dbPTM

BIEA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BIEA_HUMAN
UniProt AC	P53004
Protein Name	Biliverdin reductase A
Gene Name	BLVRA
Organism	Homo sapiens (Human).
Sequence Length	296
Subcellular Localization	Cytoplasm.
Protein Description	Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor..
Protein Sequence	MNAEPERKFGVVVVGVGRAGSVRMRDLRNPHPSSAFLNLIGFVSRRELGSIDGVQQISLEDALSSQEVEVAYICSESSSHEDYIRQFLNAGKHVLVEYPMTLSLAAAQELWELAEQKGKVLHEEHVELLMEEFAFLKKEVVGKDLLKGSLLFTAGPLEEERFGFPAFSGISRLTWLVSLFGELSLVSATLEERKEDQYMKMTVCLETEKKSPLSWIEEKGPGLKRNRYLSFHFKSGSLENVPNVGVNKNIFLKDQNIFVQKLLGQFSEKELAAEKKRILHCLGLAEEIQKYCCSRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNAEPERK -------CCCCCHHC	10.93	-
21	Phosphorylation	VGVGRAGSVRMRDLR EECCCCCCCHHHHCC	12.93	22584576
33	Phosphorylation	DLRNPHPSSAFLNLI HCCCCCCCHHHHHHH	31.12	22584576
72	Phosphorylation	SQEVEVAYICSESSS CCCEEEEEEECCCCC	13.98	15870194
83	Phosphorylation	ESSSHEDYIRQFLNA CCCCCHHHHHHHHHC	8.60	15870194
130	Sulfoxidation	EEHVELLMEEFAFLK HHHHHHHHHHHHHHH	7.88	30846556
143	Ubiquitination	LKKEVVGKDLLKGSL HHHHHCCHHHHCCCE	33.33	-
143	2-Hydroxyisobutyrylation	LKKEVVGKDLLKGSL HHHHHCCHHHHCCCE	33.33	-
147	Ubiquitination	VVGKDLLKGSLLFTA HCCHHHHCCCEEEEE	54.47	-
149	Phosphorylation	GKDLLKGSLLFTAGP CHHHHCCCEEEEECC	21.95	22065579
174	Phosphorylation	FSGISRLTWLVSLFG CCCHHHHHHHHHHHH	18.68	22817900
178	Phosphorylation	SRLTWLVSLFGELSL HHHHHHHHHHHHHHH	18.79	22817900
198	Phosphorylation	EERKEDQYMKMTVCL HHHHHHHCEEEEEEE	15.83	15870194
202	Phosphorylation	EDQYMKMTVCLETEK HHHCEEEEEEEECCC	11.53	-
207	Phosphorylation	KMTVCLETEKKSPLS EEEEEEECCCCCCCH	39.91	-
209	2-Hydroxyisobutyrylation	TVCLETEKKSPLSWI EEEEECCCCCCCHHH	67.00	-
210	Ubiquitination	VCLETEKKSPLSWIE EEEECCCCCCCHHHH	51.58	-
211	Phosphorylation	CLETEKKSPLSWIEE EEECCCCCCCHHHHH	41.98	25159151
219	Ubiquitination	PLSWIEEKGPGLKRN CCHHHHHHCCCCCCC	58.58	21890473
219	Acetylation	PLSWIEEKGPGLKRN CCHHHHHHCCCCCCC	58.58	23954790
228	Phosphorylation	PGLKRNRYLSFHFKS CCCCCCCEEEEEECC	15.39	15870194
230	Phosphorylation	LKRNRYLSFHFKSGS CCCCCEEEEEECCCC	14.03	22617229
234	Methylation	RYLSFHFKSGSLENV CEEEEEECCCCCCCC	45.39	-
234	Ubiquitination	RYLSFHFKSGSLENV CEEEEEECCCCCCCC	45.39	21890473
235	Phosphorylation	YLSFHFKSGSLENVP EEEEEECCCCCCCCC	32.44	30278072
237	Phosphorylation	SFHFKSGSLENVPNV EEEECCCCCCCCCCC	39.33	30278072
248	Malonylation	VPNVGVNKNIFLKDQ CCCCCCCCCEEECCC	49.35	26320211
248	Ubiquitination	VPNVGVNKNIFLKDQ CCCCCCCCCEEECCC	49.35	21890473
248	Acetylation	VPNVGVNKNIFLKDQ CCCCCCCCCEEECCC	49.35	19608861
253	Acetylation	VNKNIFLKDQNIFVQ CCCCEEECCCHHHHH	46.66	19608861
253	Ubiquitination	VNKNIFLKDQNIFVQ CCCCEEECCCHHHHH	46.66	21906983
253	2-Hydroxyisobutyrylation	VNKNIFLKDQNIFVQ CCCCEEECCCHHHHH	46.66	-
261	Acetylation	DQNIFVQKLLGQFSE CCHHHHHHHHHCCCH	40.14	26051181
261	Ubiquitination	DQNIFVQKLLGQFSE CCHHHHHHHHHCCCH	40.14	21890473
269	Acetylation	LLGQFSEKELAAEKK HHHCCCHHHHHHHHH	57.75	21466224
269	Succinylation	LLGQFSEKELAAEKK HHHCCCHHHHHHHHH	57.75	23954790
269	Ubiquitination	LLGQFSEKELAAEKK HHHCCCHHHHHHHHH	57.75	21890473
269	2-Hydroxyisobutyrylation	LLGQFSEKELAAEKK HHHCCCHHHHHHHHH	57.75	-
275	2-Hydroxyisobutyrylation	EKELAAEKKRILHCL HHHHHHHHHHHHHHH	42.50	-
281	Glutathionylation	EKKRILHCLGLAEEI HHHHHHHHHHHHHHH	2.64	22555962
290	Acetylation	GLAEEIQKYCCSRK- HHHHHHHHHHHCCC-	46.01	25953088
291	Phosphorylation	LAEEIQKYCCSRK-- HHHHHHHHHHCCC--	5.15	15870194

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
21	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
33	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
72	Y	Phosphorylation	Kinase	BLVRA	P53004	GPS
83	Y	Phosphorylation	Kinase	BLVRA	P53004	GPS
149	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
149	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
198	Y	Phosphorylation	Kinase	INSR	P06213	PSP
228	Y	Phosphorylation	Kinase	INSR	P06213	PSP
230	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
230	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
230	S	Phosphorylation	Kinase	PKCZ	Q05513	PSP
230	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
237	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
291	Y	Phosphorylation	Kinase	INSR	P06213	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LNX1_HUMAN	LNX1	physical	25416956
TLN1_HUMAN	TLN1	physical	26186194
TBX20_HUMAN	TBX20	physical	26186194
OSBL6_HUMAN	OSBPL6	physical	26186194
PCYOX_HUMAN	PCYOX1	physical	26186194
ARF5_HUMAN	ARF5	physical	26186194
RT4I1_HUMAN	RTN4IP1	physical	26186194
OCAD1_HUMAN	OCIAD1	physical	26186194
RRAGB_HUMAN	RRAGB	physical	26186194
SNX5_HUMAN	SNX5	physical	26186194
DDHD2_HUMAN	DDHD2	physical	26186194
TBX20_HUMAN	TBX20	physical	28514442
DDHD2_HUMAN	DDHD2	physical	28514442
PCYOX_HUMAN	PCYOX1	physical	28514442
RT4I1_HUMAN	RTN4IP1	physical	28514442
RRAGB_HUMAN	RRAGB	physical	28514442
OSBL6_HUMAN	OSBPL6	physical	28514442
TLN1_HUMAN	TLN1	physical	28514442
DNSL2_HUMAN	DNASE1L2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614156	Hyperbiliverdinemia (HBLVD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BIEA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-237, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-248 AND LYS-253, AND MASSSPECTROMETRY.	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 THR-174 AND SER-178, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-237, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.	18669648 [Abstract]