CYB5_MOUSE - dbPTM
CYB5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CYB5_MOUSE
UniProt AC P56395
Protein Name Cytochrome b5
Gene Name Cyb5a
Organism Mus musculus (Mouse).
Sequence Length 134
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein
Cytoplasmic side. Microsome membrane
Single-pass membrane protein
Cytoplasmic side.
Protein Description Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-5 double bond introduction during the C-5 desaturation..
Protein Sequence MAGQSDKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSDTLITTVESNSSWWTNWVIPAISALAVALMYRLYMAED
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
2Acetylation------MAGQSDKDV
------CCCCCHHHC
25.40-
5Phosphorylation---MAGQSDKDVKYY
---CCCCCHHHCCEE
45.7930352176
7Acetylation-MAGQSDKDVKYYTL
-CCCCCHHHCCEEEH
70.4423576753
7Ubiquitination-MAGQSDKDVKYYTL
-CCCCCHHHCCEEEH
70.44-
7Malonylation-MAGQSDKDVKYYTL
-CCCCCHHHCCEEEH
70.4426073543
10MalonylationGQSDKDVKYYTLEEI
CCCHHHCCEEEHHHH
42.5526320211
10UbiquitinationGQSDKDVKYYTLEEI
CCCHHHCCEEEHHHH
42.55-
10AcetylationGQSDKDVKYYTLEEI
CCCHHHCCEEEHHHH
42.5523576753
11PhosphorylationQSDKDVKYYTLEEIQ
CCHHHCCEEEHHHHH
11.0922817900
13PhosphorylationDKDVKYYTLEEIQKH
HHHCCEEEHHHHHHC
25.3029176673
19AcetylationYTLEEIQKHKDSKST
EEHHHHHHCCCCCCE
59.2823806337
19UbiquitinationYTLEEIQKHKDSKST
EEHHHHHHCCCCCCE
59.28-
19MalonylationYTLEEIQKHKDSKST
EEHHHHHHCCCCCCE
59.2826320211
24UbiquitinationIQKHKDSKSTWVILH
HHHCCCCCCEEEEEE
63.14-
24MalonylationIQKHKDSKSTWVILH
HHHCCCCCCEEEEEE
63.1426073543
33AcetylationTWVILHHKVYDLTKF
EEEEEEHHHHHHHHH
31.5721728379
33MalonylationTWVILHHKVYDLTKF
EEEEEEHHHHHHHHH
31.5726073543
39MalonylationHKVYDLTKFLEEHPG
HHHHHHHHHHHHCCC
56.0726073543
39UbiquitinationHKVYDLTKFLEEHPG
HHHHHHHHHHHHCCC
56.07-
39AcetylationHKVYDLTKFLEEHPG
HHHHHHHHHHHHCCC
56.0723864654
60PhosphorylationEQAGGDATENFEDVG
HHHCCCCCCCHHHCC
35.8826525534
69PhosphorylationNFEDVGHSTDARELS
CHHHCCCCCCHHHHH
23.2723684622
70PhosphorylationFEDVGHSTDARELSK
HHHCCCCCCHHHHHC
28.1826525534
77MalonylationTDARELSKTYIIGEL
CCHHHHHCEEEEEEE
58.9526320211
77UbiquitinationTDARELSKTYIIGEL
CCHHHHHCEEEEEEE
58.95-
77AcetylationTDARELSKTYIIGEL
CCHHHHHCEEEEEEE
58.9523864654
90PhosphorylationELHPDDRSKIAKPSD
EECCCCHHHCCCCCC
35.0929514104
96PhosphorylationRSKIAKPSDTLITTV
HHHCCCCCCCEEEEE
42.3929895711
111PhosphorylationESNSSWWTNWVIPAI
CCCCCHHHCCHHHHH
16.9729895711
127PhosphorylationALAVALMYRLYMAED
HHHHHHHHHHHHCCC
9.7929895711

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 CYB5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CYB5_MOUSE !!

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 CYB5_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CYB5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CYB5_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND MASS SPECTROMETRY.

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