dbPTM

HMGB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HMGB3_HUMAN
UniProt AC	O15347
Protein Name	High mobility group protein B3
Gene Name	HMGB3
Organism	Homo sapiens (Human).
Sequence Length	200
Subcellular Localization	Nucleus . Chromosome . Cytoplasm .
Protein Description	Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and 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 similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity)..
Protein Sequence	MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLNDSEKQPYITKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEDEEEEEEEEEEEEEEDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKGDPKKPK -----CCCCCCCCCC	63.65	-
12	Acetylation	DPKKPKGKMSAYAFF CCCCCCCCHHHHHHH	35.49	23749302
14	Phosphorylation	KKPKGKMSAYAFFVQ CCCCCCHHHHHHHHH	22.93	21712546
23	Cysteine derivative	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
23	Oxidation	YAFFVQTCREEHKKK HHHHHHHHHHHHHHH	2.63	-
24	Methylation	AFFVQTCREEHKKKN HHHHHHHHHHHHHHC	56.58	115478817
29	Ubiquitination	TCREEHKKKNPEVPV HHHHHHHHHCCCCCC	60.74	29967540
30	Acetylation	CREEHKKKNPEVPVN HHHHHHHHCCCCCCC	80.62	-
30	Ubiquitination	CREEHKKKNPEVPVN HHHHHHHHCCCCCCC	80.62	33845483
32	Acetylation	EEHKKKNPEVPVNFA HHHHHHCCCCCCCHH	53.49	-
34	Phosphorylation	HKKKNPEVPVNFAEF HHHHCCCCCCCHHHH	7.27	-
42	Phosphorylation	PVNFAEFSKKCSERW CCCHHHHHHHHHHHH	23.78	22817900
43	Ubiquitination	VNFAEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	22817900
43	Acetylation	VNFAEFSKKCSERWK CCHHHHHHHHHHHHH	64.22	26051181
44	Ubiquitination	NFAEFSKKCSERWKT CHHHHHHHHHHHHHH	41.62	22817900
44	Methylation	NFAEFSKKCSERWKT CHHHHHHHHHHHHHH	41.62	-
45	Oxidation	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
45	Cysteine derivative	FAEFSKKCSERWKTM HHHHHHHHHHHHHHC	6.16	-
49	Ubiquitination	SKKCSERWKTMSGKE HHHHHHHHHHCCCCC	9.09	29967540
50	Ubiquitination	KKCSERWKTMSGKEK HHHHHHHHHCCCCCH	40.34	33845483
58	Phosphorylation	TMSGKEKSKFDEMAK HCCCCCHHHHHHHHH	39.38	20068231
59	Acetylation	MSGKEKSKFDEMAKA CCCCCHHHHHHHHHH	68.83	23749302
63	Ubiquitination	EKSKFDEMAKADKVR CHHHHHHHHHHHHHH	5.09	22817900
64	Ubiquitination	KSKFDEMAKADKVRY HHHHHHHHHHHHHHH	11.22	22817900
65	Ubiquitination	SKFDEMAKADKVRYD HHHHHHHHHHHHHHC	56.67	32015554
71	Phosphorylation	AKADKVRYDREMKDY HHHHHHHHCHHHHHH	23.49	-
76	Ubiquitination	VRYDREMKDYGPAKG HHHCHHHHHHCCCCC	42.94	33845483
78	Phosphorylation	YDREMKDYGPAKGGK HCHHHHHHCCCCCCC	21.35	-
79	Ubiquitination	DREMKDYGPAKGGKK CHHHHHHCCCCCCCC	26.31	19608861
79	Acetylation	DREMKDYGPAKGGKK CHHHHHHCCCCCCCC	26.31	19608861
82	Acetylation	MKDYGPAKGGKKKKD HHHHCCCCCCCCCCC	71.92	7481243
82	Ubiquitination	MKDYGPAKGGKKKKD HHHHCCCCCCCCCCC	71.92	33845483
85	Ubiquitination	YGPAKGGKKKKDPNA HCCCCCCCCCCCCCC	70.82	32015554
96	Ubiquitination	DPNAPKRPPSGFFLF CCCCCCCCCCCCEEE	33.27	33845483
98	Phosphorylation	NAPKRPPSGFFLFCS CCCCCCCCCCEEEEC	51.41	30108239
102	Ubiquitination	RPPSGFFLFCSEFRP CCCCCCEEEECCCCC	3.85	33845483
104	Cysteine derivative	PSGFFLFCSEFRPKI CCCCEEEECCCCCCC	4.08	-
104	Oxidation	PSGFFLFCSEFRPKI CCCCEEEECCCCCCC	4.08	-
105	Phosphorylation	SGFFLFCSEFRPKIK CCCEEEECCCCCCCC	32.22	23312004
110	Ubiquitination	FCSEFRPKIKSTNPG EECCCCCCCCCCCCC	59.52	23000965
112	Ubiquitination	SEFRPKIKSTNPGIS CCCCCCCCCCCCCCC	58.30	23000965
112	Acetylation	SEFRPKIKSTNPGIS CCCCCCCCCCCCCCC	58.30	-
113	Phosphorylation	EFRPKIKSTNPGISI CCCCCCCCCCCCCCH	36.57	29396449
114	Phosphorylation	FRPKIKSTNPGISIG CCCCCCCCCCCCCHH	40.19	20068231
118	Phosphorylation	IKSTNPGISIGDVAK CCCCCCCCCHHHHHH	2.60	-
119	Phosphorylation	KSTNPGISIGDVAKK CCCCCCCCHHHHHHH	26.83	21712546
125	Acetylation	ISIGDVAKKLGEMWN CCHHHHHHHHHHHHH	48.67	25953088
125	Phosphorylation	ISIGDVAKKLGEMWN CCHHHHHHHHHHHHH	48.67	-
125	Ubiquitination	ISIGDVAKKLGEMWN CCHHHHHHHHHHHHH	48.67	23000965
126	Ubiquitination	SIGDVAKKLGEMWNN CHHHHHHHHHHHHHC	52.57	23000965
126	Acetylation	SIGDVAKKLGEMWNN CHHHHHHHHHHHHHC	52.57	26051181
130	Ubiquitination	VAKKLGEMWNNLNDS HHHHHHHHHHCCCCC	4.38	23000965
132	Ubiquitination	KKLGEMWNNLNDSEK HHHHHHHHCCCCCCC	41.63	23000965
134	Phosphorylation	LGEMWNNLNDSEKQP HHHHHHCCCCCCCCC	7.33	-
139	Ubiquitination	NNLNDSEKQPYITKA HCCCCCCCCCHHHHH	61.60	29967540
139	Acetylation	NNLNDSEKQPYITKA HCCCCCCCCCHHHHH	61.60	26051181
139	Phosphorylation	NNLNDSEKQPYITKA HCCCCCCCCCHHHHH	61.60	-
145	Ubiquitination	EKQPYITKAAKLKEK CCCCHHHHHHHHHHH	36.47	23000965
145	Acetylation	EKQPYITKAAKLKEK CCCCHHHHHHHHHHH	36.47	19608861
146	Ubiquitination	KQPYITKAAKLKEKY CCCHHHHHHHHHHHH	10.94	23000965
152	Acetylation	KAAKLKEKYEKDVAD HHHHHHHHHHHHHHH	58.06	25953088
152	Ubiquitination	KAAKLKEKYEKDVAD HHHHHHHHHHHHHHH	58.06	32015554
153	Phosphorylation	AAKLKEKYEKDVADY HHHHHHHHHHHHHHH	29.33	28152594
155	Acetylation	KLKEKYEKDVADYKS HHHHHHHHHHHHHHH	55.18	25953088
155	Ubiquitination	KLKEKYEKDVADYKS HHHHHHHHHHHHHHH	55.18	33845483
159	Ubiquitination	KYEKDVADYKSKGKF HHHHHHHHHHHCCCC	51.76	29967540
161	Succinylation	EKDVADYKSKGKFDG HHHHHHHHHCCCCCC	46.36	23954790
161	Acetylation	EKDVADYKSKGKFDG HHHHHHHHHCCCCCC	46.36	30589287
161	Ubiquitination	EKDVADYKSKGKFDG HHHHHHHHHCCCCCC	46.36	33845483
165	Acetylation	ADYKSKGKFDGAKGP HHHHHCCCCCCCCCC	43.98	23749302
165	Ubiquitination	ADYKSKGKFDGAKGP HHHHHCCCCCCCCCC	43.98	33845483
170	Acetylation	KGKFDGAKGPAKVAR CCCCCCCCCCHHHHH	71.59	23749302
170	Ubiquitination	KGKFDGAKGPAKVAR CCCCCCCCCCHHHHH	71.59	33845483
172	Ubiquitination	KFDGAKGPAKVARKK CCCCCCCCHHHHHHH	28.35	32015554
172	Acetylation	KFDGAKGPAKVARKK CCCCCCCCHHHHHHH	28.35	-
175	Ubiquitination	GAKGPAKVARKKVEE CCCCCHHHHHHHHHH	7.28	33845483
179	Methylation	PAKVARKKVEEEDEE CHHHHHHHHHHHCHH	49.69	69855
179	Acetylation	PAKVARKKVEEEDEE CHHHHHHHHHHHCHH	49.69	69855
181	Ubiquitination	KVARKKVEEEDEEEE HHHHHHHHHHCHHHH	65.63	33845483
185	Ubiquitination	KKVEEEDEEEEEEEE HHHHHHCHHHHHHHH	71.26	33845483
185	Acetylation	KKVEEEDEEEEEEEE HHHHHHCHHHHHHHH	71.26	-
190	Ubiquitination	EDEEEEEEEEEEEEE HCHHHHHHHHHHHHH	74.18	33845483
190	Acetylation	EDEEEEEEEEEEEEE HCHHHHHHHHHHHHH	74.18	-
199	Methylation	EEEEEEEDE------ HHHHHHHCC------	70.91	-

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 HMGB3_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-104 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 HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so).
45	C	Oxidation	24531895
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 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 HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so).
104	C	Oxidation	24531895
Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 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 HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so).

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 HMGB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMGA1_HUMAN	HMGA1	physical	18850631
THIC_HUMAN	ACAT2	physical	22863883
AL7A1_HUMAN	ALDH7A1	physical	22863883
DD19A_HUMAN	DDX19A	physical	22863883
GSHB_HUMAN	GSS	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
SCRN1_HUMAN	SCRN1	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
SDCB1_HUMAN	SDCBP	physical	25416956
EXOS4_HUMAN	EXOSC4	physical	26344197
NUCKS_HUMAN	NUCKS1	physical	26344197
SSRP1_HUMAN	SSRP1	physical	26344197
SP16H_HUMAN	SUPT16H	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300915	Microphthalmia, syndromic, 13 (MCOPS13)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HMGB3_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-59 AND LYS-145, AND MASSSPECTROMETRY.	19608861 [Abstract]

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