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O94916

- NFAT5_HUMAN

UniProt

O94916 - NFAT5_HUMAN

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Protein

Nuclear factor of activated T-cells 5

Gene
NFAT5, KIAA0827, TONEBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transcription factor involved in the transcriptional regulation of osmoprotective and inflammatory genes. Regulates hypertonicity-induced cellular accumulation of osmolytes.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi293 – 3008

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. cytokine production Source: Ensembl
  2. excretion Source: ProtInc
  3. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. regulation of calcineurin-NFAT signaling cascade Source: Ensembl
  5. signal transduction Source: ProtInc
  6. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor of activated T-cells 5
Short name:
NF-AT5
Alternative name(s):
T-cell transcription factor NFAT5
Tonicity-responsive enhancer-binding protein
Short name:
TonE-binding protein
Short name:
TonEBP
Gene namesi
Name:NFAT5
Synonyms:KIAA0827, TONEBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:7774. NFAT5.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Nuclear distribution increases under hypertonic conditions By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201S → A: Normal nuclear localization. 1 Publication
Mutagenesisi134 – 1341S → A: Reduced nuclear localization. 1 Publication
Mutagenesisi135 – 1351T → A: Reduced nuclear localization. 1 Publication
Mutagenesisi155 – 1551S → A: Increased nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA31581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15311531Nuclear factor of activated T-cells 5PRO_0000205183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei122 – 1221N6-acetyllysine By similarity
Modified residuei134 – 1341Phosphoserine1 Publication
Modified residuei135 – 1351Phosphothreonine; by CDK51 Publication
Modified residuei155 – 1551Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Thr-135 by CDK5 in response to osmotic stress; this phosphorylation mediates its rapid nuclear localization.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO94916.
PaxDbiO94916.
PRIDEiO94916.

PTM databases

PhosphoSiteiO94916.

Expressioni

Tissue specificityi

Highest levels in skeletal muscle, brain, heart and peripheral blood leukocytes. Also expressed in placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine and colon.

Gene expression databases

ArrayExpressiO94916.
BgeeiO94916.
CleanExiHS_NFAT5.
GenevestigatoriO94916.

Interactioni

Subunit structurei

Homodimer when bound to DNA, completely encircles its DNA target. Interacts with CIDEC; this interaction is direct and retains NFAT5 in the cytoplasm By similarity. Does not bind with Fos and Jun transcription factors.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX17Q928413EBI-308320,EBI-746012
DDX5P178444EBI-308320,EBI-351962

Protein-protein interaction databases

BioGridi115949. 3 interactions.
DIPiDIP-58524N.
IntActiO94916. 5 interactions.
STRINGi9606.ENSP00000396538.

Structurei

Secondary structure

1
1531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi275 – 2773
Beta strandi280 – 2867
Beta strandi310 – 3123
Beta strandi315 – 3206
Beta strandi325 – 33713
Beta strandi342 – 3487
Beta strandi358 – 3625
Beta strandi365 – 3728
Helixi374 – 3763
Beta strandi379 – 3813
Beta strandi384 – 3896
Helixi392 – 3965
Beta strandi410 – 42011
Beta strandi422 – 4243
Beta strandi426 – 4327
Beta strandi446 – 4516
Beta strandi454 – 4563
Beta strandi462 – 4687
Beta strandi475 – 4828
Beta strandi489 – 4924
Helixi496 – 4983
Beta strandi501 – 5077
Beta strandi520 – 5289
Beta strandi537 – 5426

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IMHX-ray2.86C/D264-544[»]
ProteinModelPortaliO94916.
SMRiO94916. Positions 264-544.

Miscellaneous databases

EvolutionaryTraceiO94916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini264 – 443180RHDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 10032Ser-richAdd
BLAST
Compositional biasi739 – 7435Poly-Gln
Compositional biasi879 – 88810Poly-Gln
Compositional biasi966 – 9716Poly-Thr
Compositional biasi1248 – 126619Poly-GlnAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG85658.
HOGENOMiHOG000236245.
HOVERGENiHBG052612.
InParanoidiO94916.
KOiK17335.
OMAiNNMTLAV.
OrthoDBiEOG79PJND.
PhylomeDBiO94916.
TreeFamiTF326480.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR008366. NFAT.
IPR015646. NFAT5.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PANTHERiPTHR12533. PTHR12533. 1 hit.
PTHR12533:SF7. PTHR12533:SF7. 1 hit.
PfamiPF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR01789. NUCFACTORATC.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50254. REL_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform C (identifier: O94916-1) [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

MPSDFISLLS ADLDLESPKS LYSRESVYDL LPKELQLPPS RETSVASMSQ     50
TSGGEAGSPP PAVVAADASS APSSSSMGGA CSSFTTSSSP TIYSTSVTDS 100
KAMQVESCSS AVGVSNRGVS EKQLTSNTVQ QHPSTPKRHT VLYISPPPED 150
LLDNSRMSCQ DEGCGLESEQ SCSMWMEDSP SNFSNMSTSS YNDNTEVPRK 200
SRKRNPKQRP GVKRRDCEES NMDIFDADSA KAPHYVLSQL TTDNKGNSKA 250
GNGTLENQKG TGVKKSPMLC GQYPVKSEGK ELKIVVQPET QHRARYLTEG 300
SRGSVKDRTQ QGFPTVKLEG HNEPVVLQVF VGNDSGRVKP HGFYQACRVT 350
GRNTTPCKEV DIEGTTVIEV GLDPSNNMTL AVDCVGILKL RNADVEARIG 400
IAGSKKKSTR ARLVFRVNIM RKDGSTLTLQ TPSSPILCTQ PAGVPEILKK 450
SLHSCSVKGE EEVFLIGKNF LKGTKVIFQE NVSDENSWKS EAEIDMELFH 500
QNHLIVKVPP YHDQHITLPV SVGIYVVTNA GRSHDVQPFT YTPDPAAAGA 550
LNVNVKKEIS SPARPCSFEE AMKAMKTTGC NLDKVNIIPN ALMTPLIPSS 600
MIKSEDVTPM EVTAEKRSST IFKTTKSVGS TQQTLENISN IAGNGSFSSP 650
SSSHLPSENE KQQQIQPKAY NPETLTTIQT QDISQPGTFP AVSASSQLPN 700
SDALLQQATQ FQTRETQSRE ILQSDGTVVN LSQLTEASQQ QQQSPLQEQA 750
QTLQQQISSN IFPSPNSVSQ LQNTIQQLQA GSFTGSTASG SSGSVDLVQQ 800
VLEAQQQLSS VLFSAPDGNE NVQEQLSADI FQQVSQIQSG VSPGMFSSTE 850
PTVHTRPDNL LPGRAESVHP QSENTLSNQQ QQQQQQQQVM ESSAAMVMEM 900
QQSICQAAAQ IQSELFPSTA SANGNLQQSP VYQQTSHMMS ALSTNEDMQM 950
QCELFSSPPA VSGNETSTTT TQQVATPGTT MFQTSSSGDG EETGTQAKQI 1000
QNSVFQTMVQ MQHSGDNQPQ VNLFSSTKSM MSVQNSGTQQ QGNGLFQQGN 1050
EMMSLQSGNF LQQSSHSQAQ LFHPQNPIAD AQNLSQETQG SLFHSPNPIV 1100
HSQTSTTSSE QMQPPMFHSQ STIAVLQGSS VPQDQQSTNI FLSQSPMNNL 1150
QTNTVAQEAF FAAPNSISPL QSTSNSEQQA AFQQQAPISH IQTPMLSQEQ 1200
AQPPQQGLFQ PQVALGSLPP NPMPQSQQGT MFQSQHSIVA MQSNSPSQEQ 1250
QQQQQQQQQQ QQQQQQSILF SNQNTMATMA SPKQPPPNMI FNPNQNPMAN 1300
QEQQNQSIFH QQSNMAPMNQ EQQPMQFQSQ STVSSLQNPG PTQSESSQTP 1350
LFHSSPQIQL VQGSPSSQEQ QVTLFLSPAS MSALQTSINQ QDMQQSPLYS 1400
PQNNMPGIQG ATSSPQPQAT LFHNTAGGTM NQLQNSPGSS QQTSGMFLFG 1450
IQNNCSQLLT SGPATLPDQL MAISQPGQPQ NEGQPPVTTL LSQQMPENSP 1500
LASSINTNQN IEKIDLLVSL QNQGNNLTGS F 1531
Length:1,531
Mass (Da):165,763
Last modified:May 1, 1999 - v1
Checksum:iA68C68088DABF69E
GO
Isoform A (identifier: O94916-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Show »
Length:1,455
Mass (Da):157,983
Checksum:i4FA637348EAC0041
GO
Isoform B (identifier: O94916-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Show »
Length:1,484
Mass (Da):160,556
Checksum:iF3E61D1947D310D3
GO
Isoform D (identifier: O94916-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: R → RDSLKLHPSQNFHRAGLLE
     546-546: Missing.

Note: No experimental confirmation available.

Show »
Length:1,548
Mass (Da):167,737
Checksum:i48E5072E004F9C09
GO
Isoform E (identifier: O94916-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: R → RDSLKLHPSQNFHRAGLLE

Show »
Length:1,549
Mass (Da):167,808
Checksum:i12DBBD89C630E445
GO

Sequence cautioni

The sequence CAB09693.1 differs from that shown. Reason: Frameshift at position 1164.
The sequence CAC42765.1 differs from that shown. Reason: Frameshift at position 20.
The sequence BAA74850.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7676Missing in isoform A. VSP_005605Add
BLAST
Alternative sequencei1 – 4747Missing in isoform B. VSP_005606Add
BLAST
Alternative sequencei24 – 241R → RDSLKLHPSQNFHRAGLLE in isoform D and isoform E. VSP_043840
Alternative sequencei546 – 5461Missing in isoform D. VSP_043841

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti666 – 6672QP → HA in AAK91166. 1 Publication
Sequence conflicti666 – 6672QP → HA in CAC42764. 1 Publication
Sequence conflicti1369 – 13691E → D in CAB09693. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF163836 mRNA. Translation: AAD48441.1.
AF089824 mRNA. Translation: AAD18136.1.
AF134870 mRNA. Translation: AAD38360.1.
AF346509 mRNA. Translation: AAK91166.1.
AJ243298 mRNA. Translation: CAC42764.1.
AJ243299 mRNA. Translation: CAC42765.1. Frameshift.
AB020634 mRNA. Translation: BAA74850.2. Different initiation.
AC009032 Genomic DNA. No translation available.
AC012321 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83281.1.
BC131509 mRNA. Translation: AAI31510.1.
BC146765 mRNA. Translation: AAI46766.1.
Z97016 mRNA. Translation: CAB09693.1. Frameshift.
CCDSiCCDS10881.1. [O94916-1]
CCDS10882.1. [O94916-2]
CCDS45518.1. [O94916-5]
CCDS45519.1. [O94916-4]
RefSeqiNP_001106649.1. NM_001113178.2. [O94916-4]
NP_006590.1. NM_006599.3. [O94916-1]
NP_619727.2. NM_138713.3. [O94916-5]
NP_619728.2. NM_138714.3. [O94916-2]
NP_775321.1. NM_173214.2. [O94916-2]
NP_775322.1. NM_173215.2. [O94916-2]
XP_006721188.1. XM_006721125.1. [O94916-3]
UniGeneiHs.371987.

Genome annotation databases

EnsembliENST00000349945; ENSP00000338806; ENSG00000102908. [O94916-2]
ENST00000354436; ENSP00000346420; ENSG00000102908. [O94916-1]
ENST00000393742; ENSP00000377343; ENSG00000102908. [O94916-2]
ENST00000432919; ENSP00000396538; ENSG00000102908. [O94916-5]
ENST00000566899; ENSP00000455628; ENSG00000102908. [O94916-2]
ENST00000567239; ENSP00000457593; ENSG00000102908. [O94916-4]
GeneIDi10725.
KEGGihsa:10725.
UCSCiuc002exi.3. human. [O94916-1]
uc002exn.2. human. [O94916-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF163836 mRNA. Translation: AAD48441.1 .
AF089824 mRNA. Translation: AAD18136.1 .
AF134870 mRNA. Translation: AAD38360.1 .
AF346509 mRNA. Translation: AAK91166.1 .
AJ243298 mRNA. Translation: CAC42764.1 .
AJ243299 mRNA. Translation: CAC42765.1 . Frameshift.
AB020634 mRNA. Translation: BAA74850.2 . Different initiation.
AC009032 Genomic DNA. No translation available.
AC012321 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83281.1 .
BC131509 mRNA. Translation: AAI31510.1 .
BC146765 mRNA. Translation: AAI46766.1 .
Z97016 mRNA. Translation: CAB09693.1 . Frameshift.
CCDSi CCDS10881.1. [O94916-1 ]
CCDS10882.1. [O94916-2 ]
CCDS45518.1. [O94916-5 ]
CCDS45519.1. [O94916-4 ]
RefSeqi NP_001106649.1. NM_001113178.2. [O94916-4 ]
NP_006590.1. NM_006599.3. [O94916-1 ]
NP_619727.2. NM_138713.3. [O94916-5 ]
NP_619728.2. NM_138714.3. [O94916-2 ]
NP_775321.1. NM_173214.2. [O94916-2 ]
NP_775322.1. NM_173215.2. [O94916-2 ]
XP_006721188.1. XM_006721125.1. [O94916-3 ]
UniGenei Hs.371987.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IMH X-ray 2.86 C/D 264-544 [» ]
ProteinModelPortali O94916.
SMRi O94916. Positions 264-544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115949. 3 interactions.
DIPi DIP-58524N.
IntActi O94916. 5 interactions.
STRINGi 9606.ENSP00000396538.

PTM databases

PhosphoSitei O94916.

Proteomic databases

MaxQBi O94916.
PaxDbi O94916.
PRIDEi O94916.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000349945 ; ENSP00000338806 ; ENSG00000102908 . [O94916-2 ]
ENST00000354436 ; ENSP00000346420 ; ENSG00000102908 . [O94916-1 ]
ENST00000393742 ; ENSP00000377343 ; ENSG00000102908 . [O94916-2 ]
ENST00000432919 ; ENSP00000396538 ; ENSG00000102908 . [O94916-5 ]
ENST00000566899 ; ENSP00000455628 ; ENSG00000102908 . [O94916-2 ]
ENST00000567239 ; ENSP00000457593 ; ENSG00000102908 . [O94916-4 ]
GeneIDi 10725.
KEGGi hsa:10725.
UCSCi uc002exi.3. human. [O94916-1 ]
uc002exn.2. human. [O94916-4 ]

Organism-specific databases

CTDi 10725.
GeneCardsi GC16P069599.
HGNCi HGNC:7774. NFAT5.
MIMi 604708. gene.
neXtProti NX_O94916.
PharmGKBi PA31581.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG85658.
HOGENOMi HOG000236245.
HOVERGENi HBG052612.
InParanoidi O94916.
KOi K17335.
OMAi NNMTLAV.
OrthoDBi EOG79PJND.
PhylomeDBi O94916.
TreeFami TF326480.

Miscellaneous databases

ChiTaRSi NFAT5. human.
EvolutionaryTracei O94916.
GeneWikii NFAT5.
GenomeRNAii 10725.
NextBioi 40713.
PROi O94916.
SOURCEi Search...

Gene expression databases

ArrayExpressi O94916.
Bgeei O94916.
CleanExi HS_NFAT5.
Genevestigatori O94916.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR008366. NFAT.
IPR015646. NFAT5.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
PANTHERi PTHR12533. PTHR12533. 1 hit.
PTHR12533:SF7. PTHR12533:SF7. 1 hit.
Pfami PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR01789. NUCFACTORATC.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Brain.
  2. "Tonicity-responsive enhancer binding protein, a rel-like protein that stimulates transcription in response to hypertonicity."
    Miyakawa H., Woo S.K., Dahl S.C., Handler J.S., Kwon H.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:2538-2542(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  3. "NFAT5, a constitutively nuclear NFAT protein that does not cooperate with Fos and Jun."
    Lopez-Rodriguez C., Aramburu J., Rakeman A.S., Rao A.
    Proc. Natl. Acad. Sci. U.S.A. 96:7214-7219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Brain.
  4. "Genomic organization of the human NFAT5 gene: exon-intron structure of the 14-kb transcript and CpG-island analysis of the promoter region."
    Dalski A., Schwinger E., Zuhlke C.
    Cytogenet. Cell Genet. 93:239-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E).
  5. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Tissue: Brain.
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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] (ISOFORMS C AND D).
  9. "Isolation and characterization of novel CAG repeat containing genes expressed in human brain."
    Zuehlke C., Kiehl R., Johannsmeyer A., Grzeschik K.H., Schwinger E.
    DNA Seq. 10:1-6(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 675-1531.
    Tissue: Brain.
  10. "Mouse TonEBP-NFAT5: expression in early development and alternative splicing."
    Maouyo D., Kim J.Y., Lee S.D., Wu Y., Woo S.K., Kwon H.M.
    Am. J. Physiol. 282:F802-F809(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "High NaCl-induced activation of CDK5 increases phosphorylation of the osmoprotective transcription factor TonEBP/OREBP at threonine 135, which contributes to its rapid nuclear localization."
    Gallazzini M., Heussler G.E., Kunin M., Izumi Y., Burg M.B., Ferraris J.D.
    Mol. Biol. Cell 22:703-714(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-120; SER-134; THR-135 AND SER-155, MUTAGENESIS OF SER-120; SER-134; THR-135 AND SER-155.
  13. "Structure of a TonEBP-DNA complex reveals DNA encircled by a transcription factor."
    Stroud J.C., Lopez-Rodriguez C., Rao A., Chen L.
    Nat. Struct. Biol. 9:90-94(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 264-544 IN COMPLEX WITH DNA, SUBUNIT.

Entry informationi

Entry nameiNFAT5_HUMAN
AccessioniPrimary (citable) accession number: O94916
Secondary accession number(s): A2RRB4
, A6H8V5, E9PHR7, O95693, Q7LA65, Q969Q8, Q96QH3, Q9UN18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 148 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 16
    Human chromosome 16: 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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