dbPTM

LDHB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LDHB_HUMAN
UniProt AC	P07195
Protein Name	L-lactate dehydrogenase B chain
Gene Name	LDHB
Organism	Homo sapiens (Human).
Sequence Length	334
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MATLKEKLIAPV ---CCCHHHHHCCCC	48.74	-
7	Acetylation	-MATLKEKLIAPVAE -CCCHHHHHCCCCCC	43.54	19608861
7	Ubiquitination	-MATLKEKLIAPVAE -CCCHHHHHCCCCCC	43.54	19608861
7	Malonylation	-MATLKEKLIAPVAE -CCCHHHHHCCCCCC	43.54	26320211
18	Phosphorylation	PVAEEEATVPNNKIT CCCCCCCCCCCCEEE	39.51	21712546
25	Phosphorylation	TVPNNKITVVGVGQV CCCCCEEEEEEECHH	15.68	26126808
36	Glutathionylation	VGQVGMACAISILGK ECHHHHHHHHHHHCH	2.28	22555962
39	Phosphorylation	VGMACAISILGKSLA HHHHHHHHHHCHHHH	8.01	-
43	Ubiquitination	CAISILGKSLADELA HHHHHHCHHHHHHHH	38.56	-
44	Phosphorylation	AISILGKSLADELAL HHHHHCHHHHHHHHH	27.30	19664994
58	Ubiquitination	LVDVLEDKLKGEMMD HHHHHHHHHCCCCEE	42.60	19608861
58	Acetylation	LVDVLEDKLKGEMMD HHHHHHHHHCCCCEE	42.60	19608861
60	Ubiquitination	DVLEDKLKGEMMDLQ HHHHHHHCCCCEECC	59.57	21890473
60	Acetylation	DVLEDKLKGEMMDLQ HHHHHHHCCCCEECC	59.57	26051181
63	Sulfoxidation	EDKLKGEMMDLQHGS HHHHCCCCEECCCCC	3.27	21406390
64	Sulfoxidation	DKLKGEMMDLQHGSL HHHCCCCEECCCCCE	3.96	30846556
75	Phosphorylation	HGSLFLQTPKIVADK CCCEEECCCCEEECC	28.79	24719451
77	Ubiquitination	SLFLQTPKIVADKDY CEEECCCCEEECCCC	53.88	21890473
82	Acetylation	TPKIVADKDYSVTAN CCCEEECCCCEEECC	49.15	23954790
82	Malonylation	TPKIVADKDYSVTAN CCCEEECCCCEEECC	49.15	26320211
82	Ubiquitination	TPKIVADKDYSVTAN CCCEEECCCCEEECC	49.15	21890473
84	Phosphorylation	KIVADKDYSVTANSK CEEECCCCEEECCCE	15.69	28152594
84	Nitration	KIVADKDYSVTANSK CEEECCCCEEECCCE	15.69	-
85	Phosphorylation	IVADKDYSVTANSKI EEECCCCEEECCCEE	24.11	28152594
87	Phosphorylation	ADKDYSVTANSKIVV ECCCCEEECCCEEEE	17.74	28442448
90	Phosphorylation	DYSVTANSKIVVVTA CCEEECCCEEEEEEE	22.69	28152594
91	Ubiquitination	YSVTANSKIVVVTAG CEEECCCEEEEEEEC	39.05	-
96	Phosphorylation	NSKIVVVTAGVRQQE CCEEEEEEECCCCCC	13.19	-
106	Phosphorylation	VRQQEGESRLNLVQR CCCCCCCHHHHHHHH	53.58	-
119	Ubiquitination	QRNVNVFKFIIPQIV HHHHCCHHHHHHHHH	31.22	21890473
119	Methylation	QRNVNVFKFIIPQIV HHHHCCHHHHHHHHH	31.22	129383
119	Acetylation	QRNVNVFKFIIPQIV HHHHCCHHHHHHHHH	31.22	19608861
127	Acetylation	FIIPQIVKYSPDCII HHHHHHHHCCCCEEE	41.46	-
156	Succinylation	WKLSGLPKHRVIGSG HHHCCCCCCCEECCC	49.43	27452117
156	Ubiquitination	WKLSGLPKHRVIGSG HHHCCCCCCCEECCC	49.43	-
156	Acetylation	WKLSGLPKHRVIGSG HHHCCCCCCCEECCC	49.43	23749302
158	Methylation	LSGLPKHRVIGSGCN HCCCCCCCEECCCCC	28.07	115481969
162	Phosphorylation	PKHRVIGSGCNLDSA CCCCEECCCCCCCHH	29.11	24114839
164	S-palmitoylation	HRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	29575903
164	Glutathionylation	HRVIGSGCNLDSARF CCEECCCCCCCHHHH	4.97	22555962
168	Phosphorylation	GSGCNLDSARFRYLM CCCCCCCHHHHHHHH	25.22	21712546
170	Methylation	GCNLDSARFRYLMAE CCCCCHHHHHHHHHH	22.11	-
172	Methylation	NLDSARFRYLMAEKL CCCHHHHHHHHHHHH	20.37	115481961
173	Phosphorylation	LDSARFRYLMAEKLG CCHHHHHHHHHHHHC	9.71	20090780
225	O-linked_Glycosylation	EMGTDNDSENWKEVH CCCCCCCCCCHHHHH	38.80	OGP
229	Acetylation	DNDSENWKEVHKMVV CCCCCCHHHHHHHHH	62.53	155569
233	Acetylation	ENWKEVHKMVVESAY CCHHHHHHHHHHHHH	38.27	26822725
233	Ubiquitination	ENWKEVHKMVVESAY CCHHHHHHHHHHHHH	38.27	21890473
234	Sulfoxidation	NWKEVHKMVVESAYE CHHHHHHHHHHHHHH	2.17	21406390
238	Phosphorylation	VHKMVVESAYEVIKL HHHHHHHHHHHHHHC	25.25	21945579
240	Phosphorylation	KMVVESAYEVIKLKG HHHHHHHHHHHHCCC	21.73	25159151
240	Nitration	KMVVESAYEVIKLKG HHHHHHHHHHHHCCC	21.73	-
244	Acetylation	ESAYEVIKLKGYTNW HHHHHHHHCCCCCCC	49.69	23749302
244	Ubiquitination	ESAYEVIKLKGYTNW HHHHHHHHCCCCCCC	49.69	21890473
246	Ubiquitination	AYEVIKLKGYTNWAI HHHHHHCCCCCCCHH	44.89	-
248	Phosphorylation	EVIKLKGYTNWAIGL HHHHCCCCCCCHHHH	8.70	22817900
249	Phosphorylation	VIKLKGYTNWAIGLS HHHCCCCCCCHHHHH	32.71	22817900
269	Phosphorylation	ESMLKNLSRIHPVST HHHHHHHHCCCCCHH	38.28	-
281	Sulfoxidation	VSTMVKGMYGIENEV CHHHHCCCCCCCCCE	1.99	28465586
291	Phosphorylation	IENEVFLSLPCILNA CCCCEEECCHHHHCC	20.85	-
302	Phosphorylation	ILNARGLTSVINQKL HHCCCCHHHHHCHHC	24.62	28450419
303	Phosphorylation	LNARGLTSVINQKLK HCCCCHHHHHCHHCC	26.49	28450419
308	Ubiquitination	LTSVINQKLKDDEVA HHHHHCHHCCCCHHH	53.68	21890473
308	Acetylation	LTSVINQKLKDDEVA HHHHHCHHCCCCHHH	53.68	23954790
310	Sumoylation	SVINQKLKDDEVAQL HHHCHHCCCCHHHHH	70.89	-
310	Acetylation	SVINQKLKDDEVAQL HHHCHHCCCCHHHHH	70.89	23749302
310	Sumoylation	SVINQKLKDDEVAQL HHHCHHCCCCHHHHH	70.89	-
310	Ubiquitination	SVINQKLKDDEVAQL HHHCHHCCCCHHHHH	70.89	20639865
318	Acetylation	DDEVAQLKKSADTLW CCHHHHHHHHHHHHH	32.38	23749302
318	Succinylation	DDEVAQLKKSADTLW CCHHHHHHHHHHHHH	32.38	23954790
318	Ubiquitination	DDEVAQLKKSADTLW CCHHHHHHHHHHHHH	32.38	-
319	Acetylation	DEVAQLKKSADTLWD CHHHHHHHHHHHHHH	60.51	23954790
319	Ubiquitination	DEVAQLKKSADTLWD CHHHHHHHHHHHHHH	60.51	21890473
320	Phosphorylation	EVAQLKKSADTLWDI HHHHHHHHHHHHHHH	29.77	25159151
323	Phosphorylation	QLKKSADTLWDIQKD HHHHHHHHHHHHHHH	29.48	28857561
329	Acetylation	DTLWDIQKDLKDL-- HHHHHHHHHHHCC--	66.42	19608861
329	Ubiquitination	DTLWDIQKDLKDL-- HHHHHHHHHHHCC--	66.42	21890473
329	Succinylation	DTLWDIQKDLKDL-- HHHHHHHHHHHCC--	66.42	23954790
332	Acetylation	WDIQKDLKDL----- HHHHHHHHCC-----	68.09	70131
332	Ubiquitination	WDIQKDLKDL----- HHHHHHHHCC-----	68.09	21906983
332	Sumoylation	WDIQKDLKDL----- HHHHHHHHCC-----	68.09	-

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
162	S	Phosphorylation	Kinase	AURA	O14965	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LDHB_HUMAN !!

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 LDHB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LDHB_HUMAN	LDHB	physical	11276087
AL7A1_HUMAN	ALDH7A1	physical	22863883
BZW1_HUMAN	BZW1	physical	22863883
KCRB_HUMAN	CKB	physical	22863883
CNDP2_HUMAN	CNDP2	physical	22863883
G6PD_HUMAN	G6PD	physical	22863883
GNAI3_HUMAN	GNAI3	physical	22863883
HMGB2_HUMAN	HMGB2	physical	22863883
ROA2_HUMAN	HNRNPA2B1	physical	22863883
ROAA_HUMAN	HNRNPAB	physical	22863883
LDHA_HUMAN	LDHA	physical	22863883
PSA_HUMAN	NPEPPS	physical	22863883
PAK2_HUMAN	PAK2	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
6PGD_HUMAN	PGD	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
TXND5_HUMAN	TXNDC5	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433B_HUMAN	YWHAB	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
LDHB_HUMAN	LDHB	physical	25416956
PEX5_HUMAN	PEX5	physical	25416956
ACADM_HUMAN	ACADM	physical	26344197
PUR8_HUMAN	ADSL	physical	26344197
SAHH_HUMAN	AHCY	physical	26344197
AL1B1_HUMAN	ALDH1B1	physical	26344197
ALDH2_HUMAN	ALDH2	physical	26344197
AL4A1_HUMAN	ALDH4A1	physical	26344197
APT_HUMAN	APRT	physical	26344197
ARF4_HUMAN	ARF4	physical	26344197
ARF5_HUMAN	ARF5	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
CATA_HUMAN	CAT	physical	26344197
TCPG_HUMAN	CCT3	physical	26344197
TCPZ_HUMAN	CCT6A	physical	26344197
TCPW_HUMAN	CCT6B	physical	26344197
CATD_HUMAN	CTSD	physical	26344197
IF4H_HUMAN	EIF4H	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
ETFA_HUMAN	ETFA	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
FUMH_HUMAN	FH	physical	26344197
G3BP1_HUMAN	G3BP1	physical	26344197
LYAG_HUMAN	GAA	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
IDE_HUMAN	IDE	physical	26344197
ECM29_HUMAN	KIAA0368	physical	26344197
MDHC_HUMAN	MDH1	physical	26344197
MIF_HUMAN	MIF	physical	26344197
NIT2_HUMAN	NIT2	physical	26344197
NDKB_HUMAN	NME2	physical	26344197
NUP50_HUMAN	NUP50	physical	26344197
PARK7_HUMAN	PARK7	physical	26344197
ODPA_HUMAN	PDHA1	physical	26344197
PEPD_HUMAN	PEPD	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
PGM1_HUMAN	PGM1	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
PPT1_HUMAN	PPT1	physical	26344197
PCP_HUMAN	PRCP	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
PRS7_HUMAN	PSMC2	physical	26344197
RAB5A_HUMAN	RAB5A	physical	26344197
RHEB_HUMAN	RHEB	physical	26344197
DHSO_HUMAN	SORD	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
UBE2N_HUMAN	UBE2N	physical	26344197
LDHC_HUMAN	LDHC	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614128	Lactate dehydrogenase B deficiency (LDHBD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LDHB_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-7; LYS-58; LYS-119; LYS-319AND LYS-329, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; TYR-248 ANDTHR-249, AND MASS SPECTROMETRY.	19690332 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASSSPECTROMETRY.	15592455 [Abstract]