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Protein

Deformed epidermal autoregulatory factor 1 homolog

Gene

Deaf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction (By similarity). Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 2. Isoform 2 may inhibit transcriptional activity of isoform 1 by interacting with it and retaining it in the cytoplasm. Transcriptional activator of EIF4G3 (By similarity). May also involved in behavior (PubMed:24726472).By similarity4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri505 – 54137MYND-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • behavioral fear response Source: UniProtKB
  • embryonic skeletal system development Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: MGI
  • neural tube closure Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: MGI
  • regulation of mammary gland epithelial cell proliferation Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • transcription from RNA polymerase II promoter Source: MGI
  • visual learning Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Deformed epidermal autoregulatory factor 1 homolog
Alternative name(s):
Nuclear DEAF-1-related transcriptional regulator
Short name:
NUDR
Gene namesi
Name:Deaf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1858496. Deaf1.

Subcellular locationi

Isoform 1 :
Isoform 2 :
  • Cytoplasm
  • Nucleus

  • Note: Displays some nuclear localization when expressed with isoform 1, suggesting that it may heterodimerize with isoform 1 and shuttle to the nucleus using the nuclear localization signal of isoform 1.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Exencephaly and skeletal abnormalities in the rib cage and cervical vertebrae but no presphenoid bone or cranial nerve defects. DEAF1 homozygous mice neonates die 100% of the time and DEAF1 heterozygous mice survived in a 2:1 ratio.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi305 – 3051K → T: Abolishes nuclear localization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Deformed epidermal autoregulatory factor 1 homologPRO_0000074085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721PhosphothreonineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei180 – 1801PhosphothreonineCombined sources
Modified residuei444 – 4441PhosphoserineBy similarity
Modified residuei449 – 4491PhosphoserineBy similarity

Post-translational modificationi

May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z1T5.
PaxDbiQ9Z1T5.
PRIDEiQ9Z1T5.

PTM databases

PhosphoSiteiQ9Z1T5.

Expressioni

Tissue specificityi

Ubiquitously expressed during embryogenesis, with higher expression in regions of the central nervous system, dorsal root ganglia, submandibular gland, epidermis and breast. In 12-week-old NOD mice, expression of isoform 2 is sevenfold higher in lymph node stromal elements than in T-cells and tenfold higher than in B-cells.1 Publication

Developmental stagei

Expressed at all stages of mammary gland development with slightly higher levels observed during pregnancy and lactation. At 4 weeks, expression levels of isoform 1 and isoform 2 do not differ in pancreatic lymph nodes of nonobese diabetic (NOD) mice compared to NOD.B10 mice which do not develop diabetes. However, at 12 weeks, expression of isoform 1 is down-regulated while expression of isoform 2 is up-regulated in NOD mice but not in NOD.B10. There is no difference in expression levels at 12 weeks in spleen.2 Publications

Gene expression databases

BgeeiQ9Z1T5.
GenevisibleiQ9Z1T5. MM.

Interactioni

Subunit structurei

Homodimer (By similarity). Isoform 1 and isoform 2 may form a heterodimer. May interact with the corepressors NCOR1 and NCRO2 (By similarity). Identified in a complex with XRCC5 and XRCC6. Interacts (via the SAND domain) with the DNA-PK complex subunit XRCC6; the interaction is direct with XRCC6 and may be inhibited by DNA-binding (By similarity). Interacts with LMO4; LMO4 blocks export from nucleus. Interacts with LMO2 and CLIM2.By similarity2 Publications

Protein-protein interaction databases

BioGridi207558. 2 interactions.
IntActiQ9Z1T5. 2 interactions.
STRINGi10090.ENSMUSP00000079395.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MBVNMR-A404-418[»]
ProteinModelPortaliQ9Z1T5.
SMRiQ9Z1T5. Positions 202-273, 502-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 27481SANDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni404 – 47976Interaction with LMO4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi300 – 3067Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 123122Ala-richAdd
BLAST
Compositional biasi383 – 44058Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
Contains 1 SAND domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri505 – 54137MYND-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00390000013479.
HOGENOMiHOG000063682.
HOVERGENiHBG051335.
InParanoidiQ9Z1T5.
OMAiQSCVNCG.
OrthoDBiEOG7VQJF5.
PhylomeDBiQ9Z1T5.
TreeFamiTF325664.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR024119. TF_DEAF-1.
IPR002893. Znf_MYND.
[Graphical view]
PANTHERiPTHR10237. PTHR10237. 1 hit.
PfamiPF01342. SAND. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z1T5-1) [UniParc]FASTAAdd to basket

Also known as: DF1

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
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAESEAEEP VLSRDEDSEE
60 70 80 90 100
DADSEAERET RRVTAVAVMA AESGHMDMGT EALPSPDEAA AAAAAFAEVT
110 120 130 140 150
TVTVANVGSS ADNVFTTSVA NAASISGHVL SGRTALQIGD SLNTEKATLI
160 170 180 190 200
VVHTDGSIVE TTGLKGPAAP LTPGPQSPPT PLAPGQEKGG TKYNWDPSVY
210 220 230 240 250
DSELPVRCRN ISGTLYKSRL GSGGRGRCIK QGENWYSPTE FEAMAGRASS
260 270 280 290 300
KDWKRSIRYA GRPLQCLIQD GILNPHAASC TCAACCDDMT LSGPVRLFVP
310 320 330 340 350
YKRRKKENEL PTTPVKKDSP KNITLLPATA ATTFTVTPSG QITTSGALTF
360 370 380 390 400
DRASTVEATA VISESPAQGD VFAGATVQEA GVQPPCRVGH PEPHYPGYQD
410 420 430 440 450
SCQIAPFPEA ALPTSHPKIV LTSLPALAVP PSTPTKAVSP TVVSGLEMSE
460 470 480 490 500
HRSWLYLEEM VNSLLNTAQQ LKTLFEQAKQ ASSCREAAVT QARMQVDTER
510 520 530 540 550
KEQSCVNCGR EAMSECTGCH KVNYCSTFCQ RKDWKDHQHV CGQSASVTVQ
560
ADDVHVEESV IEKVAV
Length:566
Mass (Da):59,633
Last modified:May 1, 1999 - v1
Checksum:i6CC4B10E914EFD83
GO
Isoform 2 (identifier: Q9Z1T5-2) [UniParc]FASTAAdd to basket

Also known as: DF1-VAR1

The sequence of this isoform differs from the canonical sequence as follows:
     19-32: Missing.
     292-308: SGPVRLFVPYKRRKKEN → AGVSLFSFPWPTSLLRI
     309-566: Missing.

Show »
Length:294
Mass (Da):30,737
Checksum:iB561AF0CDDC6A076
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei19 – 3214Missing in isoform 2. 1 PublicationVSP_038703Add
BLAST
Alternative sequencei292 – 30817SGPVR…RKKEN → AGVSLFSFPWPTSLLRI in isoform 2. 1 PublicationVSP_038704Add
BLAST
Alternative sequencei309 – 566258Missing in isoform 2. 1 PublicationVSP_038705Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102818 mRNA. Translation: AAC98511.1.
FJ377318 mRNA. Translation: ACN61629.1.
FJ377319 mRNA. Translation: ACN61630.1.
AK146546 mRNA. Translation: BAE27251.1.
CH466531 Genomic DNA. Translation: EDL18044.1.
CCDSiCCDS40185.1. [Q9Z1T5-1]
RefSeqiNP_058570.1. NM_016874.3. [Q9Z1T5-1]
UniGeneiMm.28392.

Genome annotation databases

EnsembliENSMUST00000080553; ENSMUSP00000079395; ENSMUSG00000058886. [Q9Z1T5-1]
GeneIDi54006.
KEGGimmu:54006.
UCSCiuc009kkn.2. mouse. [Q9Z1T5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF102818 mRNA. Translation: AAC98511.1.
FJ377318 mRNA. Translation: ACN61629.1.
FJ377319 mRNA. Translation: ACN61630.1.
AK146546 mRNA. Translation: BAE27251.1.
CH466531 Genomic DNA. Translation: EDL18044.1.
CCDSiCCDS40185.1. [Q9Z1T5-1]
RefSeqiNP_058570.1. NM_016874.3. [Q9Z1T5-1]
UniGeneiMm.28392.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MBVNMR-A404-418[»]
ProteinModelPortaliQ9Z1T5.
SMRiQ9Z1T5. Positions 202-273, 502-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207558. 2 interactions.
IntActiQ9Z1T5. 2 interactions.
STRINGi10090.ENSMUSP00000079395.

PTM databases

PhosphoSiteiQ9Z1T5.

Proteomic databases

MaxQBiQ9Z1T5.
PaxDbiQ9Z1T5.
PRIDEiQ9Z1T5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080553; ENSMUSP00000079395; ENSMUSG00000058886. [Q9Z1T5-1]
GeneIDi54006.
KEGGimmu:54006.
UCSCiuc009kkn.2. mouse. [Q9Z1T5-1]

Organism-specific databases

CTDi10522.
MGIiMGI:1858496. Deaf1.

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00390000013479.
HOGENOMiHOG000063682.
HOVERGENiHBG051335.
InParanoidiQ9Z1T5.
OMAiQSCVNCG.
OrthoDBiEOG7VQJF5.
PhylomeDBiQ9Z1T5.
TreeFamiTF325664.

Miscellaneous databases

ChiTaRSiDeaf1. mouse.
NextBioi310897.
PROiQ9Z1T5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1T5.
GenevisibleiQ9Z1T5. MM.

Family and domain databases

Gene3Di3.10.390.10. 1 hit.
InterProiIPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR024119. TF_DEAF-1.
IPR002893. Znf_MYND.
[Graphical view]
PANTHERiPTHR10237. PTHR10237. 1 hit.
PfamiPF01342. SAND. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTiSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMiSSF63763. SSF63763. 1 hit.
PROSITEiPS50864. SAND. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain factor, LMO-4, and CLIM coregulators."
    Sugihara T.M., Bach I., Kioussi C., Rosenfeld M.G., Andersen B.
    Proc. Natl. Acad. Sci. U.S.A. 95:15418-15423(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLIM2; LMO2 AND LMO4, TISSUE SPECIFICITY.
    Tissue: Pituitary and Skin.
  2. "Deaf1 isoforms control the expression of genes encoding peripheral tissue antigens in the pancreatic lymph nodes during type 1 diabetes."
    Yip L., Su L., Sheng D., Chang P., Atkinson M., Czesak M., Albert P.R., Collier A.R., Turley S.J., Fathman C.G., Creusot R.J.
    Nat. Immunol. 10:1026-1033(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Strain: NOD.
    Tissue: Pancreas.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Defective neural tube closure and anteroposterior patterning in mice lacking the LIM protein LMO4 or its interacting partner Deaf-1."
    Hahm K., Sum E.Y., Fujiwara Y., Lindeman G.J., Visvader J.E., Orkin S.H.
    Mol. Cell. Biol. 24:2074-2082(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Deaf-1 regulates epithelial cell proliferation and side-branching in the mammary gland."
    Barker H.E., Smyth G.K., Wettenhall J., Ward T.A., Bath M.L., Lindeman G.J., Visvader J.E.
    BMC Dev. Biol. 8:94-94(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172; SER-177 AND THR-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung and Spleen.
  8. "Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4."
    Cubeddu L., Joseph S., Richard D.J., Matthews J.M.
    PLoS ONE 7:E39218-E39218(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LMO4, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-305.
  9. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDEAF1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1T5
Secondary accession number(s): C7SHZ9, Q3UJA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.