SUB1 | ENSG00000113387 | NCBI 10923

Details for: SUB1

Gene ID: 10923

Symbol: SUB1

Ensembl ID: ENSG00000113387

Description: SUB1 regulator of transcription

Associated with

Extracellular exosome
(GO:0070062)
Identical protein binding
(GO:0042802)
Negative regulation of dna duplex unwinding
(GO:1905463)
Negative regulation of dna metabolic process
(GO:0051053)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Positive regulation of transcription initiation by rna polymerase ii
(GO:0060261)
Protein binding
(GO:0005515)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Rna binding
(GO:0003723)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)
Rna polymerase ii promoter clearance
(GO:0001111)
Single-stranded dna binding
(GO:0003697)
Transcription coactivator activity
(GO:0003713)
Transcription regulator complex
(GO:0005667)

Other Information

Proteins

Activated RNA polymerase II transcriptional coactivator p15

Genular Protein ID: 739747892

Symbol: TCP4_HUMAN

Name: Activated RNA polymerase II transcriptional coactivator p15

UniProtKB Accession Codes:

P53999 Q96L29

Database IDs:

Citations:

PubMed ID: 8062392

Title: A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators.

PubMed ID: 8062392

DOI: 10.1016/0092-8674(94)90429-4

PubMed ID: 8062391

Title: Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes.

PubMed ID: 8062391

DOI: 10.1016/0092-8674(94)90428-6

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7809103

Title: Phosphorylation negatively regulates the function of coactivator PC4.

PubMed ID: 7809103

DOI: 10.1073/pnas.91.26.12691

PubMed ID: 7628453

Title: The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation.

PubMed ID: 7628453

DOI: 10.1002/j.1460-2075.1995.tb07358.x

PubMed ID: 9482861

Title: A dynamic model for PC4 coactivator function in RNA polymerase II transcription.

PubMed ID: 9482861

DOI: 10.1073/pnas.95.5.2192

PubMed ID: 11389848

Title: Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination.

PubMed ID: 11389848

DOI: 10.1016/s1097-2765(01)00236-2

PubMed ID: 16689930

Title: Gradual phosphorylation regulates PC4 coactivator function.

PubMed ID: 16689930

DOI: 10.1111/j.1742-4658.2006.05165.x

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 9360603

Title: C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site.

PubMed ID: 9360603

DOI: 10.1038/nsb1197-900

PubMed ID: 16605275

Title: The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions.

PubMed ID: 16605275

DOI: 10.1021/bi052531b

PubMed ID: 16415882

Title: A global transcription cofactor bound to juxtaposed strands of unwound DNA.

PubMed ID: 16415882

DOI: 10.1038/nsmb1044

Sequence Information:

Length: 127
Mass: 14395
Checksum: 0DAE0CAAAD5E4E15
Sequence:

MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS SSKQSSSSRD 
DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR KGISLNPEQW SQLKEQISDI 
DDAVRKL

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: SUB1

Associated with

Other Information

A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators. PubMed ID: 8062392

Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes. PubMed ID: 8062391

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Phosphorylation negatively regulates the function of coactivator PC4. PubMed ID: 7809103

The coactivator p15 (PC4) initiates transcriptional activation during TFIIA-TFIID-promoter complex formation. PubMed ID: 7628453

A dynamic model for PC4 coactivator function in RNA polymerase II transcription. PubMed ID: 9482861

Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination. PubMed ID: 11389848

Gradual phosphorylation regulates PC4 coactivator function. PubMed ID: 16689930

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site. PubMed ID: 9360603

The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. PubMed ID: 16605275

A global transcription cofactor bound to juxtaposed strands of unwound DNA. PubMed ID: 16415882