C1QBP_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: C1QBP_RAT
• UniProt AC: O35796
• Protein Name: Complement component 1 Q subcomponent-binding protein, mitochondrial
• Gene Name: C1qbp
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 279
• 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. 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. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense..
• Protein Sequence: MLPLLRCVPRALGAAATGLRASIPAPPLRHLLQPAPRPCLRPFGLLSVRAGSARRSGLLQPPVPCACGCGALHTEGDKAFVEFLTDEIKEEKKIQKHKSLPKMSGDWELEVNGTEAKLLRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKAEEQEPELTSTPNFVVEVTKTDGKKTLVLDCHYPEDEIGHEDEAESDIFSIKEVSFQTTGDSEWRDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ

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
78	Acetylation	ALHTEGDKAFVEFLT CCCCCCHHHHHHHHH	55.36	25786129
89	Acetylation	EFLTDEIKEEKKIQK HHHHHHHHHHHHHHH	58.74	25786129
89	Succinylation	EFLTDEIKEEKKIQK HHHHHHHHHHHHHHH	58.74	26843850
92	Acetylation	TDEIKEEKKIQKHKS HHHHHHHHHHHHCCC	57.16	22902405
99	Phosphorylation	KKIQKHKSLPKMSGD HHHHHCCCCCCCCCC	50.01	23984901
102	Acetylation	QKHKSLPKMSGDWEL HHCCCCCCCCCCEEE	51.49	22902405
104	Phosphorylation	HKSLPKMSGDWELEV CCCCCCCCCCEEEEE	39.46	23984901
172	Acetylation	NFVVEVTKTDGKKTL CEEEEEEECCCCEEE	50.20	22902405
176	Acetylation	EVTKTDGKKTLVLDC EEEECCCCEEEEEEE	45.45	22902405
185	Phosphorylation	TLVLDCHYPEDEIGH EEEEEEECCHHHCCC	18.04	-
198	Phosphorylation	GHEDEAESDIFSIKE CCCCCCCCCCEEEEE	42.95	23991683
202	Phosphorylation	EAESDIFSIKEVSFQ CCCCCCEEEEEEEEE	32.84	30181290
211	Phosphorylation	KEVSFQTTGDSEWRD EEEEEEECCCCCCCC	28.36	-
277	Succinylation	EDLKSFVKSQ----- HHHHHHHHCC-----	40.92	26843850

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

Oops, there are no upstream regulatory protein records of C1QBP_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of C1QBP_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of C1QBP_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of C1QBP_RAT !!

Drug and Disease Associations

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