ALKB5_HUMAN - dbPTM
ALKB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALKB5_HUMAN
UniProt AC Q6P6C2
Protein Name RNA demethylase ALKBH5 {ECO:0000303|PubMed:24616105}
Gene Name ALKBH5
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Nucleus speckle .
Protein Description Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. [PubMed: 23177736]
Protein Sequence MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGAKRKYQEDSDPERSDYEEQQLQKEEEARKVKSGIRQMRLFSQDECAKIEARIDEVVSRAEKGLYNEHTVDRAPLRNKYFFGEGYTYGAQLQKRGPGQERLYPPGDVDEIPEWVHQLVIQKLVEHRVIPEGFVNSAVINDYQPGGCIVSHVDPIHIFERPIVSVSFFSDSALCFGCKFQFKPIRVSEPVLSLPVRRGSVTVLSGYAADEITHCIRPQDIKERRAVIILRKTRLDAPRLETKSLSSSVLPPSYASDRLSGNNRDPALKPKRSHRKADPDAAHRPRILEMDKEENRRSVLLPTHRRRGSFSSENYWRKSYESSEDCSEAAGSPARKVKMRRH
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
2Acetylation------MAAASGYTD
------CCCCCCCHH		16.2522814378
5Phosphorylation---MAAASGYTDLRE
---CCCCCCCHHHHH		27.8330815085
15UbiquitinationTDLREKLKSMTSRDN
HHHHHHHHHCCCCCC		49.6129967540
51PhosphorylationAAAAAEPYPVSGAKR
HHHHCCCCCCCCCCC		14.0520068231
54PhosphorylationAAEPYPVSGAKRKYQ
HCCCCCCCCCCCCCC		28.6420068231
57AcetylationPYPVSGAKRKYQEDS
CCCCCCCCCCCCCCC		53.6125953088
57UbiquitinationPYPVSGAKRKYQEDS
CCCCCCCCCCCCCCC		53.61-
60PhosphorylationVSGAKRKYQEDSDPE
CCCCCCCCCCCCCCC		22.5921955146
64 (in isoform 2)Phosphorylation-55.0718669648
64PhosphorylationKRKYQEDSDPERSDY
CCCCCCCCCCCCCHH		55.0719664994
69 (in isoform 2)Phosphorylation-42.7718669648
69PhosphorylationEDSDPERSDYEEQQL
CCCCCCCCHHHHHHH		42.7719664994
71PhosphorylationSDPERSDYEEQQLQK
CCCCCCHHHHHHHHH		23.7021955146
86AcetylationEEEARKVKSGIRQMR
HHHHHHHHHHHHHHH		46.1011794823
96PhosphorylationIRQMRLFSQDECAKI
HHHHHCCCHHHHHHH		41.1125850435
102UbiquitinationFSQDECAKIEARIDE
CCHHHHHHHHHHHHH		53.3833845483
102SumoylationFSQDECAKIEARIDE
CCHHHHHHHHHHHHH		53.38-
102AcetylationFSQDECAKIEARIDE
CCHHHHHHHHHHHHH		53.3826051181
112PhosphorylationARIDEVVSRAEKGLY
HHHHHHHHHHHHCCC		30.8346162431
116UbiquitinationEVVSRAEKGLYNEHT
HHHHHHHHCCCCCCC		53.9124816145
132UbiquitinationDRAPLRNKYFFGEGY
CCCCCCCCEECCCCC		36.6829967540
132AcetylationDRAPLRNKYFFGEGY
CCCCCCCCEECCCCC		36.6819608861
133PhosphorylationRAPLRNKYFFGEGYT
CCCCCCCEECCCCCC		14.0029083192
136UbiquitinationLRNKYFFGEGYTYGA
CCCCEECCCCCCCCC		19.9521890473
139PhosphorylationKYFFGEGYTYGAQLQ
CEECCCCCCCCCCCC		7.7829083192
140PhosphorylationYFFGEGYTYGAQLQK
EECCCCCCCCCCCCC		26.7429083192
141PhosphorylationFFGEGYTYGAQLQKR
ECCCCCCCCCCCCCC		11.2829083192
147 (in isoform 1)Ubiquitination-68.8421890473
147UbiquitinationTYGAQLQKRGPGQER
CCCCCCCCCCCCCCC		68.8422817900
147 (in isoform 2)Ubiquitination-68.8421890473
235UbiquitinationFGCKFQFKPIRVSEP
CCCEEEEECEEECCC		28.8429967540
235AcetylationFGCKFQFKPIRVSEP
CCCEEEEECEEECCC		28.8425825284
250MethylationVLSLPVRRGSVTVLS
EEECCEECCCEEEEE		41.81-
252PhosphorylationSLPVRRGSVTVLSGY
ECCEECCCEEEEECE		16.8925849741
254PhosphorylationPVRRGSVTVLSGYAA
CEECCCEEEEECEEH		19.8928464451
257PhosphorylationRGSVTVLSGYAADEI
CCCEEEEECEEHHHH		25.9728450419
259PhosphorylationSVTVLSGYAADEITH
CEEEEECEEHHHHCE		8.6727251275
294PhosphorylationLDAPRLETKSLSSSV
CCCCCCCCCCCCCCC		30.4420044836
295UbiquitinationDAPRLETKSLSSSVL
CCCCCCCCCCCCCCC		39.7729967540
296PhosphorylationAPRLETKSLSSSVLP
CCCCCCCCCCCCCCC		40.6920044836
299PhosphorylationLETKSLSSSVLPPSY
CCCCCCCCCCCCHHH		29.7428555341
305PhosphorylationSSSVLPPSYASDRLS
CCCCCCHHHHHHCCC		31.2425627689
306PhosphorylationSSVLPPSYASDRLSG
CCCCCHHHHHHCCCC		18.8528555341
312PhosphorylationSYASDRLSGNNRDPA
HHHHHCCCCCCCCCC		40.1325159151
321AcetylationNNRDPALKPKRSHRK
CCCCCCCCCCCCCCC		51.0723749302
321UbiquitinationNNRDPALKPKRSHRK
CCCCCCCCCCCCCCC		51.0733845483
325PhosphorylationPALKPKRSHRKADPD
CCCCCCCCCCCCCCC		33.5027282143
328SumoylationKPKRSHRKADPDAAH
CCCCCCCCCCCCHHH		52.28-
328SumoylationKPKRSHRKADPDAAH
CCCCCCCCCCCCHHH		52.2828112733
350PhosphorylationDKEENRRSVLLPTHR
CCHHHHCCCCCCCCC		17.5525159151
355PhosphorylationRRSVLLPTHRRRGSF
HCCCCCCCCCCCCCC		28.1626074081
359MethylationLLPTHRRRGSFSSEN
CCCCCCCCCCCCCCC		45.0924129315
361PhosphorylationPTHRRRGSFSSENYW
CCCCCCCCCCCCCCH		21.8322167270
361 (in isoform 2)Phosphorylation-21.8318669648
363PhosphorylationHRRRGSFSSENYWRK
CCCCCCCCCCCCHHH		38.1422167270
364PhosphorylationRRRGSFSSENYWRKS
CCCCCCCCCCCHHHC		28.0523927012
367PhosphorylationGSFSSENYWRKSYES
CCCCCCCCHHHCCCC		11.5323403867
371PhosphorylationSENYWRKSYESSEDC
CCCCHHHCCCCCCHH		26.0925159151
372PhosphorylationENYWRKSYESSEDCS
CCCHHHCCCCCCHHH		23.9023927012
374PhosphorylationYWRKSYESSEDCSEA
CHHHCCCCCCHHHHH		30.6923927012
375PhosphorylationWRKSYESSEDCSEAA
HHHCCCCCCHHHHHC		26.0523927012
375 (in isoform 2)Phosphorylation-26.0518669648
379PhosphorylationYESSEDCSEAAGSPA
CCCCCHHHHHCCCCC		42.4623927012
384PhosphorylationDCSEAAGSPARKVKM
HHHHHCCCCCHHHCC		25.5520201521
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 ALKB5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALKB5_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 ALKB5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ALKB5_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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALKB5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-64 AND SER-69, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132 AND LYS-235, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; TYR-71 AND SER-374,AND MASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-64 AND SER-69, AND MASS SPECTROMETRY.
"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-64; SER-69 AND SER-361,AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASSSPECTROMETRY.
"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-361, AND MASSSPECTROMETRY.

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