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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Integrator complex subunit 13

UniprotKB/SwissProt ID: Q9NVM9 (Q9NVM9)

Gene Name: INTS13

Organism: Homo sapiens (Human)

Function: Component of the integrator complex, a multiprotein complex that terminates RNA polymerase II (Pol II) transcription in the promoter-proximal region of genes (PubMed:38570683, PubMed:38823386). The integrator complex provides a quality checkpoint during transcription elongation by driving premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: the complex terminates transcription by (1) catalyzing dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, (2) degrading the exiting nascent RNA transcript via endonuclease activity and (3) promoting the release of Pol II from bound DNA (PubMed:38570683). The integrator complex is also involved in terminating the synthesis of non-coding Pol II transcripts, such as enhancer RNAs (eRNAs), small nuclear RNAs (snRNAs), telomerase RNAs and long non-coding RNAs (lncRNAs) (PubMed:32647223). Within the integrator complex, INTS13 is part of the integrator tail module and acts as a platform for the recruitment of transcription factors at promoters (PubMed:38823386, PubMed:38906142). At prophase, mediates recruitment of cytoplasmic dynein to the nuclear envelope, a step important for proper centrosome-nucleus coupling (PubMed:23097494, PubMed:23904267). At G2/M phase, may be required for proper spindle formation and execution of cytokinesis (PubMed:23097494, PubMed:23904267)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR019355 Cell_cycle_regulator_Mat89Bb

The S-nitrosylation sites of Q9NVM9

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 331 PRTNNIELHY C TGAYRISPVD   
2 406 LEDPPSISEG C GGRVTDYRIT   
3 494 ESLTEEDVLN C QKTIYNLVDM