Q8WUA4 · TF3C2_HUMAN
- ProteinGeneral transcription factor 3C polypeptide 2
- GeneGTF3C2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids911 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | transcription factor TFIIIC complex | |
Molecular Function | RNA polymerase III general transcription initiation factor activity | |
Biological Process | 5S class rRNA transcription by RNA polymerase III | |
Biological Process | transcription by RNA polymerase III | |
Biological Process | tRNA transcription by RNA polymerase III |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGeneral transcription factor 3C polypeptide 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WUA4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 961 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000050985 | 1-911 | UniProt | General transcription factor 3C polypeptide 2 | |||
Sequence: MDTCGVGYVALGEAGPVGNMTVVDSPGQEVLNQLDVKTSSEMTSAEASVEMSLPTPLPGFEDSPDQRRLPPEQESLSRLEQPDLSSEMSKVSKPRASKPGRKRGGRTRKGPKRPQQPNPPSAPLVPGLLDQSNPLSTPMPKKRGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERPRRRAAQVALLYLQELAEELSTALPAPVSCPEGPKVSSPTKPKKIRQPAACPGGEEVDGAPRDEDFFLQVEAEDVEESEGPSESSSEPEPVVPRSTPRGSTSGKQKPHCRGMAPNGLPNHIMAPVWKCLHLTKDFREQKHSYWEFAEWIPLAWKWHLLSELEAAPYLPQEEKSPLFSVQREGLPEDGTLYRINRFSSITAHPERWDVSFFTGGPLWALDWCPVPEGAGASQYVALFSSPDMNETHPLSQLHSGPGLLQLWGLGTLQQESCPGNRAHFVYGIACDNGCIWDLKFCPSGAWELPGTPRKAPLLPRLGLLALACSDGKVLLFSLPHPEALLAQQPPDAVKPAIYKVQCVATLQVGSMQATDPSECGQCLSLAWMPTRPHQHLAAGYYNGMVVFWNLPTNSPLQRIRLSDGSLKLYPFQCFLAHDQAVRTLQWCKANSHFLVSAGSDRKIKFWDLRRPYEPINSIKRFLSTELAWLLPYNGVTVAQDNCYASYGLCGIHYIDAGYLGFKAYFTAPRKGTVWSLSGSDWLGTIAAGDISGELIAAILPDMALNPINVKRPVERRFPIYKADLIPYQDSPEGPDHSSASSGVPNPPKARTYTETVNHHYLLFQDTDLGSFHDLLRREPMLRMQEGEGHSQLCLDRLQLEAIHKVRFSPNLDSYGWLVSGGQSGLVRIHFVRGLASPLGHRMQLESRAHFNAMFQPSSPTRRPGFSPTSHRLLPTP | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 63 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 132 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 165 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 167 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 219 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 220 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 260 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 597 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 597 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 765 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 871 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 892 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 892 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 893 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 895 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 895 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 901 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 901 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Part of the TFIIIC subcomplex TFIIIC2, consisting of six subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8WUA4 | GTF3C1 Q12789 | 3 | EBI-1237062, EBI-357956 | |
BINARY | Q8WUA4 | MTOR P42345 | 3 | EBI-1237062, EBI-359260 | |
BINARY | Q8WUA4 | RPTOR Q8N122 | 3 | EBI-1237062, EBI-1567928 | |
BINARY | Q8WUA4-2 | VAC14 Q08AM6 | 3 | EBI-11957962, EBI-2107455 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 24-187 | Disordered | ||||
Sequence: DSPGQEVLNQLDVKTSSEMTSAEASVEMSLPTPLPGFEDSPDQRRLPPEQESLSRLEQPDLSSEMSKVSKPRASKPGRKRGGRTRKGPKRPQQPNPPSAPLVPGLLDQSNPLSTPMPKKRGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERPRRRA | ||||||
Compositional bias | 25-50 | Polar residues | ||||
Sequence: SPGQEVLNQLDVKTSSEMTSAEASVE | ||||||
Compositional bias | 78-92 | Polar residues | ||||
Sequence: RLEQPDLSSEMSKVS | ||||||
Compositional bias | 95-110 | Basic residues | ||||
Sequence: RASKPGRKRGGRTRKG | ||||||
Compositional bias | 143-183 | Basic and acidic residues | ||||
Sequence: RGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERP | ||||||
Region | 205-297 | Disordered | ||||
Sequence: ALPAPVSCPEGPKVSSPTKPKKIRQPAACPGGEEVDGAPRDEDFFLQVEAEDVEESEGPSESSSEPEPVVPRSTPRGSTSGKQKPHCRGMAPN | ||||||
Compositional bias | 251-265 | Acidic residues | ||||
Sequence: QVEAEDVEESEGPSE | ||||||
Compositional bias | 266-285 | Polar residues | ||||
Sequence: SSSEPEPVVPRSTPRGSTSG | ||||||
Repeat | 366-426 | WD 1 | ||||
Sequence: PEDGTLYRINRFSSITAHPERWDVSFFTGGPLWALDWCPVPEGAGASQYVALFSSPDMNET | ||||||
Repeat | 427-483 | WD 2 | ||||
Sequence: HPLSQLHSGPGLLQLWGLGTLQQESCPGNRAHFVYGIACDNGCIWDLKFCPSGAWEL | ||||||
Repeat | 484-535 | WD 3 | ||||
Sequence: PGTPRKAPLLPRLGLLALACSDGKVLLFSLPHPEALLAQQPPDAVKPAIYKV | ||||||
Repeat | 536-603 | WD 4 | ||||
Sequence: QCVATLQVGSMQATDPSECGQCLSLAWMPTRPHQHLAAGYYNGMVVFWNLPTNSPLQRIRLSDGSLKL | ||||||
Repeat | 604-654 | WD 5 | ||||
Sequence: YPFQCFLAHDQAVRTLQWCKANSHFLVSAGSDRKIKFWDLRRPYEPINSIK | ||||||
Repeat | 655-690 | WD 6 | ||||
Sequence: RFLSTELAWLLPYNGVTVAQDNCYASYGLCGIHYID | ||||||
Region | 765-785 | Disordered | ||||
Sequence: SPEGPDHSSASSGVPNPPKAR | ||||||
Compositional bias | 768-785 | Polar residues | ||||
Sequence: GPDHSSASSGVPNPPKAR | ||||||
Region | 889-911 | Disordered | ||||
Sequence: FQPSSPTRRPGFSPTSHRLLPTP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8WUA4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length911
- Mass (Da)100,680
- Last updated2004-06-07 v2
- ChecksumB59D91DE74555192
Q8WUA4-2
- Name2
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 25-50 | Polar residues | ||||
Sequence: SPGQEVLNQLDVKTSSEMTSAEASVE | ||||||
Compositional bias | 78-92 | Polar residues | ||||
Sequence: RLEQPDLSSEMSKVS | ||||||
Compositional bias | 95-110 | Basic residues | ||||
Sequence: RASKPGRKRGGRTRKG | ||||||
Compositional bias | 143-183 | Basic and acidic residues | ||||
Sequence: RGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERP | ||||||
Compositional bias | 251-265 | Acidic residues | ||||
Sequence: QVEAEDVEESEGPSE | ||||||
Compositional bias | 266-285 | Polar residues | ||||
Sequence: SSSEPEPVVPRSTPRGSTSG | ||||||
Sequence conflict | 301 | in Ref. 3; AAP88801 and 4; AAH20981 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_010566 | 579-585 | in isoform 2 | |||
Sequence: MVVFWNL → KKNQNKT | ||||||
Alternative sequence | VSP_010567 | 586-911 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 768-785 | Polar residues | ||||
Sequence: GPDHSSASSGVPNPPKAR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D13636 EMBL· GenBank· DDBJ | BAA02800.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009799 EMBL· GenBank· DDBJ | AAP88801.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00595.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471053 EMBL· GenBank· DDBJ | EAX00596.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000212 EMBL· GenBank· DDBJ | AAH00212.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020981 EMBL· GenBank· DDBJ | AAH20981.1 EMBL· GenBank· DDBJ | mRNA | ||
AF054988 EMBL· GenBank· DDBJ | AAC09349.1 EMBL· GenBank· DDBJ | mRNA |