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P10155

- RO60_HUMAN

UniProt

P10155 - RO60_HUMAN

Protein

60 kDa SS-A/Ro ribonucleoprotein

Gene

TROVE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (27 Sep 2004)
      Previous versions | rss
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    Functioni

    RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation.1 Publication
    May play roles in cilia formation and/or maintenance.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi378 – 3781Divalent metal cationBy similarity
    Metal bindingi380 – 3801Divalent metal cationBy similarity
    Metal bindingi445 – 4451Divalent metal cationBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. RNA binding Source: ProtInc

    GO - Biological processi

    1. cilium morphogenesis Source: Ensembl
    2. transcription from RNA polymerase III promoter Source: ProtInc

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Metal-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    60 kDa SS-A/Ro ribonucleoprotein
    Short name:
    60 kDa Ro protein
    Short name:
    60 kDa ribonucleoprotein Ro
    Short name:
    RoRNP
    Alternative name(s):
    Ro 60 kDa autoantigen
    Sjoegren syndrome antigen A2
    Sjoegren syndrome type A antigen
    Short name:
    SS-A
    TROVE domain family member 2
    Gene namesi
    Name:TROVE2
    Synonyms:RO60, SSA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11313. TROVE2.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA
    3. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36137.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 53853860 kDa SS-A/Ro ribonucleoproteinPRO_0000174169Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei19 – 191Phosphoserine3 Publications
    Modified residuei224 – 2241N6-acetyllysine1 Publication
    Modified residuei359 – 3591N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP10155.
    PaxDbiP10155.
    PRIDEiP10155.

    PTM databases

    PhosphoSiteiP10155.

    Expressioni

    Gene expression databases

    ArrayExpressiP10155.
    BgeeiP10155.
    CleanExiHS_TROVE2.
    GenevestigatoriP10155.

    Organism-specific databases

    HPAiHPA002835.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Found in a complex with PUF60 and Y5 RNA. Interacts with RIP11.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PUF60Q9UHX11EBI-1049168,EBI-1053259

    Protein-protein interaction databases

    BioGridi112616. 26 interactions.
    IntActiP10155. 6 interactions.
    MINTiMINT-8395039.
    STRINGi9606.ENSP00000356411.

    Structurei

    3D structure databases

    ProteinModelPortaliP10155.
    SMRiP10155. Positions 4-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 369354TROVEPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni120 – 284165RNA-bindingBy similarityAdd
    BLAST
    Regioni361 – 538178VWFA-like domainBy similarityAdd
    BLAST

    Domaini

    The horseshoe-shaped TROVE domain is built with 7 helical HEAT-like repeats, and is closed by the VWFA-like domain giving rise to a ring-shaped monomer. Single-stranded RNA is bound in the positively charged central cavity By similarity.By similarity
    The MIDAS-like motif in the VWFA-like domain binds divalent metal cations.By similarity

    Sequence similaritiesi

    Belongs to the Ro 60 kDa family.Curated
    Contains 1 TROVE domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG74865.
    HOGENOMiHOG000075167.
    HOVERGENiHBG013234.
    InParanoidiP10155.
    KOiK11089.
    OMAiAKQEPML.
    OrthoDBiEOG78D7JR.
    PhylomeDBiP10155.
    TreeFamiTF105990.

    Family and domain databases

    InterProiIPR008858. TROVE.
    IPR018698. VWA-like_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF09967. DUF2201. 1 hit.
    PF05731. TROVE. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS50988. TROVE. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P10155-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEESVNQMQP LNEKQIANSQ DGYVWQVTDM NRLHRFLCFG SEGGTYYIKE    50
    QKLGLENAEA LIRLIEDGRG CEVIQEIKSF SQEGRTTKQE PMLFALAICS 100
    QCSDISTKQA AFKAVSEVCR IPTHLFTFIQ FKKDLKESMK CGMWGRALRK 150
    AIADWYNEKG GMALALAVTK YKQRNGWSHK DLLRLSHLKP SSEGLAIVTK 200
    YITKGWKEVH ELYKEKALSV ETEKLLKYLE AVEKVKRTRD ELEVIHLIEE 250
    HRLVREHLLT NHLKSKEVWK ALLQEMPLTA LLRNLGKMTA NSVLEPGNSE 300
    VSLVCEKLCN EKLLKKARIH PFHILIALET YKTGHGLRGK LKWRPDEEIL 350
    KALDAAFYKT FKTVEPTGKR FLLAVDVSAS MNQRVLGSIL NASTVAAAMC 400
    MVVTRTEKDS YVVAFSDEMV PCPVTTDMTL QQVLMAMSQI PAGGTDCSLP 450
    MIWAQKTNTP ADVFIVFTDN ETFAGGVHPA IALREYRKKM DIPAKLIVCG 500
    MTSNGFTIAD PDDRGMLDMC GFDTGALDVI RNFTLDMI 538
    Length:538
    Mass (Da):60,671
    Last modified:September 27, 2004 - v2
    Checksum:iCD735B1DF2B13098
    GO
    Isoform Short (identifier: P10155-2) [UniParc]FASTAAdd to Basket

    Also known as: 60E2

    The sequence of this isoform differs from the canonical sequence as follows:
         195-205: LAIVTKYITKG → KHKIFIGKKGG
         206-538: Missing.

    Show »
    Length:205
    Mass (Da):23,299
    Checksum:i31CF4F9732BEB16E
    GO
    Isoform 3 (identifier: P10155-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         515-538: GMLDMCGFDTGALDVIRNFTLDMI → DTVK

    Show »
    Length:518
    Mass (Da):58,483
    Checksum:iD3CE550ADBB2761B
    GO
    Isoform 4 (identifier: P10155-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         529-538: VIRNFTLDMI → PCKIPY

    Show »
    Length:534
    Mass (Da):60,169
    Checksum:i785F949FED553344
    GO
    Isoform 5 (identifier: P10155-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         515-538: GMLDMCGFDTGALDVIRNFTLDMI → ALQNTLLNKSF

    Show »
    Length:525
    Mass (Da):59,270
    Checksum:i9240B125E1038544
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361K → R in AAO47001. 1 PublicationCurated
    Sequence conflicti136 – 1361K → R in AAO47002. 1 PublicationCurated
    Sequence conflicti239 – 2391R → K in AAA35493. (PubMed:3200833)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei195 – 20511LAIVTKYITKG → KHKIFIGKKGG in isoform Short. CuratedVSP_005911Add
    BLAST
    Alternative sequencei206 – 538333Missing in isoform Short. CuratedVSP_005912Add
    BLAST
    Alternative sequencei515 – 53824GMLDM…TLDMI → DTVK in isoform 3. 1 PublicationVSP_045262Add
    BLAST
    Alternative sequencei515 – 53824GMLDM…TLDMI → ALQNTLLNKSF in isoform 5. 1 PublicationVSP_054041Add
    BLAST
    Alternative sequencei529 – 53810VIRNFTLDMI → PCKIPY in isoform 4. 1 PublicationVSP_045797

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04137 mRNA. Translation: AAA35493.1.
    M25077 mRNA. Translation: AAA35532.1.
    U44388 Genomic DNA. Translation: AAB81552.1. Different termination.
    U44388 Genomic DNA. Translation: AAB81553.1.
    AY205314 mRNA. Translation: AAO47001.1.
    AY205315 mRNA. Translation: AAO47002.1.
    AK314594 mRNA. Translation: BAG37166.1.
    AL136370 Genomic DNA. No translation available.
    CH471067 Genomic DNA. Translation: EAW91240.1.
    CH471067 Genomic DNA. Translation: EAW91243.1.
    CH471067 Genomic DNA. Translation: EAW91245.1.
    CH471067 Genomic DNA. Translation: EAW91247.1.
    BC036658 mRNA. Translation: AAH36658.1.
    CCDSiCCDS1379.1. [P10155-1]
    CCDS41449.1. [P10155-5]
    CCDS41450.2. [P10155-4]
    CCDS53451.1. [P10155-3]
    PIRiA31760.
    RefSeqiNP_001035828.1. NM_001042369.2. [P10155-5]
    NP_001035829.2. NM_001042370.2. [P10155-4]
    NP_001166995.1. NM_001173524.1. [P10155-1]
    NP_001166996.1. NM_001173525.1. [P10155-3]
    NP_004591.2. NM_004600.5. [P10155-1]
    XP_006711560.1. XM_006711497.1. [P10155-1]
    UniGeneiHs.288178.

    Genome annotation databases

    EnsembliENST00000367441; ENSP00000356411; ENSG00000116747. [P10155-1]
    ENST00000367443; ENSP00000356413; ENSG00000116747. [P10155-3]
    ENST00000367444; ENSP00000356414; ENSG00000116747. [P10155-5]
    ENST00000367445; ENSP00000356415; ENSG00000116747. [P10155-4]
    ENST00000367446; ENSP00000356416; ENSG00000116747. [P10155-1]
    ENST00000400968; ENSP00000383752; ENSG00000116747. [P10155-1]
    GeneIDi6738.
    KEGGihsa:6738.
    UCSCiuc001gss.3. human. [P10155-1]
    uc001gsw.3. human.
    uc009wyp.3. human.
    uc009wyq.3. human.

    Polymorphism databases

    DMDMi52788235.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04137 mRNA. Translation: AAA35493.1 .
    M25077 mRNA. Translation: AAA35532.1 .
    U44388 Genomic DNA. Translation: AAB81552.1 . Different termination.
    U44388 Genomic DNA. Translation: AAB81553.1 .
    AY205314 mRNA. Translation: AAO47001.1 .
    AY205315 mRNA. Translation: AAO47002.1 .
    AK314594 mRNA. Translation: BAG37166.1 .
    AL136370 Genomic DNA. No translation available.
    CH471067 Genomic DNA. Translation: EAW91240.1 .
    CH471067 Genomic DNA. Translation: EAW91243.1 .
    CH471067 Genomic DNA. Translation: EAW91245.1 .
    CH471067 Genomic DNA. Translation: EAW91247.1 .
    BC036658 mRNA. Translation: AAH36658.1 .
    CCDSi CCDS1379.1. [P10155-1 ]
    CCDS41449.1. [P10155-5 ]
    CCDS41450.2. [P10155-4 ]
    CCDS53451.1. [P10155-3 ]
    PIRi A31760.
    RefSeqi NP_001035828.1. NM_001042369.2. [P10155-5 ]
    NP_001035829.2. NM_001042370.2. [P10155-4 ]
    NP_001166995.1. NM_001173524.1. [P10155-1 ]
    NP_001166996.1. NM_001173525.1. [P10155-3 ]
    NP_004591.2. NM_004600.5. [P10155-1 ]
    XP_006711560.1. XM_006711497.1. [P10155-1 ]
    UniGenei Hs.288178.

    3D structure databases

    ProteinModelPortali P10155.
    SMRi P10155. Positions 4-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112616. 26 interactions.
    IntActi P10155. 6 interactions.
    MINTi MINT-8395039.
    STRINGi 9606.ENSP00000356411.

    PTM databases

    PhosphoSitei P10155.

    Polymorphism databases

    DMDMi 52788235.

    Proteomic databases

    MaxQBi P10155.
    PaxDbi P10155.
    PRIDEi P10155.

    Protocols and materials databases

    DNASUi 6738.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367441 ; ENSP00000356411 ; ENSG00000116747 . [P10155-1 ]
    ENST00000367443 ; ENSP00000356413 ; ENSG00000116747 . [P10155-3 ]
    ENST00000367444 ; ENSP00000356414 ; ENSG00000116747 . [P10155-5 ]
    ENST00000367445 ; ENSP00000356415 ; ENSG00000116747 . [P10155-4 ]
    ENST00000367446 ; ENSP00000356416 ; ENSG00000116747 . [P10155-1 ]
    ENST00000400968 ; ENSP00000383752 ; ENSG00000116747 . [P10155-1 ]
    GeneIDi 6738.
    KEGGi hsa:6738.
    UCSCi uc001gss.3. human. [P10155-1 ]
    uc001gsw.3. human.
    uc009wyp.3. human.
    uc009wyq.3. human.

    Organism-specific databases

    CTDi 6738.
    GeneCardsi GC01P193028.
    HGNCi HGNC:11313. TROVE2.
    HPAi HPA002835.
    MIMi 600063. gene.
    neXtProti NX_P10155.
    PharmGKBi PA36137.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG74865.
    HOGENOMi HOG000075167.
    HOVERGENi HBG013234.
    InParanoidi P10155.
    KOi K11089.
    OMAi AKQEPML.
    OrthoDBi EOG78D7JR.
    PhylomeDBi P10155.
    TreeFami TF105990.

    Miscellaneous databases

    ChiTaRSi TROVE2. human.
    GeneWikii TROVE2.
    GenomeRNAii 6738.
    NextBioi 26284.
    PROi P10155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10155.
    Bgeei P10155.
    CleanExi HS_TROVE2.
    Genevestigatori P10155.

    Family and domain databases

    InterProi IPR008858. TROVE.
    IPR018698. VWA-like_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF09967. DUF2201. 1 hit.
    PF05731. TROVE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS50988. TROVE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular analysis of the 60-kDa human Ro ribonucleoprotein."
      Deutscher S.L., Harley J.B., Keene J.D.
      Proc. Natl. Acad. Sci. U.S.A. 85:9479-9483(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "Isolation and characterization of a cDNA clone encoding the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen."
      Ben-Chetrit E., Gandy B.J., Tan E.M., Sulivan K.F.
      J. Clin. Invest. 83:1284-1292(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    3. "Identification and characterization of an alternative mRNA transcript of the 60-kD SS-A/Ro ribonucleoprotein encoding the N-terminal RNA binding domain alone."
      Buyon J.P., DiDonato F., Tseng C.E., Rashbaum W., Morris A., Hamel J.C., Chan E.K.L.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
    4. "A variant of the 60-kD component of the human SS-A/Ro ribonucleoprotein autoantigen involved in multidrug resistance of gastric cancer cells."
      Han Q., Wang X., Shi Y., Ding J., Fan D.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Thalamus.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Testis.
    9. Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W.
      Submitted (FEB-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-14; 271-283 AND 352-359, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Pre-B cell.
    10. "Defining a novel 75-kDa phosphoprotein associated with SS-A/Ro and identification of distinct human autoantibodies."
      Wang D., Buyon J.P., Zhu W., Chan E.K.L.
      J. Clin. Invest. 104:1265-1275(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIP11.
      Tissue: Keratinocyte.
    11. "Interaction cloning and characterization of RoBPI, a novel protein binding to human Ro ribonucleoproteins."
      Bouffard P., Barbar E., Briere F., Boire G.
      RNA 6:66-78(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PUF60 AND Y5 RNA.
    12. "Human Y5 RNA specializes a Ro ribonucleoprotein for 5S ribosomal RNA quality control."
      Hogg J.R., Collins K.
      Genes Dev. 21:3067-3072(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-224 AND LYS-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRO60_HUMAN
    AccessioniPrimary (citable) accession number: P10155
    Secondary accession number(s): B2RBB9
    , Q5LJ98, Q5LJ99, Q5LJA0, Q86WL3, Q86WL4, Q92787, Q9H1W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: September 27, 2004
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Antibodies against normal cellular SSA2 protein are found in sera from patients with systemic lupus erythematosus (SLE).

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3