dbPTM

CYBR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CYBR1_HUMAN
UniProt AC	Q53TN4
Protein Name	Cytochrome b reductase 1
Gene Name	CYBRD1
Organism	Homo sapiens (Human).
Sequence Length	286
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description	Ferric-chelate reductase that reduces Fe(3+) to Fe(2+). Present at the brush border of duodenal enterocytes where it probably reduces dietary Fe(3+) thereby facilitating its transport into the mucosal cells. Uses ascorbate as electron donor. May be involved in extracellular ascorbate recycling in erythrocyte membranes. May also act as a ferrireductase in airway epithelial cells..
Protein Sequence	MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
185	Phosphorylation	LTEKLIFSLRDPAYS HHHHHHHHCCCCCCC	18.59	-
231	N-linked_Glycosylation	WKRPKEPNSTILHPN CCCCCCCCCEEECCC	53.53	UniProtKB CARBOHYD
232	Phosphorylation	KRPKEPNSTILHPNG CCCCCCCCEEECCCC	27.78	30266825
233	Phosphorylation	RPKEPNSTILHPNGG CCCCCCCEEECCCCC	33.91	26657352
241	Phosphorylation	ILHPNGGTEQGARGS EECCCCCCCCCCCCC	26.91	26657352
248	Phosphorylation	TEQGARGSMPAYSGN CCCCCCCCCCCCCCC	18.95	21945579
252	Phosphorylation	ARGSMPAYSGNNMDK CCCCCCCCCCCCCCC	15.96	21945579
253	Phosphorylation	RGSMPAYSGNNMDKS CCCCCCCCCCCCCCC	36.83	21945579
260	Phosphorylation	SGNNMDKSDSELNSE CCCCCCCCHHHHHHH	41.95	23401153
262	Phosphorylation	NNMDKSDSELNSEVA CCCCCCHHHHHHHHH	51.58	29255136
266	Phosphorylation	KSDSELNSEVAARKR CCHHHHHHHHHHHHH	46.18	29255136
284	Phosphorylation	LDEAGQRSTM----- HHHHHHHCCC-----	22.42	23401153
285	Phosphorylation	DEAGQRSTM------ HHHHHHCCC------	29.14	22167270

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 CYBR1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CYBR1_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 CYBR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDYL_HUMAN	CDYL	physical	28514442
MIER1_HUMAN	MIER1	physical	28514442
MIER2_HUMAN	MIER2	physical	28514442
HDAC1_HUMAN	HDAC1	physical	28514442
HDAC2_HUMAN	HDAC2	physical	28514442
F136A_HUMAN	FAM136A	physical	28514442

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 CYBR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND THR-285, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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-285, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285, AND MASSSPECTROMETRY.	19369195 [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 THR-285, AND MASSSPECTROMETRY.	18669648 [Abstract]