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O75398

- DEAF1_HUMAN

UniProt

O75398 - DEAF1_HUMAN

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Protein
Deformed epidermal autoregulatory factor 1 homolog
Gene
DEAF1, SPN, ZMYND5
Organism
Homo sapiens (Human)
Status
Reviewed - 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. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri504 – 54037MYND-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. embryonic skeletal system development Source: UniProtKB
  3. germ cell development Source: ProtInc
  4. neural tube closure Source: UniProtKB
  5. regulation of mammary gland epithelial cell proliferation Source: UniProtKB
  6. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. transcription from RNA polymerase II promoter Source: ProtInc
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
Suppressin
Zinc finger MYND domain-containing protein 5
Gene namesi
Name:DEAF1
Synonyms:SPN, ZMYND5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14677. DEAF1.

Subcellular locationi

Isoform 1 : Nucleus. Cytoplasm
Note: Cytoplasmic in non-mucinous colorectal carcinoma. When expressed alone, localized almost exclusively in the nucleus but, when expressed with isoform 4, nuclear expression decreases to 32% and cytoplasmic expression increases by 270%.2 Publications
Isoform 2 : Secreted
Note: Secreted in some cell types.2 Publications
Isoform 3 : Secreted
Note: Secreted in some cell types.2 Publications
Isoform 4 : Cytoplasm. Nucleus
Note: When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular region Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
  4. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi215 – 2151Y → Q: Reduces transcription activation. 1 Publication
Mutagenesisi226 – 2261R → A: Reduces transcription activation. 1 Publication
Mutagenesisi246 – 2461R → A: Reduces transcription activation. 1 Publication
Mutagenesisi250 – 2501K → A: Abolishes DNA-binding. 1 Publication
Mutagenesisi252 – 2521W → Q: Abolishes DNA-binding. 1 Publication
Mutagenesisi253 – 2531K → A: Abolishes DNA-binding. 1 Publication
Mutagenesisi302 – 3021R → T: Abolishes nuclear localization. 1 Publication
Mutagenesisi304 – 3041K → T: Abolishes nuclear localization. 1 Publication
Mutagenesisi538 – 5381H → S: No effect on folding of MYND-type zinc finger. 1 Publication

Organism-specific databases

PharmGKBiPA27234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Deformed epidermal autoregulatory factor 1 homolog
PRO_0000074084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei448 – 4481Phosphoserine By similarity

Post-translational modificationi

May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75398.
PaxDbiO75398.
PRIDEiO75398.

PTM databases

PhosphoSiteiO75398.

Expressioni

Tissue specificityi

Expressed in various tissues and cells such as in peripheral mononuclear cells and hormone-secreting pituitary cells. Expression in pancreatic lymph nodes of patients with type 1 diabetes is 20 times higher than in healthy controls.1 Publication

Gene expression databases

ArrayExpressiO75398.
BgeeiO75398.
CleanExiHS_SPN.
GenevestigatoriO75398.

Organism-specific databases

HPAiHPA030302.

Interactioni

Subunit structurei

Homodimer. Isoform 1 and isoform 4 may form a heterodimer. Interacts with LMO2 and CLIM2 By similarity. Interacts with LMO4; LMO4 blocks export from nucleus By similarity. May interact with the corepressors NCOR1 and NCRO2. Identified in a complex with the XRCC5 and XRCC6 heterodimer. Interacts (via the SAND domain) with the DNA-PK complex subunit XRCC6; the interaction is direct and may be inhibited by DNA-binding.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDKN2AP427712EBI-718185,EBI-375053
GSK3AP498402EBI-718185,EBI-1044067
GSK3BP498412EBI-718185,EBI-373586

Protein-protein interaction databases

BioGridi115777. 21 interactions.
IntActiO75398. 18 interactions.
MINTiMINT-1420286.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi505 – 5106
Beta strandi512 – 5143
Turni516 – 5183
Beta strandi520 – 5256
Helixi526 – 5327
Turni533 – 5353
Helixi536 – 5383
Turni539 – 5413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JW6NMR-A496-544[»]
4A24NMR-A501-544[»]
ProteinModelPortaliO75398.
SMRiO75398. Positions 201-272, 501-544.

Miscellaneous databases

EvolutionaryTraceiO75398.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini193 – 27381SAND
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni403 – 47876Interaction with LMO4 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 31616Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 122121Ala-rich
Add
BLAST
Compositional biasi383 – 43957Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 1 SAND domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG291744.
HOVERGENiHBG051335.
InParanoidiO75398.
OMAiQSCVNCG.
OrthoDBiEOG7VQJF5.
PhylomeDBiO75398.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75398-1) [UniParc]FASTAAdd to Basket

Also known as: Hu-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

MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAGGEAEEP VLSRDEDSEE    50
DADSEAERET PRVTAVAVMA AEPGHMDMGA EALPGPDEAA AAAAFAEVTT 100
VTVANVGAAA DNVFTTSVAN AASISGHVLS GRTALQIGDS LNTEKATLIV 150
VHTDGSIVET TGLKGPAAPL TPGPQSPPTP LAPGQEKGGT KYNWDPSVYD 200
SELPVRCRNI SGTLYKNRLG SGGRGRCIKQ GENWYSPTEF EAMAGRASSK 250
DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDDMTL SGPVRLFVPY 300
KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD 350
RASTVEATAV ISESPAQGDV FAGATVQEAS VQPPCRASHP EPHYPGYQDS 400
CQIAPFPEAA LPTSHPKIVL TSLPALAVPP PTPTKAAPPA LVNGLELSEP 450
RSWLYLEEMV NSLLNTAQQL KTLFEQAKHA STYREAATNQ AKIHADAERK 500
EQSCVNCGRE AMSECTGCHK VNYCSTFCQR KDWKDHQHIC GQSAAVTVQA 550
DEVHVAESVM EKVTV 565
Length:565
Mass (Da):59,327
Last modified:November 1, 1998 - v1
Checksum:i3BDFEDBF6AD4BDDE
GO
Isoform 2 (identifier: O75398-3) [UniParc]FASTAAdd to Basket

Also known as: NUDR8

The sequence of this isoform differs from the canonical sequence as follows:
     15-29: EAAAVAAAAAVAAAA → D

Show »
Length:551
Mass (Da):58,262
Checksum:i9ABE2A02D3AA8DA1
GO
Isoform 3 (identifier: O75398-4) [UniParc]FASTAAdd to Basket

Also known as: Suppressin

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Note: Has no predictable signal peptide.

Show »
Length:497
Mass (Da):52,717
Checksum:i4EC4279532D8A4DE
GO
Isoform 4 (identifier: O75398-5) [UniParc]FASTAAdd to Basket

Also known as: Hu-DF1-VAR

The sequence of this isoform differs from the canonical sequence as follows:
     223-333: GRGRCIKQGE...LLPATAATTF → WDLKPSRCLLHLCCLLRRHDLI
     501-501: E → EVIHPPRLPKVLGLQ

Show »
Length:490
Mass (Da):51,277
Checksum:iAD1869382C23FF2A
GO

Sequence cautioni

The sequence AAC25718.1 differs from that shown. Reason: Several sequencing errors.
The sequence AAC25719.1 differs from that shown. Reason: Frameshift at positions 222 and 236.
Isoform 3 : The sequence AAC25718.1 differs from that shown. Reason: Frameshift at positions 222 and 236.
Isoform 3 : The sequence AAC25719.1 differs from that shown. Reason: Frameshift at positions 222 and 236.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861E → V in a primary colorectal cancer. 1 Publication
VAR_013725
Natural varianti191 – 1911K → I in a primary colorectal cancer. 1 Publication
VAR_013726
Natural varianti191 – 1911K → N in a primary colorectal cancer. 1 Publication
VAR_013727
Natural varianti199 – 2024YDSE → CDND in a primary colorectal cancer.
VAR_013728
Natural varianti202 – 2021E → D in a primary colorectal cancer. 1 Publication
VAR_013729
Natural varianti218 – 2181R → K in a primary colorectal cancer. 1 Publication
VAR_013730
Natural varianti228 – 2281I → S De novo variant found in a patient with mental retardation. 1 Publication
VAR_065089
Natural varianti350 – 3523DRA → GQT in a primary colorectal cancer.
VAR_013731
Natural varianti356 – 3561E → H in a primary colorectal cancer; requires 2 nucleotide substitutions. 1 Publication
VAR_013732
Natural varianti364 – 3641S → N in a primary colorectal cancer. 1 Publication
VAR_013733
Natural varianti367 – 3671Q → H in a primary colorectal cancer. 1 Publication
VAR_013734
Natural varianti370 – 3701V → L in a primary colorectal cancer. 1 Publication
VAR_013735
Natural varianti397 – 3971Y → F in a primary colorectal cancer. 1 Publication
VAR_013736
Natural varianti442 – 4421V → A in a primary colorectal cancer. 1 Publication
VAR_013737
Natural varianti449 – 4491E → K in a primary colorectal cancer. 1 Publication
VAR_013738
Natural varianti451 – 4522RS → GI in a primary colorectal cancer.
VAR_013739
Natural varianti468 – 4681Q → H in a primary colorectal cancer. 1 Publication
VAR_013740
Natural varianti479 – 4791H → L in a primary colorectal cancer. 1 Publication
VAR_013741
Natural varianti498 – 4981E → K in a primary colorectal cancer. 1 Publication
VAR_013742
Natural varianti526 – 5261T → N in a primary colorectal cancer. 1 Publication
VAR_013743
Natural varianti530 – 5301R → L in a primary colorectal cancer. 1 Publication
VAR_013744
Natural varianti537 – 5382QH → HL in a primary colorectal cancer.
VAR_013745
Natural varianti542 – 5421Q → H in a primary colorectal cancer. 1 Publication
VAR_013746
Natural varianti545 – 5451A → G in a primary colorectal cancer. 1 Publication
Corresponds to variant rs34114147 [ dbSNP | Ensembl ].
VAR_013747
Natural varianti545 – 5451A → V in a primary colorectal cancer. 1 Publication
VAR_013748

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 3.
VSP_005966Add
BLAST
Alternative sequencei15 – 2915EAAAV…VAAAA → D in isoform 2.
VSP_005967Add
BLAST
Alternative sequencei223 – 333111GRGRC…AATTF → WDLKPSRCLLHLCCLLRRHD LI in isoform 4.
VSP_038701Add
BLAST
Alternative sequencei501 – 5011E → EVIHPPRLPKVLGLQ in isoform 4.
VSP_038702

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → E in ACU88060. 1 Publication
Sequence conflicti72 – 721E → D in AAB62704. 1 Publication
Sequence conflicti166 – 1661P → Q in ACU88060. 1 Publication
Sequence conflicti247 – 2471A → T in AAB62704. 1 Publication
Sequence conflicti294 – 2941V → L in AAB62704. 1 Publication
Sequence conflicti399 – 3991D → G in ACU88060. 1 Publication
Sequence conflicti522 – 5221N → K in AAB62704. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF049459 mRNA. Translation: AAC79676.1.
AF049460 mRNA. Translation: AAC79677.1.
AF068893 mRNA. Translation: AAC25715.1.
AF068894 mRNA. Translation: AAC25716.1.
AF068895 mRNA. Translation: AAC25717.1.
AF068896 mRNA. Translation: AAC25718.1. Sequence problems.
AF068897 mRNA. Translation: AAC25719.1. Frameshift.
FJ985253 mRNA. Translation: ACU88060.1.
AF007165 mRNA. Translation: AAB62704.1.
AK291383 mRNA. Translation: BAF84072.1.
AK289873 mRNA. Translation: BAF82562.1.
BC053322 mRNA. Translation: AAH53322.1.
CCDSiCCDS31327.1. [O75398-1]
RefSeqiNP_066288.2. NM_021008.3. [O75398-1]
UniGeneiHs.243994.

Genome annotation databases

EnsembliENST00000338675; ENSP00000341902; ENSG00000177030. [O75398-5]
ENST00000382409; ENSP00000371846; ENSG00000177030. [O75398-1]
GeneIDi10522.
KEGGihsa:10522.
UCSCiuc001lqq.1. human. [O75398-1]
uc021qbn.1. human. [O75398-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF049459 mRNA. Translation: AAC79676.1 .
AF049460 mRNA. Translation: AAC79677.1 .
AF068893 mRNA. Translation: AAC25715.1 .
AF068894 mRNA. Translation: AAC25716.1 .
AF068895 mRNA. Translation: AAC25717.1 .
AF068896 mRNA. Translation: AAC25718.1 . Sequence problems.
AF068897 mRNA. Translation: AAC25719.1 . Frameshift.
FJ985253 mRNA. Translation: ACU88060.1 .
AF007165 mRNA. Translation: AAB62704.1 .
AK291383 mRNA. Translation: BAF84072.1 .
AK289873 mRNA. Translation: BAF82562.1 .
BC053322 mRNA. Translation: AAH53322.1 .
CCDSi CCDS31327.1. [O75398-1 ]
RefSeqi NP_066288.2. NM_021008.3. [O75398-1 ]
UniGenei Hs.243994.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JW6 NMR - A 496-544 [» ]
4A24 NMR - A 501-544 [» ]
ProteinModelPortali O75398.
SMRi O75398. Positions 201-272, 501-544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115777. 21 interactions.
IntActi O75398. 18 interactions.
MINTi MINT-1420286.

PTM databases

PhosphoSitei O75398.

Proteomic databases

MaxQBi O75398.
PaxDbi O75398.
PRIDEi O75398.

Protocols and materials databases

DNASUi 10522.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338675 ; ENSP00000341902 ; ENSG00000177030 . [O75398-5 ]
ENST00000382409 ; ENSP00000371846 ; ENSG00000177030 . [O75398-1 ]
GeneIDi 10522.
KEGGi hsa:10522.
UCSCi uc001lqq.1. human. [O75398-1 ]
uc021qbn.1. human. [O75398-5 ]

Organism-specific databases

CTDi 10522.
GeneCardsi GC11M000644.
H-InvDB HIX0026125.
HGNCi HGNC:14677. DEAF1.
HPAi HPA030302.
MIMi 602635. gene.
neXtProti NX_O75398.
PharmGKBi PA27234.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291744.
HOVERGENi HBG051335.
InParanoidi O75398.
OMAi QSCVNCG.
OrthoDBi EOG7VQJF5.
PhylomeDBi O75398.
TreeFami TF325664.

Miscellaneous databases

EvolutionaryTracei O75398.
GenomeRNAii 10522.
NextBioi 39912.
PROi O75398.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75398.
Bgeei O75398.
CleanExi HS_SPN.
Genevestigatori O75398.

Family and domain databases

Gene3Di 3.10.390.10. 1 hit.
InterProi IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR024119. TF_DEAF-1.
IPR002893. Znf_MYND.
[Graphical view ]
PANTHERi PTHR10237. PTHR10237. 1 hit.
Pfami PF01342. SAND. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view ]
SMARTi SM00258. SAND. 1 hit.
[Graphical view ]
SUPFAMi SSF63763. SSF63763. 1 hit.
PROSITEi PS50864. SAND. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a nuclear deformed epidermal autoregulatory factor-1 (DEAF-1)-related (NUDR) transcriptional regulator protein."
    Huggenvik J.I., Michelson R.J., Collard M.W., Ziemba A.J., Gurley P., Mowen K.A.
    Mol. Endocrinol. 12:1619-1639(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF ARG-302 AND LYS-304.
    Tissue: Choriocarcinoma.
  2. "Altered subcellular localization of suppressin, a novel inhibitor of cell-cycle entry, is an independent prognostic factor in colorectal adenocarcinomas."
    Manne U., Gary B.D., Oelschlager D.K., Weiss H.L., Frost A.R., Grizzle W.E.
    Clin. Cancer Res. 7:3495-3503(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANTS VAL-186; ASN-191; ILE-191; 199-CYS-ASP-ASN-ASP-202; ASP-202; LYS-218; 350-GLY-GLN-THR-352; HIS-356; ASN-364; HIS-367; LEU-370; PHE-397; ALA-442; LYS-449; 451-GLY-ILE-452; HIS-468; LEU-479; LYS-498; ASN-526; LEU-530; 537-HIS-LEU-538; HIS-542; GLY-545 AND VAL-545, ROLE IN NEOPLASIA.
    Tissue: Colon and Colon adenocarcinoma.
  3. "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] (ISOFORM 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Pancreas.
  4. "Cloning and sequence analysis of the cDNA for human suppressin (spn)."
    LeBoeuf R.D., Blalock J.E., Tauber J.D.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Mammary gland.
  5. "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 3).
    Tissue: Brain and Caudate nucleus.
  6. "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] (ISOFORM 1).
    Tissue: Ovary.
  7. "Nuclear DEAF-1-related (NUDR) protein contains a novel DNA binding domain and represses transcription of the heterogeneous nuclear ribonucleoprotein A2/B1 promoter."
    Michelson R.J., Collard M.W., Ziemba A.J., Persinger J., Bartholomew B., Huggenvik J.I.
    J. Biol. Chem. 274:30510-30519(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation."
    Bottomley M.J., Collard M.W., Huggenvik J.I., Liu Z., Gibson T.J., Sattler M.
    Nat. Struct. Biol. 8:626-633(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF SAND DOMAIN, MUTAGENESIS OF TYR-215; ARG-226; ARG-246; LYS-250; TRP-252 AND LYS-253.
  9. "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.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex."
    Jensik P.J., Huggenvik J.I., Collard M.W.
    PLoS ONE 7:E33404-E33404(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH XRCC5 AND XRCC6, SUBCELLULAR LOCATION, PHOSPHORYLATION BY DNA-PK COMPLEX.
  12. Cited for: STRUCTURE BY NMR OF 496-544 IN COMPLEX WITH ZINC IONS.
  13. "Retraction notice to 'Structure and functional analysis of the MYND domain' [J. Mol. Biol. (2006) 358, 498-508]."
    Spadaccini R., Perrin H., Bottomley M.J., Ansieau S., Sattler M.
    J. Mol. Biol. 376:1523-1523(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: RETRACTION: STRUCTURE BY NMR OF 496-544 IN COMPLEX WITH ZINC IONS.
  14. Cited for: STRUCTURE BY NMR OF 501-544 IN COMPLEX WITH ZINC IONS, SUBUNIT, INTERACTION WITH NCOR1 AND NCOR2, MUTAGENESIS OF HIS-538.
  15. Cited for: VARIANT SER-228.

Entry informationi

Entry nameiDEAF1_HUMAN
AccessioniPrimary (citable) accession number: O75398
Secondary accession number(s): A8K1F8
, A8K5R8, C7T5V5, O15152, O75399, O75510, O75511, O75512, O75513, Q9UET1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: November 1, 1998
Last modified: September 3, 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

Miscellaneous

Defective DEAF1 could confer a growth advantage to the mutated cells influencing the development and progression of neoplasia, e.g. in the case of colorectal carcinomas. Subcellular location in colorectal carcinomas (cytoplasmic or nuclear) is a prognostic factor that identifies a subgroup of patients with reduced survival. In addition, changes in the subcellular location correlates with the proliferative status of the cells.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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