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P31483

- TIA1_HUMAN

UniProt

P31483 - TIA1_HUMAN

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Protein

Nucleolysin TIA-1 isoform p40

Gene

TIA1

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

Functioni

Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). 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) binding Source: ProtInc
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. negative regulation of cytokine biosynthetic process Source: Ensembl
  3. negative regulation of translation Source: Ensembl
  4. regulation of mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolysin TIA-1 isoform p40
Alternative name(s):
RNA-binding protein TIA-1
T-cell-restricted intracellular antigen-1
Short name:
TIA-1
p40-TIA-1
Gene namesi
Name:TIA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11802. TIA1.

Subcellular locationi

Cytoplasmic granule. Nucleus
Note: Accumulates in cytoplasmic stress granules (SG) following cellular damage.

GO - Cellular componenti

  1. cytoplasmic stress granule Source: MGI
  2. nuclear stress granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Welander distal myopathy (WDM) [MIM:604454]: An autosomal dominant disorder characterized by adult onset of distal muscle weakness predominantly affecting the distal long extensors of the hands, with slow progression to involve all small hand muscles and the lower legs. Skeletal muscle biopsy shows myopathic changes and prominent rimmed vacuoles. Rare homozygous patients showed earlier onset, faster progression, and proximal muscle involvement.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti384 – 3841E → K in WDM; results in a mild increase of stress granule numbers compared to controls. 2 Publications
VAR_069897

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi604454. phenotype.
Orphaneti603. Distal myopathy, Welander type.
PharmGKBiPA36511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Nucleolysin TIA-1 isoform p40PRO_0000031031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP31483.
PaxDbiP31483.
PRIDEiP31483.

PTM databases

PhosphoSiteiP31483.

Expressioni

Gene expression databases

BgeeiP31483.
CleanExiHS_TIA1.
ExpressionAtlasiP31483. baseline and differential.
GenevestigatoriP31483.

Interactioni

Protein-protein interaction databases

BioGridi112928. 22 interactions.
IntActiP31483. 23 interactions.
MINTiMINT-4823992.
STRINGi9606.ENSP00000401371.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1127Combined sources
Helixi119 – 1268Combined sources
Helixi127 – 1293Combined sources
Beta strandi132 – 1398Combined sources
Turni141 – 1433Combined sources
Beta strandi146 – 15611Combined sources
Helixi157 – 16711Combined sources
Beta strandi178 – 1825Combined sources
Helixi202 – 2065Combined sources
Beta strandi215 – 2195Combined sources
Helixi227 – 2348Combined sources
Turni235 – 2373Combined sources
Beta strandi240 – 2467Combined sources
Turni247 – 2504Combined sources
Beta strandi251 – 2588Combined sources
Helixi259 – 26911Combined sources
Beta strandi280 – 2834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MJNNMR-A105-285[»]
3BS9X-ray1.95A/B105-186[»]
ProteinModelPortaliP31483.
SMRiP31483. Positions 1-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31483.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 8377RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini106 – 18479RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 28673RRM 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000119252.
HOGENOMiHOG000206748.
HOVERGENiHBG105006.
InParanoidiP31483.
KOiK13201.
OMAiXTAGNDP.
OrthoDBiEOG7XH6QJ.
PhylomeDBiP31483.
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 Long (identifier: P31483-1) [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

        10         20         30         40         50
MEDEMPKTLY VGNLSRDVTE ALILQLFSQI GPCKNCKMIM DTAGNDPYCF
60 70 80 90 100
VEFHEHRHAA AALAAMNGRK IMGKEVKVNW ATTPSSQKKD TSSSTVVSTQ
110 120 130 140 150
RSQDHFHVFV GDLSPEITTE DIKAAFAPFG RISDARVVKD MATGKSKGYG
160 170 180 190 200
FVSFFNKWDA ENAIQQMGGQ WLGGRQIRTN WATRKPPAPK STYESNTKQL
210 220 230 240 250
SYDEVVNQSS PSNCTVYCGG VTSGLTEQLM RQTFSPFGQI MEIRVFPDKG
260 270 280 290 300
YSFVRFNSHE SAAHAIVSVN GTTIEGHVVK CYWGKETLDM INPVQQQNQI
310 320 330 340 350
GYPQPYGQWG QWYGNAQQIG QYMPNGWQVP AYGMYGQAWN QQGFNQTQSS
360 370 380
APWMGPNYGV QPPQGQNGSM LPNQPSGYRV AGYETQ
Length:386
Mass (Da):42,963
Last modified:September 23, 2008 - v3
Checksum:i4FD2E8B7AF57A0D6
GO
Isoform Short (identifier: P31483-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-104: SSTVVSTQRSQD → N

Show »
Length:375
Mass (Da):41,801
Checksum:i067CB6A801563505
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161E → Q in M77142. (PubMed:1934064)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti384 – 3841E → K in WDM; results in a mild increase of stress granule numbers compared to controls. 2 Publications
VAR_069897

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 10412SSTVV…QRSQD → N in isoform Short. 1 PublicationVSP_005892Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77142 mRNA. No translation available.
S70114 Genomic DNA. Translation: AAD14053.1.
AC016700 Genomic DNA. Translation: AAX93193.1.
CH471053 Genomic DNA. Translation: EAW99824.1.
CCDSiCCDS1900.1. [P31483-2]
CCDS1901.1. [P31483-1]
PIRiA39293.
RefSeqiNP_071320.2. NM_022037.2. [P31483-2]
NP_071505.2. NM_022173.2. [P31483-1]
UniGeneiHs.413123.

Genome annotation databases

EnsembliENST00000415783; ENSP00000404023; ENSG00000116001. [P31483-2]
ENST00000433529; ENSP00000401371; ENSG00000116001. [P31483-1]
GeneIDi7072.
KEGGihsa:7072.
UCSCiuc002sgj.4. human. [P31483-1]
uc002sgk.4. human. [P31483-2]

Polymorphism databases

DMDMi206729905.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77142 mRNA. No translation available.
S70114 Genomic DNA. Translation: AAD14053.1 .
AC016700 Genomic DNA. Translation: AAX93193.1 .
CH471053 Genomic DNA. Translation: EAW99824.1 .
CCDSi CCDS1900.1. [P31483-2 ]
CCDS1901.1. [P31483-1 ]
PIRi A39293.
RefSeqi NP_071320.2. NM_022037.2. [P31483-2 ]
NP_071505.2. NM_022173.2. [P31483-1 ]
UniGenei Hs.413123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MJN NMR - A 105-285 [» ]
3BS9 X-ray 1.95 A/B 105-186 [» ]
ProteinModelPortali P31483.
SMRi P31483. Positions 1-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112928. 22 interactions.
IntActi P31483. 23 interactions.
MINTi MINT-4823992.
STRINGi 9606.ENSP00000401371.

PTM databases

PhosphoSitei P31483.

Polymorphism databases

DMDMi 206729905.

Proteomic databases

MaxQBi P31483.
PaxDbi P31483.
PRIDEi P31483.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000415783 ; ENSP00000404023 ; ENSG00000116001 . [P31483-2 ]
ENST00000433529 ; ENSP00000401371 ; ENSG00000116001 . [P31483-1 ]
GeneIDi 7072.
KEGGi hsa:7072.
UCSCi uc002sgj.4. human. [P31483-1 ]
uc002sgk.4. human. [P31483-2 ]

Organism-specific databases

CTDi 7072.
GeneCardsi GC02M070437.
HGNCi HGNC:11802. TIA1.
MIMi 603518. gene.
604454. phenotype.
neXtProti NX_P31483.
Orphaneti 603. Distal myopathy, Welander type.
PharmGKBi PA36511.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
GeneTreei ENSGT00760000119252.
HOGENOMi HOG000206748.
HOVERGENi HBG105006.
InParanoidi P31483.
KOi K13201.
OMAi XTAGNDP.
OrthoDBi EOG7XH6QJ.
PhylomeDBi P31483.
TreeFami TF312915.

Miscellaneous databases

ChiTaRSi TIA1. human.
EvolutionaryTracei P31483.
GenomeRNAii 7072.
NextBioi 27655.
PROi P31483.
SOURCEi Search...

Gene expression databases

Bgeei P31483.
CleanExi HS_TIA1.
ExpressionAtlasi P31483. baseline and differential.
Genevestigatori P31483.

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. "A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells."
    Tian Q., Streuli M., Saito H., Schlossman S.F., Anderson P.
    Cell 67:629-639(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
  2. "Intron-exon organization and chromosomal localization of the human TIA-1 gene."
    Kawakami A., Tian Q., Streuli M., Poe M., Edelhoff S., Disteche C.M., Anderson P.
    J. Immunol. 152:4937-4945(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Tissue: Leukocyte.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Stress granule assembly is mediated by prion-like aggregation of TIA-1."
    Gilks N., Kedersha N., Ayodele M., Shen L., Stoecklin G., Dember L.M., Anderson P.
    Mol. Biol. Cell 15:5383-5398(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution."
    Kumar A.O., Swenson M.C., Benning M.M., Kielkopf C.L.
    Biochem. Biophys. Res. Commun. 367:813-819(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 105-186, SUBCELLULAR LOCATION.
  9. Cited for: VARIANT WDM LYS-384, CHARACTERIZATION OF VARIANT WDM LYS-384.
  10. "Welander distal myopathy caused by an ancient founder mutation in TIA1 associated with perturbed splicing."
    Klar J., Sobol M., Melberg A., Maebert K., Ameur A., Johansson A.C., Feuk L., Entesarian M., Orlen H., Casar-Borota O., Dahl N.
    Hum. Mutat. 34:572-577(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WDM LYS-384.

Entry informationi

Entry nameiTIA1_HUMAN
AccessioniPrimary (citable) accession number: P31483
Secondary accession number(s): Q53SS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 23, 2008
Last modified: November 26, 2014
This is version 141 of the entry and version 3 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3