dbPTM

QCR1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	QCR1_MOUSE
UniProt AC	Q9CZ13
Protein Name	Cytochrome b-c1 complex subunit 1, mitochondrial
Gene Name	Uqcrc1
Organism	Mus musculus (Mouse).
Sequence Length	480
Subcellular Localization	Mitochondrion inner membrane.
Protein Description	This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (By similarity)..
Protein Sequence	MAASAVCRAACSGTQVLLRTRRSPALLRLPALRGTATFAQALQSVPETQVSILDNGLRVASEQSSHATCTVGVWIDAGSRYETEKNNGAGYFLEHLAFKGTKNRPGNALEKEVESIGAHLNAYSTREHTAYLIKALSKDLPKVVELLADIVQNSSLEDSQIEKERDVILREMQENDASMQNVVFDYLHATAFQGTPLAQAVEGPSENVRRLSRTDLTDYLNRHYKAPRMVLAAAGGVEHQQLLDLAQKHLSSVSRVYEEDAVPGLTPCRFTGSEIRHRDDALPLAHVAIAVEGPGWANPDNVTLQVANAIIGHYDCTYGGGVHLSSPLASVAVANKLCQSFQTFNISYSDTGLLGAHFVCDAMSIDDMVFFLQGQWMRLCTSATESEVTRGKNILRNALVSHLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIQEVDAQMLRDICSKYFYDQCPAVAGYGPIEQLPDYNRIRSGMFWLRF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
69	S-nitrosylation	EQSSHATCTVGVWID CCCCCCEEEEEEEEE	2.77	21278135
69	S-nitrosocysteine	EQSSHATCTVGVWID CCCCCCEEEEEEEEE	2.77	-
85	Acetylation	GSRYETEKNNGAGYF CCCEEECCCCCCCHH	64.23	23864654
85	Succinylation	GSRYETEKNNGAGYF CCCEEECCCCCCCHH	64.23	24315375
99	Acetylation	FLEHLAFKGTKNRPG HHHHHHHCCCCCCCC	61.13	24062335
111	Acetylation	RPGNALEKEVESIGA CCCCHHHHHHHHHHH	68.83	23576753
111	Succinylation	RPGNALEKEVESIGA CCCCHHHHHHHHHHH	68.83	24315375
134	Acetylation	EHTAYLIKALSKDLP HHHHHHHHHHHCCHH	40.45	23201123
138	Malonylation	YLIKALSKDLPKVVE HHHHHHHCCHHHHHH	65.22	26320211
138	Ubiquitination	YLIKALSKDLPKVVE HHHHHHHCCHHHHHH	65.22	27667366
138	Succinylation	YLIKALSKDLPKVVE HHHHHHHCCHHHHHH	65.22	23806337
138	Acetylation	YLIKALSKDLPKVVE HHHHHHHCCHHHHHH	65.22	23576753
142	Acetylation	ALSKDLPKVVELLAD HHHCCHHHHHHHHHH	67.23	24062335
154	Phosphorylation	LADIVQNSSLEDSQI HHHHHHCCCCCHHHH	21.14	30352176
155	Phosphorylation	ADIVQNSSLEDSQIE HHHHHCCCCCHHHHH	43.24	30352176
159	Phosphorylation	QNSSLEDSQIEKERD HCCCCCHHHHHHHHH	24.55	29899451
163	Succinylation	LEDSQIEKERDVILR CCHHHHHHHHHHHHH	60.73	23806337
163	Succinylation	LEDSQIEKERDVILR CCHHHHHHHHHHHHH	60.73	-
163	Acetylation	LEDSQIEKERDVILR CCHHHHHHHHHHHHH	60.73	23576753
212	Phosphorylation	SENVRRLSRTDLTDY CHHHHHHCHHCHHHH	31.18	26824392
214	Phosphorylation	NVRRLSRTDLTDYLN HHHHHCHHCHHHHHH	31.80	28542873
217	O-linked_Glycosylation	RLSRTDLTDYLNRHY HHCHHCHHHHHHHHC	25.96	55414539
217	Phosphorylation	RLSRTDLTDYLNRHY HHCHHCHHHHHHHHC	25.96	28609623
219	Phosphorylation	SRTDLTDYLNRHYKA CHHCHHHHHHHHCCC	10.71	29899451
248	Succinylation	QLLDLAQKHLSSVSR HHHHHHHHHHHHHHH	40.69	24315375
248	Ubiquitination	QLLDLAQKHLSSVSR HHHHHHHHHHHHHHH	40.69	-
248	Acetylation	QLLDLAQKHLSSVSR HHHHHHHHHHHHHHH	40.69	23576753
268	S-palmitoylation	AVPGLTPCRFTGSEI CCCCCCCCCCCCCCC	4.75	28526873
268	S-nitrosylation	AVPGLTPCRFTGSEI CCCCCCCCCCCCCCC	4.75	24895380
268	S-nitrosocysteine	AVPGLTPCRFTGSEI CCCCCCCCCCCCCCC	4.75	-
380	S-palmitoylation	QGQWMRLCTSATESE HHHHHHHHCCCCCCH	1.67	28526873
380	S-nitrosylation	QGQWMRLCTSATESE HHHHHHHHCCCCCCH	1.67	22178444
380	Glutathionylation	QGQWMRLCTSATESE HHHHHHHHCCCCCCH	1.67	24333276
380	S-nitrosocysteine	QGQWMRLCTSATESE HHHHHHHHCCCCCCH	1.67	-
410	S-nitrosocysteine	LDGTTPVCEDIGRSL CCCCCCCCHHHHHHH	4.02	-
410	Glutathionylation	LDGTTPVCEDIGRSL CCCCCCCCHHHHHHH	4.02	24333276
410	S-nitrosylation	LDGTTPVCEDIGRSL CCCCCCCCHHHHHHH	4.02	22178444
410	S-palmitoylation	LDGTTPVCEDIGRSL CCCCCCCCHHHHHHH	4.02	28526873
420	Phosphorylation	IGRSLLTYGRRIPLA HHHHHHHHCCCCCHH	14.49	25195567
447	Acetylation	MLRDICSKYFYDQCP HHHHHHHHHHHHHCC	34.66	23864654
447	Succinylation	MLRDICSKYFYDQCP HHHHHHHHHHHHHCC	34.66	26388266
453	S-palmitoylation	SKYFYDQCPAVAGYG HHHHHHHCCCCCCCC	1.82	28526873
453	S-nitrosylation	SKYFYDQCPAVAGYG HHHHHHHCCCCCCCC	1.82	21278135
453	Glutathionylation	SKYFYDQCPAVAGYG HHHHHHHCCCCCCCC	1.82	24333276
453	S-nitrosocysteine	SKYFYDQCPAVAGYG HHHHHHHCCCCCCCC	1.82	-
473	Phosphorylation	PDYNRIRSGMFWLRF CCCCCCCCCCCEECC	32.04	22817900

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 QCR1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
138	K	Acetylation		23576753
Acetylation of Lys-138 is observed in liver mitochondria from fasted mice but not from fed mice.

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 QCR1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of QCR1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of QCR1_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-138 AND LYS-248, AND MASSSPECTROMETRY.	16916647 [Abstract]

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