POLR1G | ENSG00000117877 | NCBI 10849

Details for: POLR1G

Gene ID: 10849

Symbol: POLR1G

Ensembl ID: ENSG00000117877

Description: RNA polymerase I subunit G

Associated with

B-wich complex positively regulates rrna expression
(R-HSA-5250924)
Epigenetic regulation of gene expression
(R-HSA-212165)
Gene expression (transcription)
(R-HSA-74160)
Negative epigenetic regulation of rrna expression
(R-HSA-5250941)
Norc negatively regulates rrna expression
(R-HSA-427413)
Positive epigenetic regulation of rrna expression
(R-HSA-5250913)
Rna polymerase i promoter clearance
(R-HSA-73854)
Rna polymerase i promoter escape
(R-HSA-73772)
Rna polymerase i transcription
(R-HSA-73864)
Rna polymerase i transcription initiation
(R-HSA-73762)
Rna polymerase i transcription termination
(R-HSA-73863)
Chromosome
(GO:0005694)
Cytosol
(GO:0005829)
Fibrillar center
(GO:0001650)
Mitochondrion
(GO:0005739)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Rna binding
(GO:0003723)
Rna polymerase i complex
(GO:0005736)
Rna polymerase i transcription regulator complex
(GO:0000120)
Rrna transcription
(GO:0009303)
Transcription by rna polymerase i
(GO:0006360)
Transmembrane receptor protein tyrosine kinase signaling pathway
(GO:0007169)

Other Information

Proteins

A34.5

Genular Protein ID: 659030310

Symbol: RPA34_HUMAN

Name: A34.5

UniProtKB Accession Codes:

O15446 Q32N11 Q7Z5U2 Q9UPF6

Database IDs:

Citations:

PubMed ID: 9426281

Title: ASE-1: a novel protein of the fibrillar centres of the nucleolus and nucleolus organizer region of mitotic chromosomes.

PubMed ID: 9426281

DOI: 10.1007/s004120050271

PubMed ID: 10373416

Title: CAST, a novel CD3epsilon-binding protein transducing activation signal for interleukin-2 production in T cells.

PubMed ID: 10373416

DOI: 10.1074/jbc.274.26.18173

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: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16809778

Title: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor.

PubMed ID: 16809778

DOI: 10.1128/mcb.00230-06

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

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: 20068231

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

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

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: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

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: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

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

Sequence Information:

Length: 510
Mass: 54986
Checksum: D460FB944412D393
Sequence:

MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH 
VPLSGSQIVK GKLAGKRHRY RVLSSCPQAG EATLLAPSTE AGGGLTCASA PQGTLRILEG 
PQQSLSGSPL QPIPASPPPQ IPPGLRPRFC AFGGNPPVTG PRSALAPNLL TSGKKKKEMQ 
VTEAPVTQEA VNGHGALEVD MALGSPEMDV RKKKKKKNQQ LKEPEAAGPV GTEPTVETLE 
PLGVLFPSTT KKRKKPKGKE TFEPEDKTVK QEQINTEPLE DTVLSPTKKR KRQKGTEGME 
PEEGVTVESQ PQVKVEPLEE AIPLPPTKKR KKEKGQMAMM EPGTEAMEPV EPEMKPLESP 
GGTMAPQQPE GAKPQAQAAL AAPKKKTKKE KQQDATVEPE TEVVGPELPD DLEPQAAPTS 
TKKKKKKKER GHTVTEPIQP LEPELPGEGQ PEARATPGST KKRKKQSQES RMPETVPQEE 
MPGPPLNSES GEEAPTGRDK KRKQQQQQPV

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: POLR1G

Associated with

Other Information

ASE-1: a novel protein of the fibrillar centres of the nucleolus and nucleolus organizer region of mitotic chromosomes. PubMed ID: 9426281

CAST, a novel CD3epsilon-binding protein transducing activation signal for interleukin-2 production in T cells. PubMed ID: 10373416

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

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. PubMed ID: 16809778

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PubMed ID: 17525332

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

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

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

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

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

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

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

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