CY24B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CY24B_HUMAN
• UniProt AC: P04839
• Protein Name: Cytochrome b-245 heavy chain
• Gene Name: CYBB {ECO:0000312|HGNC:HGNC:2578}
• Organism: Homo sapiens (Human).
• Sequence Length: 570
• Subcellular Localization: Cell membrane; Multi-pass membrane protein.
• Protein Description: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc..
• Protein Sequence: MGNWAVNEGLSIFVILVWLGLNVFLFVWYYRVYDIPPKFFYTRKLLGSALALARAPAACLNFNCMLILLPVCRNLLSFLRGSSACCSTRVRRQLDRNLTFHKMVAWMIALHSAIHTIAHLFNVEWCVNARVNNSDPYSVALSELGDRQNESYLNFARKRIKNPEGGLYLAVTLLAGITGVVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERIVRGQTAESLAVHNITVCEQKISEWGKIKECPIPQFAGNPPMTWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYCNNATNLKLKKIYFYWLCRDTHAFEWFADLLQLLESQMQERNNAGFLSYNIYLTGWDESQANHFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASQHPNTRIGVFLCGPEALAETLSKQSISNSESGPRGVHFIFNKENF

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
41	Phosphorylation	DIPPKFFYTRKLLGS CCCCHHHCHHHHHHH	14.57	-
42	Phosphorylation	IPPKFFYTRKLLGSA CCCHHHCHHHHHHHH	19.03	-
44	Ubiquitination	PKFFYTRKLLGSALA CHHHCHHHHHHHHHH	40.02	21906983
88	Phosphorylation	GSSACCSTRVRRQLD CCCHHCHHHHHHHHH	21.19	24719451
132	N-linked_Glycosylation	WCVNARVNNSDPYSV HHEECCCCCCCCCCE	36.41	19159218
149	N-linked_Glycosylation	SELGDRQNESYLNFA HHHCCCCCHHHHHHH	40.87	19159218
168	Phosphorylation	KNPEGGLYLAVTLLA CCCCCHHHHHHHHHH	8.90	-
178	Phosphorylation	VTLLAGITGVVITLC HHHHHHHHHHHHHHH	24.01	22210691
193	Phosphorylation	LILIITSSTKTIRRS HHHHHHCCCCHHHHH	25.85	22210691
194	Phosphorylation	ILIITSSTKTIRRSY HHHHHCCCCHHHHHH	31.79	22210691
240	N-linked_Glycosylation	AESLAVHNITVCEQK HHHHHCCCEEEEEEH	25.65	19159218
253	Ubiquitination	QKISEWGKIKECPIP EHHHHCCCCCCCCCC	52.24	-
294	Ubiquitination	RFWRSQQKVVITKVV HHHHHCCCEEEEEEE	30.72	-
298	Phosphorylation	SQQKVVITKVVTHPF HCCCEEEEEEECCCC	13.23	19764811
313	2-Hydroxyisobutyrylation	KTIELQMKKKGFKME CEEEEEEHHCCCEEE	38.07	-
324	Phosphorylation	FKMEVGQYIFVKCPK CEEEECEEEEEECCC	7.15	-
334	Ubiquitination	VKCPKVSKLEWHPFT EECCCCCEEEEECEE	54.11	-
418	Phosphorylation	IGVTPFASILKSVWY CCCCCHHHHHHHHHH	28.91	24719451
486	Phosphorylation	YLTGWDESQANHFAV EEECCCHHHHCEEEE	31.92	-
545	Phosphorylation	GPEALAETLSKQSIS CHHHHHHHHHHHCCC	30.63	28857561
548	Ubiquitination	ALAETLSKQSISNSE HHHHHHHHHCCCCCC	51.70	-
552	Phosphorylation	TLSKQSISNSESGPR HHHHHCCCCCCCCCC	39.28	23532336

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
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:23023377

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CY24B_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 CY24B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACTB_HUMAN	ACTB	physical	16179592

Drug and Disease Associations

• Kegg Disease
• H00098: Chronic granulomatous disease, including the following four diseases: X-linked CGD (gp91 phox CGD);
• H01167: Gluconobacter infection
• OMIM Disease
• 306400: Granulomatous disease, chronic, X-linked (CGD)
• 300645: Immunodeficiency 34 (IMD34)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00514: Dextromethorphan

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-132; ASN-149 AND ASN-240,AND MASS SPECTROMETRY.
PubMed: 19159218