dbPTM

HMGB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGB2_HUMAN
UniProt AC	P26583
Protein Name	High mobility group protein B2
Gene Name	HMGB2
Organism	Homo sapiens (Human).
Sequence Length	209
Subcellular Localization	Nucleus . Chromosome . Cytoplasm . Secreted . In basal state predominantly nuclear.
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. [PubMed: 7797075]
Protein Sequence	MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MGKGDPNKPR -----CCCCCCCCCC	59.86	15005629
8	Ubiquitination	MGKGDPNKPRGKMSS CCCCCCCCCCCCHHH	41.29	24816145
10	Methylation	KGDPNKPRGKMSSYA CCCCCCCCCCHHHHH	60.00	82955321
12	Acetylation	DPNKPRGKMSSYAFF CCCCCCCCHHHHHHH	36.57	26051181
12	Ubiquitination	DPNKPRGKMSSYAFF CCCCCCCCHHHHHHH	36.57	21890473
14	Phosphorylation	NKPRGKMSSYAFFVQ CCCCCCHHHHHHHHH	24.55	28152594
15	Phosphorylation	KPRGKMSSYAFFVQT CCCCCHHHHHHHHHH	19.58	28152594
16	Phosphorylation	PRGKMSSYAFFVQTC CCCCHHHHHHHHHHH	10.50	28152594
23	Glutathionylation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	22555962
23	Oxidation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
23	Cysteine derivative	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
24	Methylation	AFFVQTCREEHKKKH HHHHHHHHHHHHHHC	56.58	-
29	Ubiquitination	TCREEHKKKHPDSSV HHHHHHHHHCCCCCC	59.21	29967540
30	Ubiquitination	CREEHKKKHPDSSVN HHHHHHHHCCCCCCC	66.24	33845483
30	Acetylation	CREEHKKKHPDSSVN HHHHHHHHCCCCCCC	66.24	19608861
30	Malonylation	CREEHKKKHPDSSVN HHHHHHHHCCCCCCC	66.24	26320211
34	Phosphorylation	HKKKHPDSSVNFAEF HHHHCCCCCCCHHHH	40.41	23401153
35	Phosphorylation	KKKHPDSSVNFAEFS HHHCCCCCCCHHHHH	28.58	25159151
42	Phosphorylation	SVNFAEFSKKCSERW CCCHHHHHHHHHHHH	23.78	30576142
43	Ubiquitination	VNFAEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	22817900
43	Acetylation	VNFAEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	19608861
44	Acetylation	NFAEFSKKCSERWKT CHHHHHHHHHHHHHH	41.62	24467947
44	Ubiquitination	NFAEFSKKCSERWKT CHHHHHHHHHHHHHH	41.62	22817900
45	Oxidation	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
45	Cysteine derivative	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
50	Ubiquitination	KKCSERWKTMSAKEK HHHHHHHHHCCHHHH	40.34	32142685
50	Neddylation	KKCSERWKTMSAKEK HHHHHHHHHCCHHHH	40.34	32015554
51	Phosphorylation	KCSERWKTMSAKEKS HHHHHHHHCCHHHHH	14.92	22673903
53	Phosphorylation	SERWKTMSAKEKSKF HHHHHHCCHHHHHHH	41.23	30624053
55	Ubiquitination	RWKTMSAKEKSKFED HHHHCCHHHHHHHHH	59.37	21890473
55	Acetylation	RWKTMSAKEKSKFED HHHHCCHHHHHHHHH	59.37	129519
59	Acetylation	MSAKEKSKFEDMAKS CCHHHHHHHHHHHHH	64.93	23749302
59	Ubiquitination	MSAKEKSKFEDMAKS CCHHHHHHHHHHHHH	64.93	19608861
65	Acetylation	SKFEDMAKSDKARYD HHHHHHHHHHHHHHH	53.18	25953088
66	Phosphorylation	KFEDMAKSDKARYDR HHHHHHHHHHHHHHH	34.50	24719451
76	Ubiquitination	ARYDREMKNYVPPKG HHHHHHHHHCCCCCC	40.13	32142685
78	Phosphorylation	YDREMKNYVPPKGDK HHHHHHHCCCCCCCC	14.60	-
82	Acetylation	MKNYVPPKGDKKGKK HHHCCCCCCCCCCCC	73.92	15005629
85	Acetylation	YVPPKGDKKGKKKDP CCCCCCCCCCCCCCC	72.58	25953088
90	Acetylation	GDKKGKKKDPNAPKR CCCCCCCCCCCCCCC	80.19	-
100	Phosphorylation	NAPKRPPSAFFLFCS CCCCCCCCHHEHHCC	40.15	20058876
106	Cysteine derivative	PSAFFLFCSEHRPKI CCHHEHHCCCCCCCC	5.19	-
106	Oxidation	PSAFFLFCSEHRPKI CCHHEHHCCCCCCCC	5.19	-
107	Phosphorylation	SAFFLFCSEHRPKIK CHHEHHCCCCCCCCC	29.15	29978859
110	Dimethylation	FLFCSEHRPKIKSEH EHHCCCCCCCCCCCC	30.10	-
110	Methylation	FLFCSEHRPKIKSEH EHHCCCCCCCCCCCC	30.10	24390045
112	Methylation	FCSEHRPKIKSEHPG HCCCCCCCCCCCCCC	63.82	-
112	Ubiquitination	FCSEHRPKIKSEHPG HCCCCCCCCCCCCCC	63.82	22817900
112	"N6,N6-dimethyllysine"	FCSEHRPKIKSEHPG HCCCCCCCCCCCCCC	63.82	-
114	Sumoylation	SEHRPKIKSEHPGLS CCCCCCCCCCCCCCC	56.78	-
114	Acetylation	SEHRPKIKSEHPGLS CCCCCCCCCCCCCCC	56.78	26051181
114	Ubiquitination	SEHRPKIKSEHPGLS CCCCCCCCCCCCCCC	56.78	21906983
115	Phosphorylation	EHRPKIKSEHPGLSI CCCCCCCCCCCCCCH	44.61	28348404
121	Phosphorylation	KSEHPGLSIGDTAKK CCCCCCCCHHHHHHH	30.36	23312004
125	Phosphorylation	PGLSIGDTAKKLGEM CCCCHHHHHHHHHHH	34.85	28555341
127	Acetylation	LSIGDTAKKLGEMWS CCHHHHHHHHHHHHC	51.10	25953088
127	Ubiquitination	LSIGDTAKKLGEMWS CCHHHHHHHHHHHHC	51.10	32015554
128	Acetylation	SIGDTAKKLGEMWSE CHHHHHHHHHHHHCH	60.30	25953088
128	Ubiquitination	SIGDTAKKLGEMWSE CHHHHHHHHHHHHCH	60.30	22505724
132	Sulfoxidation	TAKKLGEMWSEQSAK HHHHHHHHHCHHHHC	4.53	30846556
134	Phosphorylation	KKLGEMWSEQSAKDK HHHHHHHCHHHHCCC	25.17	28152594
137	Phosphorylation	GEMWSEQSAKDKQPY HHHHCHHHHCCCCCH	32.98	28152594
139	Acetylation	MWSEQSAKDKQPYEQ HHCHHHHCCCCCHHH	71.37	25953088
139	Ubiquitination	MWSEQSAKDKQPYEQ HHCHHHHCCCCCHHH	71.37	21906983
141	Acetylation	SEQSAKDKQPYEQKA CHHHHCCCCCHHHHH	53.09	25953088
141	Ubiquitination	SEQSAKDKQPYEQKA CHHHHCCCCCHHHHH	53.09	23000965
147	Ubiquitination	DKQPYEQKAAKLKEK CCCCHHHHHHHHHHH	38.07	23000965
147	Acetylation	DKQPYEQKAAKLKEK CCCCHHHHHHHHHHH	38.07	23749302
150	Ubiquitination	PYEQKAAKLKEKYEK CHHHHHHHHHHHHHH	66.02	23000965
152	Ubiquitination	EQKAAKLKEKYEKDI HHHHHHHHHHHHHHH	51.99	23000965
154	Ubiquitination	KAAKLKEKYEKDIAA HHHHHHHHHHHHHHH	58.06	23000965
154	Acetylation	KAAKLKEKYEKDIAA HHHHHHHHHHHHHHH	58.06	16201319
155	Phosphorylation	AAKLKEKYEKDIAAY HHHHHHHHHHHHHHH	29.33	28152594
157	Acetylation	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	88037
157	Ubiquitination	KLKEKYEKDIAAYRA HHHHHHHHHHHHHHH	51.88	23000965
162	Phosphorylation	YEKDIAAYRAKGKSE HHHHHHHHHHCCCCC	11.33	25839225
167	Ubiquitination	AAYRAKGKSEAGKKG HHHHHCCCCCCCCCC	44.40	24816145
168	Phosphorylation	AYRAKGKSEAGKKGP HHHHCCCCCCCCCCC	41.15	-
172	Acetylation	KGKSEAGKKGPGRPT CCCCCCCCCCCCCCC	62.70	19608861
173	Acetylation	GKSEAGKKGPGRPTG CCCCCCCCCCCCCCC	70.22	19608861
179	Phosphorylation	KKGPGRPTGSKKKNE CCCCCCCCCCCCCCC	53.37	30576142
181	Phosphorylation	GPGRPTGSKKKNEPE CCCCCCCCCCCCCCC	43.72	20363803
182	Acetylation	PGRPTGSKKKNEPED CCCCCCCCCCCCCCC	69.94	129515
183	Acetylation	GRPTGSKKKNEPEDE CCCCCCCCCCCCCCH	63.63	7706911

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
23	C	Oxidation	24531895
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	24531895
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	24531895
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PO2F2_HUMAN	POU2F2	physical	7720710
RAG1_HUMAN	RAG1	physical	10490593
EBNA1_EBVB9	BKRF1	physical	22345443
A4_HUMAN	APP	physical	21832049
SCAF8_HUMAN	SCAF8	physical	22939629
HMGA1_HUMAN	HMGA1	physical	18850631
KCRB_HUMAN	CKB	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
PKNX1_HUMAN	PKNOX1	physical	25416956
HMGB1_HUMAN	HMGB1	physical	26344197
SP16H_HUMAN	SUPT16H	physical	26344197
PSD12_HUMAN	PSMD12	physical	27226596

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.

Regulatory Network of HMGB2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-30; LYS-59; LYS-172 ANDLYS-173, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; TYR-155 AND TYR-162,AND MASS SPECTROMETRY.	17287340 [Abstract]

show

show

show