VIR_HUMAN
ID VIR_HUMAN Reviewed; 1812 AA.
AC Q69YN4; Q2M1N0; Q6AHX9; Q6NT78; Q7Z6C7; Q8IXH4; Q9BTH4; Q9H9C9; Q9NWR3;
AC Q9P2B8; Q9UFW1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein virilizer homolog {ECO:0000305};
GN Name=VIRMA {ECO:0000312|HGNC:HGNC:24500};
GN Synonyms=KIAA1429 {ECO:0000303|PubMed:10718198}; ORFNames=MSTP054;
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=Fetal kidney, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 615-1812 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 648-1812 (ISOFORM 2).
RC TISSUE=Cervix, Lung, and Uterus;
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 [3]
RP PROTEIN SEQUENCE OF 2-16; 385-393; 534-545; 666-674; 1198-1216; 1256-1268;
RP 1389-1402 AND 1446-1458, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1812 (ISOFORM 4).
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1812 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1812 (ISOFORM 1).
RC TISSUE=Ileal mucosa, and Teratocarcinoma;
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 [7]
RP IDENTIFICATION.
RX PubMed=11156988; DOI=10.1093/genetics/157.2.679;
RA Niessen M., Schneiter R., Nothiger R.;
RT "Molecular identification of virilizer, a gene required for the expression
RT of the sex-determining gene Sex-lethal in Drosophila melanogaster.";
RL Genetics 157:679-688(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND THR-184, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-1579 AND THR-1708,
RP AND IDENTIFICATION BY 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; TYR-914 AND SER-1579,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-222 AND SER-1579,
RP AND 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184, 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 [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH WTAP, AND IDENTIFICATION IN A
RP MACOM-LIKE COMPLEX.
RX PubMed=24100041; DOI=10.1074/jbc.m113.500397;
RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
RA Hamakubo T.;
RT "Identification of Wilms' tumor 1-associating protein complex and its role
RT in alternative splicing and the cell cycle.";
RL J. Biol. Chem. 288:33292-33302(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-138; SER-173;
RP THR-184 AND SER-1579, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP FUNCTION, AND ASSOCIATION WITH THE WMM COMPLEX.
RX PubMed=24981863; DOI=10.1016/j.celrep.2014.05.048;
RA Schwartz S., Mumbach M.R., Jovanovic M., Wang T., Maciag K., Bushkin G.G.,
RA Mertins P., Ter-Ovanesyan D., Habib N., Cacchiarelli D., Sanjana N.E.,
RA Freinkman E., Pacold M.E., Satija R., Mikkelsen T.S., Hacohen N., Zhang F.,
RA Carr S.A., Lander E.S., Regev A.;
RT "Perturbation of m6A writers reveals two distinct classes of mRNA
RT methylation at internal and 5' sites.";
RL Cell Rep. 8:284-296(2014).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND THR-184, AND
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 [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1723; ARG-1773; ARG-1775 AND
RP ARG-1793, AND 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 [21]
RP FUNCTION, IDENTIFICATION IN THE WMM COMPLEX, AND INTERACTION WITH NUDT21
RP AND CPSF6.
RX PubMed=29507755; DOI=10.1038/s41421-018-0019-0;
RA Yue Y., Liu J., Cui X., Cao J., Luo G., Zhang Z., Cheng T., Gao M., Shu X.,
RA Ma H., Wang F., Wang X., Shen B., Wang Y., Feng X., He C., Liu J.;
RT "VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop
RT codon and associates with alternative polyadenylation.";
RL Cell Discov. 4:10-10(2018).
CC -!- FUNCTION: Associated component of the WMM complex, a complex that
CC mediates N6-methyladenosine (m6A) methylation of RNAs, a modification
CC that plays a role in the efficiency of mRNA splicing and RNA processing
CC (PubMed:24981863, PubMed:29507755). Acts as a key regulator of m6A
CC methylation by promoting m6A methylation of mRNAs in the 3'-UTR near
CC the stop codon: recruits the catalytic core components METTL3 and
CC METTL14, thereby guiding m6A methylation at specific sites
CC (PubMed:29507755). Required for mRNA polyadenylation via its role in
CC selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near
CC the stop codon correlating with alternative polyadenylation (APA)
CC (PubMed:29507755). {ECO:0000269|PubMed:24981863,
CC ECO:0000269|PubMed:29507755}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:29507755). The MAC subcomplex is
CC composed of METTL3 and METTL14. The MACOM subcomplex is composed of
CC WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or
CC RBM15B) (PubMed:24981863, PubMed:29507755). Interacts with WTAP
CC (PubMed:24100041). Also a component of a MACOM-like complex, named WTAP
CC complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and
CC THRAP3 (PubMed:24100041). Interacts with NUDT21 and CPSF6
CC (PubMed:29507755). {ECO:0000269|PubMed:24100041,
CC ECO:0000269|PubMed:24981863, ECO:0000269|PubMed:29507755}.
CC -!- INTERACTION:
CC Q69YN4-4; Q6B0K9: HBM; NbExp=3; IntAct=EBI-18054817, EBI-12805802;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:24100041}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}. Cytoplasm
CC {ECO:0000250|UniProtKB:A2AIV2}. Note=Mainly nuclear with some fraction
CC located in the cytoplasm. ZC3H13 is required to anchor component of the
CC MACOM subcomplex, such as VIRMA, in the nucleus.
CC {ECO:0000250|UniProtKB:A2AIV2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q69YN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69YN4-2; Sequence=VSP_029019, VSP_029020;
CC Name=3;
CC IsoId=Q69YN4-3; Sequence=VSP_029021;
CC Name=4;
CC IsoId=Q69YN4-4; Sequence=VSP_029017, VSP_029018;
CC -!- SIMILARITY: Belongs to the vir family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91316.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB55922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL117434; CAB55922.1; ALT_INIT; mRNA.
DR EMBL; AL832487; CAH10773.1; -; mRNA.
DR EMBL; CR627454; CAH10535.1; -; mRNA.
DR EMBL; BC003701; AAH03701.2; -; mRNA.
DR EMBL; BC053875; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC069239; AAH69239.1; -; mRNA.
DR EMBL; BC112288; AAI12289.1; -; mRNA.
DR EMBL; BC113380; AAI13381.1; -; mRNA.
DR EMBL; AF116724; AAO15300.1; -; mRNA.
DR EMBL; AB037850; BAA92667.1; -; mRNA.
DR EMBL; AK000668; BAA91316.1; ALT_INIT; mRNA.
DR EMBL; AK022906; BAB14301.1; ALT_INIT; mRNA.
DR CCDS; CCDS34923.1; -. [Q69YN4-1]
DR CCDS; CCDS47894.1; -. [Q69YN4-4]
DR PIR; T17232; T17232.
DR RefSeq; NP_056311.2; NM_015496.4. [Q69YN4-1]
DR RefSeq; NP_892121.1; NM_183009.2. [Q69YN4-4]
DR AlphaFoldDB; Q69YN4; -.
DR BioGRID; 117452; 2915.
DR ComplexPortal; CPX-1605; WMM N6-adenosine-methyltransferase complex.
DR CORUM; Q69YN4; -.
DR IntAct; Q69YN4; 36.
DR MINT; Q69YN4; -.
DR STRING; 9606.ENSP00000297591; -.
DR iPTMnet; Q69YN4; -.
DR PhosphoSitePlus; Q69YN4; -.
DR BioMuta; VIRMA; -.
DR DMDM; 160221326; -.
DR EPD; Q69YN4; -.
DR jPOST; Q69YN4; -.
DR MassIVE; Q69YN4; -.
DR MaxQB; Q69YN4; -.
DR PaxDb; Q69YN4; -.
DR PeptideAtlas; Q69YN4; -.
DR PRIDE; Q69YN4; -.
DR ProteomicsDB; 66164; -. [Q69YN4-1]
DR ProteomicsDB; 66165; -. [Q69YN4-2]
DR ProteomicsDB; 66166; -. [Q69YN4-3]
DR ProteomicsDB; 66167; -. [Q69YN4-4]
DR Antibodypedia; 25815; 52 antibodies from 16 providers.
DR DNASU; 25962; -.
DR Ensembl; ENST00000297591.10; ENSP00000297591.5; ENSG00000164944.12. [Q69YN4-1]
DR Ensembl; ENST00000421249.2; ENSP00000398390.2; ENSG00000164944.12. [Q69YN4-4]
DR GeneID; 25962; -.
DR KEGG; hsa:25962; -.
DR MANE-Select; ENST00000297591.10; ENSP00000297591.5; NM_015496.5; NP_056311.2.
DR UCSC; uc003ygo.3; human. [Q69YN4-1]
DR CTD; 25962; -.
DR DisGeNET; 25962; -.
DR GeneCards; VIRMA; -.
DR HGNC; HGNC:24500; VIRMA.
DR HPA; ENSG00000164944; Low tissue specificity.
DR MIM; 616447; gene.
DR neXtProt; NX_Q69YN4; -.
DR OpenTargets; ENSG00000164944; -.
DR PharmGKB; PA142671611; -.
DR VEuPathDB; HostDB:ENSG00000164944; -.
DR eggNOG; KOG4822; Eukaryota.
DR GeneTree; ENSGT00390000002833; -.
DR HOGENOM; CLU_002368_0_0_1; -.
DR InParanoid; Q69YN4; -.
DR OMA; CERKQIP; -.
DR OrthoDB; 210051at2759; -.
DR PhylomeDB; Q69YN4; -.
DR TreeFam; TF323505; -.
DR PathwayCommons; Q69YN4; -.
DR SignaLink; Q69YN4; -.
DR BioGRID-ORCS; 25962; 684 hits in 1088 CRISPR screens.
DR ChiTaRS; KIAA1429; human.
DR GenomeRNAi; 25962; -.
DR Pharos; Q69YN4; Tbio.
DR PRO; PR:Q69YN4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q69YN4; protein.
DR Bgee; ENSG00000164944; Expressed in ventricular zone and 181 other tissues.
DR ExpressionAtlas; Q69YN4; baseline and differential.
DR Genevisible; Q69YN4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; IDA:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR031801; VIR_N.
DR InterPro; IPR026736; Virilizer.
DR PANTHER; PTHR23185; PTHR23185; 1.
DR Pfam; PF15912; VIR_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Direct protein sequencing; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330"
FT CHAIN 2..1812
FT /note="Protein virilizer homolog"
FT /id="PRO_0000308605"
FT REGION 132..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..302
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 914
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1708
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1723
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1741
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AIV2"
FT MOD_RES 1741
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:A2AIV2"
FT MOD_RES 1773
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1775
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1793
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1132..1147
FT /note="IEPHDISVALNTRKLW -> SLPYNMHLINDCSNTF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_029017"
FT VAR_SEQ 1148..1812
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_029018"
FT VAR_SEQ 1366..1377
FT /note="SSLRKNSSALHS -> RDAVEMIMVSWK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029019"
FT VAR_SEQ 1378..1812
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029020"
FT VAR_SEQ 1684..1812
FT /note="ISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRG
FT NYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASANSGSGGSRG
FT KFVSGGSGRGRHVRSFTR -> EQEAPVGVLRILLEEITMKVVEARAILTEALFHHYDP
FT LVLQVTAQVLGTVLLEVVGDLDLPGLVQIAAVEAQEESLLVEAVVEVVMYAPLHDKNPF
FT GNILTVYEHFTRTIKIRH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_029021"
FT VARIANT 753
FT /note="I -> V (in dbSNP:rs7814840)"
FT /id="VAR_036845"
FT CONFLICT 97
FT /note="S -> P (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="Missing (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="R -> G (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="A -> P (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="Missing (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
FT CONFLICT 1183
FT /note="Q -> E (in Ref. 1; CAB55922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1434
FT /note="N -> D (in Ref. 6; BAB14301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1563
FT /note="F -> I (in Ref. 1; CAH10773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1812 AA; 202025 MW; FFF7F006B5EF5B75 CRC64;
MAVDSAMELL FLDTFKHPSA EQSSHIDVVR FPCVVYINEV RVIPPGVRAH SSLPDNRAYG
ETSPHTFQLD LFFNNVSKPS APVFDRLGSL EYDENTSIIF RPNSKVNTDG LVLRGWYNCL
TLAIYGSVDR VISHDRDSPP PPPPPPPPPQ PQPSLKRNPK HADGEKEDQF NGSPPRPQPR
GPRTPPGPPP PDDDEDDPVP LPVSGDKEED APHREDYFEP ISPDRNSVPQ EGQYSDEGEV
EEEQQEEGEE DEDDVDVEEE EDEDEDDRRT VDSIPEEEEE DEEEEGEEDE EGEGDDGYEQ
ISSDEDGIAD LERETFKYPN FDVEYTAEDL ASVPPMTYDP YDRELVPLLY FSCPYKTTFE
IEISRMKDQG PDKENSGAIE ASVKLTELLD LYREDRGAKW VTALEEIPSL IIKGLSYLQL
KNTKQDSLGQ LVDWTMQALN LQVALRQPIA LNVRQLKAGT KLVSSLAECG AQGVTGLLQA
GVISGLFELL FADHVSSSLK LNAFKALDSV ISMTEGMEAF LRGRQNEKSG YQKLLELILL
DQTVRVVTAG SAILQKCHFY EVLSEIKRLG DHLAEKTSSL PNHSEPDHDT DAGLERTNPE
YENEVEASMD MDLLESSNIS EGEIERLINL LEEVFHLMET APHTMIQQPV KSFPTMARIT
GPPERDDPYP VLFRYLHSHH FLELVTLLLS IPVTSAHPGV LQATKDVLKF LAQSQKGLLF
FMSEYEATNL LIRALCHFYD QDEEEGLQSD GVIDDAFALW LQDSTQTLQC ITELFSHFQR
CTASEETDHS DLLGTLHNLY LITFNPVGRS AVGHVFSLEK NLQSLITLME YYSKEALGDS
KSKKSVAYNY ACILILVVVQ SSSDVQMLEQ HAASLLKLCK ADENNAKLQE LGKWLEPLKN
LRFEINCIPN LIEYVKQNID NLMTPEGVGL TTALRVLCNV ACPPPPVEGQ QKDLKWNLAV
IQLFSAEGMD TFIRVLQKLN SILTQPWRLH VNMGTTLHRV TTISMARCTL TLLKTMLTEL
LRGGSFEFKD MRVPSALVTL HMLLCSIPLS GRLDSDEQKI QNDIIDILLT FTQGVNEKLT
ISEETLANNT WSLMLKEVLS SILKVPEGFF SGLILLSELL PLPLPMQTTQ VIEPHDISVA
LNTRKLWSMH LHVQAKLLQE IVRSFSGTTC QPIQHMLRRI CVQLCDLASP TALLIMRTVL
DLIVEDLQST SEDKEKQYTS QTTRLLALLD ALASHKACKL AILHLINGTI KGDERYAEIF
QDLLALVRSP GDSVIRQQCV EYVTSILQSL CDQDIALILP SSSEGSISEL EQLSNSLPNK
ELMTSICDCL LATLANSESS YNCLLTCVRT MMFLAEHDYG LFHLKSSLRK NSSALHSLLK
RVVSTFSKDT GELASSFLEF MRQILNSDTI GCCGDDNGLM EVEGAHTSRT MSINAAELKQ
LLQSKEESPE NLFLELEKLV LEHSKDDDNL DSLLDSVVGL KQMLESSGDP LPLSDQDVEP
VLSAPESLQN LFNNRTAYVL ADVMDDQLKS MWFTPFQAEE IDTDLDLVKV DLIELSEKCC
SDFDLHSELE RSFLSEPSSP GRTKTTKGFK LGKHKHETFI TSSGKSEYIE PAKRAHVVPP
PRGRGRGGFG QGIRPHDIFR QRKQNTSRPP SMHVDDFVAA ESKEVVPQDG IPPPKRPLKV
SQKISSRGGF SGNRGGRGAF HSQNRFFTPP ASKGNYSRRE GTRGSSWSAQ NTPRGNYNES
RGGQSNFNRG PLPPLRPLSS TGYRPSPRDR ASRGRGGLGP SWASANSGSG GSRGKFVSGG
SGRGRHVRSF TR
