RO60_HUMAN
ID RO60_HUMAN Reviewed; 538 AA.
AC P10155; B2RBB9; Q5LJ98; Q5LJ99; Q5LJA0; Q86WL3; Q86WL4; Q92787; Q9H1W6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=RNA-binding protein RO60 {ECO:0000312|HGNC:HGNC:11313};
DE AltName: Full=60 kDa SS-A/Ro ribonucleoprotein {ECO:0000305};
DE Short=60 kDa Ro protein;
DE Short=60 kDa ribonucleoprotein Ro;
DE Short=RoRNP;
DE AltName: Full=Ro 60 kDa autoantigen {ECO:0000303|PubMed:26382853};
DE Short=Ro60 autoantigen {ECO:0000303|PubMed:26382853};
DE AltName: Full=Sjoegren syndrome antigen A2 {ECO:0000312|HGNC:HGNC:11313};
DE AltName: Full=Sjoegren syndrome type A antigen {ECO:0000303|PubMed:2649513};
DE Short=SS-A {ECO:0000303|PubMed:2649513};
DE AltName: Full=TROVE domain family member 2 {ECO:0000312|HGNC:HGNC:11313};
GN Name=RO60 {ECO:0000312|HGNC:HGNC:11313};
GN Synonyms=SSA2 {ECO:0000312|HGNC:HGNC:11313},
GN TROVE2 {ECO:0000312|HGNC:HGNC:11313};
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 [MRNA] (ISOFORM LONG).
RX PubMed=3200833; DOI=10.1073/pnas.85.24.9479;
RA Deutscher S.L., Harley J.B., Keene J.D.;
RT "Molecular analysis of the 60-kDa human Ro ribonucleoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9479-9483(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=2649513; DOI=10.1172/jci114013;
RA Ben-Chetrit E., Gandy B.J., Tan E.M., Sulivan K.F.;
RT "Isolation and characterization of a cDNA clone encoding the 60-kD
RT component of the human SS-A/Ro ribonucleoprotein autoantigen.";
RL J. Clin. Invest. 83:1284-1292(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RA Buyon J.P., DiDonato F., Tseng C.E., Rashbaum W., Morris A., Hamel J.C.,
RA Chan E.K.L.;
RT "Identification and characterization of an alternative mRNA transcript of
RT the 60-kD SS-A/Ro ribonucleoprotein encoding the N-terminal RNA binding
RT domain alone.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RA Han Q., Wang X., Shi Y., Ding J., Fan D.;
RT "A variant of the 60-kD component of the human SS-A/Ro ribonucleoprotein
RT autoantigen involved in multidrug resistance of gastric cancer cells.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Thalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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 [9]
RP PROTEIN SEQUENCE OF 1-14; 271-283 AND 352-359, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pre-B cell;
RA Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W.;
RL Submitted (FEB-2009) to UniProtKB.
RN [10]
RP INTERACTION WITH RAB11FIP5.
RC TISSUE=Keratinocyte;
RX PubMed=10545525; DOI=10.1172/jci8003;
RA Wang D., Buyon J.P., Zhu W., Chan E.K.L.;
RT "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and
RT identification of distinct human autoantibodies.";
RL J. Clin. Invest. 104:1265-1275(1999).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH PUF60 AND Y5 RNA.
RX PubMed=10668799; DOI=10.1017/s1355838200990277;
RA Bouffard P., Barbar E., Briere F., Boire G.;
RT "Interaction cloning and characterization of RoBPI, a novel protein binding
RT to human Ro ribonucleoproteins.";
RL RNA 6:66-78(2000).
RN [12]
RP FUNCTION.
RX PubMed=18056422; DOI=10.1101/gad.1603907;
RA Hogg J.R., Collins K.;
RT "Human Y5 RNA specializes a Ro ribonucleoprotein for 5S ribosomal RNA
RT quality control.";
RL Genes Dev. 21:3067-3072(2007).
RN [13]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224 AND LYS-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-19, 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 [23]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=26382853; DOI=10.1126/science.aac7442;
RA Hung T., Pratt G.A., Sundararaman B., Townsend M.J., Chaivorapol C.,
RA Bhangale T., Graham R.R., Ortmann W., Criswell L.A., Yeo G.W.,
RA Behrens T.W.;
RT "The Ro60 autoantigen binds endogenous retroelements and regulates
RT inflammatory gene expression.";
RL Science 350:455-459(2015).
CC -!- FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs,
CC pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y
CC RNAs (PubMed:18056422, PubMed:26382853). Binds to endogenous Alu
CC retroelements which are induced by type I interferon and stimulate
CC porinflammatory cytokine secretion (PubMed:26382853). Regulates the
CC expression of Alu retroelements as well as inflammatory genes
CC (PubMed:26382853). May play roles in cilia formation and/or maintenance
CC (By similarity). {ECO:0000250|UniProtKB:O08848,
CC ECO:0000269|PubMed:18056422, ECO:0000269|PubMed:26382853}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs (PubMed:17289661). Found in a complex
CC with PUF60 and Y5 RNA (PubMed:10668799). Interacts with RAB11FIP5
CC (PubMed:10545525). {ECO:0000269|PubMed:10545525,
CC ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:17289661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17289661}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000269|PubMed:17289661}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Long;
CC IsoId=P10155-1; Sequence=Displayed;
CC Name=Short; Synonyms=60E2;
CC IsoId=P10155-2; Sequence=VSP_005911, VSP_005912;
CC Name=3;
CC IsoId=P10155-3; Sequence=VSP_045262;
CC Name=4;
CC IsoId=P10155-4; Sequence=VSP_045797;
CC Name=5;
CC IsoId=P10155-5; Sequence=VSP_054041;
CC -!- DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical HEAT-
CC like repeats, and is closed by the VWFA-like domain giving rise to a
CC ring-shaped monomer. Single-stranded RNA is bound in the positively
CC charged central cavity (By similarity). {ECO:0000250|UniProtKB:P42700}.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds divalent
CC metal cations. {ECO:0000250|UniProtKB:P42700}.
CC -!- MISCELLANEOUS: Antibodies against normal cellular SSA2 protein are
CC found in sera from patients with systemic lupus erythematosus (SLE).
CC -!- SIMILARITY: Belongs to the Ro 60 kDa 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; J04137; AAA35493.1; -; mRNA.
DR EMBL; M25077; AAA35532.1; -; mRNA.
DR EMBL; U44388; AAB81552.1; ALT_TERM; Genomic_DNA.
DR EMBL; U44388; AAB81553.1; -; Genomic_DNA.
DR EMBL; AY205314; AAO47001.1; -; mRNA.
DR EMBL; AY205315; AAO47002.1; -; mRNA.
DR EMBL; AK314594; BAG37166.1; -; mRNA.
DR EMBL; AL136370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91240.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91243.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91245.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91247.1; -; Genomic_DNA.
DR EMBL; BC036658; AAH36658.1; -; mRNA.
DR CCDS; CCDS1379.1; -. [P10155-1]
DR CCDS; CCDS41449.1; -. [P10155-5]
DR CCDS; CCDS41450.2; -. [P10155-4]
DR CCDS; CCDS53451.1; -. [P10155-3]
DR PIR; A31760; A31760.
DR RefSeq; NP_001035828.1; NM_001042369.2. [P10155-5]
DR RefSeq; NP_001035829.2; NM_001042370.2. [P10155-4]
DR RefSeq; NP_001166995.1; NM_001173524.1. [P10155-1]
DR RefSeq; NP_001166996.1; NM_001173525.1. [P10155-3]
DR RefSeq; NP_004591.2; NM_004600.5. [P10155-1]
DR RefSeq; XP_006711560.1; XM_006711497.3. [P10155-1]
DR RefSeq; XP_016857670.1; XM_017002181.1. [P10155-1]
DR RefSeq; XP_016857671.1; XM_017002182.1. [P10155-1]
DR AlphaFoldDB; P10155; -.
DR SMR; P10155; -.
DR BioGRID; 112616; 80.
DR CORUM; P10155; -.
DR IntAct; P10155; 18.
DR MINT; P10155; -.
DR STRING; 9606.ENSP00000356416; -.
DR GlyGen; P10155; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P10155; -.
DR MetOSite; P10155; -.
DR PhosphoSitePlus; P10155; -.
DR SwissPalm; P10155; -.
DR BioMuta; TROVE2; -.
DR DMDM; 52788235; -.
DR EPD; P10155; -.
DR jPOST; P10155; -.
DR MassIVE; P10155; -.
DR MaxQB; P10155; -.
DR PaxDb; P10155; -.
DR PeptideAtlas; P10155; -.
DR PRIDE; P10155; -.
DR ProteomicsDB; 52574; -. [P10155-1]
DR ProteomicsDB; 52575; -. [P10155-2]
DR ProteomicsDB; 63552; -.
DR ProteomicsDB; 63553; -.
DR ProteomicsDB; 63554; -.
DR Antibodypedia; 1048; 381 antibodies from 35 providers.
DR DNASU; 6738; -.
DR Ensembl; ENST00000367441.1; ENSP00000356411.1; ENSG00000116747.13. [P10155-1]
DR Ensembl; ENST00000367443.5; ENSP00000356413.1; ENSG00000116747.13. [P10155-3]
DR Ensembl; ENST00000367444.7; ENSP00000356414.3; ENSG00000116747.13. [P10155-5]
DR Ensembl; ENST00000367445.7; ENSP00000356415.3; ENSG00000116747.13. [P10155-4]
DR Ensembl; ENST00000367446.7; ENSP00000356416.3; ENSG00000116747.13. [P10155-1]
DR Ensembl; ENST00000400968.7; ENSP00000383752.2; ENSG00000116747.13. [P10155-1]
DR GeneID; 6738; -.
DR KEGG; hsa:6738; -.
DR MANE-Select; ENST00000400968.7; ENSP00000383752.2; NM_001173524.2; NP_001166995.1.
DR UCSC; uc001gss.4; human. [P10155-1]
DR CTD; 6738; -.
DR DisGeNET; 6738; -.
DR GeneCards; RO60; -.
DR HGNC; HGNC:11313; RO60.
DR HPA; ENSG00000116747; Low tissue specificity.
DR MIM; 600063; gene.
DR neXtProt; NX_P10155; -.
DR OpenTargets; ENSG00000116747; -.
DR PharmGKB; PA36137; -.
DR VEuPathDB; HostDB:ENSG00000116747; -.
DR eggNOG; KOG4465; Eukaryota.
DR GeneTree; ENSGT00390000006200; -.
DR HOGENOM; CLU_024421_1_0_1; -.
DR InParanoid; P10155; -.
DR OMA; WWYEWLK; -.
DR OrthoDB; 472016at2759; -.
DR PhylomeDB; P10155; -.
DR TreeFam; TF105990; -.
DR PathwayCommons; P10155; -.
DR SignaLink; P10155; -.
DR BioGRID-ORCS; 6738; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; TROVE2; human.
DR GeneWiki; TROVE2; -.
DR GenomeRNAi; 6738; -.
DR Pharos; P10155; Tbio.
DR PRO; PR:P10155; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P10155; protein.
DR Bgee; ENSG00000116747; Expressed in nipple and 208 other tissues.
DR ExpressionAtlas; P10155; baseline and differential.
DR Genevisible; P10155; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IEA:Ensembl.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0002520; P:immune system development; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0006383; P:transcription by RNA polymerase III; TAS:ProtInc.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR040322; TROVE2.
DR InterPro; IPR008858; TROVE_dom.
DR InterPro; IPR037214; TROVE_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR14202; PTHR14202; 1.
DR Pfam; PF05731; TROVE; 1.
DR SUPFAM; SSF140864; SSF140864; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50988; TROVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cilium biogenesis/degradation;
KW Cytoplasm; Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..538
FT /note="RNA-binding protein RO60"
FT /id="PRO_0000174169"
FT DOMAIN 16..369
FT /note="TROVE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00343"
FT REGION 120..284
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 361..538
FT /note="VWFA-like domain"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT BINDING 380
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT BINDING 445
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P42700"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 359
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 195..205
FT /note="LAIVTKYITKG -> KHKIFIGKKGG (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005911"
FT VAR_SEQ 206..538
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005912"
FT VAR_SEQ 515..538
FT /note="GMLDMCGFDTGALDVIRNFTLDMI -> DTVK (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045262"
FT VAR_SEQ 515..538
FT /note="GMLDMCGFDTGALDVIRNFTLDMI -> ALQNTLLNKSF (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:2649513"
FT /id="VSP_054041"
FT VAR_SEQ 529..538
FT /note="VIRNFTLDMI -> PCKIPY (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045797"
FT CONFLICT 136
FT /note="K -> R (in Ref. 4; AAO47001/AAO47002)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> K (in Ref. 1; AAA35493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60671 MW; CD735B1DF2B13098 CRC64;
MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE QKLGLENAEA
LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS QCSDISTKQA AFKAVSEVCR
IPTHLFTFIQ FKKDLKESMK CGMWGRALRK AIADWYNEKG GMALALAVTK YKQRNGWSHK
DLLRLSHLKP SSEGLAIVTK YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD
ELEVIHLIEE HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE
VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL KALDAAFYKT
FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC MVVTRTEKDS YVVAFSDEMV
PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA
IALREYRKKM DIPAKLIVCG MTSNGFTIAD PDDRGMLDMC GFDTGALDVI RNFTLDMI
