLKTFLR
HHCCHHHHHHHHHHH		69.0433845483
860UbiquitinationGEFAKNLKTFLRHTG
CHHHHHHHHHHHHHC		46.7733845483
866PhosphorylationLKTFLRHTGPEEEAT
HHHHHHHHCCCCCCE		48.2629116813
873PhosphorylationTGPEEEATVHDGSEE
HCCCCCCEECCCCCC		22.9629116813
878PhosphorylationEATVHDGSEEEDDDY
CCEECCCCCCCCCCC		48.1429116813
885PhosphorylationSEEEDDDYGLISSVE
CCCCCCCCCCCCCCC		22.3318669648
889PhosphorylationDDDYGLISSVEEIPE
CCCCCCCCCCCCCCC		33.1128857561
890PhosphorylationDDYGLISSVEEIPED
CCCCCCCCCCCCCCC		26.9328857561
900PhosphorylationEIPEDAASITMRREN
CCCCCHHHHHHHCHH		21.9518669648
902PhosphorylationPEDAASITMRRENSF
CCCHHHHHHHCHHHH		11.3523836654
916PhosphorylationFRRTLSRSSRSNGRH
HHHHHCCCCCCCCHH		27.0820068231
919PhosphorylationTLSRSSRSNGRHLKS
HHCCCCCCCCHHHHH		45.6524719451
926PhosphorylationSNGRHLKSLRNSLKT
CCCHHHHHHHHHHHH		38.6323186163
930PhosphorylationHLKSLRNSLKTRNVN
HHHHHHHHHHHCCCC		25.4723312004
938PhosphorylationLKTRNVNSLKEDEEL
HHHCCCCCCCCCHHH		36.2124972180
940UbiquitinationTRNVNSLKEDEELVK
HCCCCCCCCCHHHHH		64.0421906983
947UbiquitinationKEDEELVKGQKLIKK
CCCHHHHHHCCEEHH		69.1521906983
950UbiquitinationEELVKGQKLIKKEFI
HHHHHHCCEEHHHHH		61.9322817900
952UbiquitinationLVKGQKLIKKEFIET
HHHHCCEEHHHHHHC		8.4722817900
953UbiquitinationVKGQKLIKKEFIETG
HHHCCEEHHHHHHCC		57.6033845483
954UbiquitinationKGQKLIKKEFIETGK
HHCCEEHHHHHHCCC		51.3633845483
961UbiquitinationKEFIETGKVKFSIYL
HHHHHCCCEEEHHHH		50.0733845483
1011N-linked_GlycosylationTSDSKIFNSTDYPAS
CCCCCCCCCCCCCCH		47.69UniProtKB CARBOHYD
1045UbiquitinationVFIAHFWSAFGFVHA
HHHHHHHHHHHHHHH		16.8721963094
1056UbiquitinationFVHASNILHKQLLNN
HHHHHHHHHHHHHHH		4.8923503661
1065UbiquitinationKQLLNNILRAPMRFF
HHHHHHHHHCCCCCC		4.0927667366
1108UbiquitinationSWITCFLGIISTLVM
HHHHHHHHHHHHHHH		8.5727667366
1144UbiquitinationVQMFYVSTSRQLRRL
HHEEECCCHHHHHCC		20.2023503661
1153PhosphorylationRQLRRLDSVTRSPIY
HHHHCCCCCCCCCCH		29.9455146001
1184UbiquitinationEHQQRFLKHNEVRID
HHHHHHHHCCCEEEC		41.4921906983
1277UbiquitinationERITEYTKVENEAPW
EECHHCCCCCCCCCC		46.8021906983
1286PhosphorylationENEAPWVTDKRPPPD
CCCCCCCCCCCCCCC		31.7525841592
1288UbiquitinationEAPWVTDKRPPPDWP
CCCCCCCCCCCCCCC		58.3923503661
1296PhosphorylationRPPPDWPSKGKIQFN
CCCCCCCCCCCEEEC		50.1969012629
1297UbiquitinationPPPDWPSKGKIQFNN
CCCCCCCCCCEEECC		61.2127667366
1312UbiquitinationYQVRYRPELDLVLRG
EEEEECCHHCEEECC		46.0121963094
1326PhosphorylationGITCDIGSMEKIGVV
CEEECCCCCCEEEEE		24.8969009237
1329UbiquitinationCDIGSMEKIGVVGRT
ECCCCCCEEEEECCC		35.8033845483
1340UbiquitinationVGRTGAGKSSLTNCL
ECCCCCCHHHHHHHH		36.0227667366
1376UbiquitinationGLHDLREKLTIIPQD
CCHHHHHHCEECCCC		44.4923503661
1378PhosphorylationHDLREKLTIIPQDPI
HHHHHHCEECCCCCC		28.1120068231
1388PhosphorylationPQDPILFSGSLRMNL
CCCCCCCCCEECCCC		24.8320068231
1390PhosphorylationDPILFSGSLRMNLDP
CCCCCCCEECCCCCC		16.1720068231
1408UbiquitinationYSDEEIWKALELAHL
CCHHHHHHHHHHHHH		49.0733845483
1438PhosphorylationTEAGGNLSIGQRQLL
HHCCCCCCHHHHHHH		28.7711266082
1501PhosphorylationRLHTIMDSDKVMVLD
HHHHHCCCCCEEEEE		23.1946156739
1542PhosphorylationAGIENVNSTKF----
HCCCCCCCCCC----		28.7925072903
1543PhosphorylationGIENVNSTKF-----
CCCCCCCCCC-----		31.1325072903
1544UbiquitinationIENVNSTKF------
CCCCCCCCC------		49.2321906983
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 MRP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRP2_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 MRP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF1_HUMANSLC9A3R1physical
12615054
NHRF4_HUMANPDZD3physical
12615054
RADI_MOUSERdxphysical
12068294
NDUA2_HUMANNDUFA2physical
22939629
VAMP2_HUMANVAMP2physical
22939629
RM23_HUMANMRPL23physical
22939629
OXA1L_HUMANOXA1Lphysical
22939629
RAB14_HUMANRAB14physical
22939629
TOM70_HUMANTOMM70Aphysical
22939629
RM37_HUMANMRPL37physical
22939629
RT63_HUMANMRPL57physical
22939629
NDUB9_HUMANNDUFB9physical
22939629
SSRA_HUMANSSR1physical
22939629
TOM22_HUMANTOMM22physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
RM24_HUMANMRPL24physical
22939629
RB11B_HUMANRAB11Bphysical
22939629
RT26_HUMANMRPS26physical
22939629
PTH2_HUMANPTRH2physical
22939629
ZNT5_HUMANSLC30A5physical
22939629
PLAK_HUMANJUPphysical
22939629
TOM20_HUMANTOMM20physical
22939629
VPP3_HUMANTCIRG1physical
22939629
PRR3_HUMANPRR3physical
22939629
NDUS8_HUMANNDUFS8physical
22939629
RM10_HUMANMRPL10physical
22939629
NDUAA_HUMANNDUFA10physical
22939629
RAB31_HUMANRAB31physical
22939629
NDUA9_HUMANNDUFA9physical
22939629
UCRI_HUMANUQCRFS1physical
22939629
RT35_HUMANMRPS35physical
22939629
PICAL_HUMANPICALMphysical
22939629
RT28_HUMANMRPS28physical
22939629
SYJ2B_HUMANSYNJ2BPphysical
22939629
NFKB1_HUMANNFKB1physical
21988832
UBQL1_HUMANUBQLN1physical
21988832
AZIN1_HUMANAZIN1physical
21988832
MCPH1_HUMANMCPH1physical
21988832
SHAN3_HUMANSHANK3physical
21988832
NHRF3_HUMANPDZK1physical
21059598
HSP74_HUMANHSPA4physical
21059598
TBB3_HUMANTUBB3physical
21059598
Drug and Disease Associations
Kegg Disease
H00208 Hyperbilirubinemia; Crigler-Najjar syndrome, type I (CN1); Crigler-Najjar syndrome, type II (CN2); G
OMIM Disease
237500Dubin-Johnson syndrome (DJS)
Kegg Drug
D00125 Etoposide (JP16/USP/INN); Vepesid (TN)
D00142 Methotrexate (JP16/USP/INN); Mexate (TN)
D00184 Ciclosporin (JP16); Cyclosporine (USP); Gengraf (TN); Neoral (TN); Restasis (TN); Sandimmune (TN)
D00197 Reserpine (JP16/USP/INN); Apoplon (TN); Serpalan (TN)
D00211 Rifampicin (JP16/INN); Rifampin (USP); Rifadin (TN); Rimactane (TN)
D00336 Glibenclamide (JP16/INN); Glyburide (USP); Diabeta (TN); Glynase (TN); Micronase (TN)
D00355 Lansoprazole (JAN/USP/INN); Prevacid (TN)
D00364 Loratadine (JAN/USAN/INN); Claritin (TN)
D00400 Valsartan (JP16/USAN/INN); Diovan (TN)
D00475 Probenecid (JP16/USP/INN); Benemid (TN)
D00565 Fenofibrate (JAN/INN); Antara (TN); Lipantil (TN); Lipofen (TN); Tricor (TN); Triglide (TN)
D00895 Delavirdine mesilate (JAN); Delavirdine mesylate (USAN); Rescriptor (TN)
D00896 Efavirenz (JAN/INN); Sustiva (TN)
D00904 Diclofenac sodium (JP16/USP); Solaraze (TN); Voltaren (TN)
D00966 Tamoxifen citrate (JP16/USP); Nolvadex (TN)
D01056 Benzbromarone (JP16/USAN/INN); Uroleap (TN)
D01199 Emtricitabine (JAN/USAN/INN); Emtriva (TN)
D01204 Olmesartan medoxomil (JAN/USAN); Benicar (TN); Olmetec (TN)
D01966 Ezetimibe (JAN/USAN/INN); Zetia (TN)
D02115 Methotrexate sodium; Trexall (TN)
D02166 Mitoxantrone hydrochloride (JAN/USP); Novantron (TN)
D04107 Etoposide phosphate (USAN); Etopophos preservative free (TN)
D05246 Olmesartan (USAN/INN)
D07782 Delavirdine (INN)
D08224 Mitoxantrone (INN); Misostol (TN)
D08479 Rifampicin sodium; Rifadine (TN)
D08559 Tamoxifen (INN); Tamoxifen (TN); Tamoplex (TN)
DrugBank
DB00171Adenosine triphosphate
DB00345Aminohippurate
DB01169Arsenic trioxide
DB01076Atorvastatin
DB08907Canagliflozin
DB00564Carbamazepine
DB00958Carboplatin
DB02659Cholic Acid
DB00515Cisplatin
DB00257Clotrimazole
DB00286Conjugated Estrogens
DB00091Cyclosporine
DB00694Daunorubicin
DB01234Dexamethasone
DB01248Docetaxel
DB00997Doxorubicin
DB00876Eprosartan
DB00977Ethinyl Estradiol
DB00773Etoposide
DB00973Ezetimibe
DB00695Furosemide
DB02703Fusidic Acid
DB08884Gadoxetate
DB00143Glutathione
DB01016Glyburide
DB00224Indinavir
DB00328Indomethacin
DB00762Irinotecan
DB00602Ivermectin
DB00709Lamivudine
DB00650Leucovorin
DB01202Levetiracetam
DB00978Lomefloxacin
DB00227Lovastatin
DB00563Methotrexate
DB00688Mycophenolate mofetil
DB01115Nifedipine
DB00957Norgestimate
DB01165Ofloxacin
DB00275Olmesartan
DB00526Oxaliplatin
DB01229Paclitaxel
DB01174Phenobarbital
DB00252Phenytoin
DB08860Pitavastatin
DB01411Pranlukast
DB00175Pravastatin
DB01032Probenecid
DB00908Quinidine
DB00206Reserpine
DB01045Rifampicin
DB00503Ritonavir
DB01232Saquinavir
DB00641Simvastatin
DB00398Sorafenib
DB01208Sparfloxacin
DB00421Spironolactone
DB00795Sulfasalazine
DB01138Sulfinpyrazone
DB01268Sunitinib
DB00675Tamoxifen
DB00966Telmisartan
DB00300Tenofovir
DB00116Tetrahydrofolic acid
DB01586Ursodeoxycholic acid
DB00067Vasopressin
DB00661Verapamil
DB00570Vinblastine
DB00541Vincristine
Regulatory Network of MRP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-878, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASSSPECTROMETRY.

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