RPAP2

RPAP2
Identifiers
Aliases	RPAP2, C1orf82, Rtr1, RNA polymerase II associated protein 2
External IDs	OMIM: 611476; MGI: 2141142; GeneCards: RPAP2
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.3.16 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 1 (human) Band 1p22.1 Start 92,299,059 bp End 92,402,056 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 F Start 107,745,239 bp End 107,809,704 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon cerebellar vermis corpus callosum Skeletal muscle tissue of biceps brachii gonad epithelium of colon ventricular zone pons tonsil testicle Top expressed in zygote primary oocyte secondary oocyte spermatocyte genital tubercle seminiferous tubule tail of embryo spermatid facial motor nucleus muscle of thigh More reference expression data BioGPS n/a
Gene ontology Molecular function phosphoprotein phosphatase activity metal ion binding hydrolase activity RNA polymerase II CTD heptapeptide repeat phosphatase activity protein serine/threonine phosphatase activity protein binding RNA polymerase core enzyme binding Cellular component nucleolus RNA polymerase II, holoenzyme cytoplasm nucleus nucleoplasm cytosol Biological process snRNA transcription transcription, DNA-templated dephosphorylation of RNA polymerase II C-terminal domain regulation of transcription, DNA-templated snRNA transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 79871 231571 Ensembl ENSG00000122484 ENSMUSG00000033773 UniProt Q8IXW5 Q8VC34 RefSeq (mRNA) NM_024813 NM_001163461 NM_001163462 NM_001289569 NM_001289570 NM_144911 NM_001359916 NM_001359917 NM_001359918 RefSeq (protein) NP_079089 NP_001156933 NP_001156934 NP_001276498 NP_001276499 NP_659160 NP_001346845 NP_001346846 NP_001346847 Location (UCSC) Chr 1: 92.3 – 92.4 Mb Chr 5: 107.75 – 107.81 Mb PubMed search
Wikidata
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RNA polymerase II associated protein 2, also known as RPAP2, is a human gene.

Further reading

• Jeronimo C, Forget D, Bouchard A, Li Q, Chua G, Poitras C, Thérien C, Bergeron D, Bourassa S, Greenblatt J, Chabot B, Poirier GG, Hughes TR, Blanchette M, Price DH, Coulombe B (Jul 2007). "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme". Molecular Cell. 27 (2): 262–74. doi:10.1016/j.molcel.2007.06.027. PMC 4498903. PMID 17643375.
• Ingham RJ, Colwill K, Howard C, Dettwiler S, Lim CS, Yu J, Hersi K, Raaijmakers J, Gish G, Mbamalu G, Taylor L, Yeung B, Vassilovski G, Amin M, Chen F, Matskova L, Winberg G, Ernberg I, Linding R, O'donnell P, Starostine A, Keller W, Metalnikov P, Stark C, Pawson T (Aug 2005). "WW domains provide a platform for the assembly of multiprotein networks". Molecular and Cellular Biology. 25 (16): 7092–106. doi:10.1128/MCB.25.16.7092-7106.2005. PMC 1190255. PMID 16055720.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Sowa ME, Bennett EJ, Gygi SP, Harper JW (Jul 2009). "Defining the human deubiquitinating enzyme interaction landscape". Cell. 138 (2): 389–403. doi:10.1016/j.cell.2009.04.042. PMC 2716422. PMID 19615732.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.