KDM4D_HUMAN - dbPTM
KDM4D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM4D_HUMAN
UniProt AC Q6B0I6
Protein Name Lysine-specific demethylase 4D
Gene Name KDM4D
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Nucleus .
Protein Description Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate..
Protein Sequence METMKSKANCAQNPNCNIMIFHPTKEEFNDFDKYIAYMESQGAHRAGLAKIIPPKEWKARETYDNISEILIATPLQQVASGRAGVFTQYHKKKKAMTVGEYRHLANSKKYQTPPHQNFEDLERKYWKNRIYNSPIYGADISGSLFDENTKQWNLGHLGTIQDLLEKECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHLGEPKTWYVVPPEHGQRLERLARELFPGSSRGCGAFLRHKVALISPTVLKENGIPFNRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGEARVTFSMDAFVRILQPERYDLWKRGQDRAVVDHMEPRVPASQELSTQKEVQLPRRAALGLRQLPSHWARHSPWPMAARSGTRCHTLVCSSLPRRSAVSGTATQPRAAAVHSSKKPSSTPSSTPGPSAQIIHPSNGRRGRGRPPQKLRAQELTLQTPAKRPLLAGTTCTASGPEPEPLPEDGALMDKPVPLSPGLQHPVKASGCSWAPVP
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
3Phosphorylation-----METMKSKANC
-----CCCHHHHCCC
28.7122210691
6Phosphorylation--METMKSKANCAQN
--CCCHHHHCCCCCC
26.6122210691
26ADP-ribosylationMIFHPTKEEFNDFDK
EEECCCHHHHCCHHH
71.0123102699
26PolyADP-ribosyl glutamic acidMIFHPTKEEFNDFDK
EEECCCHHHHCCHHH
71.01-
27PolyADP-ribosyl glutamic acidIFHPTKEEFNDFDKY
EECCCHHHHCCHHHH
51.83-
27ADP-ribosylationIFHPTKEEFNDFDKY
EECCCHHHHCCHHHH
51.8323102699
33UbiquitinationEEFNDFDKYIAYMES
HHHCCHHHHHHHHHH
38.2529967540
55UbiquitinationLAKIIPPKEWKARET
CCCCCCCHHHHHHHH
71.50-
94UbiquitinationTQYHKKKKAMTVGEY
HHHHHHCCCCCHHHH
52.88-
303PhosphorylationATPRWIDYGKMASQC
CCCCCCCHHHHHHCC
14.98-
362UbiquitinationSQELSTQKEVQLPRR
HHHCCCCCCCCCCHH
61.00-
395PhosphorylationPMAARSGTRCHTLVC
CCCCCCCCCEEEEEE
31.22-
403PhosphorylationRCHTLVCSSLPRRSA
CEEEEEECCCCCCCC
27.6829262532
404PhosphorylationCHTLVCSSLPRRSAV
EEEEEECCCCCCCCC
36.9524719451
409PhosphorylationCSSLPRRSAVSGTAT
ECCCCCCCCCCCCCC
34.0119007248
412PhosphorylationLPRRSAVSGTATQPR
CCCCCCCCCCCCCCC
30.0922210691
414PhosphorylationRRSAVSGTATQPRAA
CCCCCCCCCCCCCCC
21.0122210691
416PhosphorylationSAVSGTATQPRAAAV
CCCCCCCCCCCCCCC
38.66-
469PhosphorylationAQELTLQTPAKRPLL
HHEEECCCCCCCCCC
28.4628555341
505PhosphorylationMDKPVPLSPGLQHPV
CCCCCCCCCCCCCCC
15.7329978859

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 KDM4D_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM4D_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 KDM4D_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM4D_HUMANKDM4Dphysical
17207460
ANDR_HUMANARphysical
17555712
P53_HUMANTP53physical
22514644

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 KDM4D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASSSPECTROMETRY.

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