dbPTM

HMGB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGB2_MOUSE
UniProt AC	P30681
Protein Name	High mobility group protein B2
Gene Name	Hmgb2
Organism	Mus musculus (Mouse).
Sequence Length	210
Subcellular Localization	Nucleus . Chromosome . Cytoplasm . Secreted .
Protein Description	Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (By similarity). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). [PubMed: 9184213 Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors]
Protein Sequence	MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDLAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSENRPKIKIEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEEEEDDEEEEEDEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MGKGDPNKPR -----CCCCCCCCCC	59.86	-
12	Acetylation	DPNKPRGKMSSYAFF CCCCCCCCHHHHHHH	36.57	129513
14	Phosphorylation	NKPRGKMSSYAFFVQ CCCCCCHHHHHHHHH	24.55	20139300
15	Phosphorylation	KPRGKMSSYAFFVQT CCCCCHHHHHHHHHH	19.58	25293948
16	Phosphorylation	PRGKMSSYAFFVQTC CCCCHHHHHHHHHHH	10.50	26643407
23	Cysteine derivative	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
23	S-nitrosylation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	21278135
23	Oxidation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
29	Acetylation	TCREEHKKKHPDSSV HHHHHHHHHCCCCCC	59.21	22826441
30	Acetylation	CREEHKKKHPDSSVN HHHHHHHHCCCCCCC	66.24	23806337
34	Phosphorylation	HKKKHPDSSVNFAEF HHHHCCCCCCCHHHH	40.41	28833060
35	Phosphorylation	KKKHPDSSVNFAEFS HHHCCCCCCCHHHHH	28.58	14729942
42	Phosphorylation	SVNFAEFSKKCSERW CCCHHHHHHHHHHHH	23.78	18779572
43	Acetylation	VNFAEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	-
45	Cysteine derivative	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
45	Oxidation	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
50	Ubiquitination	KKCSERWKTMSAKEK HHHHHHHHHCCHHHH	40.34	27667366
50	Malonylation	KKCSERWKTMSAKEK HHHHHHHHHCCHHHH	40.34	26320211
51	Phosphorylation	KCSERWKTMSAKEKS HHHHHHHHCCHHHHH	14.92	-
53	Phosphorylation	SERWKTMSAKEKSKF HHHHHHCCHHHHHHH	41.23	-
55	Acetylation	RWKTMSAKEKSKFED HHHHCCHHHHHHHHH	59.37	129521
59	Acetylation	MSAKEKSKFEDLAKS CCHHHHHHHHHHHHH	64.93	23806337
65	Acetylation	SKFEDLAKSDKARYD HHHHHHHHHHHHHHH	67.49	19861841
66	Phosphorylation	KFEDLAKSDKARYDR HHHHHHHHHHHHHHH	38.44	28066266
82	Acetylation	MKNYVPPKGDKKGKK HHHCCCCCCCCCCCC	73.92	23806337
85	Acetylation	YVPPKGDKKGKKKDP CCCCCCCCCCCCCCC	72.58	23806337
90	Acetylation	GDKKGKKKDPNAPKR CCCCCCCCCCCCCCC	80.19	-
100	Phosphorylation	NAPKRPPSAFFLFCS CCCCCCCCEEEEEEE	40.15	26239621
106	Oxidation	PSAFFLFCSENRPKI CCEEEEEEECCCCCC	5.62	-
106	Cysteine derivative	PSAFFLFCSENRPKI CCEEEEEEECCCCCC	5.62	-
106	Glutathionylation	PSAFFLFCSENRPKI CCEEEEEEECCCCCC	5.62	24333276
114	Ubiquitination	SENRPKIKIEHPGLS ECCCCCCEEECCCCC	48.44	-
114	Acetylation	SENRPKIKIEHPGLS ECCCCCCEEECCCCC	48.44	23806337
121	Phosphorylation	KIEHPGLSIGDTAKK EEECCCCCHHHHHHH	30.36	29514104
128	Ubiquitination	SIGDTAKKLGEMWSE CHHHHHHHHHHHHCH	60.30	-
128	Succinylation	SIGDTAKKLGEMWSE CHHHHHHHHHHHHCH	60.30	23806337
128	Acetylation	SIGDTAKKLGEMWSE CHHHHHHHHHHHHCH	60.30	23806337
134	Phosphorylation	KKLGEMWSEQSAKDK HHHHHHHCHHHHCCC	25.17	25890499
137	Phosphorylation	GEMWSEQSAKDKQPY HHHHCHHHHCCCCCH	32.98	25890499
139	Acetylation	MWSEQSAKDKQPYEQ HHCHHHHCCCCCHHH	71.37	70405
139	Ubiquitination	MWSEQSAKDKQPYEQ HHCHHHHCCCCCHHH	71.37	-
141	Acetylation	SEQSAKDKQPYEQKA CHHHHCCCCCHHHHH	53.09	-
141	Ubiquitination	SEQSAKDKQPYEQKA CHHHHCCCCCHHHHH	53.09	-
147	Ubiquitination	DKQPYEQKAAKLKEK CCCCHHHHHHHHHHH	38.07	-
147	Acetylation	DKQPYEQKAAKLKEK CCCCHHHHHHHHHHH	38.07	23806337
154	Ubiquitination	KAAKLKEKYEKDIAA HHHHHHHHHHHHHHH	58.06	-
154	Acetylation	KAAKLKEKYEKDIAA HHHHHHHHHHHHHHH	58.06	22826441
157	Ubiquitination	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	27667366
157	Malonylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	26320211
157	Succinylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	23806337
157	Acetylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	22826441
162	Phosphorylation	YEKDIAAYRAKGKSE HHHHHHHHHHCCCCC	11.33	-
179	Phosphorylation	KKGPGRPTGSKKKNE CCCCCCCCCCCCCCC	53.37	27149854
181	Phosphorylation	GPGRPTGSKKKNEPE CCCCCCCCCCCCCCC	43.72	23375375
182	Acetylation	PGRPTGSKKKNEPED CCCCCCCCCCCCCCC	69.94	129517

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 HMGB2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
23	C	Oxidation	-
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
45	C	Oxidation	-
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
106	C	Oxidation	-
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).

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 HMGB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
LEF1_MOUSE	Lef1	physical	19805379
CTNB1_MOUSE	Ctnnb1	physical	19805379

Drug and Disease Associations

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

Regulatory Network of HMGB2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.	14729942 [Abstract]

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