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O75398 (DEAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DEAF1
Synonyms:SPN, ZMYND5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.7 Ref.8 Ref.9

Subunit structure

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. Ref.11 Ref.14

Subcellular location

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%. Ref.3 Ref.11

Isoform 2: Secreted. Note: Secreted in some cell types. Ref.3 Ref.11

Isoform 3: Secreted. Note: Secreted in some cell types. Ref.3 Ref.11

Isoform 4: Cytoplasm. Nucleus. Note: When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced. Ref.3 Ref.11

Tissue specificity

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. Ref.3

Post-translational modification

May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro). Ref.11

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.

Sequence similarities

Contains 1 MYND-type zinc finger.

Contains 1 SAND domain.

Caution

This protein was first known as suppressin (characterized in bovine neuroendocrine and immune cells). However, according to Ref.1, it is uncertain whether it corresponds really to the suppressin also described in Ref.4. DEAF1 has been described as a nuclear dimeric protein and suppressin as a secreted monomeric protein.

Sequence caution

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.

Ontologies

Keywords
   Biological processNeurogenesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.1. Source: ProtInc

embryonic skeletal system development

Inferred from sequence or structural similarity. Source: UniProtKB

germ cell development

Traceable author statement Ref.1. Source: ProtInc

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mammary gland epithelial cell proliferation

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.3. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20368287PubMed 21988832. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75398-1)

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.
Isoform 2 (identifier: O75398-3)

Also known as: NUDR8;

The sequence of this isoform differs from the canonical sequence as follows:
     15-29: EAAAVAAAAAVAAAA → D
Isoform 3 (identifier: O75398-4)

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.
Isoform 4 (identifier: O75398-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Deformed epidermal autoregulatory factor 1 homolog
PRO_0000074084

Regions

Domain193 – 27381SAND
Zinc finger504 – 54037MYND-type
Region403 – 47876Interaction with LMO4 By similarity
Motif301 – 31616Nuclear localization signal Potential
Compositional bias2 – 122121Ala-rich
Compositional bias383 – 43957Pro-rich

Amino acid modifications

Modified residue4481Phosphoserine By similarity

Natural variations

Alternative sequence1 – 6868Missing in isoform 3.
VSP_005966
Alternative sequence15 – 2915EAAAV…VAAAA → D in isoform 2.
VSP_005967
Alternative sequence223 – 333111GRGRC…AATTF → WDLKPSRCLLHLCCLLRRHD LI in isoform 4.
VSP_038701
Alternative sequence5011E → EVIHPPRLPKVLGLQ in isoform 4.
VSP_038702
Natural variant1861E → V in a primary colorectal cancer. Ref.2
VAR_013725
Natural variant1911K → I in a primary colorectal cancer. Ref.2
VAR_013726
Natural variant1911K → N in a primary colorectal cancer. Ref.2
VAR_013727
Natural variant199 – 2024YDSE → CDND in a primary colorectal cancer.
VAR_013728
Natural variant2021E → D in a primary colorectal cancer. Ref.2
VAR_013729
Natural variant2181R → K in a primary colorectal cancer. Ref.2
VAR_013730
Natural variant2281I → S De novo variant found in a patient with mental retardation. Ref.15
VAR_065089
Natural variant350 – 3523DRA → GQT in a primary colorectal cancer.
VAR_013731
Natural variant3561E → H in a primary colorectal cancer; requires 2 nucleotide substitutions. Ref.2
VAR_013732
Natural variant3641S → N in a primary colorectal cancer. Ref.2
VAR_013733
Natural variant3671Q → H in a primary colorectal cancer. Ref.2
VAR_013734
Natural variant3701V → L in a primary colorectal cancer. Ref.2
VAR_013735
Natural variant3971Y → F in a primary colorectal cancer. Ref.2
VAR_013736
Natural variant4421V → A in a primary colorectal cancer. Ref.2
VAR_013737
Natural variant4491E → K in a primary colorectal cancer. Ref.2
VAR_013738
Natural variant451 – 4522RS → GI in a primary colorectal cancer.
VAR_013739
Natural variant4681Q → H in a primary colorectal cancer. Ref.2
VAR_013740
Natural variant4791H → L in a primary colorectal cancer. Ref.2
VAR_013741
Natural variant4981E → K in a primary colorectal cancer. Ref.2
VAR_013742
Natural variant5261T → N in a primary colorectal cancer. Ref.2
VAR_013743
Natural variant5301R → L in a primary colorectal cancer. Ref.2
VAR_013744
Natural variant537 – 5382QH → HL in a primary colorectal cancer.
VAR_013745
Natural variant5421Q → H in a primary colorectal cancer. Ref.2
VAR_013746
Natural variant5451A → G in a primary colorectal cancer. Ref.2
Corresponds to variant rs34114147 [ dbSNP | Ensembl ].
VAR_013747
Natural variant5451A → V in a primary colorectal cancer. Ref.2
VAR_013748

Experimental info

Mutagenesis2151Y → Q: Reduces transcription activation. Ref.8
Mutagenesis2261R → A: Reduces transcription activation. Ref.8
Mutagenesis2461R → A: Reduces transcription activation. Ref.8
Mutagenesis2501K → A: Abolishes DNA-binding. Ref.8
Mutagenesis2521W → Q: Abolishes DNA-binding. Ref.8
Mutagenesis2531K → A: Abolishes DNA-binding. Ref.8
Mutagenesis3021R → T: Abolishes nuclear localization. Ref.1
Mutagenesis3041K → T: Abolishes nuclear localization. Ref.1
Mutagenesis5381H → S: No effect on folding of MYND-type zinc finger. Ref.14
Sequence conflict651A → E in ACU88060. Ref.3
Sequence conflict721E → D in AAB62704. Ref.4
Sequence conflict1661P → Q in ACU88060. Ref.3
Sequence conflict2471A → T in AAB62704. Ref.4
Sequence conflict2941V → L in AAB62704. Ref.4
Sequence conflict3991D → G in ACU88060. Ref.3
Sequence conflict5221N → K in AAB62704. Ref.4

Secondary structure

............. 565
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Hu-DF1) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3BDFEDBF6AD4BDDE

FASTA56559,327
        10         20         30         40         50         60 
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAGGEAEEP VLSRDEDSEE DADSEAERET 

        70         80         90        100        110        120 
PRVTAVAVMA AEPGHMDMGA EALPGPDEAA AAAAFAEVTT VTVANVGAAA DNVFTTSVAN 

       130        140        150        160        170        180 
AASISGHVLS GRTALQIGDS LNTEKATLIV VHTDGSIVET TGLKGPAAPL TPGPQSPPTP 

       190        200        210        220        230        240 
LAPGQEKGGT KYNWDPSVYD SELPVRCRNI SGTLYKNRLG SGGRGRCIKQ GENWYSPTEF 

       250        260        270        280        290        300 
EAMAGRASSK DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDDMTL SGPVRLFVPY 

       310        320        330        340        350        360 
KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD RASTVEATAV 

       370        380        390        400        410        420 
ISESPAQGDV FAGATVQEAS VQPPCRASHP EPHYPGYQDS CQIAPFPEAA LPTSHPKIVL 

       430        440        450        460        470        480 
TSLPALAVPP PTPTKAAPPA LVNGLELSEP RSWLYLEEMV NSLLNTAQQL KTLFEQAKHA 

       490        500        510        520        530        540 
STYREAATNQ AKIHADAERK EQSCVNCGRE AMSECTGCHK VNYCSTFCQR KDWKDHQHIC 

       550        560 
GQSAAVTVQA DEVHVAESVM EKVTV 

« Hide

Isoform 2 (NUDR8) [UniParc].

Checksum: 9ABE2A02D3AA8DA1
Show »

FASTA55158,262
Isoform 3 (Suppressin) [UniParc].

Checksum: 4EC4279532D8A4DE
Show »

FASTA49752,717
Isoform 4 (Hu-DF1-VAR) [UniParc].

Checksum: AD1869382C23FF2A
Show »

FASTA49051,277

References

« Hide 'large scale' references
[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. 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 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]"Structure and functional analysis of the MYND domain."
Spadaccini R., Perrin H., Bottomley M.J., Ansieau S., Sattler M.
J. Mol. Biol. 358:498-508(2006) [PubMed] [Europe PMC] [Abstract]
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]"Structural and functional analysis of the DEAF-1 and BS69 MYND domains."
Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., Franzmann T.M., Buchner J., Ansieau S., Sattler M.
PLoS ONE 8:E54715-E54715(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 501-544 IN COMPLEX WITH ZINC IONS, SUBUNIT, INTERACTION WITH NCOR1 AND NCOR2, MUTAGENESIS OF HIS-538.
[15]"A de novo paradigm for mental retardation."
Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M., de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M., van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.
Nat. Genet. 42:1109-1112(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-228.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31327.1. [O75398-1]
RefSeqNP_066288.2. NM_021008.2. [O75398-1]
UniGeneHs.243994.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JW6NMR-A496-544[»]
4A24NMR-A501-544[»]
ProteinModelPortalO75398.
SMRO75398. Positions 201-272, 501-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115777. 21 interactions.
IntActO75398. 18 interactions.
MINTMINT-1420286.

PTM databases

PhosphoSiteO75398.

Proteomic databases

MaxQBO75398.
PaxDbO75398.
PRIDEO75398.

Protocols and materials databases

DNASU10522.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338675; ENSP00000341902; ENSG00000177030. [O75398-5]
ENST00000382409; ENSP00000371846; ENSG00000177030. [O75398-1]
GeneID10522.
KEGGhsa:10522.
UCSCuc001lqq.1. human. [O75398-1]
uc021qbn.1. human. [O75398-5]

Organism-specific databases

CTD10522.
GeneCardsGC11M000644.
H-InvDBHIX0026125.
HGNCHGNC:14677. DEAF1.
HPAHPA030302.
MIM602635. gene.
neXtProtNX_O75398.
PharmGKBPA27234.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291744.
HOVERGENHBG051335.
InParanoidO75398.
OMAQSCVNCG.
OrthoDBEOG7VQJF5.
PhylomeDBO75398.
TreeFamTF325664.

Gene expression databases

ArrayExpressO75398.
BgeeO75398.
CleanExHS_SPN.
GenevestigatorO75398.

Family and domain databases

Gene3D3.10.390.10. 1 hit.
InterProIPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR024119. TF_DEAF-1.
IPR002893. Znf_MYND.
[Graphical view]
PANTHERPTHR10237. PTHR10237. 1 hit.
PfamPF01342. SAND. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]
SMARTSM00258. SAND. 1 hit.
[Graphical view]
SUPFAMSSF63763. SSF63763. 1 hit.
PROSITEPS50864. SAND. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75398.
GenomeRNAi10522.
NextBio39912.
PROO75398.
SOURCESearch...

Entry information

Entry nameDEAF1_HUMAN
AccessionPrimary (citable) accession number: O75398
Secondary accession number(s): A8K1F8 expand/collapse secondary AC list , A8K5R8, C7T5V5, O15152, O75399, O75510, O75511, O75512, O75513, Q9UET1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 147 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM