CYB5B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYB5B_HUMAN
• UniProt AC: O43169
• Protein Name: Cytochrome b5 type B
• Gene Name: CYB5B
• Organism: Homo sapiens (Human).
• Sequence Length: 146
• Subcellular Localization: Mitochondrion outer membrane.
• Protein Description: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases..
• Protein Sequence: MATAEASGSDGKGQEVETSVTYYRLEEVAKRNSLKELWLVIHGRVYDVTRFLNEHPGGEEVLLEQAGVDASESFEDVGHSSDAREMLKQYYIGDIHPSDLKPESGSKDPSKNDTCKSCWAYWILPIIGAVLLGFLYRYYTSESKSS

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
2	Phosphorylation	------MATAEASGS ------CCCCCCCCC	18.60	25159151
2	Acetylation	------MATAEASGS ------CCCCCCCCC	18.60	25944712
2	Phosphorylation	------MATAEASGS ------CCCCCCCCC	18.60	18491316
4	Phosphorylation	----MATAEASGSDG ----CCCCCCCCCCC	10.79	23663014
4	Phosphorylation	----MATAEASGSDG ----CCCCCCCCCCC	10.79	27251275
7	Phosphorylation	-MATAEASGSDGKGQ -CCCCCCCCCCCCCC	30.27	30108239
7	Phosphorylation	-MATAEASGSDGKGQ -CCCCCCCCCCCCCC	30.27	-
9	Phosphorylation	ATAEASGSDGKGQEV CCCCCCCCCCCCCEE	40.47	25159151
11	Phosphorylation	AEASGSDGKGQEVET CCCCCCCCCCCEEEE	37.38	30108239
11	Phosphorylation	AEASGSDGKGQEVET CCCCCCCCCCCEEEE	37.38	27251275
13	Phosphorylation	ASGSDGKGQEVETSV CCCCCCCCCEEEEEE	34.12	25849741
13	Phosphorylation	ASGSDGKGQEVETSV CCCCCCCCCEEEEEE	34.12	-
16	Ubiquitination	SDGKGQEVETSVTYY CCCCCCEEEEEEEEE	8.16	33845483
18	Phosphorylation	GKGQEVETSVTYYRL CCCCEEEEEEEEEEH	33.40	25159151
19	Phosphorylation	KGQEVETSVTYYRLE CCCEEEEEEEEEEHH	10.04	23401153
21	Phosphorylation	QEVETSVTYYRLEEV CEEEEEEEEEEHHHH	18.01	27794612
22	Phosphorylation	EVETSVTYYRLEEVA EEEEEEEEEEHHHHH	5.61	23663014
23	Phosphorylation	VETSVTYYRLEEVAK EEEEEEEEEHHHHHH	10.19	28152594
25	Phosphorylation	TSVTYYRLEEVAKRN EEEEEEEHHHHHHHC	3.68	22210691
30	Ubiquitination	YRLEEVAKRNSLKEL EEHHHHHHHCCCHHE	58.23	21890473
30	Acetylation	YRLEEVAKRNSLKEL EEHHHHHHHCCCHHE	58.23	19608861
30	Succinylation	YRLEEVAKRNSLKEL EEHHHHHHHCCCHHE	58.23	23954790
33	Phosphorylation	EEVAKRNSLKELWLV HHHHHHCCCHHEEEE	44.87	23927012
34	Ubiquitination	EVAKRNSLKELWLVI HHHHHCCCHHEEEEE	5.96	27667366
34	Acetylation	EVAKRNSLKELWLVI HHHHHCCCHHEEEEE	5.96	19608861
34	2-Hydroxyisobutyrylation	EVAKRNSLKELWLVI HHHHHCCCHHEEEEE	5.96	-
35	Acetylation	VAKRNSLKELWLVIH HHHHCCCHHEEEEEC	51.05	26051181
35	Ubiquitination	VAKRNSLKELWLVIH HHHHCCCHHEEEEEC	51.05	21890473
35	Methylation	VAKRNSLKELWLVIH HHHHCCCHHEEEEEC	51.05	24129315
37	Phosphorylation	KRNSLKELWLVIHGR HHCCCHHEEEEECCC	4.02	24719451
39	Ubiquitination	NSLKELWLVIHGRVY CCCHHEEEEECCCEE	3.97	22817900
39	Methylation	NSLKELWLVIHGRVY CCCHHEEEEECCCEE	3.97	24129315
71	Phosphorylation	EQAGVDASESFEDVG HHCCCCCCCCHHHCC	29.34	28270605
73	Phosphorylation	AGVDASESFEDVGHS CCCCCCCCHHHCCCC	31.29	28270605
80	Phosphorylation	SFEDVGHSSDAREML CHHHCCCCHHHHHHH	24.80	30624053
81	Phosphorylation	FEDVGHSSDAREMLK HHHCCCCHHHHHHHH	29.61	30624053
84	Phosphorylation	VGHSSDAREMLKQYY CCCCHHHHHHHHHHC	34.54	-
88	Ubiquitination	SDAREMLKQYYIGDI HHHHHHHHHHCCCCC	34.64	21890473
88	Acetylation	SDAREMLKQYYIGDI HHHHHHHHHHCCCCC	34.64	25825284
90	Phosphorylation	AREMLKQYYIGDIHP HHHHHHHHCCCCCCH	8.75	27080861
91	Phosphorylation	REMLKQYYIGDIHPS HHHHHHHCCCCCCHH	8.92	27080861
92	Acetylation	EMLKQYYIGDIHPSD HHHHHHCCCCCCHHH	3.21	-
92	Ubiquitination	EMLKQYYIGDIHPSD HHHHHHCCCCCCHHH	3.21	21890473
92	2-Hydroxyisobutyrylation	EMLKQYYIGDIHPSD HHHHHHCCCCCCHHH	3.21	-
98	Phosphorylation	YIGDIHPSDLKPESG CCCCCCHHHCCCCCC	41.22	25159151
101	Ubiquitination	DIHPSDLKPESGSKD CCCHHHCCCCCCCCC	52.29	21906983
104	Phosphorylation	PSDLKPESGSKDPSK HHHCCCCCCCCCCCC	57.82	25849741
105	Ubiquitination	SDLKPESGSKDPSKN HHCCCCCCCCCCCCC	36.73	33845483
106	Phosphorylation	DLKPESGSKDPSKND HCCCCCCCCCCCCCC	43.07	25849741
110	Phosphorylation	ESGSKDPSKNDTCKS CCCCCCCCCCCCCHH	54.98	27080861
111	Ubiquitination	SGSKDPSKNDTCKSC CCCCCCCCCCCCHHH	65.32	32142685
115	Ubiquitination	DPSKNDTCKSCWAYW CCCCCCCCHHHHHHH	3.22	33845483
148	Ubiquitination	SESKSS--------- HCCCCC---------		33845483

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CYB5B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYB5B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CYB5B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RM42_HUMAN	MRPL42	physical	22939629
CCD47_HUMAN	CCDC47	physical	26344197
TCPB_HUMAN	CCT2	physical	26344197
NB5R1_HUMAN	CYB5R1	physical	26344197
NB5R3_HUMAN	CYB5R3	physical	26344197
CYC_HUMAN	CYCS	physical	26344197
INO1_HUMAN	ISYNA1	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
STML2_HUMAN	STOML2	physical	26344197
TSR1_HUMAN	TSR1	physical	26344197
UCRI_HUMAN	UQCRFS1	physical	26344197
SYVC_HUMAN	VARS	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-30, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-33, AND MASSSPECTROMETRY.
PubMed: 18669648