H2A1F_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2A1F_MOUSE
• UniProt AC: Q8CGP5
• Protein Name: Histone H2A type 1-F
• Gene Name: Hist1h2af
• Organism: Mus musculus (Mouse).
• Sequence Length: 130
• Subcellular Localization: Nucleus. Chromosome.
• Protein Description: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling..
• Protein Sequence: MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKPKGK

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
2	Phosphorylation	------MSGRGKQGG ------CCCCCCCCC	36.88	7217105
2	Acetylation	------MSGRGKQGG ------CCCCCCCCC	36.88	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	-
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	16699504
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	-
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCCHHCH	44.39	13553831
6	Other	--MSGRGKQGGKARA --CCCCCCCCCHHCH	44.39	27105115
10	Acetylation	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	13553821
10	Lactoylation	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	24681537
14	Acetylation	QGGKARAKAKTRSSR CCCHHCHHHHHHHHC	44.88	15612627
17	Phosphorylation	KARAKAKTRSSRAGL HHCHHHHHHHHCCCC	40.41	26643407
19	Phosphorylation	RAKAKTRSSRAGLQF CHHHHHHHHCCCCCC	29.43	26643407
20	Phosphorylation	AKAKTRSSRAGLQFP HHHHHHHHCCCCCCC	23.90	26643407
37	N6-crotonyl-L-lysine	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
37	Crotonylation	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	21925322
37	Other	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	27105115
37	Ubiquitination	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
51	Phosphorylation	VGAGAPVYLAAVLEY CCCCHHHHHHHHHHH	6.92	26239621
58	Phosphorylation	YLAAVLEYLTAEILE HHHHHHHHHHHHHHH	12.75	26239621
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	24681537
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	24681537
96	Acetylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	15604215
96	Ubiquitination	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	27667366
96	Other	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	24681537
96	Glutarylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	-
102	Phosphorylation	NKLLGRVTIAQGGVL HHHHCCEEECCCCCC	14.83	27180971
105	Methylation	LGRVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	24352239
119	Ubiquitination	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	27667366
119	Crotonylation	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	21925322
119	Other	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	24681537
119	Glutarylation	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	-
119	"N6,N6-dimethyllysine"	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	-
119	Acetylation	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	13553827
119	Methylation	IQAVLLPKKTESHHK EEEEECCCCCCCCCC	72.76	-
120	Ubiquitination	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	15509584
120	Crotonylation	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	15509584
120	Glutarylation	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	-
120	Acetylation	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	13553825
120	N6-crotonyl-L-lysine	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	-
120	Other	QAVLLPKKTESHHKP EEEECCCCCCCCCCC	56.43	27105115
121	Phosphorylation	AVLLPKKTESHHKPK EEECCCCCCCCCCCC	49.17	25266776
123	Phosphorylation	LLPKKTESHHKPKGK ECCCCCCCCCCCCCC	35.80	25266776
126	Other	KKTESHHKPKGK--- CCCCCCCCCCCC---	42.89	27105115
126	N6-crotonyl-L-lysine	KKTESHHKPKGK--- CCCCCCCCCCCC---	42.89	-
126	Ubiquitination	KKTESHHKPKGK--- CCCCCCCCCCCC---	42.89	-
126	Crotonylation	KKTESHHKPKGK--- CCCCCCCCCCCC---	42.89	-
126	Glutarylation	KKTESHHKPKGK--- CCCCCCCCCCCC---	42.89	-
128	Ubiquitination	TESHHKPKGK----- CCCCCCCCCC-----	81.68	-

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
2	S	Phosphorylation	Kinase	RPS6KA5	Q8C050	Uniprot
121	T	Phosphorylation	Kinase	DCAF1	Q80TR8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	S	Acetylation	Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.	-
2	S	Phosphorylation	Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.	-
2	S	Phosphorylation	Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.	-
2	S	Phosphorylation	Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription.	-
4	R	Methylation	Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.	16699504
14	K	ubiquitylation	Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.	15509584
16	K	ubiquitylation	Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.	15509584
27	K	Methylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	15509584
27	K	ubiquitylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	15509584
63	K	ubiquitylation	Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage.	15509584
105	Q	Methylation	Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I.	24352239
120	K	ubiquitylation	Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals.	15525528
121	T	Phosphorylation	Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2A1F_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of H2A1F_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Ubiquitylation

"Ring1b-mediated H2A ubiquitination associates with inactive Xchromosomes and is involved in initiation of X inactivation.";
Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
J. Biol. Chem. 279:52812-52815(2004).
Cited for: UBIQUITINATION AT LYS-120.
PubMed: 15509584

"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2Ato heritable gene silencing and X inactivation.";
de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M.,Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H.,Brockdorff N.;
Dev. Cell 7:663-676(2004).
Cited for: UBIQUITINATION AT LYS-120.
PubMed: 15525528