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9.B.103.1.1
Putative trimeric, Calvecin-like, β-stranded, glyco-conjugated Ca2+ uniporter, gC1qR. (282 aas) (MAM33 Superfamily) (Starkov, 2010).

Accession Number:Q07021
Protein Name:Complement component 1 Q subcomponent-binding protein, mitochondrial
Length:282
Molecular Weight:31362.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Mitochondrion matrix1
Substrate Ca2+

Cross database links:

Genevestigator: Q07021
eggNOG: prNOG15115
HEGENOM: HBG715847
Entrez Gene ID: 708   
Pfam: PF02330   
KEGG: hsa:708   

Gene Ontology

GO:0005759 C:mitochondrial matrix
GO:0005634 C:nucleus
GO:0005886 C:plasma membrane
GO:0007597 P:blood coagulation, intrinsic pathway
GO:0006955 P:immune response
GO:0044419 P:interspecies interaction between organisms

References (15)

[1] “Cloning and expression of a cDNA covering the complete coding region of the P32 subunit of human pre-mRNA splicing factor SF2.”  Honore B.et.al.   8262387
[2] “Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular 'heads' of C1q.”  Ghebrehiwet B.et.al.   8195709
[3] “The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter analysis.”  Tye A.J.et.al.   11278463
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.”  Krainer A.R.et.al.   1830244
[6] “Molecular cloning of human fibroblast hyaluronic acid-binding protein confirms its identity with P-32, a protein co-purified with splicing factor SF2. Hyaluronic acid-binding protein as P-32 protein, co-purified with splicing factor SF2.”  Deb T.B.et.al.   8567680
[7] “Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria.”  Beatch M.D.et.al.   10823864
[8] “CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-associated protein p32 and affects splicing in vivo.”  Even Y.et.al.   16721827
[9] “Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32.”  Berro R.et.al.   16537587
[10] “Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.”  Tang L.-Y.et.al.   17693683
[11] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[12] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.”  Mayya V.et.al.   19690332
[13] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[14] “Initial characterization of the human central proteome.”  Burkard T.R.et.al.   21269460
[15] “Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein.”  Jiang J.et.al.   10097078
Structure:
1P32   3RPX   6SZW     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR 
61:	PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL 
121:	VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK 
181:	ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM 
241:	DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ