Full text data of TROVE2
TROVE2
(RO60, SSA2)
[Confidence: low (only semi-automatic identification from reviews)]
60 kDa SS-A/Ro ribonucleoprotein; 60 kDa Ro protein; 60 kDa ribonucleoprotein Ro; RoRNP (Ro 60 kDa autoantigen; Sjoegren syndrome antigen A2; Sjoegren syndrome type A antigen; SS-A; TROVE domain family member 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60 kDa SS-A/Ro ribonucleoprotein; 60 kDa Ro protein; 60 kDa ribonucleoprotein Ro; RoRNP (Ro 60 kDa autoantigen; Sjoegren syndrome antigen A2; Sjoegren syndrome type A antigen; SS-A; TROVE domain family member 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P10155
ID RO60_HUMAN Reviewed; 538 AA.
AC P10155; B2RBB9; Q5LJ98; Q5LJ99; Q86WL3; Q86WL4; Q92787; Q9H1W6;
read moreDT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=60 kDa SS-A/Ro ribonucleoprotein;
DE Short=60 kDa Ro protein;
DE Short=60 kDa ribonucleoprotein Ro;
DE Short=RoRNP;
DE AltName: Full=Ro 60 kDa autoantigen;
DE AltName: Full=Sjoegren syndrome antigen A2;
DE AltName: Full=Sjoegren syndrome type A antigen;
DE Short=SS-A;
DE AltName: Full=TROVE domain family member 2;
GN Name=TROVE2; Synonyms=RO60, SSA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 LONG).
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.,
RA Hamel J.C., Chan E.K.L.;
RT "Identification and characterization of an alternative mRNA transcript
RT of the 60-kD SS-A/Ro ribonucleoprotein encoding the N-terminal RNA
RT binding 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
RT ribonucleoprotein autoantigen involved in multidrug resistance of
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 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 RIP11.
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
RT binding 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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: RNA-binding protein that binds to misfolded non-coding
CC RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules
CC known as Y RNAs. May stabilize some of these RNAs and protect them
CC from degradation.
CC -!- FUNCTION: May play roles in cilia formation and/or maintenance (By
CC similarity).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Found in a complex with PUF60 and
CC Y5 RNA. Interacts with RIP11.
CC -!- INTERACTION:
CC Q9UHX1:PUF60; NbExp=1; IntAct=EBI-1049168, EBI-1053259;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 -!- DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical
CC HEAT-like repeats, and is closed by the VWFA-like domain giving
CC rise to a ring-shaped monomer. Single-stranded RNA is bound in the
CC positively charged central cavity (By similarity).
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds
CC divalent metal cations (By similarity).
CC -!- MISCELLANEOUS: Antibodies against normal cellular SSA2 protein are
CC found in sera from patients with systemic lupus erythematosus
CC (SLE).
CC -!- SIMILARITY: Belongs to the Ro 60 kDa family.
CC -!- SIMILARITY: Contains 1 TROVE domain.
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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; CAC17589.1; -; Genomic_DNA.
DR EMBL; AL136370; CAI10823.1; -; Genomic_DNA.
DR EMBL; AL136370; CAI10824.1; -; 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; BC036658; AAH36658.1; -; mRNA.
DR PIR; A31760; A31760.
DR RefSeq; NP_001035828.1; NM_001042369.2.
DR RefSeq; NP_001035829.2; NM_001042370.2.
DR RefSeq; NP_001166995.1; NM_001173524.1.
DR RefSeq; NP_001166996.1; NM_001173525.1.
DR RefSeq; NP_004591.2; NM_004600.5.
DR UniGene; Hs.288178; -.
DR ProteinModelPortal; P10155; -.
DR SMR; P10155; 4-537.
DR IntAct; P10155; 4.
DR MINT; MINT-8395039; -.
DR STRING; 9606.ENSP00000356411; -.
DR PhosphoSite; P10155; -.
DR DMDM; 52788235; -.
DR PaxDb; P10155; -.
DR PRIDE; P10155; -.
DR DNASU; 6738; -.
DR Ensembl; ENST00000367441; ENSP00000356411; ENSG00000116747.
DR Ensembl; ENST00000367443; ENSP00000356413; ENSG00000116747.
DR Ensembl; ENST00000367445; ENSP00000356415; ENSG00000116747.
DR Ensembl; ENST00000367446; ENSP00000356416; ENSG00000116747.
DR Ensembl; ENST00000400968; ENSP00000383752; ENSG00000116747.
DR GeneID; 6738; -.
DR KEGG; hsa:6738; -.
DR UCSC; uc001gss.3; human.
DR CTD; 6738; -.
DR GeneCards; GC01P193028; -.
DR HGNC; HGNC:11313; TROVE2.
DR HPA; HPA002835; -.
DR MIM; 600063; gene.
DR neXtProt; NX_P10155; -.
DR PharmGKB; PA36137; -.
DR eggNOG; NOG74865; -.
DR HOGENOM; HOG000075167; -.
DR HOVERGEN; HBG013234; -.
DR InParanoid; P10155; -.
DR KO; K11089; -.
DR OMA; AKQEPML; -.
DR OrthoDB; EOG78D7JR; -.
DR PhylomeDB; P10155; -.
DR ChiTaRS; TROVE2; human.
DR GeneWiki; TROVE2; -.
DR GenomeRNAi; 6738; -.
DR NextBio; 26284; -.
DR PRO; PR:P10155; -.
DR ArrayExpress; P10155; -.
DR Bgee; P10155; -.
DR CleanEx; HS_TROVE2; -.
DR Genevestigator; P10155; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0060271; P:cilium morphogenesis; IEA:Ensembl.
DR GO; GO:0006383; P:transcription from RNA polymerase III promoter; TAS:ProtInc.
DR InterPro; IPR008858; TROVE.
DR InterPro; IPR018698; VWA-like_dom.
DR Pfam; PF09967; DUF2201; 1.
DR Pfam; PF05731; TROVE; 1.
DR PROSITE; PS50988; TROVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cilium biogenesis/degradation;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1 538 60 kDa SS-A/Ro ribonucleoprotein.
FT /FTId=PRO_0000174169.
FT DOMAIN 16 369 TROVE.
FT REGION 120 284 RNA-binding (By similarity).
FT REGION 361 538 VWFA-like domain (By similarity).
FT METAL 378 378 Divalent metal cation (By similarity).
FT METAL 380 380 Divalent metal cation (By similarity).
FT METAL 445 445 Divalent metal cation (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 224 224 N6-acetyllysine.
FT MOD_RES 359 359 N6-acetyllysine.
FT VAR_SEQ 195 205 LAIVTKYITKG -> KHKIFIGKKGG (in isoform
FT Short).
FT /FTId=VSP_005911.
FT VAR_SEQ 206 538 Missing (in isoform Short).
FT /FTId=VSP_005912.
FT VAR_SEQ 515 538 GMLDMCGFDTGALDVIRNFTLDMI -> DTVK (in
FT isoform 3).
FT /FTId=VSP_045262.
FT VAR_SEQ 529 538 VIRNFTLDMI -> PCKIPY (in isoform 4).
FT /FTId=VSP_045797.
FT CONFLICT 136 136 K -> R (in Ref. 4; AAO47001/AAO47002).
FT CONFLICT 239 239 R -> K (in Ref. 1; AAA35493).
FT CONFLICT 515 538 GMLDMCGFDTGALDVIRNFTLDMI -> ALQNTLLNKSF
FT (in Ref. 2; AAB81552).
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
//
ID RO60_HUMAN Reviewed; 538 AA.
AC P10155; B2RBB9; Q5LJ98; Q5LJ99; Q86WL3; Q86WL4; Q92787; Q9H1W6;
read moreDT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=60 kDa SS-A/Ro ribonucleoprotein;
DE Short=60 kDa Ro protein;
DE Short=60 kDa ribonucleoprotein Ro;
DE Short=RoRNP;
DE AltName: Full=Ro 60 kDa autoantigen;
DE AltName: Full=Sjoegren syndrome antigen A2;
DE AltName: Full=Sjoegren syndrome type A antigen;
DE Short=SS-A;
DE AltName: Full=TROVE domain family member 2;
GN Name=TROVE2; Synonyms=RO60, SSA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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 LONG).
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.,
RA Hamel J.C., Chan E.K.L.;
RT "Identification and characterization of an alternative mRNA transcript
RT of the 60-kD SS-A/Ro ribonucleoprotein encoding the N-terminal RNA
RT binding 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
RT ribonucleoprotein autoantigen involved in multidrug resistance of
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 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 RIP11.
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
RT binding 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,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: RNA-binding protein that binds to misfolded non-coding
CC RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules
CC known as Y RNAs. May stabilize some of these RNAs and protect them
CC from degradation.
CC -!- FUNCTION: May play roles in cilia formation and/or maintenance (By
CC similarity).
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Found in a complex with PUF60 and
CC Y5 RNA. Interacts with RIP11.
CC -!- INTERACTION:
CC Q9UHX1:PUF60; NbExp=1; IntAct=EBI-1049168, EBI-1053259;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 -!- DOMAIN: The horseshoe-shaped TROVE domain is built with 7 helical
CC HEAT-like repeats, and is closed by the VWFA-like domain giving
CC rise to a ring-shaped monomer. Single-stranded RNA is bound in the
CC positively charged central cavity (By similarity).
CC -!- DOMAIN: The MIDAS-like motif in the VWFA-like domain binds
CC divalent metal cations (By similarity).
CC -!- MISCELLANEOUS: Antibodies against normal cellular SSA2 protein are
CC found in sera from patients with systemic lupus erythematosus
CC (SLE).
CC -!- SIMILARITY: Belongs to the Ro 60 kDa family.
CC -!- SIMILARITY: Contains 1 TROVE domain.
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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; CAC17589.1; -; Genomic_DNA.
DR EMBL; AL136370; CAI10823.1; -; Genomic_DNA.
DR EMBL; AL136370; CAI10824.1; -; 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; BC036658; AAH36658.1; -; mRNA.
DR PIR; A31760; A31760.
DR RefSeq; NP_001035828.1; NM_001042369.2.
DR RefSeq; NP_001035829.2; NM_001042370.2.
DR RefSeq; NP_001166995.1; NM_001173524.1.
DR RefSeq; NP_001166996.1; NM_001173525.1.
DR RefSeq; NP_004591.2; NM_004600.5.
DR UniGene; Hs.288178; -.
DR ProteinModelPortal; P10155; -.
DR SMR; P10155; 4-537.
DR IntAct; P10155; 4.
DR MINT; MINT-8395039; -.
DR STRING; 9606.ENSP00000356411; -.
DR PhosphoSite; P10155; -.
DR DMDM; 52788235; -.
DR PaxDb; P10155; -.
DR PRIDE; P10155; -.
DR DNASU; 6738; -.
DR Ensembl; ENST00000367441; ENSP00000356411; ENSG00000116747.
DR Ensembl; ENST00000367443; ENSP00000356413; ENSG00000116747.
DR Ensembl; ENST00000367445; ENSP00000356415; ENSG00000116747.
DR Ensembl; ENST00000367446; ENSP00000356416; ENSG00000116747.
DR Ensembl; ENST00000400968; ENSP00000383752; ENSG00000116747.
DR GeneID; 6738; -.
DR KEGG; hsa:6738; -.
DR UCSC; uc001gss.3; human.
DR CTD; 6738; -.
DR GeneCards; GC01P193028; -.
DR HGNC; HGNC:11313; TROVE2.
DR HPA; HPA002835; -.
DR MIM; 600063; gene.
DR neXtProt; NX_P10155; -.
DR PharmGKB; PA36137; -.
DR eggNOG; NOG74865; -.
DR HOGENOM; HOG000075167; -.
DR HOVERGEN; HBG013234; -.
DR InParanoid; P10155; -.
DR KO; K11089; -.
DR OMA; AKQEPML; -.
DR OrthoDB; EOG78D7JR; -.
DR PhylomeDB; P10155; -.
DR ChiTaRS; TROVE2; human.
DR GeneWiki; TROVE2; -.
DR GenomeRNAi; 6738; -.
DR NextBio; 26284; -.
DR PRO; PR:P10155; -.
DR ArrayExpress; P10155; -.
DR Bgee; P10155; -.
DR CleanEx; HS_TROVE2; -.
DR Genevestigator; P10155; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0060271; P:cilium morphogenesis; IEA:Ensembl.
DR GO; GO:0006383; P:transcription from RNA polymerase III promoter; TAS:ProtInc.
DR InterPro; IPR008858; TROVE.
DR InterPro; IPR018698; VWA-like_dom.
DR Pfam; PF09967; DUF2201; 1.
DR Pfam; PF05731; TROVE; 1.
DR PROSITE; PS50988; TROVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cilium biogenesis/degradation;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding.
FT CHAIN 1 538 60 kDa SS-A/Ro ribonucleoprotein.
FT /FTId=PRO_0000174169.
FT DOMAIN 16 369 TROVE.
FT REGION 120 284 RNA-binding (By similarity).
FT REGION 361 538 VWFA-like domain (By similarity).
FT METAL 378 378 Divalent metal cation (By similarity).
FT METAL 380 380 Divalent metal cation (By similarity).
FT METAL 445 445 Divalent metal cation (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 224 224 N6-acetyllysine.
FT MOD_RES 359 359 N6-acetyllysine.
FT VAR_SEQ 195 205 LAIVTKYITKG -> KHKIFIGKKGG (in isoform
FT Short).
FT /FTId=VSP_005911.
FT VAR_SEQ 206 538 Missing (in isoform Short).
FT /FTId=VSP_005912.
FT VAR_SEQ 515 538 GMLDMCGFDTGALDVIRNFTLDMI -> DTVK (in
FT isoform 3).
FT /FTId=VSP_045262.
FT VAR_SEQ 529 538 VIRNFTLDMI -> PCKIPY (in isoform 4).
FT /FTId=VSP_045797.
FT CONFLICT 136 136 K -> R (in Ref. 4; AAO47001/AAO47002).
FT CONFLICT 239 239 R -> K (in Ref. 1; AAA35493).
FT CONFLICT 515 538 GMLDMCGFDTGALDVIRNFTLDMI -> ALQNTLLNKSF
FT (in Ref. 2; AAB81552).
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
//
MIM
600063
*RECORD*
*FIELD* NO
600063
*FIELD* TI
*600063 TROVE DOMAIN FAMILY, MEMBER 2; TROVE2
;;AUTOANTIGEN Ro/SSA, 60-KD; RO60;;
SJOGREN SYNDROME ANTIGEN A2; SSA2
read more*FIELD* TX
CLONING
The cDNA that encodes the 60-kD Ro/SSA autoantigen recognized by
autoantibodies in certain lupus erythematosus (152700) and Sjogren
syndrome (270150) sera was cloned and sequenced by Deutscher et al.
(1988) and confirmed with minor differences by Ben-Chetrit et al.
(1989).
GENE FUNCTION
Ro autoantigens are of clinical significance because antibodies directed
against them are found in most patients with primary Sjogren syndrome,
subacute cutaneous lupus erythematosus, neonatal lupus erythematosus,
ANA-negative lupus erythematosus, and systemic lupus erythematosus-like
disease secondary to homozygous C2 (217000) or C4 complement deficiency
(see 120810). Ro antibody is a frequent cause of congenital heart block
(234700). Alspaugh and Tan (1975) described 3 types of precipitating
antibodies in the serum of Sjogren patients; they designated the 3 types
as SS-A, SS-B, and SS-C. SS-A antibodies were later shown to be
immunologically equivalent to the Ro antibodies. Hartung et al. (1992)
found that the presence of Ro antibody was strongly associated with HLA
type DR3. La antibodies (109090) showed the same association.
MAPPING
Frank and Mattei (1994) used in situ hybridization to demonstrate that
the RO60 gene maps to 1q31-q32.1 in the same region as the genes for
regulators of complement activation, e.g., CR1 (120620). By fluorescence
in situ hybridization, Chan et al. (1994) mapped the SSA2 gene to 1q31.
The gene encoding the 52-kD Ro/SSA autoantigen (SSA1; 109092) maps to
11p15.5.
ANIMAL MODEL
Antibodies against a conserved RNA-binding protein, the Ro60-kD
autoantigen, occur in 24 to 60% of all patients with systemic lupus
erythematosus (152700). Anti-Ro antibodies are correlated with
photosensitivity and cutaneous lesions in these patients and with
neonatal lupus, a syndrome in which mothers with anti-Ro antibodies give
birth to children with complete congenital heart block (see 234700) and
photosensitive skin lesions. In higher eukaryotes, the Ro protein binds
small RNAs of unknown function known as Y RNAs. Because the Ro protein
also binds misfolded 5S rRNA precursors, it may function in a
quality-control pathway for ribosome biogenesis. Consistent with a role
in the recognition or repair of intracellular damage, an ortholog of Ro
in the radiation-resistant eubacterium Deinococcus radiodurans
contributes to survival of this bacterium after UV irradiation. Xue et
al. (2003) showed that mice lacking the Ro protein develop an autoimmune
syndrome characterized by anti-ribosome antibodies, antichromatin
antibodies, and glomerulonephritis. Moreover, in one strain background,
Ro -/- mice displayed increased sensitivity to irradiation with UV
light. Thus, one function of this major human autoantigen may be to
protect against autoantibody development, possibly by sequestering
defective ribonucleoproteins from immune surveillance. Furthermore, the
finding that mice lacking the Ro protein are photosensitive suggests
that loss of Ro function could contribute to the photosensitivity
associated with anti-Ro antibodies in humans.
*FIELD* RF
1. Alspaugh, M. A.; Tan, E. M.: Antibodies to cellular antigens in
Sjogren's syndrome. J. Clin. Invest. 55: 1067-1073, 1975.
2. Ben-Chetrit, E.; Gandy, B. J.; Tan, E. M.; Sullivan, K. F.: Isolation
and characterization of a cDNA clone encoding the 60-kD component
of the human SS-A/Ro ribonucleoprotein autoantigen. J. Clin. Invest. 83:
1284-1292, 1989.
3. Chan, E. K. L.; Tan, E. M.; Ward, D. C.; Matera, A. G.: Human
60-kDa SS-A/Ro ribonucleoprotein autoantigen gene (SSA2) localized
to 1q31 by fluorescence in situ hybridization. Genomics 23: 298-300,
1994.
4. Deutscher, S. L.; Harley, J. B.; Keene, J. D.: Molecular analysis
of the 60-kDa human Ro ribonucleoprotein. Proc. Nat. Acad. Sci. 85:
9479-9483, 1988.
5. Frank, M. B.; Mattei, M.-G.: Mapping of the human 60000 M(r) Ro/SSA
locus: the genes for three Ro/SSA autoantigens are located on separate
chromosomes. Immunogenetics 39: 428-431, 1994.
6. Hartung, K.; Ehrfeld, H.; Lakomek, H. J.; Coldewey, R.; Lang, B.;
Krapf, F.; Muller, R.; Schendel, D.; Deicher, H.; Seelig, H. P.; the
members of the SLE Study Group: The genetic basis of Ro and La antibody
formation in systemic lupus erythematosus: results of a multicenter
study. Rheum. Int. 11: 243-249, 1992.
7. Xue, D.; Shi, H.; Smith, J. D.; Chen, X.; Noe, D. A.; Cedervall,
T.; Yang, D. D.; Eynon, E.; Brash, D. E.; Kashgarian, M.; Flavell,
R. A.; Wolin, S. L.: A lupus-like syndrome develops in mice lacking
the Ro 60-kDa protein, a major lupus autoantigen. Proc. Nat. Acad.
Sci. 100: 7503-7508, 2003.
*FIELD* CN
Victor A. McKusick - updated: 7/1/2003
*FIELD* CD
Victor A. McKusick: 7/28/1994
*FIELD* ED
carol: 04/25/2011
wwang: 2/26/2007
alopez: 7/3/2003
terry: 7/1/2003
mimadm: 9/23/1995
carol: 11/30/1994
terry: 11/7/1994
mimadm: 7/30/1994
*RECORD*
*FIELD* NO
600063
*FIELD* TI
*600063 TROVE DOMAIN FAMILY, MEMBER 2; TROVE2
;;AUTOANTIGEN Ro/SSA, 60-KD; RO60;;
SJOGREN SYNDROME ANTIGEN A2; SSA2
read more*FIELD* TX
CLONING
The cDNA that encodes the 60-kD Ro/SSA autoantigen recognized by
autoantibodies in certain lupus erythematosus (152700) and Sjogren
syndrome (270150) sera was cloned and sequenced by Deutscher et al.
(1988) and confirmed with minor differences by Ben-Chetrit et al.
(1989).
GENE FUNCTION
Ro autoantigens are of clinical significance because antibodies directed
against them are found in most patients with primary Sjogren syndrome,
subacute cutaneous lupus erythematosus, neonatal lupus erythematosus,
ANA-negative lupus erythematosus, and systemic lupus erythematosus-like
disease secondary to homozygous C2 (217000) or C4 complement deficiency
(see 120810). Ro antibody is a frequent cause of congenital heart block
(234700). Alspaugh and Tan (1975) described 3 types of precipitating
antibodies in the serum of Sjogren patients; they designated the 3 types
as SS-A, SS-B, and SS-C. SS-A antibodies were later shown to be
immunologically equivalent to the Ro antibodies. Hartung et al. (1992)
found that the presence of Ro antibody was strongly associated with HLA
type DR3. La antibodies (109090) showed the same association.
MAPPING
Frank and Mattei (1994) used in situ hybridization to demonstrate that
the RO60 gene maps to 1q31-q32.1 in the same region as the genes for
regulators of complement activation, e.g., CR1 (120620). By fluorescence
in situ hybridization, Chan et al. (1994) mapped the SSA2 gene to 1q31.
The gene encoding the 52-kD Ro/SSA autoantigen (SSA1; 109092) maps to
11p15.5.
ANIMAL MODEL
Antibodies against a conserved RNA-binding protein, the Ro60-kD
autoantigen, occur in 24 to 60% of all patients with systemic lupus
erythematosus (152700). Anti-Ro antibodies are correlated with
photosensitivity and cutaneous lesions in these patients and with
neonatal lupus, a syndrome in which mothers with anti-Ro antibodies give
birth to children with complete congenital heart block (see 234700) and
photosensitive skin lesions. In higher eukaryotes, the Ro protein binds
small RNAs of unknown function known as Y RNAs. Because the Ro protein
also binds misfolded 5S rRNA precursors, it may function in a
quality-control pathway for ribosome biogenesis. Consistent with a role
in the recognition or repair of intracellular damage, an ortholog of Ro
in the radiation-resistant eubacterium Deinococcus radiodurans
contributes to survival of this bacterium after UV irradiation. Xue et
al. (2003) showed that mice lacking the Ro protein develop an autoimmune
syndrome characterized by anti-ribosome antibodies, antichromatin
antibodies, and glomerulonephritis. Moreover, in one strain background,
Ro -/- mice displayed increased sensitivity to irradiation with UV
light. Thus, one function of this major human autoantigen may be to
protect against autoantibody development, possibly by sequestering
defective ribonucleoproteins from immune surveillance. Furthermore, the
finding that mice lacking the Ro protein are photosensitive suggests
that loss of Ro function could contribute to the photosensitivity
associated with anti-Ro antibodies in humans.
*FIELD* RF
1. Alspaugh, M. A.; Tan, E. M.: Antibodies to cellular antigens in
Sjogren's syndrome. J. Clin. Invest. 55: 1067-1073, 1975.
2. Ben-Chetrit, E.; Gandy, B. J.; Tan, E. M.; Sullivan, K. F.: Isolation
and characterization of a cDNA clone encoding the 60-kD component
of the human SS-A/Ro ribonucleoprotein autoantigen. J. Clin. Invest. 83:
1284-1292, 1989.
3. Chan, E. K. L.; Tan, E. M.; Ward, D. C.; Matera, A. G.: Human
60-kDa SS-A/Ro ribonucleoprotein autoantigen gene (SSA2) localized
to 1q31 by fluorescence in situ hybridization. Genomics 23: 298-300,
1994.
4. Deutscher, S. L.; Harley, J. B.; Keene, J. D.: Molecular analysis
of the 60-kDa human Ro ribonucleoprotein. Proc. Nat. Acad. Sci. 85:
9479-9483, 1988.
5. Frank, M. B.; Mattei, M.-G.: Mapping of the human 60000 M(r) Ro/SSA
locus: the genes for three Ro/SSA autoantigens are located on separate
chromosomes. Immunogenetics 39: 428-431, 1994.
6. Hartung, K.; Ehrfeld, H.; Lakomek, H. J.; Coldewey, R.; Lang, B.;
Krapf, F.; Muller, R.; Schendel, D.; Deicher, H.; Seelig, H. P.; the
members of the SLE Study Group: The genetic basis of Ro and La antibody
formation in systemic lupus erythematosus: results of a multicenter
study. Rheum. Int. 11: 243-249, 1992.
7. Xue, D.; Shi, H.; Smith, J. D.; Chen, X.; Noe, D. A.; Cedervall,
T.; Yang, D. D.; Eynon, E.; Brash, D. E.; Kashgarian, M.; Flavell,
R. A.; Wolin, S. L.: A lupus-like syndrome develops in mice lacking
the Ro 60-kDa protein, a major lupus autoantigen. Proc. Nat. Acad.
Sci. 100: 7503-7508, 2003.
*FIELD* CN
Victor A. McKusick - updated: 7/1/2003
*FIELD* CD
Victor A. McKusick: 7/28/1994
*FIELD* ED
carol: 04/25/2011
wwang: 2/26/2007
alopez: 7/3/2003
terry: 7/1/2003
mimadm: 9/23/1995
carol: 11/30/1994
terry: 11/7/1994
mimadm: 7/30/1994