dbPTM

QCR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	QCR2_HUMAN
UniProt AC	P22695
Protein Name	Cytochrome b-c1 complex subunit 2, mitochondrial
Gene Name	UQCRC2
Organism	Homo sapiens (Human).
Sequence Length	453
Subcellular Localization	Mitochondrion inner membrane Peripheral membrane protein Matrix side.
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. The core protein 2 is required for the assembly of the complex..
Protein Sequence	MKLLTRAGSFSRFYSLKVAPKVKATAAPAGAPPQPQDLEFTKLPNGLVIASLENYSPVSRIGLFIKAGSRYEDFSNLGTTHLLRLTSSLTTKGASSFKITRGIEAVGGKLSVTATRENMAYTVECLRGDVDILMEFLLNVTTAPEFRRWEVADLQPQLKIDKAVAFQNPQTHVIENLHAAAYRNALANPLYCPDYRIGKVTSEELHYFVQNHFTSARMALIGLGVSHPVLKQVAEQFLNMRGGLGLSGAKANYRGGEIREQNGDSLVHAAFVAESAVAGSAEANAFSVLQHVLGAGPHVKRGSNTTSHLHQAVAKATQQPFDVSAFNASYSDSGLFGIYTISQATAAGDVIKAAYNQVKTIAQGNLSNTDVQAAKNKLKAGYLMSVESSECFLEEVGSQALVAGSYMPPSTVLQQIDSVANADIINAAKKFVSGQKSMAASGNLGHTPFVDEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	KLLTRAGSFSRFYSL CCCCCCCCCHHEEEE	21.04	24719451
15	Phosphorylation	GSFSRFYSLKVAPKV CCCHHEEEEECCCCC	20.99	24719451
17	Ubiquitination	FSRFYSLKVAPKVKA CHHEEEEECCCCCCC	30.34	27667366
21	Ubiquitination	YSLKVAPKVKATAAP EEEECCCCCCCCCCC	46.78	22817900
23	Ubiquitination	LKVAPKVKATAAPAG EECCCCCCCCCCCCC	46.26	21906983
42	Ubiquitination	PQDLEFTKLPNGLVI CCCCCEEECCCCEEE	68.23	16196087
42	Acetylation	PQDLEFTKLPNGLVI CCCCCEEECCCCEEE	68.23	25038526
55	Phosphorylation	VIASLENYSPVSRIG EEEEECCCCCCCEEE	12.65	-
56	Phosphorylation	IASLENYSPVSRIGL EEEECCCCCCCEEEE	30.33	-
59	Phosphorylation	LENYSPVSRIGLFIK ECCCCCCCEEEEEEE	22.89	-
66	Ubiquitination	SRIGLFIKAGSRYED CEEEEEEECCCCCHH	39.08	23503661
66	Acetylation	SRIGLFIKAGSRYED CEEEEEEECCCCCHH	39.08	25825284
69	Phosphorylation	GLFIKAGSRYEDFSN EEEEECCCCCHHHCC	36.23	28152594
71	Phosphorylation	FIKAGSRYEDFSNLG EEECCCCCHHHCCCC	22.88	28152594
75	Phosphorylation	GSRYEDFSNLGTTHL CCCCHHHCCCCHHHH	43.39	28152594
80	Phosphorylation	DFSNLGTTHLLRLTS HHCCCCHHHHHHHHH	14.55	25332170
86	Phosphorylation	TTHLLRLTSSLTTKG HHHHHHHHHCCCCCC	15.16	20068231
87	Phosphorylation	THLLRLTSSLTTKGA HHHHHHHHCCCCCCC	28.13	20068231
88	Phosphorylation	HLLRLTSSLTTKGAS HHHHHHHCCCCCCCC	25.21	20068231
90	Phosphorylation	LRLTSSLTTKGASSF HHHHHCCCCCCCCCC	28.54	20068231
91	Phosphorylation	RLTSSLTTKGASSFK HHHHCCCCCCCCCCE	32.54	20068231
92	Malonylation	LTSSLTTKGASSFKI HHHCCCCCCCCCCEE	47.44	26320211
92	Succinylation	LTSSLTTKGASSFKI HHHCCCCCCCCCCEE	47.44	23954790
92	2-Hydroxyisobutyrylation	LTSSLTTKGASSFKI HHHCCCCCCCCCCEE	47.44	-
92	Ubiquitination	LTSSLTTKGASSFKI HHHCCCCCCCCCCEE	47.44	32142685
98	Succinylation	TKGASSFKITRGIEA CCCCCCCEEEECEEE	45.15	23954790
98	2-Hydroxyisobutyrylation	TKGASSFKITRGIEA CCCCCCCEEEECEEE	45.15	-
98	Ubiquitination	TKGASSFKITRGIEA CCCCCCCEEEECEEE	45.15	27667366
98	Methylation	TKGASSFKITRGIEA CCCCCCCEEEECEEE	45.15	51163891
98	Acetylation	TKGASSFKITRGIEA CCCCCCCEEEECEEE	45.15	25953088
100	Phosphorylation	GASSFKITRGIEAVG CCCCCEEEECEEEEC	24.35	-
109	2-Hydroxyisobutyrylation	GIEAVGGKLSVTATR CEEEECCEEEEEEEE	31.49	-
109	Ubiquitination	GIEAVGGKLSVTATR CEEEECCEEEEEEEE	31.49	23503661
111	Phosphorylation	EAVGGKLSVTATREN EEECCEEEEEEEECH	22.40	-
113	Phosphorylation	VGGKLSVTATRENMA ECCEEEEEEEECHHE	20.95	-
134	Sulfoxidation	RGDVDILMEFLLNVT HCCHHHHHHHHHCCC	3.32	28183972
159	Succinylation	ADLQPQLKIDKAVAF CCCCCCCCCCEEHHC	43.54	23954790
159	Acetylation	ADLQPQLKIDKAVAF CCCCCCCCCCEEHHC	43.54	23236377
159	Ubiquitination	ADLQPQLKIDKAVAF CCCCCCCCCCEEHHC	43.54	22817900
162	2-Hydroxyisobutyrylation	QPQLKIDKAVAFQNP CCCCCCCEEHHCCCC	48.51	-
162	Ubiquitination	QPQLKIDKAVAFQNP CCCCCCCEEHHCCCC	48.51	21906983
182	Phosphorylation	ENLHAAAYRNALANP HHHHHHHHHHHHCCC	10.32	-
191	Phosphorylation	NALANPLYCPDYRIG HHHCCCCCCCCCCCC	11.82	28152594
192	S-palmitoylation	ALANPLYCPDYRIGK HHCCCCCCCCCCCCE	2.45	26865113
195	Phosphorylation	NPLYCPDYRIGKVTS CCCCCCCCCCCEECH	6.83	28152594
199	Ubiquitination	CPDYRIGKVTSEELH CCCCCCCEECHHHHH	39.71	21906983
199	Acetylation	CPDYRIGKVTSEELH CCCCCCCEECHHHHH	39.71	-
201	Phosphorylation	DYRIGKVTSEELHYF CCCCCEECHHHHHHH	33.63	28857561
202	Phosphorylation	YRIGKVTSEELHYFV CCCCEECHHHHHHHH	31.87	28857561
207	Phosphorylation	VTSEELHYFVQNHFT ECHHHHHHHHHHCCH	20.33	28152594
214	Phosphorylation	YFVQNHFTSARMALI HHHHHCCHHHHHHHH	17.58	28152594
215	Phosphorylation	FVQNHFTSARMALIG HHHHCCHHHHHHHHH	16.97	28152594
226	Phosphorylation	ALIGLGVSHPVLKQV HHHHCCCCCHHHHHH	21.92	24719451
231	Ubiquitination	GVSHPVLKQVAEQFL CCCCHHHHHHHHHHH	42.85	16196087
240	Sulfoxidation	VAEQFLNMRGGLGLS HHHHHHHCCCCCCCC	4.60	28465586
241	Methylation	AEQFLNMRGGLGLSG HHHHHHCCCCCCCCC	34.65	115919545
247	Phosphorylation	MRGGLGLSGAKANYR CCCCCCCCCCCCCCC	34.60	26437602
250	2-Hydroxyisobutyrylation	GLGLSGAKANYRGGE CCCCCCCCCCCCCCC	40.46	-
250	Acetylation	GLGLSGAKANYRGGE CCCCCCCCCCCCCCC	40.46	27452117
250	Succinylation	GLGLSGAKANYRGGE CCCCCCCCCCCCCCC	40.46	23954790
250	Ubiquitination	GLGLSGAKANYRGGE CCCCCCCCCCCCCCC	40.46	27667366
254	Methylation	SGAKANYRGGEIREQ CCCCCCCCCCCCCCC	46.58	115919549
301	Methylation	GAGPHVKRGSNTTSH CCCCCCCCCCCCHHH	53.32	115919553
303	Phosphorylation	GPHVKRGSNTTSHLH CCCCCCCCCCHHHHH	34.73	25850435
305	Phosphorylation	HVKRGSNTTSHLHQA CCCCCCCCHHHHHHH	31.22	25850435
306	Phosphorylation	VKRGSNTTSHLHQAV CCCCCCCHHHHHHHH	20.57	26657352
307	Phosphorylation	KRGSNTTSHLHQAVA CCCCCCHHHHHHHHH	23.24	25850435
317	Phosphorylation	HQAVAKATQQPFDVS HHHHHHHHCCCCCCE	27.34	28985074
329	Phosphorylation	DVSAFNASYSDSGLF CCEEEECCCCCCCEE	26.69	28985074
342	Phosphorylation	LFGIYTISQATAAGD EEEEEEEECCHHHHH	13.13	28985074
359	Acetylation	KAAYNQVKTIAQGNL HHHHHHHHHHHCCCC	25.17	23236377
359	Succinylation	KAAYNQVKTIAQGNL HHHHHHHHHHHCCCC	25.17	27452117
359	Ubiquitination	KAAYNQVKTIAQGNL HHHHHHHHHHHCCCC	25.17	21963094
359	Malonylation	KAAYNQVKTIAQGNL HHHHHHHHHHHCCCC	25.17	32601280
360	Phosphorylation	AAYNQVKTIAQGNLS HHHHHHHHHHCCCCC	23.76	27251275
367	O-linked_Glycosylation	TIAQGNLSNTDVQAA HHHCCCCCHHHHHHH	41.50	29351928
367	Phosphorylation	TIAQGNLSNTDVQAA HHHCCCCCHHHHHHH	41.50	28857561
369	Phosphorylation	AQGNLSNTDVQAAKN HCCCCCHHHHHHHHH	33.88	28857561
369	O-linked_Glycosylation	AQGNLSNTDVQAAKN HCCCCCHHHHHHHHH	33.88	29351928
375	2-Hydroxyisobutyrylation	NTDVQAAKNKLKAGY HHHHHHHHHHCCCCE	58.60	-
375	Ubiquitination	NTDVQAAKNKLKAGY HHHHHHHHHHCCCCE	58.60	27667366
377	Ubiquitination	DVQAAKNKLKAGYLM HHHHHHHHCCCCEEE	51.13	22817900
379	Ubiquitination	QAAKNKLKAGYLMSV HHHHHHCCCCEEEEE	41.18	22817900
429	Acetylation	ADIINAAKKFVSGQK HHHHHHHHHHHCCCC	44.31	30593273
430	Ubiquitination	DIINAAKKFVSGQKS HHHHHHHHHHCCCCC	46.39	27667366
436	Ubiquitination	KKFVSGQKSMAASGN HHHHCCCCCHHCCCC	45.80	23503661
447	Phosphorylation	ASGNLGHTPFVDEL- CCCCCCCCCCCCCC-	19.34	-

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 QCR2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of QCR2_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 QCR2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RTN4_HUMAN	RTN4	physical	12067236
SRSF5_HUMAN	SRSF5	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
AFG32_HUMAN	AFG3L2	physical	26344197
ATD3A_HUMAN	ATAD3A	physical	26344197
ATPA_HUMAN	ATP5A1	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
TCPQ_HUMAN	CCT8	physical	26344197
CLH1_HUMAN	CLTC	physical	26344197
COPB_HUMAN	COPB1	physical	26344197
COX41_HUMAN	COX4I1	physical	26344197
DX39B_HUMAN	DDX39B	physical	26344197
ROA3_HUMAN	HNRNPA3	physical	26344197
HNRPK_HUMAN	HNRNPK	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
IDE_HUMAN	IDE	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
NDUAC_HUMAN	NDUFA12	physical	26344197
NDUA9_HUMAN	NDUFA9	physical	26344197
NDUB8_HUMAN	NDUFB8	physical	26344197
NDUS1_HUMAN	NDUFS1	physical	26344197
NDUS3_HUMAN	NDUFS3	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
GLU2B_HUMAN	PRKCSH	physical	26344197
RAB1B_HUMAN	RAB1B	physical	26344197
RAB6B_HUMAN	RAB6B	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
ACOD_HUMAN	SCD	physical	26344197
SCD5_HUMAN	SCD5	physical	26344197
S61A1_HUMAN	SEC61A1	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
TMCO1_HUMAN	TMCO1	physical	26344197
TOM22_HUMAN	TOMM22	physical	26344197
TPM2_HUMAN	TPM2	physical	26344197
TPM3_HUMAN	TPM3	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197
VDAC1_HUMAN	VDAC1	physical	26344197
VDAC2_HUMAN	VDAC2	physical	26344197
STOM_HUMAN	STOM	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615160	Mitochondrial complex III deficiency, nuclear 5 (MC3DN5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of QCR2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, AND MASSSPECTROMETRY.	18187866 [Abstract]