NB5R3_HUMAN - dbPTM
NB5R3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NB5R3_HUMAN
UniProt AC P00387
Protein Name NADH-cytochrome b5 reductase 3
Gene Name CYB5R3
Organism Homo sapiens (Human).
Sequence Length 301
Subcellular Localization Isoform 1: Endoplasmic reticulum membrane
Lipid-anchor
Cytoplasmic side. Mitochondrion outer membrane
Lipid-anchor
Cytoplasmic side.
Isoform 2: Cytoplasm. Produces the soluble form found in erythrocytes.
Protein Description Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction..
Protein Sequence MGAQLSTLGHMVLFPVWFLYSLLMKLFQRSTPAITLESPDIKYPLRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIRPDKKSNPIIRTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFVF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGAQLSTLG
------CCCCHHHHH		23.25-
2Myristoylation------MGAQLSTLG
------CCCCHHHHH		23.252498303
4 (in isoform 3)Phosphorylation-30.1626552605
6Phosphorylation--MGAQLSTLGHMVL
--CCCCHHHHHHHHH		14.9824043423
7Phosphorylation-MGAQLSTLGHMVLF
-CCCCHHHHHHHHHH		45.4024043423
12 (in isoform 3)Phosphorylation-4.0726552605
19UbiquitinationVLFPVWFLYSLLMKL
HHHHHHHHHHHHHHH		1.3423000965
19 (in isoform 2)Ubiquitination-1.3421890473
19AcetylationVLFPVWFLYSLLMKL
HHHHHHHHHHHHHHH		1.3419608861
20PhosphorylationLFPVWFLYSLLMKLF
HHHHHHHHHHHHHHH		6.4424043423
21PhosphorylationFPVWFLYSLLMKLFQ
HHHHHHHHHHHHHHH		19.7124043423
30O-linked_GlycosylationLMKLFQRSTPAITLE
HHHHHHHCCCCEEEC		28.1432870666
30PhosphorylationLMKLFQRSTPAITLE
HHHHHHHCCCCEEEC		28.1429449344
31PhosphorylationMKLFQRSTPAITLES
HHHHHHCCCCEEECC		20.9423911959
31O-linked_GlycosylationMKLFQRSTPAITLES
HHHHHHCCCCEEECC		20.9432870666
35PhosphorylationQRSTPAITLESPDIK
HHCCCCEEECCCCCC		26.9530266825
38PhosphorylationTPAITLESPDIKYPL
CCCEEECCCCCCCCC		30.8730266825
42AcetylationTLESPDIKYPLRLID
EECCCCCCCCCEEEC		48.4719608861
42UbiquitinationTLESPDIKYPLRLID
EECCCCCCCCCEEEC		48.4723000965
43PhosphorylationLESPDIKYPLRLIDR
ECCCCCCCCCEEECH		14.0828152594
54PhosphorylationLIDREIISHDTRRFR
EECHHHHCCCCCEEE		22.4428152594
57PhosphorylationREIISHDTRRFRFAL
HHHHCCCCCEEEEEC		20.5128152594
66PhosphorylationRFRFALPSPQHILGL
EEEEECCCHHHCCCC		37.73-
75UbiquitinationQHILGLPVGQHIYLS
HHCCCCCCCCEEEEE		16.1423000965
75 (in isoform 3)Ubiquitination-16.14-
75UbiquitinationQHILGLPVGQHIYLS
HHCCCCCCCCEEEEE		16.1421890473
75AcetylationQHILGLPVGQHIYLS
HHCCCCCCCCEEEEE		16.1419608861
75 (in isoform 1)Ubiquitination-16.1421890473
80PhosphorylationLPVGQHIYLSARIDG
CCCCCEEEEEEEECC		7.7721253578
82PhosphorylationVGQHIYLSARIDGNL
CCCEEEEEEEECCCE		9.87-
88UbiquitinationLSARIDGNLVVRPYT
EEEEECCCEEEEECC		26.3923503661
92UbiquitinationIDGNLVVRPYTPISS
ECCCEEEEECCCCCC		15.8423000965
92 (in isoform 2)Ubiquitination-15.84-
94PhosphorylationGNLVVRPYTPISSDD
CCEEEEECCCCCCCC		18.0028450419
95PhosphorylationNLVVRPYTPISSDDD
CEEEEECCCCCCCCC		19.4828450419
97UbiquitinationVVRPYTPISSDDDKG
EEEECCCCCCCCCCC		4.7923000965
97 (in isoform 2)Ubiquitination-4.7921890473
98PhosphorylationVRPYTPISSDDDKGF
EEECCCCCCCCCCCC		28.9928450419
99PhosphorylationRPYTPISSDDDKGFV
EECCCCCCCCCCCCE		45.8628450419
103UbiquitinationPISSDDDKGFVDLVI
CCCCCCCCCCEEEEE		62.3323000965
103 (in isoform 2)Ubiquitination-62.3321890473
111UbiquitinationGFVDLVIKVYFKDTH
CCEEEEEEEEECCCC		24.3323503661
113PhosphorylationVDLVIKVYFKDTHPK
EEEEEEEEECCCCCC		10.4228152594
115UbiquitinationLVIKVYFKDTHPKFP
EEEEEEECCCCCCCC		43.9923000965
115AcetylationLVIKVYFKDTHPKFP
EEEEEEECCCCCCCC		43.9926051181
117PhosphorylationIKVYFKDTHPKFPAG
EEEEECCCCCCCCCC		40.4428152594
120AcetylationYFKDTHPKFPAGGKM
EECCCCCCCCCCCCH		57.2725953088
120UbiquitinationYFKDTHPKFPAGGKM
EECCCCCCCCCCCCH		57.2723000965
123PhosphorylationDTHPKFPAGGKMSQY
CCCCCCCCCCCHHHH		42.3732142685
126UbiquitinationPKFPAGGKMSQYLES
CCCCCCCCHHHHHHH		34.1723000965
130PhosphorylationAGGKMSQYLESMQIG
CCCCHHHHHHHCCCC		12.7221082442
131UbiquitinationGGKMSQYLESMQIGD
CCCHHHHHHHCCCCC		2.8132142685
140UbiquitinationSMQIGDTIEFRGPSG
HCCCCCEEEEECCCC		5.8421890473
140 (in isoform 2)Ubiquitination-5.8421890473
141UbiquitinationMQIGDTIEFRGPSGL
CCCCCEEEEECCCCE		31.2432142685
144UbiquitinationGDTIEFRGPSGLLVY
CCEEEEECCCCEEEE		26.5023503661
146PhosphorylationTIEFRGPSGLLVYQG
EEEEECCCCEEEEEC		44.9221712546
148UbiquitinationEFRGPSGLLVYQGKG
EEECCCCEEEEECCC		3.2523000965
150UbiquitinationRGPSGLLVYQGKGKF
ECCCCEEEEECCCEE		3.9423000965
150 (in isoform 2)Ubiquitination-3.9421890473
151PhosphorylationGPSGLLVYQGKGKFA
CCCCEEEEECCCEEE		16.1227251275
153UbiquitinationSGLLVYQGKGKFAIR
CCEEEEECCCEEEEC		24.0123000965
153 (in isoform 3)Ubiquitination-24.01-
153UbiquitinationSGLLVYQGKGKFAIR
CCEEEEECCCEEEEC		24.0121890473
153 (in isoform 1)Ubiquitination-24.0121890473
154UbiquitinationGLLVYQGKGKFAIRP
CEEEEECCCEEEECC		43.3232142685
154AcetylationGLLVYQGKGKFAIRP
CEEEEECCCEEEECC		43.3226051181
159UbiquitinationQGKGKFAIRPDKKSN
ECCCEEEECCCCCCC		8.0623000965
159 (in isoform 3)Ubiquitination-8.06-
159UbiquitinationQGKGKFAIRPDKKSN
ECCCEEEECCCCCCC		8.0621890473
159 (in isoform 1)Ubiquitination-8.0621890473
163UbiquitinationKFAIRPDKKSNPIIR
EEEECCCCCCCCCEE		61.8621906983
163AcetylationKFAIRPDKKSNPIIR
EEEECCCCCCCCCEE		61.8625953088
164UbiquitinationFAIRPDKKSNPIIRT
EEECCCCCCCCCEEE		63.9532142685
164MalonylationFAIRPDKKSNPIIRT
EEECCCCCCCCCEEE		63.9526320211
165PhosphorylationAIRPDKKSNPIIRTV
EECCCCCCCCCEEEE		54.2926437602
171PhosphorylationKSNPIIRTVKSVGMI
CCCCCEEEEEECCEE		23.1328674151
173UbiquitinationNPIIRTVKSVGMIAG
CCCEEEEEECCEECC		38.5223000965
174PhosphorylationPIIRTVKSVGMIAGG
CCEEEEEECCEECCC		21.4022777824
179 (in isoform 3)Phosphorylation-11.0627251275
179PhosphorylationVKSVGMIAGGTGITP
EEECCEECCCCCCHH		11.0632142685
182PhosphorylationVGMIAGGTGITPMLQ
CCEECCCCCCHHHHH		25.2120068231
185PhosphorylationIAGGTGITPMLQVIR
ECCCCCCHHHHHHHH		12.1820071362
187UbiquitinationGGTGITPMLQVIRAI
CCCCCHHHHHHHHHH		2.8332142685
189 (in isoform 3)Ubiquitination-23.49-
191UbiquitinationITPMLQVIRAIMKDP
CHHHHHHHHHHHCCC		1.2621890473
191 (in isoform 2)Ubiquitination-1.2621890473
196AcetylationQVIRAIMKDPDDHTV
HHHHHHHCCCCCCCH		61.0626822725
196UbiquitinationQVIRAIMKDPDDHTV
HHHHHHHCCCCCCCH		61.0622817900
196 (in isoform 3)Ubiquitination-61.06-
196UbiquitinationQVIRAIMKDPDDHTV
HHHHHHHCCCCCCCH		61.0621890473
196 (in isoform 1)Ubiquitination-61.0621890473
197UbiquitinationVIRAIMKDPDDHTVC
HHHHHHCCCCCCCHH		34.1832142685
206UbiquitinationDDHTVCHLLFANQTE
CCCCHHHEEECCCCC		3.3923000965
206 (in isoform 3)Ubiquitination-3.39-
206UbiquitinationDDHTVCHLLFANQTE
CCCCHHHEEECCCCC		3.3921890473
206 (in isoform 1)Ubiquitination-3.3921890473
207 (in isoform 3)Phosphorylation-1.3724719451
211UbiquitinationCHLLFANQTEKDILL
HHEEECCCCCCCCHH		47.8321890473
211 (in isoform 2)Ubiquitination-47.8321890473
214UbiquitinationLFANQTEKDILLRPE
EECCCCCCCCHHCHH		54.1532015554
229UbiquitinationLEELRNKHSARFKLW
HHHHHCCCCHHHEEE		30.1822817900
234UbiquitinationNKHSARFKLWYTLDR
CCCCHHHEEEEECCC		32.3421890473
247UbiquitinationDRAPEAWDYGQGFVN
CCCCHHHHCCCCCCC		44.7421890473
247 (in isoform 3)Ubiquitination-44.74-
247UbiquitinationDRAPEAWDYGQGFVN
CCCCHHHHCCCCCCC		44.7421890473
247 (in isoform 1)Ubiquitination-44.7421890473
248PhosphorylationRAPEAWDYGQGFVNE
CCCHHHHCCCCCCCH		10.7222817900
257SulfoxidationQGFVNEEMIRDHLPP
CCCCCHHHHHHCCCC		2.1930846556
267UbiquitinationDHLPPPEEEPLVLMC
HCCCCCCCCCEEEEE		71.3521890473
267 (in isoform 3)Ubiquitination-71.35-
267UbiquitinationDHLPPPEEEPLVLMC
HCCCCCCCCCEEEEE		71.3521890473
267 (in isoform 1)Ubiquitination-71.3521890473
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 NB5R3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NB5R3_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 NB5R3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS7_HUMANRPS7physical
22939629
AT5F1_HUMANATP5F1physical
26344197
Drug and Disease Associations
Kegg Disease
H00235 Methemoglobinemia
OMIM Disease
250800Methemoglobinemia CYB5R3-related (METHB-CYB5R3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NB5R3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-42, AND MASS SPECTROMETRY.
Myristoylation
ReferencePubMed
"The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases.";
Murakami K., Yubisui T., Takeshita M., Miyata T.;
J. Biochem. 105:312-317(1989).
Cited for: PROTEIN SEQUENCE OF 2-25, AND MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"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 TYR-43, AND MASSSPECTROMETRY.

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