Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Probable alpha-ketoglutarate-dependent dioxygenase ABH5  

UniProtKB / Swiss-Prot ID :  ALKB5_HUMAN

Gene Name (Synonyms) : 
ALKBH5, ABH5, OFOXD1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Membrane; Single-pass membrane protein (Potential). 

Protein Function :  Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). 

Transmembrane Topology (topPTM) : ALKB5_HUMAN 

Protein Sequence MAAASGYTDLREKLKSMTSRDNYKAGSREAAAAAAAAVAAAAAAAAAAEPYPVSGAKRKYQEDSDPERSD...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCCHHHCCCCCCCCCHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAASG
---CCCCCH
16.25UniProtKB
Link-
54PhosphoserinePYPVSGAKR
CCCCCCHHH
28.64HPRD
Link-
54PhosphoserinePYPVSGAKR
CCCCCCHHH
28.64Phosphositeplus
Link-
64PhosphoserineYQEDSDPER
CCCCCCCCH
55.07HPRD
Link-
64PhosphoserineYQEDSDPER
CCCCCCCCH
55.07PhosphoELM
Link-
64PhosphoserineYQEDSDPER
CCCCCCCCH
55.07Phosphositeplus
Link-
64PhosphoserineYQEDSDPER
CCCCCCCCH
55.07SysPTM
Link-
64Phosphoserine.YQEDSDPER
CCCCCCCCH
55.07UniProtKB
Link-
69PhosphoserineDPERSDYEE
CCCHHHHHH
42.77HPRD
Link
69PhosphoserineDPERSDYEE
CCCHHHHHH
42.77PhosphoELM
Link
69PhosphoserineDPERSDYEE
CCCHHHHHH
42.77Phosphositeplus
Link
69PhosphoserineDPERSDYEE
CCCHHHHHH
42.77SysPTM
Link
69Phosphoserine.DPERSDYEE
CCCHHHHHH
42.77UniProtKB
Link
71PhosphotyrosineERSDYEEQQ
CHHHHHHCC
23.70HPRD
Link
71PhosphotyrosineERSDYEEQQ
CHHHHHHCC
23.70Phosphositeplus
Link
71Phosphotyrosine.ERSDYEEQQ
CHHHHHHCC
23.70UniProtKB
Link
132N6-acetyllysinePLRNKYFFG
CCCCCEEEC
36.68HPRD
Link
132N6-acetyllysinePLRNKYFFG
CCCCCEEEC
36.68Phosphositeplus
Link
132N6-acetyllysine.PLRNKYFFG
CCCCCEEEC
36.68UniProtKB
Link
147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AQLQKRGPG
HHHHCCCCC
68.84Phosphositeplus
Link-
235N6-acetyllysineKFQFKPIRV
EEEEEEEEE
28.84HPRD
Link
235N6-acetyllysineKFQFKPIRV
EEEEEEEEE
28.84Phosphositeplus
Link
235N6-acetyllysine.KFQFKPIRV
EEEEEEEEE
28.84UniProtKB
Link
294PhosphothreoninePRLETKSLS
CCHHHHHCC
30.44Phosphositeplus
Link-
296PhosphoserineLETKSLSSS
HHHHHCCCC
40.69Phosphositeplus
Link-
350PhosphoserineENRRSVLLP
CCCCEECCC
17.55HPRD
Link-
350PhosphoserineENRRSVLLP
CCCCEECCC
17.55SysPTM
Link-
361PhosphoserineRRRGSFSSE
CCCCCCCCH
21.83HPRD
Link-
361PhosphoserineRRRGSFSSE
CCCCCCCCH
21.83PhosphoELM
Link-
361PhosphoserineRRRGSFSSE
CCCCCCCCH
21.83Phosphositeplus
Link-
361PhosphoserineRRRGSFSSE
CCCCCCCCH
21.83SysPTM
Link-
361Phosphoserine.RRRGSFSSE
CCCCCCCCH
21.83UniProtKB
Link-
363PhosphoserineRGSFSSENY
CCCCCCHHH
38.14HPRD
Link-
363PhosphoserineRGSFSSENY
CCCCCCHHH
38.14SysPTM
Link-
374Phosphoserine.KSYESSEDC
HHCCCCCCC
30.69UniProtKB
Link-
375PhosphoserineSYESSEDCS
HCCCCCCCH
26.05HPRD
Link-
375PhosphoserineSYESSEDCS
HCCCCCCCH
26.05PhosphoELM
Link-
379PhosphoserineSEDCSEAAG
CCCCHHCCC
42.46HPRD
Link-
384PhosphoserineEAAGSPGNS
HCCCCCCCC
25.55HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures