ID ARGL1_HUMAN Reviewed; 273 AA. AC Q9NWB6; B4E0Y3; Q5T257; Q6IQ34; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Arginine and glutamate-rich protein 1; GN Name=ARGLU1; 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] (ISOFORMS 1 AND 3). RC TISSUE=Embryo, and Thymus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [4] 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-60 AND SER-77, AND 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 [7] 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 [8] RP FUNCTION, INTERACTION WITH MED1, AND SUBCELLULAR LOCATION. RX PubMed=21454576; DOI=10.1074/jbc.m110.206029; RA Zhang D., Jiang P., Xu Q., Zhang X.; RT "Arginine and glutamate-rich 1 (ARGLU1) interacts with mediator subunit 1 RT (MED1) and is required for estrogen receptor-mediated gene transcription RT and breast cancer cell growth."; RL J. Biol. Chem. 286:17746-17754(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-61 AND SER-77, AND RP IDENTIFICATION BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-77 AND SER-266, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY RP 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). CC -!- FUNCTION: Required for the estrogen-dependent expression of ESR1 target CC genes. Can act in cooperation with MED1. {ECO:0000269|PubMed:21454576}. CC -!- SUBUNIT: Directly interacts with MED1. {ECO:0000269|PubMed:21454576}. CC -!- INTERACTION: CC Q9NWB6; P78362: SRPK2; NbExp=2; IntAct=EBI-2808785, EBI-593303; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21454576}. CC Note=Recruited, in an estrogen-dependent manner, to ESR1 target gene CC promoters. Colocalizes with MED1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NWB6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NWB6-2; Sequence=VSP_025674; CC Name=3; CC IsoId=Q9NWB6-3; Sequence=VSP_053685, VSP_025674; CC -!- SIMILARITY: Belongs to the UPF0430 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK001016; BAA91467.1; -; mRNA. DR EMBL; AK303575; BAG64595.1; -; mRNA. DR EMBL; AL442127; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050434; AAH50434.1; -; mRNA. DR EMBL; BC071587; AAH71587.1; -; mRNA. DR CCDS; CCDS41906.1; -. [Q9NWB6-1] DR RefSeq; NP_060481.3; NM_018011.3. [Q9NWB6-1] DR AlphaFoldDB; Q9NWB6; -. DR SMR; Q9NWB6; -. DR BioGRID; 120397; 170. DR IntAct; Q9NWB6; 137. DR MINT; Q9NWB6; -. DR STRING; 9606.ENSP00000383059; -. DR GlyCosmos; Q9NWB6; 1 site, 1 glycan. DR GlyGen; Q9NWB6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NWB6; -. DR PhosphoSitePlus; Q9NWB6; -. DR SwissPalm; Q9NWB6; -. DR BioMuta; ARGLU1; -. DR DMDM; 74753014; -. DR EPD; Q9NWB6; -. DR jPOST; Q9NWB6; -. DR MassIVE; Q9NWB6; -. DR MaxQB; Q9NWB6; -. DR PaxDb; 9606-ENSP00000383059; -. DR PeptideAtlas; Q9NWB6; -. DR ProteomicsDB; 82923; -. [Q9NWB6-1] DR ProteomicsDB; 82924; -. [Q9NWB6-2] DR Pumba; Q9NWB6; -. DR Antibodypedia; 25410; 89 antibodies from 20 providers. DR DNASU; 55082; -. DR Ensembl; ENST00000400198.8; ENSP00000383059.3; ENSG00000134884.15. [Q9NWB6-1] DR GeneID; 55082; -. DR KEGG; hsa:55082; -. DR MANE-Select; ENST00000400198.8; ENSP00000383059.3; NM_018011.4; NP_060481.3. DR UCSC; uc001vqk.5; human. [Q9NWB6-1] DR AGR; HGNC:25482; -. DR CTD; 55082; -. DR DisGeNET; 55082; -. DR GeneCards; ARGLU1; -. DR HGNC; HGNC:25482; ARGLU1. DR HPA; ENSG00000134884; Low tissue specificity. DR MIM; 614046; gene. DR neXtProt; NX_Q9NWB6; -. DR OpenTargets; ENSG00000134884; -. DR PharmGKB; PA162376869; -. DR VEuPathDB; HostDB:ENSG00000134884; -. DR eggNOG; ENOG502QPR5; Eukaryota. DR GeneTree; ENSGT00730000111249; -. DR HOGENOM; CLU_076749_0_0_1; -. DR InParanoid; Q9NWB6; -. DR OMA; PRQHQRD; -. DR PhylomeDB; Q9NWB6; -. DR TreeFam; TF324123; -. DR PathwayCommons; Q9NWB6; -. DR SignaLink; Q9NWB6; -. DR BioGRID-ORCS; 55082; 634 hits in 1176 CRISPR screens. DR ChiTaRS; ARGLU1; human. DR GeneWiki; ARGLU1; -. DR GenomeRNAi; 55082; -. DR Pharos; Q9NWB6; Tbio. DR PRO; PR:Q9NWB6; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9NWB6; Protein. DR Bgee; ENSG00000134884; Expressed in sural nerve and 203 other cell types or tissues. DR ExpressionAtlas; Q9NWB6; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR InterPro; IPR033371; ARGLU1. DR PANTHER; PTHR31711; ARGININE AND GLUTAMATE-RICH PROTEIN 1; 1. DR PANTHER; PTHR31711:SF1; ARGININE AND GLUTAMATE-RICH PROTEIN 1; 1. DR Pfam; PF15346; ARGLU; 1. DR Genevisible; Q9NWB6; HS. PE 1: Evidence at protein level; KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..273 FT /note="Arginine and glutamate-rich protein 1" FT /id="PRO_0000288438" FT REGION 1..113 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 238..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..55 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 56..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 238..258 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 61 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 76 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 16..90 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053685" FT VAR_SEQ 192..273 FT /note="EEERAKREELERILEENNRKIAEAQAKLAEEQLRIVEEQRKIHEERMKLEQE FT RQRQQKEEQKIILGKGKSRPKLSFSLKTQD -> VTLGRLESRDSPWQNFQCWVLPPAQ FT FRKRWNTDYLIPFSSKLNIAAKVNFLAYSEVLTDNLKVGSFYKTYSRILFDLMELAI FT (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_025674" SQ SEQUENCE 273 AA; 33216 MW; 70B88496BF18AAE0 CRC64; MGRSRSRSSS RSKHTKSSKH NKKRSRSRSR SRDKERVRKR SKSRESKRNR RRESRSRSRS TNTAVSRRER DRERASSPPD RIDIFGRTVS KRSSLDEKQK REEEEKKAEF ERQRKIRQQE IEEKLIEEET ARRVEELVAK RVEEELEKRK DEIEREVLRR VEEAKRIMEK QLLEELERQR QAELAAQKAR EEEERAKREE LERILEENNR KIAEAQAKLA EEQLRIVEEQ RKIHEERMKL EQERQRQQKE EQKIILGKGK SRPKLSFSLK TQD //