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Q01085

- TIAR_HUMAN

UniProt

Q01085 - TIAR_HUMAN

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Protein
Nucleolysin TIAR
Gene
TIAL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. RNA binding Source: ProtInc
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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.

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Nucleolysin TIAR
PRO_0000081978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221N6-acetyllysine1 Publication
Modified residuei201 – 2011Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by MAPK14 following DNA damage, releasing TIAR from GADD45A mRNA.1 Publication

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. 15 interactions.
MINTiMINT-1203913.
STRINGi9606.ENSP00000358089.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ01085.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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.
VSP_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...

Protein-protein interaction databases

BioGridi 112929. 39 interactions.
DIPi DIP-42425N.
IntActi Q01085. 15 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 140 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

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