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Q01085 (TIAR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolysin TIAR
Alternative name(s):
TIA-1-related protein
Gene names
Name:TIAL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

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.

Post-translational modification

Phosphorylated by MAPK14 following DNA damage, releasing TIAR from GADD45A mRNA. Ref.5

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01085-1)

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.
Isoform 2 (identifier: Q01085-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-43: E → EQPDSRRVNSSVGFSVLQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Nucleolysin TIAR
PRO_0000081978

Regions

Domain9 – 8577RRM 1
Domain97 – 17579RRM 2
Domain205 – 27773RRM 3

Amino acid modifications

Modified residue1221N6-acetyllysine Ref.4
Modified residue2011Phosphoserine Ref.6

Natural variations

Alternative sequence431E → EQPDSRRVNSSVGFSVLQ in isoform 2.
VSP_043700

Secondary structure

........................................... 375
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 2F8D1C7169A7817E

FASTA37541,591
        10         20         30         40         50         60 
MMEDDGQPRT LYVGNLSRDV TEVLILQLFS QIGPCKSCKM ITEHTSNDPY CFVEFYEHRD 

        70         80         90        100        110        120 
AAAALAAMNG RKILGKEVKV NWATTPSSQK KDTSNHFHVF VGDLSPEITT EDIKSAFAPF 

       130        140        150        160        170        180 
GKISDARVVK DMATGKSKGY GFVSFYNKLD AENAIVHMGG QWLGGRQIRT NWATRKPPAP 

       190        200        210        220        230        240 
KSTQENNTKQ LRFEDVVNQS SPKNCTVYCG GIASGLTDQL MRQTFSPFGQ IMEIRVFPEK 

       250        260        270        280        290        300 
GYSFVRFSTH ESAAHAIVSV NGTTIEGHVV KCYWGKESPD MTKNFQQVDY SQWGQWSQVY 

       310        320        330        340        350        360 
GNPQQYGQYM ANGWQVPPYG VYGQPWNQQG FGVDQSPSAA WMGGFGAQPP QGQAPPPVIP 

       370 
PPNQAGYGMA SYQTQ 

« Hide

Isoform 2 [UniParc].

Checksum: F81DA9563C041D75
Show »

FASTA39243,449

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96954 mRNA. Translation: AAA36384.1.
AK290695 mRNA. Translation: BAF83384.1.
AK290984 mRNA. Translation: BAF83673.1.
PIRA46174.
RefSeqNP_001029097.1. NM_001033925.1.
NP_003243.1. NM_003252.3.
UniGeneHs.501203.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4GNMR-A187-282[»]
2CQINMR-A1-90[»]
2DH7NMR-A89-180[»]
ProteinModelPortalQ01085.
SMRQ01085. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112929. 35 interactions.
DIPDIP-42425N.
IntActQ01085. 15 interactions.
MINTMINT-1203913.
STRING9606.ENSP00000358089.

PTM databases

PhosphoSiteQ01085.

Polymorphism databases

DMDM267131.

Proteomic databases

PaxDbQ01085.
PRIDEQ01085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369093; ENSP00000358089; ENSG00000151923. [Q01085-2]
ENST00000436547; ENSP00000394902; ENSG00000151923. [Q01085-1]
GeneID7073.
KEGGhsa:7073.
UCSCuc001leh.1. human. [Q01085-2]
uc001lei.1. human. [Q01085-1]

Organism-specific databases

CTD7073.
GeneCardsGC10M121324.
HGNCHGNC:11804. TIAL1.
MIM603413. gene.
neXtProtNX_Q01085.
PharmGKBPA36513.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000206748.
HOVERGENHBG105006.
KOK13201.
OMACKMITEM.
OrthoDBEOG7XH6QJ.
PhylomeDBQ01085.
TreeFamTF312915.

Gene expression databases

ArrayExpressQ01085.
BgeeQ01085.
CleanExHS_TIAL1.
GenevestigatorQ01085.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTIAL1. human.
EvolutionaryTraceQ01085.
GeneWikiTIAL1.
GenomeRNAi7073.
NextBio27661.
PROQ01085.
SOURCESearch...

Entry information

Entry nameTIAR_HUMAN
AccessionPrimary (citable) accession number: Q01085
Secondary accession number(s): A8K3T0, A8K4L9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM