SCAF8_HUMAN
ID SCAF8_HUMAN Reviewed; 1271 AA.
AC Q9UPN6; B7Z888; Q5TBU6; Q6NSK3; Q9BQN8; Q9BX43;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=SR-related and CTD-associated factor 8 {ECO:0000303|PubMed:9528809};
DE AltName: Full=CDC5L complex-associated protein 7 {ECO:0000303|PubMed:11101529};
DE AltName: Full=RNA-binding motif protein 16 {ECO:0000305};
GN Name=SCAF8 {ECO:0000303|PubMed:9528809, ECO:0000312|HGNC:HGNC:20959};
GN Synonyms=CCAP7 {ECO:0000303|PubMed:11101529},
GN KIAA1116 {ECO:0000303|PubMed:10470851},
GN RBM16 {ECO:0000312|HGNC:HGNC:20959};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH POLR2A, AND SUBCELLULAR LOCATION.
RX PubMed=9528809; DOI=10.1128/mcb.18.4.2406;
RA Patturajan M., Wei X., Berezney R., Corden J.L.;
RT "A nuclear matrix protein interacts with the phosphorylated C-terminal
RT domain of RNA polymerase II.";
RL Mol. Cell. Biol. 18:2406-2415(1998).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH CDC5L AND SPLICEOSOMAL PROTEINS, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11101529; DOI=10.1093/emboj/19.23.6569;
RA Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.;
RT "Functional analysis of the human CDC5L complex and identification of its
RT components by mass spectrometry.";
RL EMBO J. 19:6569-6581(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-615, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP SUMOYLATION AT LYS-18, AND PHOSPHORYLATION AT THR-6.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-617 AND SER-779, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-917; ARG-927 AND ARG-938, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP STRUCTURE BY NMR OF 1-140.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RPR domain of putative RNA-binding protein 16.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-136 IN COMPLEX WITH POLR2A
RP PEPTIDE, INTERACTION WITH POLR2A, AND SUBUNIT.
RX PubMed=18550522; DOI=10.1074/jbc.m803540200;
RA Becker R., Loll B., Meinhart A.;
RT "Snapshots of the RNA processing factor SCAF8 bound to different
RT phosphorylated forms of the carboxyl-terminal domain of RNA polymerase
RT II.";
RL J. Biol. Chem. 283:22659-22669(2008).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH POLR2A.
RX PubMed=31104839; DOI=10.1016/j.cell.2019.04.038;
RA Gregersen L.H., Mitter R., Ugalde A.P., Nojima T., Proudfoot N.J.,
RA Agami R., Stewart A., Svejstrup J.Q.;
RT "SCAF4 and SCAF8, mRNA anti-terminator proteins.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: Anti-terminator protein required to prevent early mRNA
CC termination during transcription (PubMed:31104839). Together with
CC SCAF4, acts by suppressing the use of early, alternative poly(A) sites,
CC thereby preventing the accumulation of non-functional truncated
CC proteins (PubMed:31104839). Mechanistically, associates with the
CC phosphorylated C-terminal heptapeptide repeat domain (CTD) of the
CC largest RNA polymerase II subunit (POLR2A), and subsequently binds
CC nascent RNA upstream of early polyadenylation sites to prevent
CC premature mRNA transcript cleavage and polyadenylation
CC (PubMed:31104839). Independently of SCAF4, also acts as a positive
CC regulator of transcript elongation (PubMed:31104839).
CC {ECO:0000269|PubMed:31104839}.
CC -!- SUBUNIT: Interacts with POLR2A; via C-terminal heptapeptide repeat
CC domain (CTD) phosphorylated at 'Ser-2' and 'Ser-5' (PubMed:18550522,
CC PubMed:9528809, PubMed:31104839). Identified in a complex with CDC5L
CC and other spliceosomal proteins (PubMed:11101529).
CC {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:18550522,
CC ECO:0000269|PubMed:31104839, ECO:0000269|PubMed:9528809}.
CC -!- INTERACTION:
CC Q9UPN6; O75420: GIGYF1; NbExp=3; IntAct=EBI-7954236, EBI-947774;
CC Q9UPN6; Q08379: GOLGA2; NbExp=4; IntAct=EBI-7954236, EBI-618309;
CC Q9UPN6; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-7954236, EBI-11523345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11101529,
CC ECO:0000269|PubMed:31104839, ECO:0000269|PubMed:9528809}. Nucleus
CC matrix {ECO:0000269|PubMed:9528809}. Note=Detected in granular nuclear
CC foci which correspond to sites of active transcription.
CC {ECO:0000269|PubMed:31104839, ECO:0000269|PubMed:9528809}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPN6-2; Sequence=VSP_056149, VSP_056150;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83068.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB029039; BAA83068.2; ALT_INIT; mRNA.
DR EMBL; AK303001; BAH13874.1; -; mRNA.
DR EMBL; AL121952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC070071; AAH70071.1; -; mRNA.
DR CCDS; CCDS5247.1; -. [Q9UPN6-1]
DR CCDS; CCDS69226.1; -. [Q9UPN6-2]
DR RefSeq; NP_001273117.1; NM_001286188.1.
DR RefSeq; NP_001273118.1; NM_001286189.1. [Q9UPN6-2]
DR RefSeq; NP_001273123.1; NM_001286194.1.
DR RefSeq; NP_001273128.1; NM_001286199.1. [Q9UPN6-1]
DR RefSeq; NP_055707.3; NM_014892.4. [Q9UPN6-1]
DR PDB; 2DIW; NMR; -; A=1-137.
DR PDB; 3D9I; X-ray; 1.91 A; A/B=1-136.
DR PDB; 3D9J; X-ray; 1.60 A; A/B=1-136.
DR PDB; 3D9K; X-ray; 2.20 A; A/B=1-136.
DR PDB; 3D9L; X-ray; 2.20 A; A/B=1-136.
DR PDB; 3D9M; X-ray; 1.75 A; A/B=1-136.
DR PDB; 3D9N; X-ray; 1.60 A; A/B=1-136.
DR PDB; 3D9O; X-ray; 2.00 A; A/B=1-136.
DR PDB; 3D9P; X-ray; 2.10 A; A/B=1-136.
DR PDBsum; 2DIW; -.
DR PDBsum; 3D9I; -.
DR PDBsum; 3D9J; -.
DR PDBsum; 3D9K; -.
DR PDBsum; 3D9L; -.
DR PDBsum; 3D9M; -.
DR PDBsum; 3D9N; -.
DR PDBsum; 3D9O; -.
DR PDBsum; 3D9P; -.
DR AlphaFoldDB; Q9UPN6; -.
DR SMR; Q9UPN6; -.
DR BioGRID; 116503; 48.
DR CORUM; Q9UPN6; -.
DR IntAct; Q9UPN6; 20.
DR MINT; Q9UPN6; -.
DR STRING; 9606.ENSP00000413098; -.
DR GlyGen; Q9UPN6; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q9UPN6; -.
DR PhosphoSitePlus; Q9UPN6; -.
DR BioMuta; SCAF8; -.
DR DMDM; 30580495; -.
DR EPD; Q9UPN6; -.
DR jPOST; Q9UPN6; -.
DR MassIVE; Q9UPN6; -.
DR MaxQB; Q9UPN6; -.
DR PaxDb; Q9UPN6; -.
DR PeptideAtlas; Q9UPN6; -.
DR PRIDE; Q9UPN6; -.
DR ProteomicsDB; 6932; -.
DR ProteomicsDB; 85390; -. [Q9UPN6-1]
DR Antibodypedia; 33407; 101 antibodies from 22 providers.
DR DNASU; 22828; -.
DR Ensembl; ENST00000367178.8; ENSP00000356146.3; ENSG00000213079.10. [Q9UPN6-1]
DR Ensembl; ENST00000367186.7; ENSP00000356154.4; ENSG00000213079.10. [Q9UPN6-2]
DR GeneID; 22828; -.
DR KEGG; hsa:22828; -.
DR MANE-Select; ENST00000367178.8; ENSP00000356146.3; NM_014892.5; NP_055707.3.
DR UCSC; uc003qpz.5; human. [Q9UPN6-1]
DR CTD; 22828; -.
DR DisGeNET; 22828; -.
DR GeneCards; SCAF8; -.
DR HGNC; HGNC:20959; SCAF8.
DR HPA; ENSG00000213079; Low tissue specificity.
DR MIM; 616024; gene.
DR neXtProt; NX_Q9UPN6; -.
DR OpenTargets; ENSG00000213079; -.
DR PharmGKB; PA128394587; -.
DR VEuPathDB; HostDB:ENSG00000213079; -.
DR eggNOG; KOG0132; Eukaryota.
DR GeneTree; ENSGT00530000063946; -.
DR HOGENOM; CLU_005263_1_0_1; -.
DR InParanoid; Q9UPN6; -.
DR OrthoDB; 821342at2759; -.
DR PhylomeDB; Q9UPN6; -.
DR TreeFam; TF324527; -.
DR PathwayCommons; Q9UPN6; -.
DR SignaLink; Q9UPN6; -.
DR BioGRID-ORCS; 22828; 37 hits in 1087 CRISPR screens.
DR ChiTaRS; SCAF8; human.
DR EvolutionaryTrace; Q9UPN6; -.
DR GenomeRNAi; 22828; -.
DR Pharos; Q9UPN6; Tbio.
DR PRO; PR:Q9UPN6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UPN6; protein.
DR Bgee; ENSG00000213079; Expressed in secondary oocyte and 216 other tissues.
DR ExpressionAtlas; Q9UPN6; baseline and differential.
DR Genevisible; Q9UPN6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IPI:UniProtKB.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR CDD; cd12462; RRM_SCAF8; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00590; -.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034370; SCAF8_RRM.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1271
FT /note="SR-related and CTD-associated factor 8"
FT /id="PRO_0000081780"
FT DOMAIN 1..139
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 477..551
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..441
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20388717"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 917
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 927
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 938
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1073
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6DID3"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT VAR_SEQ 1
FT /note="M -> MPQPLLPALPPLSSPSGAGSCGPSGGECSGRRLFRRRARGLRSDNM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056149"
FT VAR_SEQ 10
FT /note="E -> EDCASTPACTDCFSSSMDTRSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056150"
FT VARIANT 865
FT /note="S -> N (in dbSNP:rs34802160)"
FT /id="VAR_052220"
FT CONFLICT 297
FT /note="N -> I (in Ref. 4; AAH70071)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:3D9J"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3D9J"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3D9J"
SQ SEQUENCE 1271 AA; 140519 MW; 9856758DB7622319 CRC64;
MEAVKTFNSE LYSLNDYKPP ISKAKMTQIT KAAIKAIKFY KHVVQSVEKF IQKCKPEYKV
PGLYVIDSIV RQSRHQFGQE KDVFAPRFSN NIISTFQNLY RCPGDDKSKI VRVLNLWQKN
NVFKSEIIQP LLDMAAGIPP PVVTPVLAST TTAMSNTPGT PVTPVTPANV VQGLPDPWVS
QITNTDTLAA VAQILQSPQG QQLQQLIQTL QIQQQKPQPS ILQALDAGLV VQLQALTAQL
TAAAAAANTL TPLEQGVSFN KKLMDRFDFG EDSEHSEEPK KEIPASQLSH VSESVNNSIF
HQIAEQLQQQ NLEHLRQQLL EQQQPQKATP QDSQEGTFGS EHSASPSQGS SQQHFLEPEV
NLDDSIDIQQ QDMDIDEGQD GVEEEVFEQE AKKVAVRSRS RTHSRSRSRS PRKRRSRSRS
GSRKRKHRKR SRSRSRERKR KSSRSYSSER RAREREKERQ KKGLPPIRSK TLSVCSTTLW
VGQVDKKATQ QDLTNLFEEF GQIESINMIP PRGCAYVCMV HRQDAFRALQ KLSSGSYKIG
SKVIKIAWAL NKGVKTEYKQ FWDVDLGVTY IPWEKVKVDD LEGFAEGGMI DQETVNTEWE
TVKSSEPVKE TVQTTQSPTP VEKETVVTTQ AEVFPPPVAM LQIPVAPAVP TVSLVPPAFP
VSMPVPPPGF SPIPPPPFLR ASFNPSQPPP GFMPPPVPPP VVPPPTIPPV VPTSLVQPSL
SMTPETVKDV GFGSLVIPGG SVASNLATSA LPAGNVFNAP TKQAEPEEKV PHLIDHQISS
GENTRSVIPN DISSNAAILG GQPPNVTSNS GILGVQRPNV SSNSEILGVR PSNVSSSSGI
IAAQPPNILN NSGILGIQPP SVSNSSGLLG VLPPNIPNNS GLVGVQPPNV PNTPGLLGTQ
PPAGPQNLPP LSIPNQRMPT MPMLDIRPGL IPQAPGPRFP LIQPGIPPQR GIPPPSVLDS
ALHPPPRGPF PPGDIFSQPE RPFLAPGRQS VDNVTNPEKR IPLGNDNIQQ EGDRDYRFPP
IETRESISRP PPVDVRDVVG RPIDPREGPG RPPLDGRDHF GRPPVDIREN LVRPGIDHLG
RRDHFGFNPE KPWGHRGDFD EREHRVLPVY GGPKGLHEER GRFRSGNYRF DPRSGPWNRG
FGQEVHRDFD DRRRPWERQR DRDDRDFDFC REMNGNRLGR DRIQNTWVPP PHARVFDYFE
GATSQRKGDN VPQVNGENTE RHAQPPPIPV QNDPELYEKL TSSNEINKEK SDTVADIESE
PVVESTETEG T
