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Q01085

- TIAR_HUMAN

UniProt

Q01085 - TIAR_HUMAN

Protein

Nucleolysin TIAR

Gene

TIAL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    RNA-binding protein. Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.

    GO - Molecular functioni

    1. AU-rich element binding Source: Ensembl
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. defense response Source: ProtInc
    3. germ cell development Source: Ensembl
    4. positive regulation of cell proliferation Source: Ensembl
    5. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    6. stem cell division Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleolysin TIAR
    Alternative name(s):
    TIA-1-related protein
    Gene namesi
    Name:TIAL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:11804. TIAL1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cytoplasmic granule
    Note: The cytoplasmic granules are stress granules which are a dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. Colocalizes with NANOS3 in the stress granules By similarity. Cytoplasmic granules of cytolytic T-lymphocytes.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic stress granule Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. lysosome Source: ProtInc
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36513.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Nucleolysin TIARPRO_0000081978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221N6-acetyllysine1 Publication
    Modified residuei201 – 2011Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by MAPK14 following DNA damage, releasing TIAR from GADD45A mRNA.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ01085.
    PaxDbiQ01085.
    PRIDEiQ01085.

    PTM databases

    PhosphoSiteiQ01085.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01085.
    BgeeiQ01085.
    CleanExiHS_TIAL1.
    GenevestigatoriQ01085.

    Interactioni

    Protein-protein interaction databases

    BioGridi112929. 39 interactions.
    DIPiDIP-42425N.
    IntActiQ01085. 16 interactions.
    MINTiMINT-1203913.
    STRINGi9606.ENSP00000358089.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 156
    Helixi22 – 3211
    Beta strandi35 – 417
    Beta strandi50 – 578
    Helixi58 – 6811
    Beta strandi71 – 733
    Beta strandi76 – 827
    Beta strandi97 – 1026
    Helixi110 – 1167
    Turni118 – 1203
    Beta strandi123 – 1308
    Beta strandi132 – 1343
    Beta strandi136 – 14712
    Helixi148 – 15710
    Turni158 – 1603
    Beta strandi164 – 1663
    Helixi193 – 1997
    Beta strandi206 – 2105
    Helixi218 – 22811
    Beta strandi231 – 2377
    Turni238 – 2414
    Beta strandi242 – 2498
    Helixi250 – 26011
    Beta strandi271 – 2733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4GNMR-A187-282[»]
    2CQINMR-A1-90[»]
    2DH7NMR-A89-180[»]
    ProteinModelPortaliQ01085.
    SMRiQ01085. Positions 1-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01085.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 8577RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 17579RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini205 – 27773RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000206748.
    HOVERGENiHBG105006.
    KOiK13201.
    OMAiCKMITEM.
    OrthoDBiEOG7XH6QJ.
    PhylomeDBiQ01085.
    TreeFamiTF312915.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q01085-1) [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

    MMEDDGQPRT LYVGNLSRDV TEVLILQLFS QIGPCKSCKM ITEHTSNDPY    50
    CFVEFYEHRD AAAALAAMNG RKILGKEVKV NWATTPSSQK KDTSNHFHVF 100
    VGDLSPEITT EDIKSAFAPF GKISDARVVK DMATGKSKGY GFVSFYNKLD 150
    AENAIVHMGG QWLGGRQIRT NWATRKPPAP KSTQENNTKQ LRFEDVVNQS 200
    SPKNCTVYCG GIASGLTDQL MRQTFSPFGQ IMEIRVFPEK GYSFVRFSTH 250
    ESAAHAIVSV NGTTIEGHVV KCYWGKESPD MTKNFQQVDY SQWGQWSQVY 300
    GNPQQYGQYM ANGWQVPPYG VYGQPWNQQG FGVDQSPSAA WMGGFGAQPP 350
    QGQAPPPVIP PPNQAGYGMA SYQTQ 375
    Length:375
    Mass (Da):41,591
    Last modified:April 1, 1993 - v1
    Checksum:i2F8D1C7169A7817E
    GO
    Isoform 2 (identifier: Q01085-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-43: E → EQPDSRRVNSSVGFSVLQ

    Note: No experimental confirmation available.

    Show »
    Length:392
    Mass (Da):43,449
    Checksum:iF81DA9563C041D75
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei43 – 431E → EQPDSRRVNSSVGFSVLQ in isoform 2. 1 PublicationVSP_043700

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96954 mRNA. Translation: AAA36384.1.
    AK290695 mRNA. Translation: BAF83384.1.
    AK290984 mRNA. Translation: BAF83673.1.
    CCDSiCCDS31295.1. [Q01085-2]
    CCDS7613.1. [Q01085-1]
    PIRiA46174.
    RefSeqiNP_001029097.1. NM_001033925.1. [Q01085-2]
    NP_003243.1. NM_003252.3. [Q01085-1]
    UniGeneiHs.501203.

    Genome annotation databases

    EnsembliENST00000369093; ENSP00000358089; ENSG00000151923. [Q01085-2]
    ENST00000436547; ENSP00000394902; ENSG00000151923. [Q01085-1]
    GeneIDi7073.
    KEGGihsa:7073.
    UCSCiuc001leh.1. human. [Q01085-2]
    uc001lei.1. human. [Q01085-1]

    Polymorphism databases

    DMDMi267131.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96954 mRNA. Translation: AAA36384.1 .
    AK290695 mRNA. Translation: BAF83384.1 .
    AK290984 mRNA. Translation: BAF83673.1 .
    CCDSi CCDS31295.1. [Q01085-2 ]
    CCDS7613.1. [Q01085-1 ]
    PIRi A46174.
    RefSeqi NP_001029097.1. NM_001033925.1. [Q01085-2 ]
    NP_003243.1. NM_003252.3. [Q01085-1 ]
    UniGenei Hs.501203.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4G NMR - A 187-282 [» ]
    2CQI NMR - A 1-90 [» ]
    2DH7 NMR - A 89-180 [» ]
    ProteinModelPortali Q01085.
    SMRi Q01085. Positions 1-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112929. 39 interactions.
    DIPi DIP-42425N.
    IntActi Q01085. 16 interactions.
    MINTi MINT-1203913.
    STRINGi 9606.ENSP00000358089.

    PTM databases

    PhosphoSitei Q01085.

    Polymorphism databases

    DMDMi 267131.

    Proteomic databases

    MaxQBi Q01085.
    PaxDbi Q01085.
    PRIDEi Q01085.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369093 ; ENSP00000358089 ; ENSG00000151923 . [Q01085-2 ]
    ENST00000436547 ; ENSP00000394902 ; ENSG00000151923 . [Q01085-1 ]
    GeneIDi 7073.
    KEGGi hsa:7073.
    UCSCi uc001leh.1. human. [Q01085-2 ]
    uc001lei.1. human. [Q01085-1 ]

    Organism-specific databases

    CTDi 7073.
    GeneCardsi GC10M121324.
    HGNCi HGNC:11804. TIAL1.
    MIMi 603413. gene.
    neXtProti NX_Q01085.
    PharmGKBi PA36513.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000206748.
    HOVERGENi HBG105006.
    KOi K13201.
    OMAi CKMITEM.
    OrthoDBi EOG7XH6QJ.
    PhylomeDBi Q01085.
    TreeFami TF312915.

    Miscellaneous databases

    ChiTaRSi TIAL1. human.
    EvolutionaryTracei Q01085.
    GeneWikii TIAL1.
    GenomeRNAii 7073.
    NextBioi 27661.
    PROi Q01085.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01085.
    Bgeei Q01085.
    CleanExi HS_TIAL1.
    Genevestigatori Q01085.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and functional characterization of a TIA-1-related nucleolysin."
      Kawakami A., Tian Q., Duan X., Streuli M., Schlossman S.F., Anderson P.
      Proc. Natl. Acad. Sci. U.S.A. 89:8681-8685(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Lung.
    3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    4. "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-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization."
      Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.
      Mol. Cell 40:34-49(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK14.
    6. "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-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Solution structure of the RNA binding domains of nucleolysin TIAR."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-282.

    Entry informationi

    Entry nameiTIAR_HUMAN
    AccessioniPrimary (citable) accession number: Q01085
    Secondary accession number(s): A8K3T0, A8K4L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3