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Protein

Deformed epidermal autoregulatory factor 1 homolog

Gene

DEAF1

Organism
Homo sapiens (Human)
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. 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. Transcriptional activator of EIF4G3.6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri504 – 540MYND-typePROSITE-ProRule annotationAdd BLAST37

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000177030-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: 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%.
Isoform 2 :
  • Secreted

  • Note: Secreted in some cell types.
Isoform 3 :
  • Secreted

  • Note: Secreted in some cell types.
Isoform 4 :
  • Cytoplasm
  • Nucleus

  • Note: When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: UniProtKB-SubCell
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 24 (MRD24)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:615828
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071371224R → W in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; decreased interaction with XRCC6. 1 PublicationCorresponds to variant rs587777408dbSNPEnsembl.1
Natural variantiVAR_065089228I → S in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6. 2 PublicationsCorresponds to variant rs587777406dbSNPEnsembl.1
Natural variantiVAR_071373254R → S in MRD24; loss of DEAF1-promoter repression; gain of transcriptional activation of EIF4G3; a 9-fold reduction in DNA binding. 1 PublicationCorresponds to variant rs587777409dbSNPEnsembl.1
Natural variantiVAR_071374264Q → P in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6. 1 PublicationCorresponds to variant rs587777407dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi215Y → Q: Reduces transcription activation. 1 Publication1
Mutagenesisi226R → A: Reduces transcription activation. 1 Publication1
Mutagenesisi246R → A: Reduces transcription activation. 1 Publication1
Mutagenesisi250K → A: Abolishes DNA-binding. Loss of DEAF1-promoter repression; when associated with A-253. Loss of transcriptional activation of EIF4G3; when associated with A-253. Loss of interaction with XRCC6; when associated with A-253. Loss of DNA binding; when associated with A-253. 2 Publications1
Mutagenesisi252W → Q: Abolishes DNA-binding. 1 Publication1
Mutagenesisi253K → A: Abolishes DNA-binding. oss of DEAF1-promoter repression; when associated with A-250. Loss of transcriptional activation of EIF4G3; when associated with A-250. Loss of interaction with XRCC6; when associated with A-250. Loss of DNA binding; when associated with A-250. 2 Publications1
Mutagenesisi302R → T: Abolishes nuclear localization. 1 Publication1
Mutagenesisi304K → T: Abolishes nuclear localization. 1 Publication1
Mutagenesisi538H → S: No effect on folding of MYND-type zinc finger. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi10522.
MalaCardsiDEAF1.
MIMi615828. phenotype.
OpenTargetsiENSG00000177030.
PharmGKBiPA27234.

Polymorphism and mutation databases

BioMutaiDEAF1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000740841 – 565Deformed epidermal autoregulatory factor 1 homologAdd BLAST565

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei171PhosphothreonineBy similarity1
Modified residuei176PhosphoserineCombined sources1
Modified residuei179PhosphothreonineBy similarity1
Modified residuei432PhosphothreonineCombined sources1
Modified residuei448PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75398.
MaxQBiO75398.
PaxDbiO75398.
PeptideAtlasiO75398.
PRIDEiO75398.

PTM databases

iPTMnetiO75398.
PhosphoSitePlusiO75398.

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. Highly expressed in fetal and adult brain.2 Publications

Gene expression databases

BgeeiENSG00000177030.
CleanExiHS_SPN.
ExpressionAtlasiO75398. baseline and differential.
GenevisibleiO75398. HS.

Organism-specific databases

HPAiHPA030301.
HPA030302.

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.By similarity4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi115777. 22 interactors.
IntActiO75398. 20 interactors.
MINTiMINT-1420286.
STRINGi9606.ENSP00000371846.

Structurei

Secondary structure

1565
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi505 – 510Combined sources6
Beta strandi512 – 514Combined sources3
Turni516 – 518Combined sources3
Beta strandi520 – 525Combined sources6
Helixi526 – 532Combined sources7
Turni533 – 535Combined sources3
Helixi536 – 538Combined sources3
Turni539 – 541Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JW6NMR-A496-544[»]
4A24NMR-A501-544[»]
ProteinModelPortaliO75398.
SMRiO75398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75398.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini193 – 273SANDPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni403 – 478Interaction with LMO4By similarityAdd BLAST76

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi301 – 316Nuclear localization signalSequence analysisAdd BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 122Ala-richAdd BLAST121
Compositional biasi383 – 439Pro-richAdd BLAST57

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri504 – 540MYND-typePROSITE-ProRule annotationAdd BLAST37

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00390000013479.
HOVERGENiHBG051335.
InParanoidiO75398.
OMAiQSCVNCG.
OrthoDBiEOG091G0PAX.
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. AlignAdd to basket

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

        10         20         30         40         50
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAGGEAEEP VLSRDEDSEE
60 70 80 90 100
DADSEAERET PRVTAVAVMA AEPGHMDMGA EALPGPDEAA AAAAFAEVTT
110 120 130 140 150
VTVANVGAAA DNVFTTSVAN AASISGHVLS GRTALQIGDS LNTEKATLIV
160 170 180 190 200
VHTDGSIVET TGLKGPAAPL TPGPQSPPTP LAPGQEKGGT KYNWDPSVYD
210 220 230 240 250
SELPVRCRNI SGTLYKNRLG SGGRGRCIKQ GENWYSPTEF EAMAGRASSK
260 270 280 290 300
DWKRSIRYAG RPLQCLIQDG ILNPHAASCT CAACCDDMTL SGPVRLFVPY
310 320 330 340 350
KRRKKENELP TTPVKKDSPK NITLLPATAA TTFTVTPSGQ ITTSGALTFD
360 370 380 390 400
RASTVEATAV ISESPAQGDV FAGATVQEAS VQPPCRASHP EPHYPGYQDS
410 420 430 440 450
CQIAPFPEAA LPTSHPKIVL TSLPALAVPP PTPTKAAPPA LVNGLELSEP
460 470 480 490 500
RSWLYLEEMV NSLLNTAQQL KTLFEQAKHA STYREAATNQ AKIHADAERK
510 520 530 540 550
EQSCVNCGRE AMSECTGCHK VNYCSTFCQR KDWKDHQHIC GQSAAVTVQA
560
DEVHVAESVM EKVTV
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.Curated
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 differs from that shown. Several sequencing errors.Curated
Isoform 3 : The sequence AAC25718 differs from that shown. Reason: Frameshift at positions 222 and 236.Curated
The sequence AAC25719 differs from that shown. Reason: Frameshift at positions 222 and 236.Curated
Isoform 3 : The sequence AAC25719 differs from that shown. Reason: Frameshift at positions 222 and 236.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65A → E in ACU88060 (PubMed:19668219).Curated1
Sequence conflicti72E → D in AAB62704 (Ref. 4) Curated1
Sequence conflicti166P → Q in ACU88060 (PubMed:19668219).Curated1
Sequence conflicti247A → T in AAB62704 (Ref. 4) Curated1
Sequence conflicti294V → L in AAB62704 (Ref. 4) Curated1
Sequence conflicti399D → G in ACU88060 (PubMed:19668219).Curated1
Sequence conflicti522N → K in AAB62704 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013725186E → V in a primary colorectal cancer. 1 PublicationCorresponds to variant rs751727919dbSNPEnsembl.1
Natural variantiVAR_013726191K → I in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013727191K → N in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013728199 – 202YDSE → CDND in a primary colorectal cancer. 4
Natural variantiVAR_013729202E → D in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013730218R → K in a primary colorectal cancer. 1 PublicationCorresponds to variant rs1127312dbSNPEnsembl.1
Natural variantiVAR_071371224R → W in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; decreased interaction with XRCC6. 1 PublicationCorresponds to variant rs587777408dbSNPEnsembl.1
Natural variantiVAR_071372226R → W.1 PublicationCorresponds to variant rs587777623dbSNPEnsembl.1
Natural variantiVAR_065089228I → S in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6. 2 PublicationsCorresponds to variant rs587777406dbSNPEnsembl.1
Natural variantiVAR_071373254R → S in MRD24; loss of DEAF1-promoter repression; gain of transcriptional activation of EIF4G3; a 9-fold reduction in DNA binding. 1 PublicationCorresponds to variant rs587777409dbSNPEnsembl.1
Natural variantiVAR_071374264Q → P in MRD24; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6. 1 PublicationCorresponds to variant rs587777407dbSNPEnsembl.1
Natural variantiVAR_013731350 – 352DRA → GQT in a primary colorectal cancer. 3
Natural variantiVAR_013732356E → H in a primary colorectal cancer; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_013733364S → N in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013734367Q → H in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013735370V → L in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013736397Y → F in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013737442V → A in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013738449E → K in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013739451 – 452RS → GI in a primary colorectal cancer. 2
Natural variantiVAR_013740468Q → H in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013741479H → L in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013742498E → K in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013743526T → N in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013744530R → L in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013745537 – 538QH → HL in a primary colorectal cancer. 2
Natural variantiVAR_013746542Q → H in a primary colorectal cancer. 1 Publication1
Natural variantiVAR_013747545A → G in a primary colorectal cancer. 1 PublicationCorresponds to variant rs34114147dbSNPEnsembl.1
Natural variantiVAR_013748545A → V in a primary colorectal cancer. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0059661 – 68Missing in isoform 3. 3 PublicationsAdd BLAST68
Alternative sequenceiVSP_00596715 – 29EAAAV…VAAAA → D in isoform 2. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_038701223 – 333GRGRC…AATTF → WDLKPSRCLLHLCCLLRRHD LI in isoform 4. 1 PublicationAdd BLAST111
Alternative sequenceiVSP_038702501E → EVIHPPRLPKVLGLQ in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001280563.1. NM_001293634.1. [O75398-5]
NP_066288.2. NM_021008.3. [O75398-1]
UniGeneiHs.243994.

Genome annotation databases

EnsembliENST00000382409; ENSP00000371846; ENSG00000177030. [O75398-1]
GeneIDi10522.
KEGGihsa:10522.
UCSCiuc001lqq.2. human. [O75398-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001280563.1. NM_001293634.1. [O75398-5]
NP_066288.2. NM_021008.3. [O75398-1]
UniGeneiHs.243994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JW6NMR-A496-544[»]
4A24NMR-A501-544[»]
ProteinModelPortaliO75398.
SMRiO75398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115777. 22 interactors.
IntActiO75398. 20 interactors.
MINTiMINT-1420286.
STRINGi9606.ENSP00000371846.

PTM databases

iPTMnetiO75398.
PhosphoSitePlusiO75398.

Polymorphism and mutation databases

BioMutaiDEAF1.

Proteomic databases

EPDiO75398.
MaxQBiO75398.
PaxDbiO75398.
PeptideAtlasiO75398.
PRIDEiO75398.

Protocols and materials databases

DNASUi10522.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382409; ENSP00000371846; ENSG00000177030. [O75398-1]
GeneIDi10522.
KEGGihsa:10522.
UCSCiuc001lqq.2. human. [O75398-1]

Organism-specific databases

CTDi10522.
DisGeNETi10522.
GeneCardsiDEAF1.
H-InvDBHIX0026125.
HGNCiHGNC:14677. DEAF1.
HPAiHPA030301.
HPA030302.
MalaCardsiDEAF1.
MIMi602635. gene.
615828. phenotype.
neXtProtiNX_O75398.
OpenTargetsiENSG00000177030.
PharmGKBiPA27234.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4333. Eukaryota.
ENOG410ZMTP. LUCA.
GeneTreeiENSGT00390000013479.
HOVERGENiHBG051335.
InParanoidiO75398.
OMAiQSCVNCG.
OrthoDBiEOG091G0PAX.
PhylomeDBiO75398.
TreeFamiTF325664.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000177030-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO75398.
GenomeRNAii10522.
PROiO75398.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000177030.
CleanExiHS_SPN.
ExpressionAtlasiO75398. baseline and differential.
GenevisibleiO75398. HS.

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...

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: November 30, 2016
This is version 169 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.

Caution

This protein was first known as suppressin (characterized in bovine neuroendocrine and immune cells). However, according to PubMed:9773984, 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.Curated

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

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.