O14776 · TCRG1_HUMAN
- ProteinTranscription elongation regulator 1
- GeneTCERG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1098 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA polymerase binding | |
Molecular Function | RNA polymerase II-specific DNA-binding transcription factor binding | |
Molecular Function | transcription coactivator activity | |
Molecular Function | transcription coregulator activity | |
Molecular Function | transcription corepressor activity | |
Molecular Function | transcription elongation factor activity | |
Molecular Function | ubiquitin-like protein conjugating enzyme binding | |
Biological Process | mRNA processing | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | negative regulation of transcription elongation by RNA polymerase II | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription elongation by RNA polymerase II | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription elongation regulator 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO14776
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 148-150 | Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448. | ||||
Sequence: YYY → AAA | ||||||
Mutagenesis | 446-448 | Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150. | ||||
Sequence: YYY → AAA | ||||||
Mutagenesis | 545-547 | No effect. | ||||
Sequence: FFY → AAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 988 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, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000076063 | 1-1098 | UniProt | Transcription elongation regulator 1 | |||
Sequence: MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMPPVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKWQFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK | |||||||
Modified residue | 11 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 20 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 28 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 30 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 41 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 48 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 503 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 507 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 591 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 608 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 638 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 832 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 833 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 834 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 933 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via the second WW domain) with TREX1 (via proline-rich region) (By similarity).
Binds RNA polymerase II, HD and SF1
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O14776 | BARD1 Q99728 | 2 | EBI-473271, EBI-473181 | |
BINARY | O14776 | HTT P42858 | 9 | EBI-473271, EBI-466029 | |
BINARY | O14776 | TCERG1 O14776 | 4 | EBI-473271, EBI-473271 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-105 | Disordered | ||||
Sequence: MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMS | ||||||
Compositional bias | 36-105 | Pro residues | ||||
Sequence: PNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMS | ||||||
Domain | 131-164 | WW 1 | ||||
Sequence: PPTEEIWVENKTPDGKVYYYNARTRESAWTKPDG | ||||||
Coiled coil | 184-244 | |||||
Sequence: QAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQ | ||||||
Compositional bias | 259-327 | Polar residues | ||||
Sequence: STPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTAT | ||||||
Region | 259-348 | Disordered | ||||
Sequence: STPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSV | ||||||
Compositional bias | 328-348 | Pro residues | ||||
Sequence: PVQTVPQPHPQTLPPAVPHSV | ||||||
Domain | 429-462 | WW 2 | ||||
Sequence: ATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQE | ||||||
Compositional bias | 469-484 | Basic and acidic residues | ||||
Sequence: LEEKIKEPIKEPSEEP | ||||||
Region | 469-526 | Disordered | ||||
Sequence: LEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVAT | ||||||
Compositional bias | 496-520 | Basic and acidic residues | ||||
Sequence: EEPIKEIKEEPKEEEMTEEEKAAQK | ||||||
Domain | 528-561 | WW 3 | ||||
Sequence: PIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDD | ||||||
Coiled coil | 606-655 | |||||
Sequence: AIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERA | ||||||
Region | 615-640 | Disordered | ||||
Sequence: EEINEDEPVKAKKRKRDDNKDIDSEK | ||||||
Compositional bias | 618-640 | Basic and acidic residues | ||||
Sequence: NEDEPVKAKKRKRDDNKDIDSEK | ||||||
Motif | 626-630 | Nuclear localization signal | ||||
Sequence: KKRKR | ||||||
Domain | 659-712 | FF 1 | ||||
Sequence: LEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKT | ||||||
Domain | 725-779 | FF 2 | ||||
Sequence: IMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAA | ||||||
Domain | 791-846 | FF 3 | ||||
Sequence: RGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEK | ||||||
Coiled coil | 844-906 | |||||
Sequence: IEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKAL | ||||||
Region | 870-895 | Disordered | ||||
Sequence: REREREVQKARSEQTKEIDREREQHK | ||||||
Domain | 896-952 | FF 4 | ||||
Sequence: REEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEA | ||||||
Domain | 954-1010 | FF 5 | ||||
Sequence: TKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRD | ||||||
Domain | 1012-1077 | FF 6 | ||||
Sequence: YITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDD | ||||||
Region | 1076-1098 | Disordered | ||||
Sequence: DDLDRRGPPPPPTASEPTRRSTK |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O14776-1
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
- Length1,098
- Mass (Da)123,901
- Last updated2007-07-24 v2
- Checksum5F0A0C3A07EBF00F
O14776-2
- Name2
- Differences from canonical
- 379-399: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7P0T8N8 | A0A7P0T8N8_HUMAN | TCERG1 | 1115 | ||
G3V220 | G3V220_HUMAN | TCERG1 | 1032 | ||
A0AA34QVF9 | A0AA34QVF9_HUMAN | TCERG1 | 42 | ||
A0AA34QVU1 | A0AA34QVU1_HUMAN | TCERG1 | 674 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 36-105 | Pro residues | ||||
Sequence: PNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMS | ||||||
Compositional bias | 259-327 | Polar residues | ||||
Sequence: STPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTAT | ||||||
Sequence conflict | 324 | in Ref. 1; AAB80727 | ||||
Sequence: P → R | ||||||
Compositional bias | 328-348 | Pro residues | ||||
Sequence: PVQTVPQPHPQTLPPAVPHSV | ||||||
Alternative sequence | VSP_026933 | 379-399 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 469-484 | Basic and acidic residues | ||||
Sequence: LEEKIKEPIKEPSEEP | ||||||
Compositional bias | 496-520 | Basic and acidic residues | ||||
Sequence: EEPIKEIKEEPKEEEMTEEEKAAQK | ||||||
Compositional bias | 618-640 | Basic and acidic residues | ||||
Sequence: NEDEPVKAKKRKRDDNKDIDSEK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017789 EMBL· GenBank· DDBJ | AAB80727.1 EMBL· GenBank· DDBJ | mRNA | ||
AB209910 EMBL· GenBank· DDBJ | BAD93147.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC111727 EMBL· GenBank· DDBJ | AAI11728.1 EMBL· GenBank· DDBJ | mRNA |