Q62018 · CTR9_MOUSE
- ProteinRNA polymerase-associated protein CTR9 homolog
- GeneCtr9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1173 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription (By similarity).
Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3
Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA polymerase-associated protein CTR9 homolog
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ62018
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000231589 | 1-1173 | RNA polymerase-associated protein CTR9 homolog | |||
Sequence: MSRGSIEIPLRDTDEVIELDFDQLPEGDEVISILKQEHTQLHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDYRDHEKDQMTCLDTLAAYYVQQARKEKNKDNKKDLITQATLLYTMADKIIMYDQNHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNNIPALLGKACISFNKKDYRGALAYYKKALRTNPGCPAEVRLGMGHCFVKLNKLEKARLAFSRALELNSKCVGALVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSNPMVLNHLANHFFFKKDYSKVQHLALHAFHNTEVEAMQAESCYQLARSFHVQEDYDQAFQYYYQATQFASSSFVLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNNYETMKILGSLYAASEDQEKRDIAKGHLKKVTEQYPDDVEAWIELAQILEQTDIQGALSAYGTATRILQEKVQADVPPEILNNVGALHFRLGNLGEAKKYFLASLDRAKAEAEHDEHYYNAISVTTSYNLARLYEAMCEFHEAEKLYKNILREHPNYVDCYLRLGAMARDKGNFYEASDWFKEALQINQDHPDAWSLIGNLHLAKQEWGPGQKKFERILKQPATQSDTYSMLALGNVWLQTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKNLYAANGIGAVLAHKGYFREARDVFAQVREATADISDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKHQNTEVVLYLARALFKCGKLQECKQTLLKARHVAPSDTVLMFNVALVLQRLATSVLKDEKSNLKEVLNAVKELELAHRYFSYLSKVGDKMRFDLALAASEARQCSDLLSQAQYHVARARKQDEEERELRAKQEQEKELLRQKLLKEQEEKRLREKEEQKKLLEQRAQYVEKTKNILMFTGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPVSKKKKRRKGSGSEQEGEEEEGGERKKKRRRRPPKGEEGSEEEETENGPKPKKRRPPRAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQNKSGSEAGSPRRSGRQESDEDSDSDQPSRKRRRSGSEQSDNESVQSGRSPSGASENENDSRPASPSAESDHESEQGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD | ||||||
Modified residue | 925 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 932 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 941 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 943 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 970 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1020 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1021 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1037 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1039 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1041 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1079 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1083 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1085 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1095 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1100 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and SKIC8 (By similarity).
The PAF1 complex interacts with PHF5A (PubMed:27749823).
Interacts with KMT2A/MLL1 (By similarity).
Interacts with STAT3 (PubMed:17911113).
Interacts with SETD5 (PubMed:27864380).
Interacts with ERCC6 (By similarity).
The PAF1 complex interacts with PHF5A (PubMed:27749823).
Interacts with KMT2A/MLL1 (By similarity).
Interacts with STAT3 (PubMed:17911113).
Interacts with SETD5 (PubMed:27864380).
Interacts with ERCC6 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 41-75 | TPR 1 | ||||
Sequence: LHIWIALALEYYKQGKTEEFVKLLEAARIDGNLDY | ||||||
Repeat | 129-162 | TPR 2 | ||||
Sequence: NHLLGRACFCLLEGDKMDQADAQFHFVLNQSPNN | ||||||
Repeat | 163-196 | TPR 3 | ||||
Sequence: IPALLGKACISFNKKDYRGALAYYKKALRTNPGC | ||||||
Repeat | 198-231 | TPR 4 | ||||
Sequence: AEVRLGMGHCFVKLNKLEKARLAFSRALELNSKC | ||||||
Repeat | 235-268 | TPR 5 | ||||
Sequence: LVGLAVLELNNKEADSIKNGVQLLSRAYTIDPSN | ||||||
Repeat | 306-339 | TPR 6 | ||||
Sequence: AESCYQLARSFHVQEDYDQAFQYYYQATQFASSS | ||||||
Repeat | 341-374 | TPR 7 | ||||
Sequence: VLPFFGLGQMYIYRGDKENASQCFEKVLKAYPNN | ||||||
Repeat | 412-444 | TPR 8 | ||||
Sequence: VEAWIELAQILEQTDIQGALSAYGTATRILQEK | ||||||
Repeat | 451-484 | TPR 9 | ||||
Sequence: PEILNNVGALHFRLGNLGEAKKYFLASLDRAKAE | ||||||
Repeat | 497-530 | TPR 10 | ||||
Sequence: VTTSYNLARLYEAMCEFHEAEKLYKNILREHPNY | ||||||
Repeat | 531-564 | TPR 11 | ||||
Sequence: VDCYLRLGAMARDKGNFYEASDWFKEALQINQDH | ||||||
Repeat | 566-598 | TPR 12 | ||||
Sequence: DAWSLIGNLHLAKQEWGPGQKKFERILKQPATQ | ||||||
Repeat | 613-646 | TPR 13 | ||||
Sequence: QTLHQPTRDREKEKRHQDRALAIYKQVLRNDAKN | ||||||
Repeat | 647-680 | TPR 14 | ||||
Sequence: LYAANGIGAVLAHKGYFREARDVFAQVREATADI | ||||||
Repeat | 681-714 | TPR 15 | ||||
Sequence: SDVWLNLAHIYVEQKQYISAVQMYENCLRKFYKH | ||||||
Repeat | 717-750 | TPR 16 | ||||
Sequence: TEVVLYLARALFKCGKLQECKQTLLKARHVAPSD | ||||||
Region | 892-1173 | Disordered | ||||
Sequence: TGETEATKEKKRGGGGGRRSKKGGEFDEFVNDDTDDDLPVSKKKKRRKGSGSEQEGEEEEGGERKKKRRRRPPKGEEGSEEEETENGPKPKKRRPPRAEKKKAPKPERLPPSMKGKIKSKAIISSSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQNKSGSEAGSPRRSGRQESDEDSDSDQPSRKRRRSGSEQSDNESVQSGRSPSGASENENDSRPASPSAESDHESEQGSDNEGSGQGSGNESEPEGSNNEASDRGSEHGSDDSD | ||||||
Compositional bias | 895-919 | Basic and acidic residues | ||||
Sequence: TEATKEKKRGGGGGRRSKKGGEFDE | ||||||
Compositional bias | 926-957 | Basic and acidic residues | ||||
Sequence: DDDLPVSKKKKRRKGSGSEQEGEEEEGGERKK | ||||||
Compositional bias | 964-983 | Basic and acidic residues | ||||
Sequence: PKGEEGSEEEETENGPKPKK | ||||||
Compositional bias | 991-1005 | Basic and acidic residues | ||||
Sequence: KKKAPKPERLPPSMK | ||||||
Compositional bias | 1016-1061 | Basic and acidic residues | ||||
Sequence: SSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQ | ||||||
Compositional bias | 1073-1099 | Basic and acidic residues | ||||
Sequence: RSGRQESDEDSDSDQPSRKRRRSGSEQ | ||||||
Compositional bias | 1100-1124 | Polar residues | ||||
Sequence: SDNESVQSGRSPSGASENENDSRPA | ||||||
Compositional bias | 1139-1155 | Polar residues | ||||
Sequence: DNEGSGQGSGNESEPEG | ||||||
Compositional bias | 1156-1173 | Basic and acidic residues | ||||
Sequence: SNNEASDRGSEHGSDDSD |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q62018-1
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
- Length1,173
- Mass (Da)133,408
- Last updated2006-04-04 v2
- Checksum2FB84564F1BEFD79
Q62018-2
- Name2
Q62018-3
- Name3
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 144 | in Ref. 1; AAC42083 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 223 | in Ref. 3; AAH53910 | ||||
Sequence: R → S | ||||||
Sequence conflict | 242 | in Ref. 2; BAC32223 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 390 | in Ref. 3; AAH53910 | ||||
Sequence: D → Y | ||||||
Alternative sequence | VSP_017846 | 704-721 | in isoform 2 | |||
Sequence: YENCLRKFYKHQNTEVVL → VTSLLLRIVACNVEPWLP | ||||||
Sequence conflict | 719 | in Ref. 2; BAE22373 | ||||
Sequence: V → I | ||||||
Alternative sequence | VSP_017847 | 722-1173 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_017848 | 816-860 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 877 | in Ref. 3; AAH80719 | ||||
Sequence: Q → R | ||||||
Compositional bias | 895-919 | Basic and acidic residues | ||||
Sequence: TEATKEKKRGGGGGRRSKKGGEFDE | ||||||
Sequence conflict | 900 | in Ref. 3; AAH80719 | ||||
Sequence: E → K | ||||||
Compositional bias | 926-957 | Basic and acidic residues | ||||
Sequence: DDDLPVSKKKKRRKGSGSEQEGEEEEGGERKK | ||||||
Compositional bias | 964-983 | Basic and acidic residues | ||||
Sequence: PKGEEGSEEEETENGPKPKK | ||||||
Compositional bias | 991-1005 | Basic and acidic residues | ||||
Sequence: KKKAPKPERLPPSMK | ||||||
Alternative sequence | VSP_017849 | 995-1032 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 1016-1061 | Basic and acidic residues | ||||
Sequence: SSDDSSDEDKLKIADEGHPRNSNSDSDDDERPNRRASSESDSDDNQ | ||||||
Compositional bias | 1073-1099 | Basic and acidic residues | ||||
Sequence: RSGRQESDEDSDSDQPSRKRRRSGSEQ | ||||||
Compositional bias | 1100-1124 | Polar residues | ||||
Sequence: SDNESVQSGRSPSGASENENDSRPA | ||||||
Compositional bias | 1139-1155 | Polar residues | ||||
Sequence: DNEGSGQGSGNESEPEG | ||||||
Compositional bias | 1156-1173 | Basic and acidic residues | ||||
Sequence: SNNEASDRGSEHGSDDSD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L49502 EMBL· GenBank· DDBJ | AAC42083.1 EMBL· GenBank· DDBJ | mRNA | ||
AK040205 EMBL· GenBank· DDBJ | BAC30540.1 EMBL· GenBank· DDBJ | mRNA | ||
AK040331 EMBL· GenBank· DDBJ | BAC30566.1 EMBL· GenBank· DDBJ | mRNA | ||
AK045101 EMBL· GenBank· DDBJ | BAC32223.1 EMBL· GenBank· DDBJ | mRNA | ||
AK083921 EMBL· GenBank· DDBJ | BAC39065.2 EMBL· GenBank· DDBJ | mRNA | ||
AK134990 EMBL· GenBank· DDBJ | BAE22373.1 EMBL· GenBank· DDBJ | mRNA | ||
AK148536 EMBL· GenBank· DDBJ | BAE28606.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053910 EMBL· GenBank· DDBJ | AAH53910.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC080719 EMBL· GenBank· DDBJ | AAH80719.1 EMBL· GenBank· DDBJ | mRNA | ||
AB093211 EMBL· GenBank· DDBJ | BAC41395.1 EMBL· GenBank· DDBJ | Transcribed RNA |