KDM1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KDM1A_MOUSE
• UniProt AC: Q6ZQ88
• Protein Name: Lysine-specific histone demethylase 1A
• Gene Name: Kdm1a
• Organism: Mus musculus (Mouse).
• Sequence Length: 853
• Subcellular Localization: Nucleus.
• Protein Description: Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation (By similarity). Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7..
• Protein Sequence: MLSGKKAAAAAAAAAAAAAAGTEAGSGAAGGAENGSEVAAPPAGLTGPTDMATGAAGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTAGPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPIKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM

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
3	Phosphorylation	-----MLSGKKAAAA -----CCCHHHHHHH	47.47	22006019
5	Acetylation	---MLSGKKAAAAAA ---CCCHHHHHHHHH	35.54	22902405
22	Phosphorylation	AAAAAAGTEAGSGAA HHHHHHCCCCCCCCC	20.24	25619855
26	Phosphorylation	AAGTEAGSGAAGGAE HHCCCCCCCCCCCCC	32.10	25619855
36	Phosphorylation	AGGAENGSEVAAPPA CCCCCCCCCCCCCCC	40.24	25619855
46	Phosphorylation	AAPPAGLTGPTDMAT CCCCCCCCCCCCCCC	39.95	25619855
49	Phosphorylation	PAGLTGPTDMATGAA CCCCCCCCCCCCCCC	39.49	25619855
53	Phosphorylation	TGPTDMATGAAGERT CCCCCCCCCCCCCCC	22.25	25619855
60	Phosphorylation	TGAAGERTPRKKEPP CCCCCCCCCCCCCCC	24.12	25619855
70	Phosphorylation	KKEPPRASPPGGLAE CCCCCCCCCCCCCCC	32.67	27087446
81	Phosphorylation	GLAEPPGSAGPQAGP CCCCCCCCCCCCCCC	35.51	25619855
89	Phosphorylation	AGPQAGPTAGPGSAT CCCCCCCCCCCCCCC	43.24	25619855
94	Phosphorylation	GPTAGPGSATPMETG CCCCCCCCCCCCCCC	31.91	25619855
96	Phosphorylation	TAGPGSATPMETGIA CCCCCCCCCCCCCCC	25.51	25619855
100	Phosphorylation	GSATPMETGIAETPE CCCCCCCCCCCCCCC	27.86	25619855
105	Phosphorylation	METGIAETPEGRRTS CCCCCCCCCCCCCCC	20.02	25619855
112	Phosphorylation	TPEGRRTSRRKRAKV CCCCCCCCHHHHHHH	28.42	-
121	Phosphorylation	RKRAKVEYREMDESL HHHHHHHHHHHHHHH	18.17	23984901
127	Phosphorylation	EYREMDESLANLSED HHHHHHHHHHCCCHH	28.63	22802335
132	Phosphorylation	DESLANLSEDEYYSE HHHHHCCCHHHHCCH	42.69	25521595
136	Phosphorylation	ANLSEDEYYSEEERN HCCCHHHHCCHHHHH	25.31	21082442
137	Phosphorylation	NLSEDEYYSEEERNA CCCHHHHCCHHHHHH	13.93	27087446
138	Phosphorylation	LSEDEYYSEEERNAK CCHHHHCCHHHHHHH	37.32	27087446
167	Phosphorylation	PPEEENESEPEEPSG CCCCCCCCCCCCCCC	70.77	27087446
173	Phosphorylation	ESEPEEPSGVEGAAF CCCCCCCCCCCHHHH	59.77	22942356
182	Phosphorylation	VEGAAFQSRLPHDRM CCHHHHHHCCCCCCC	29.36	25619855
336	Phosphorylation	DLGAMVVTGLGGNPM ECCCEEEECCCCCCH	18.45	27357545
347	Phosphorylation	GNPMAVVSKQVNMEL CCCHHHEEHHHCHHH	15.69	27357545
612	Phosphorylation	AVNTRSTSQTFIYKC EEECCCCCCCEEEEC	28.59	-
808	Phosphorylation	GEHTIRNYPATVHGA CCCCHHCCCHHHHHH	5.61	20495213
811	Phosphorylation	TIRNYPATVHGALLS CHHCCCHHHHHHHHH	14.45	20495213
842	Phosphorylation	YTLPRQATPGVPAQQ HCCCCCCCCCCCCCC	16.55	22006019
850	Phosphorylation	PGVPAQQSPSM---- CCCCCCCCCCC----	13.58	25521595
852	Phosphorylation	VPAQQSPSM------ CCCCCCCCC------	42.23	29895711

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
112	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KDM1A_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KDM1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NANOG_MOUSE	Nanog	physical	18454139
ANDR_MOUSE	Ar	physical	16079795
KDM4C_MOUSE	Kdm4c	physical	17277772
ANDR_MOUSE	Ar	physical	17277772
MEF2D_MOUSE	Mef2d	physical	20833138
MYOD1_MOUSE	Myod1	physical	20833138
CAF1A_MOUSE	Chaf1a	physical	26365490

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.