dbPTM

HMGB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGB1_MOUSE
UniProt AC	P63158
Protein Name	High mobility group protein B1
Gene Name	Hmgb1
Organism	Mus musculus (Mouse).
Sequence Length	215
Subcellular Localization	Nucleus . Cytoplasm . Secreted . Chromosome . Cell membrane Peripheral membrane protein Extracellular side . Endosome . Endoplasmic reticulum-Golgi intermediate compartment . In basal state predominantly nuclear. Shuttles between the cytoplasm an
Protein Description	Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. [PubMed: 23519706]
Protein Sequence	MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MGKGDPKKPR -----CCCCCCCCCC	59.86	14532127
7	Acetylation	-MGKGDPKKPRGKMS -CCCCCCCCCCCCCH	78.96	14532127
8	Acetylation	MGKGDPKKPRGKMSS CCCCCCCCCCCCCHH	45.39	14532127
12	Acetylation	DPKKPRGKMSSYAFF CCCCCCCCCHHHHHH	36.57	22826441
14	Phosphorylation	KKPRGKMSSYAFFVQ CCCCCCCHHHHHHHH	24.55	20139300
15	Phosphorylation	KPRGKMSSYAFFVQT CCCCCCHHHHHHHHH	19.58	25293948
16	Phosphorylation	PRGKMSSYAFFVQTC CCCCCHHHHHHHHHH	10.50	26643407
23	Oxidation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
23	Cysteine derivative	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
28	Acetylation	QTCREEHKKKHPDAS HHHHHHHHHHCCCCC	67.79	14532127
29	Acetylation	TCREEHKKKHPDASV HHHHHHHHHCCCCCC	59.21	14532127
30	Malonylation	CREEHKKKHPDASVN HHHHHHHHCCCCCCC	66.24	26320211
30	Ubiquitination	CREEHKKKHPDASVN HHHHHHHHCCCCCCC	66.24	-
30	Acetylation	CREEHKKKHPDASVN HHHHHHHHCCCCCCC	66.24	23806337
35	Phosphorylation	KKKHPDASVNFSEFS HHHCCCCCCCHHHHH	25.60	25521595
39	Phosphorylation	PDASVNFSEFSKKCS CCCCCCHHHHHHHHH	32.31	28833060
42	Phosphorylation	SVNFSEFSKKCSERW CCCHHHHHHHHHHHH	27.44	28833060
43	Ubiquitination	VNFSEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	22790023
43	Acetylation	VNFSEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	23806337
45	Cysteine derivative	FSEFSKKCSERWKTM HHHHHHHHHHHHHCC	6.16	-
45	Oxidation	FSEFSKKCSERWKTM HHHHHHHHHHHHHCC	6.16	-
50	Malonylation	KKCSERWKTMSAKEK HHHHHHHHCCCHHHC	40.34	26320211
51	Phosphorylation	KCSERWKTMSAKEKG HHHHHHHCCCHHHCC	14.92	-
53	Phosphorylation	SERWKTMSAKEKGKF HHHHHCCCHHHCCCH	41.23	-
55	Acetylation	RWKTMSAKEKGKFED HHHCCCHHHCCCHHH	53.29	129713
59	Malonylation	MSAKEKGKFEDMAKA CCHHHCCCHHHHHHH	57.56	26320211
59	Acetylation	MSAKEKGKFEDMAKA CCHHHCCCHHHHHHH	57.56	21728379
65	Acetylation	GKFEDMAKADKARYE CCHHHHHHHHHHHHH	50.94	22826441
65	Malonylation	GKFEDMAKADKARYE CCHHHHHHHHHHHHH	50.94	26320211
75	Sulfoxidation	KARYEREMKTYIPPK HHHHHHHHHHCCCCC	5.01	21406390
76	Ubiquitination	ARYEREMKTYIPPKG HHHHHHHHHCCCCCC	33.16	22790023
82	Ubiquitination	MKTYIPPKGETKKKF HHHCCCCCCCCCCCC	65.11	22790023
88	Acetylation	PKGETKKKFKDPNAP CCCCCCCCCCCCCCC	60.24	23806337
90	Acetylation	GETKKKFKDPNAPKR CCCCCCCCCCCCCCC	79.67	23806337
90	Malonylation	GETKKKFKDPNAPKR CCCCCCCCCCCCCCC	79.67	26320211
90	Ubiquitination	GETKKKFKDPNAPKR CCCCCCCCCCCCCCC	79.67	-
100	Phosphorylation	NAPKRPPSAFFLFCS CCCCCCCCCEEHHCC	40.15	26239621
106	Glutathionylation	PSAFFLFCSEYRPKI CCCEEHHCCCCCCCC	3.08	24333276
106	Oxidation	PSAFFLFCSEYRPKI CCCEEHHCCCCCCCC	3.08	-
106	S-palmitoylation	PSAFFLFCSEYRPKI CCCEEHHCCCCCCCC	3.08	26165157
106	Cysteine derivative	PSAFFLFCSEYRPKI CCCEEHHCCCCCCCC	3.08	-
114	Malonylation	SEYRPKIKGEHPGLS CCCCCCCCCCCCCCC	65.46	26320211
114	Ubiquitination	SEYRPKIKGEHPGLS CCCCCCCCCCCCCCC	65.46	-
114	Acetylation	SEYRPKIKGEHPGLS CCCCCCCCCCCCCCC	65.46	23806337
121	Phosphorylation	KGEHPGLSIGDVAKK CCCCCCCCHHHHHHH	30.36	29514104
127	Acetylation	LSIGDVAKKLGEMWN CCHHHHHHHHHHHHH	48.67	14532127
127	Ubiquitination	LSIGDVAKKLGEMWN CCHHHHHHHHHHHHH	48.67	22790023
128	Ubiquitination	SIGDVAKKLGEMWNN CHHHHHHHHHHHHHC	52.57	-
128	Malonylation	SIGDVAKKLGEMWNN CHHHHHHHHHHHHHC	52.57	26320211
128	Acetylation	SIGDVAKKLGEMWNN CHHHHHHHHHHHHHC	52.57	-
136	Phosphorylation	LGEMWNNTAADDKQP HHHHHHCCCCCCCCH	21.73	25890499
141	Acetylation	NNTAADDKQPYEKKA HCCCCCCCCHHHHHH	54.44	23806337
146	Acetylation	DDKQPYEKKAAKLKE CCCCHHHHHHHHHHH	41.70	23806337
146	Ubiquitination	DDKQPYEKKAAKLKE CCCCHHHHHHHHHHH	41.70	-
146	Succinylation	DDKQPYEKKAAKLKE CCCCHHHHHHHHHHH	41.70	23806337
147	Ubiquitination	DKQPYEKKAAKLKEK CCCHHHHHHHHHHHH	41.45	-
154	Ubiquitination	KAAKLKEKYEKDIAA HHHHHHHHHHHHHHH	58.06	22790023
157	Ubiquitination	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	-
157	Malonylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	26073543
157	Acetylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	60628451
162	Phosphorylation	YEKDIAAYRAKGKPD HHHHHHHHHHCCCCC	11.33	-
172	Acetylation	KGKPDAAKKGVVKAE CCCCCHHHHCCCHHH	52.35	14532127
173	Acetylation	GKPDAAKKGVVKAEK CCCCHHHHCCCHHHH	52.81	14532127
177	Acetylation	AAKKGVVKAEKSKKK HHHHCCCHHHHHHCC	48.71	14532127
180	Acetylation	KGVVKAEKSKKKKEE HCCCHHHHHHCCCCC	72.87	14532127
181	ADP-ribosylation	GVVKAEKSKKKKEEE CCCHHHHHHCCCCCC	41.01	-
182	Acetylation	VVKAEKSKKKKEEED CCHHHHHHCCCCCCC	78.62	14532127
183	Acetylation	VKAEKSKKKKEEEDD CHHHHHHCCCCCCCC	75.95	14532127
184	Acetylation	KAEKSKKKKEEEDDE HHHHHHCCCCCCCCC	69.98	14532127
185	Acetylation	AEKSKKKKEEEDDEE HHHHHCCCCCCCCCC	78.29	14532127

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 HMGB1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
3	K	Acetylation	23806337
Acetylation on Lys-3 results in preferential binding to DNA ends and impairs DNA bending activity (By similarity).
23	C	Oxidation	22105604
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 HGMB1 (HMGB1C23hC45hC106h), 2- Disulfide HMGB1 (HMGB1C23-C45C106h) and 3- Sulfonyl HMGB1 (HMGB1C23soC45soC106so).
45	C	Oxidation	22105604
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 HGMB1 (HMGB1C23hC45hC106h), 2- Disulfide HMGB1 (HMGB1C23-C45C106h) and 3- Sulfonyl HMGB1 (HMGB1C23soC45soC106so).
106	C	Oxidation	22105604
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 HGMB1 (HMGB1C23hC45hC106h), 2- Disulfide HMGB1 (HMGB1C23-C45C106h) and 3- Sulfonyl HMGB1 (HMGB1C23soC45soC106so).

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 HMGB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HMGB1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HMGB1_MOUSE

Related Literatures of Post-Translational Modification

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