KDM6A_MOUSE - dbPTM
KDM6A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM6A_MOUSE
UniProt AC O70546
Protein Name Lysine-specific demethylase 6A
Gene Name Kdm6a
Organism Mus musculus (Mouse).
Sequence Length 1401
Subcellular Localization Nucleus .
Protein Description Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (By similarity). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression. [PubMed: 21095589]
Protein Sequence MKSCGVSLATAAAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATILQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAPPPVEQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGILNGPTVDSSLPTNSVSGQQPQLPLTRMPSVSQPGVHTACPRQTLANGPFSAGHVPCSTSRTLGSTDTVLIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGPSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTVPETSRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDKVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQNVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
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
290PhosphorylationPNSGQSWYFLGRCYS
CCCCCCEEECCHHHH
8.32-
397UbiquitinationSGLAARIKYLQAQLC
CHHHHHHHHHHHHHC
34.06-
519MethylationQTGVAQVRPTGILNG
HHCCCCCCCCCCCCC
15.8124129315
549MethylationQPQLPLTRMPSVSQP
CCCCCCCCCCCCCCC
42.5724129315
554O-linked_GlycosylationLTRMPSVSQPGVHTA
CCCCCCCCCCCCCCC
34.6930059200
719AcetylationITLTKESKPSGNTLT
EEEECCCCCCCCEEE
44.2723954790
769PhosphorylationPSHGDSKSPGLLSSD
CCCCCCCCCCCCCCC
28.3121082442
774PhosphorylationSKSPGLLSSDNPQLS
CCCCCCCCCCCHHHH
40.4621183079
775PhosphorylationKSPGLLSSDNPQLSA
CCCCCCCCCCHHHHH
41.1823984901
781PhosphorylationSSDNPQLSALLMGKA
CCCCHHHHHHHHCCC
16.1828285833
799AcetylationVGPGTCDKVNNIHPT
CCCCCCCCCCCCCCE
49.3523806337
806PhosphorylationKVNNIHPTVHTKTDN
CCCCCCCEEECCCCC
15.68-
809PhosphorylationNIHPTVHTKTDNSVA
CCCCEEECCCCCCCC
31.16-
811PhosphorylationHPTVHTKTDNSVASS
CCEEECCCCCCCCCC
41.3826239621
814PhosphorylationVHTKTDNSVASSPSS
EECCCCCCCCCCCCC
23.1326239621
817PhosphorylationKTDNSVASSPSSAIS
CCCCCCCCCCCCCCC
40.4028833060
818PhosphorylationTDNSVASSPSSAIST
CCCCCCCCCCCCCCC
21.0424723360
820PhosphorylationNSVASSPSSAISTAT
CCCCCCCCCCCCCCC
34.0628833060
821PhosphorylationSVASSPSSAISTATP
CCCCCCCCCCCCCCC
32.7628833060
824PhosphorylationSSPSSAISTATPSPK
CCCCCCCCCCCCCCC
16.2328833060
825PhosphorylationSPSSAISTATPSPKS
CCCCCCCCCCCCCCC
28.5628833060
827PhosphorylationSSAISTATPSPKSTE
CCCCCCCCCCCCCCC
25.1228833060
829PhosphorylationAISTATPSPKSTEQT
CCCCCCCCCCCCCCC
40.3724723360
846PhosphorylationNSVTSLNSPHSGLHT
CCCCCCCCCCCCCEE
29.3225338131
864PhosphorylationEGMEESQSPIKTDLL
CCCCCCCCCCCCCEE
37.5625338131
874PhosphorylationKTDLLLVSHRPSPQI
CCCEEEEECCCCCCC
17.4726643407
878PhosphorylationLLVSHRPSPQIIPSM
EEEECCCCCCCCCCC
29.4126643407
940PhosphorylationKDKLNPPTPSIYLEN
CCCCCCCCCCEECCC
30.8128066266
942PhosphorylationKLNPPTPSIYLENKR
CCCCCCCCEECCCCC
26.7528066266
944PhosphorylationNPPTPSIYLENKRDA
CCCCCCEECCCCCCC
16.5828066266
1055PhosphorylationREENEKRSHHKDHSD
HHHHHHHHCCCCCCC
40.80-
1061PhosphorylationRSHHKDHSDSESTSS
HHCCCCCCCCCCCCC
53.6327087446
1063PhosphorylationHHKDHSDSESTSSDN
CCCCCCCCCCCCCCC
36.1423375375
1065PhosphorylationKDHSDSESTSSDNSG
CCCCCCCCCCCCCCC
37.2323684622
1066PhosphorylationDHSDSESTSSDNSGK
CCCCCCCCCCCCCCC
28.3523684622
1067PhosphorylationHSDSESTSSDNSGKR
CCCCCCCCCCCCCCC
45.0023684622
1068PhosphorylationSDSESTSSDNSGKRR
CCCCCCCCCCCCCCC
40.6823684622
1303S-nitrosylationLLRTLKQCQTLREAL
HHHHHHHHHHHHHHH
2.9721278135
1303S-nitrosocysteineLLRTLKQCQTLREAL
HHHHHHHHHHHHHHH
2.97-

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 KDM6A_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM6A_MOUSE !!

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 KDM6A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KDM6A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KDM6A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND MASSSPECTROMETRY.

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