dbPTM

C1QBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	C1QBP_HUMAN
UniProt AC	Q07021
Protein Name	Complement component 1 Q subcomponent-binding protein, mitochondrial
Gene Name	C1QBP
Organism	Homo sapiens (Human).
Sequence Length	282
Subcellular Localization	Mitochondrion matrix . Nucleus . Cell membrane Peripheral membrane protein Extracellular side. Secreted. Cytoplasm . Nucleus, nucleolus . Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes.
Protein Description	Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. [PubMed: 28942965 In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection.; (Microbial infection) Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA.; (Microbial infection) In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A.; (Microbial infection) Involved in replication of Rubella virus.]
Protein Sequence	MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	VPRVLGSSVAGLRAA HHHHHCCCHHHHHHC	17.75	24719451
26	Phosphorylation	LRAAAPASPFRQLLQ HHHCCCCCHHHHHHC	24.42	28674419
80	Ubiquitination	SLHTDGDKAFVDFLS CCCCCCCHHHHHHHC	49.61	-
80	Acetylation	SLHTDGDKAFVDFLS CCCCCCCHHHHHHHC	49.61	30582509
87	Phosphorylation	KAFVDFLSDEIKEER HHHHHHHCHHHHHHH	32.94	30266825
91	2-Hydroxyisobutyrylation	DFLSDEIKEERKIQK HHHCHHHHHHHHHHH	52.02	-
91	Ubiquitination	DFLSDEIKEERKIQK HHHCHHHHHHHHHHH	52.02	19608861
91	Succinylation	DFLSDEIKEERKIQK HHHCHHHHHHHHHHH	52.02	23954790
91	Acetylation	DFLSDEIKEERKIQK HHHCHHHHHHHHHHH	52.02	19608861
95	Ubiquitination	DEIKEERKIQKHKTL HHHHHHHHHHHCCCC	53.41	23503661
98	Ubiquitination	KEERKIQKHKTLPKM HHHHHHHHCCCCCCC	51.01	23503661
100	Ubiquitination	ERKIQKHKTLPKMSG HHHHHHCCCCCCCCC	59.81	22817900
101	Phosphorylation	RKIQKHKTLPKMSGG HHHHHCCCCCCCCCC	48.27	24719451
104	Ubiquitination	QKHKTLPKMSGGWEL HHCCCCCCCCCCEEE	49.13	22817900
104	Acetylation	QKHKTLPKMSGGWEL HHCCCCCCCCCCEEE	49.13	23954790
106	Phosphorylation	HKTLPKMSGGWELEL CCCCCCCCCCEEEEE	40.04	21601212
130	Phosphorylation	KVAGEKITVTFNINN ECCCCEEEEEEEECC	25.26	20873877
132	Phosphorylation	AGEKITVTFNINNSI CCCEEEEEEEECCCC	11.43	20873877
138	Phosphorylation	VTFNINNSIPPTFDG EEEEECCCCCCCCCC	31.80	20873877
142	Phosphorylation	INNSIPPTFDGEEEP ECCCCCCCCCCCCCC	29.07	20873877
150	Phosphorylation	FDGEEEPSQGQKVEE CCCCCCCCCCCCCCC	50.66	20873877
163	Phosphorylation	EEQEPELTSTPNFVV CCCCCCCCCCCCEEE	28.97	25022875
164	Phosphorylation	EQEPELTSTPNFVVE CCCCCCCCCCCEEEE	55.26	27050516
165	Phosphorylation	QEPELTSTPNFVVEV CCCCCCCCCCEEEEE	19.60	27050516
174	2-Hydroxyisobutyrylation	NFVVEVIKNDDGKKA CEEEEEEECCCCCEE	60.54	-
174	Ubiquitination	NFVVEVIKNDDGKKA CEEEEEEECCCCCEE	60.54	21906983
179	Acetylation	VIKNDDGKKALVLDC EEECCCCCEEEEEEE	41.70	25953088
179	Ubiquitination	VIKNDDGKKALVLDC EEECCCCCEEEEEEE	41.70	22817900
180	Ubiquitination	IKNDDGKKALVLDCH EECCCCCEEEEEEEE	53.10	23503661
180	Acetylation	IKNDDGKKALVLDCH EECCCCCEEEEEEEE	53.10	11994287
180	2-Hydroxyisobutyrylation	IKNDDGKKALVLDCH EECCCCCEEEEEEEE	53.10	-
186	Glutathionylation	KKALVLDCHYPEDEV CEEEEEEEECCCCCC	2.64	22555962
188	Phosphorylation	ALVLDCHYPEDEVGQ EEEEEEECCCCCCCC	18.04	26552605
201	Phosphorylation	GQEDEAESDIFSIRE CCCCCCCCCCEEEEE	42.95	30266825
205	Phosphorylation	EAESDIFSIREVSFQ CCCCCCEEEEEEEEE	22.52	30266825
210	Phosphorylation	IFSIREVSFQSTGES CEEEEEEEEECCCCC	16.89	30266825
213	Phosphorylation	IREVSFQSTGESEWK EEEEEEECCCCCCCC	36.05	30266825
214	Phosphorylation	REVSFQSTGESEWKD EEEEEECCCCCCCCC	33.90	30266825
217	Phosphorylation	SFQSTGESEWKDTNY EEECCCCCCCCCCCE	50.53	30266825
220	Methylation	STGESEWKDTNYTLN CCCCCCCCCCCEEEC	51.10	-
228	Phosphorylation	DTNYTLNTDSLDWAL CCCEEECHHCHHHHH	30.03	27732954
230	Phosphorylation	NYTLNTDSLDWALYD CEEECHHCHHHHHHH	26.62	27732954
251	Phosphorylation	ADRGVDNTFADELVE HHCCCCCCCHHHHHH	18.75	27732954
261	Phosphorylation	DELVELSTALEHQEY HHHHHHHHHHHHHHH	48.13	25338102
280	Ubiquitination	EDLKSFVKSQ----- HHHHHHHHCC-----	40.92	-
281	Phosphorylation	DLKSFVKSQ------ HHHHHHHCC------	35.50	24719451

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 C1QBP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of C1QBP_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 C1QBP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRC2A_HUMAN	PRRC2A	physical	14667819
SRSF9_HUMAN	SRSF9	physical	10022843
SRSF1_HUMAN	SRSF1	physical	10022843
KPCD1_HUMAN	PRKD1	physical	10831594
KPCA_HUMAN	PRKCA	physical	10831594
KPCD_HUMAN	PRKCD	physical	10831594
KPCZ_HUMAN	PRKCZ	physical	10831594
PRKN_HUMAN	PARK2	physical	22008525
SPHM_HUMAN	SGSH	physical	22939629
CND1_HUMAN	NCAPD2	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
RPAC1_HUMAN	POLR1C	physical	22939629
YBOX3_HUMAN	YBX3	physical	22939629
NU107_HUMAN	NUP107	physical	22939629
NU153_HUMAN	NUP153	physical	22939629
RT10_HUMAN	MRPS10	physical	22904065
RT26_HUMAN	MRPS26	physical	22904065
RT34_HUMAN	MRPS34	physical	22904065
RM12_HUMAN	MRPL12	physical	22904065
RM38_HUMAN	MRPL38	physical	22904065
CH60_HUMAN	HSPD1	physical	22904065
ERAL1_HUMAN	ERAL1	physical	22904065
LPPRC_HUMAN	LRPPRC	physical	22904065
LONM_HUMAN	LONP1	physical	22904065
TFB2M_HUMAN	TFB2M	physical	22904065
PHB_HUMAN	PHB	physical	22904065
RT02_HUMAN	MRPS2	physical	22904065
RT27_HUMAN	MRPS27	physical	22904065
RT05_HUMAN	MRPS5	physical	22904065
RM18_HUMAN	MRPL18	physical	22904065
RM04_HUMAN	MRPL4	physical	22904065
GRP75_HUMAN	HSPA9	physical	22904065
EFTS_HUMAN	TSFM	physical	22904065
PTCD3_HUMAN	PTCD3	physical	22904065
CLPX_HUMAN	CLPX	physical	22904065
TFAM_HUMAN	TFAM	physical	22904065
PHB2_HUMAN	PHB2	physical	22904065
RT22_HUMAN	MRPS22	physical	22904065
RT28_HUMAN	MRPS28	physical	22904065
RT09_HUMAN	MRPS9	physical	22904065
RM19_HUMAN	MRPL19	physical	22904065
RM44_HUMAN	MRPL44	physical	22904065
HSP7C_HUMAN	HSPA8	physical	22904065
EFTU_HUMAN	TUFM	physical	22904065
RT23_HUMAN	MRPS23	physical	22904065
RT29_HUMAN	DAP3	physical	22904065
RT07_HUMAN	MRPS7	physical	22904065
RM21_HUMAN	MRPL21	physical	22904065
TRAP1_HUMAN	TRAP1	physical	22904065
RT25_HUMAN	MRPS25	physical	22904065
RT30_HUMAN	MRPS30	physical	22904065
RM22_HUMAN	MRPL22	physical	22904065
RM46_HUMAN	MRPL46	physical	22904065
RM03_HUMAN	MRPL3	physical	22904065
TFAM_MOUSE	Tfam	physical	22904065
RM03_MOUSE	Mrpl3	physical	22904065
RT22_MOUSE	Mrps22	physical	22904065
IKBE_HUMAN	NFKBIE	physical	21988832
CEBPA_HUMAN	CEBPA	physical	21988832
PLAK_HUMAN	JUP	physical	22863883
PDIA6_HUMAN	PDIA6	physical	22863883
SAP_HUMAN	PSAP	physical	22863883
PSME3_HUMAN	PSME3	physical	22863883
SAHH2_HUMAN	AHCYL1	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
UIMC1_HUMAN	UIMC1	physical	28842250

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
DB08818	Hyaluronan

Regulatory Network of C1QBP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-91, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-201, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND MASSSPECTROMETRY.	17693683 [Abstract]