HMGN3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HMGN3_HUMAN
• UniProt AC: Q15651
• Protein Name: High mobility group nucleosome-binding domain-containing protein 3
• Gene Name: HMGN3
• Organism: Homo sapiens (Human).
• Sequence Length: 99
• Subcellular Localization: Nucleus.
• Protein Description: Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity)..
• Protein Sequence: MPKRKSPENTEGKDGSKVTKQEPTRRSARLSAKPAPPKPEPKPRKTSAKKEPGAKISRGAKGKKEEKQEAGKEGTAPSENGETKAEEAQKTESVDNEGE

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
6	Phosphorylation	--MPKRKSPENTEGK --CCCCCCCCCCCCC	41.29	22167270
6 (in isoform 2)	Phosphorylation	-	41.29	-
10	Phosphorylation	KRKSPENTEGKDGSK CCCCCCCCCCCCCCC	44.44	28176443
10 (in isoform 2)	Phosphorylation	-	44.44	-
13 (in isoform 2)	Ubiquitination	-	53.32	21906983
13 (in isoform 1)	Ubiquitination	-	53.32	21906983
13	Acetylation	SPENTEGKDGSKVTK CCCCCCCCCCCCCCC	53.32	23954790
13	Ubiquitination	SPENTEGKDGSKVTK CCCCCCCCCCCCCCC	53.32	21906983
16	Phosphorylation	NTEGKDGSKVTKQEP CCCCCCCCCCCCCCC	33.80	24732914
17	Acetylation	TEGKDGSKVTKQEPT CCCCCCCCCCCCCCC	60.50	26051181
19	Phosphorylation	GKDGSKVTKQEPTRR CCCCCCCCCCCCCHH	30.65	24719451
27	Phosphorylation	KQEPTRRSARLSAKP CCCCCHHHHHHCCCC	17.91	25159151
27 (in isoform 2)	Phosphorylation	-	17.91	-
31	Phosphorylation	TRRSARLSAKPAPPK CHHHHHHCCCCCCCC	28.79	23401153
31 (in isoform 2)	Phosphorylation	-	28.79	-
33	Acetylation	RSARLSAKPAPPKPE HHHHHCCCCCCCCCC	38.03	19608861
33 (in isoform 2)	Acetylation	-	38.03	-
33	Ubiquitination	RSARLSAKPAPPKPE HHHHHCCCCCCCCCC	38.03	19608861
38	Ubiquitination	SAKPAPPKPEPKPRK CCCCCCCCCCCCCCC	62.04	19608861
38	Sumoylation	SAKPAPPKPEPKPRK CCCCCCCCCCCCCCC	62.04	-
38 (in isoform 2)	Acetylation	-	62.04	-
38	Acetylation	SAKPAPPKPEPKPRK CCCCCCCCCCCCCCC	62.04	19608861
38	Sumoylation	SAKPAPPKPEPKPRK CCCCCCCCCCCCCCC	62.04	19608861
55 (in isoform 2)	Ubiquitination	-	47.32	21906983
55 (in isoform 1)	Ubiquitination	-	47.32	21906983
55	Acetylation	AKKEPGAKISRGAKG CCCCCCCCCCCCCCC	47.32	25953088
55	Ubiquitination	AKKEPGAKISRGAKG CCCCCCCCCCCCCCC	47.32	21906983
57	Phosphorylation	KEPGAKISRGAKGKK CCCCCCCCCCCCCCH	24.77	29496963
72	Acetylation	EEKQEAGKEGTAPSE HHHHHHCCCCCCCCC	61.08	26051181
75	Phosphorylation	QEAGKEGTAPSENGE HHHCCCCCCCCCCCC	36.16	30266825
78	Phosphorylation	GKEGTAPSENGETKA CCCCCCCCCCCCCHH	41.03	29255136
83	Phosphorylation	APSENGETKAEEAQK CCCCCCCCHHHHHHH	36.63	30266825
84	Ubiquitination	PSENGETKAEEAQKT CCCCCCCHHHHHHHH	49.88	-
84	Acetylation	PSENGETKAEEAQKT CCCCCCCHHHHHHHH	49.88	26051181
90	Ubiquitination	TKAEEAQKTESVDNE CHHHHHHHHHCCCCC	62.40	19608861
90 (in isoform 1)	Ubiquitination	-	62.40	21906983
90	Acetylation	TKAEEAQKTESVDNE CHHHHHHHHHCCCCC	62.40	19608861
91	Phosphorylation	KAEEAQKTESVDNEG HHHHHHHHHCCCCCC	22.78	23401153
93	Phosphorylation	EEAQKTESVDNEGE- HHHHHHHCCCCCCC-	39.75	29255136
103	Phosphorylation	NEGE----------- CCCC-----------		24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HMGN3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HMGN3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HMGN3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of HMGN3_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-33; LYS-38 AND LYS-90, ANDMASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-27; SER-31 AND SER-93,AND MASS SPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND MASSSPECTROMETRY.
PubMed: 17081983