O75398 (DEAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DEAF1
Synonyms:	SPN, ZMYND5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Protein existence	Evidence 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 Probable. Isoform 1 and isoform 4 may form a heterodimer. Binds to LMO4 (via its C-terminus), LMO2 and CLIM2 By similarity. May interact with the corepressor NCOR.
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 Isoform 2: Secreted. Note: Secreted in some cell types. Ref.3 Isoform 3: Secreted. Note: Secreted in some cell types. Ref.3 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
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
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	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 process	Neurogenesis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm 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: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN2A	P42771	2	EBI-718185,EBI-375053
GSK3A	P49840	2	EBI-718185,EBI-1044067
GSK3B	P49841	2	EBI-718185,EBI-373586

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 565

565

Deformed epidermal autoregulatory factor 1 homolog

PRO_0000074084

Regions

Domain

193 – 273

81

SAND

Zinc finger

504 – 540

37

MYND-type

Motif

301 – 316

16

Nuclear localization signal Potential

Compositional bias

2 – 122

121

Ala-rich

Compositional bias

383 – 439

57

Pro-rich

Natural variations

Alternative sequence

1 – 68

68

Missing in isoform 3.

VSP_005966

Alternative sequence

15 – 29

15

EAAAV…VAAAA → D in isoform 2.

VSP_005967

Alternative sequence

223 – 333

111

GRGRC…AATTF → WDLKPSRCLLHLCCLLRRHD LI in isoform 4.

VSP_038701

Alternative sequence

501

1

E → EVIHPPRLPKVLGLQ in isoform 4.

VSP_038702

Natural variant

186

1

E → V in a primary colorectal cancer. Ref.2

VAR_013725

Natural variant

191

1

K → I in a primary colorectal cancer. Ref.2

VAR_013726

Natural variant

191

1

K → N in a primary colorectal cancer. Ref.2

VAR_013727

Natural variant

199 – 202

4

YDSE → CDND in a primary colorectal cancer.

VAR_013728

Natural variant

202

1

E → D in a primary colorectal cancer. Ref.2

VAR_013729

Natural variant

218

1

R → K in a primary colorectal cancer. Ref.2

VAR_013730

Natural variant

228

1

I → S De novo variant found in a patient with mental retardation. Ref.10

VAR_065089

Natural variant

350 – 352

3

DRA → GQT in a primary colorectal cancer.

VAR_013731

Natural variant

356

1

E → H in a primary colorectal cancer; requires 2 nucleotide substitutions. Ref.2

VAR_013732

Natural variant

364

1

S → N in a primary colorectal cancer. Ref.2

VAR_013733

Natural variant

367

1

Q → H in a primary colorectal cancer. Ref.2

VAR_013734

Natural variant

370

1

V → L in a primary colorectal cancer. Ref.2

VAR_013735

Natural variant

397

1

Y → F in a primary colorectal cancer. Ref.2

VAR_013736

Natural variant

442

1

V → A in a primary colorectal cancer. Ref.2

VAR_013737

Natural variant

449

1

E → K in a primary colorectal cancer. Ref.2

VAR_013738

Natural variant

451 – 452

2

RS → GI in a primary colorectal cancer.

VAR_013739

Natural variant

468

1

Q → H in a primary colorectal cancer. Ref.2

VAR_013740

Natural variant

479

1

H → L in a primary colorectal cancer. Ref.2

VAR_013741

Natural variant

498

1

E → K in a primary colorectal cancer. Ref.2

VAR_013742

Natural variant

526

1

T → N in a primary colorectal cancer. Ref.2

VAR_013743

Natural variant

530

1

R → L in a primary colorectal cancer. Ref.2

VAR_013744

Natural variant

537 – 538

2

QH → HL in a primary colorectal cancer.

VAR_013745

Natural variant

542

1

Q → H in a primary colorectal cancer. Ref.2

VAR_013746

Natural variant

545

1

A → G in a primary colorectal cancer. Ref.2

VAR_013747

Natural variant

545

1

A → V in a primary colorectal cancer. Ref.2

VAR_013748

Experimental info

Mutagenesis

215

1

Y → Q: Reduces transcription activation. Ref.8

Mutagenesis

226

1

R → A: Reduces transcription activation. Ref.8

Mutagenesis

246

1

R → A: Reduces transcription activation. Ref.8

Mutagenesis

250

1

K → A: Abolishes DNA-binding. Ref.8

Mutagenesis

252

1

W → Q: Abolishes DNA-binding. Ref.8

Mutagenesis

253

1

K → A: Abolishes DNA-binding. Ref.8

Mutagenesis

302

1

R → T: Abolishes nuclear localization. Ref.1

Mutagenesis

304

1

K → T: Abolishes nuclear localization. Ref.1

Sequence conflict

65

1

A → E in ACU88060. Ref.3

Sequence conflict

72

1

E → D in AAB62704. Ref.4

Sequence conflict

166

1

P → Q in ACU88060. Ref.3

Sequence conflict

247

1

A → T in AAB62704. Ref.4

Sequence conflict

294

1

V → L in AAB62704. Ref.4

Sequence conflict

380

1

S → I in AAC25718. Ref.2

Sequence conflict

399

1

D → G in ACU88060. Ref.3

Sequence conflict

440

1

A → E in AAC25718. Ref.2

Sequence conflict

457

1

E → K in AAC25718. Ref.2

Sequence conflict

482

1

T → S in AAC25718. Ref.2

Sequence conflict

487

1

A → G in AAC25718. Ref.2

Sequence conflict

496 – 497

2

DA → VS in AAC25718. Ref.2

Sequence conflict

502

1

Q → H in AAC25718. Ref.2

Sequence conflict

522

1

N → K in AAB62704. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

565

Helix Strand Turn

Details...

Beta strand

505 – 510

6

Beta strand

512 – 514

3

Turn

516 – 518

3

Beta strand

520 – 525

6

Helix

526 – 532

7

Turn

533 – 535

3

Helix

536 – 538

3

Turn

539 – 541

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Hu-DF1) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 3BDFEDBF6AD4BDDE	FASTA	565	59,327
	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
	Isoform 2 (NUDR8) [UniParc]. Checksum: 9ABE2A02D3AA8DA1	FASTA	551	58,262
	10 20 30 40 50 60 MEDSDSAAKQ LGLADAAAAG GEAEEPVLSR DEDSEEDADS EAERETPRVT AVAVMAAEPG 70 80 90 100 110 120 HMDMGAEALP GPDEAAAAAA FAEVTTVTVA NVGAAADNVF TTSVANAASI SGHVLSGRTA 130 140 150 160 170 180 LQIGDSLNTE KATLIVVHTD GSIVETTGLK GPAAPLTPGP QSPPTPLAPG QEKGGTKYNW 190 200 210 220 230 240 DPSVYDSELP VRCRNISGTL YKNRLGSGGR GRCIKQGENW YSPTEFEAMA GRASSKDWKR 250 260 270 280 290 300 SIRYAGRPLQ CLIQDGILNP HAASCTCAAC CDDMTLSGPV RLFVPYKRRK KENELPTTPV 310 320 330 340 350 360 KKDSPKNITL LPATAATTFT VTPSGQITTS GALTFDRAST VEATAVISES PAQGDVFAGA 370 380 390 400 410 420 TVQEASVQPP CRASHPEPHY PGYQDSCQIA PFPEAALPTS HPKIVLTSLP ALAVPPPTPT 430 440 450 460 470 480 KAAPPALVNG LELSEPRSWL YLEEMVNSLL NTAQQLKTLF EQAKHASTYR EAATNQAKIH 490 500 510 520 530 540 ADAERKEQSC VNCGREAMSE CTGCHKVNYC STFCQRKDWK DHQHICGQSA AVTVQADEVH 550 VAESVMEKVT V
	Isoform 3 (Suppressin) [UniParc]. Checksum: 4EC4279532D8A4DE	FASTA	497	52,717
	10 20 30 40 50 60 MAAEPGHMDM GAEALPGPDE AAAAAAFAEV TTVTVANVGA AADNVFTTSV ANAASISGHV 70 80 90 100 110 120 LSGRTALQIG DSLNTEKATL IVVHTDGSIV ETTGLKGPAA PLTPGPQSPP TPLAPGQEKG 130 140 150 160 170 180 GTKYNWDPSV YDSELPVRCR NISGTLYKNR LGSGGRGRCI KQGENWYSPT EFEAMAGRAS 190 200 210 220 230 240 SKDWKRSIRY AGRPLQCLIQ DGILNPHAAS CTCAACCDDM TLSGPVRLFV PYKRRKKENE 250 260 270 280 290 300 LPTTPVKKDS PKNITLLPAT AATTFTVTPS GQITTSGALT FDRASTVEAT AVISESPAQG 310 320 330 340 350 360 DVFAGATVQE ASVQPPCRAS HPEPHYPGYQ DSCQIAPFPE AALPTSHPKI VLTSLPALAV 370 380 390 400 410 420 PPPTPTKAAP PALVNGLELS EPRSWLYLEE MVNSLLNTAQ QLKTLFEQAK HASTYREAAT 430 440 450 460 470 480 NQAKIHADAE RKEQSCVNCG REAMSECTGC HKVNYCSTFC QRKDWKDHQH ICGQSAAVTV 490 QADEVHVAES VMEKVTV
	Isoform 4 (Hu-DF1-VAR) [UniParc]. Checksum: AD1869382C23FF2A	FASTA	490	51,277
	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 SGWDLKPSRC LLHLCCLLRR 250 260 270 280 290 300 HDLITVTPSG QITTSGALTF DRASTVEATA VISESPAQGD VFAGATVQEA SVQPPCRASH 310 320 330 340 350 360 PEPHYPGYQD SCQIAPFPEA ALPTSHPKIV LTSLPALAVP PPTPTKAAPP ALVNGLELSE 370 380 390 400 410 420 PRSWLYLEEM VNSLLNTAQQ LKTLFEQAKH ASTYREAATN QAKIHADAER KEVIHPPRLP 430 440 450 460 470 480 KVLGLQQSCV NCGREAMSEC TGCHKVNYCS TFCQRKDWKD HQHICGQSAA VTVQADEVHV 490 AESVMEKVTV

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. Frameshift.
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.

IPI

IPI00216889.
IPI00742784.
IPI00784235.
IPI00954833.

RefSeq

NP_066288.2. NM_021008.2.

UniGene

Hs.243994.
Hs.448664.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JW6	NMR	-	A	496-544	[»]
4A24	NMR	-	A	501-544	[»]

ProteinModelPortal

O75398.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75398. 9 interactions.

MINT

MINT-1420286.

PTM databases

PhosphoSite

O75398.

Proteomic databases

PaxDb

O75398.

PRIDE

O75398.

Protocols and materials databases

DNASU

10522.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338675; ENSP00000341902; ENSG00000177030.
ENST00000382409; ENSP00000371846; ENSG00000177030.

GeneID

10522.

KEGG

hsa:10522.

UCSC

uc001lqq.1. human.
uc021qbn.1. human.

Organism-specific databases

CTD

10522.

GeneCards

GC11M000634.

H-InvDB

HIX0026125.

HGNC

HGNC:14677. DEAF1.

HPA

HPA030302.

MIM

602635. gene.

neXtProt

NX_O75398.

PharmGKB

PA27234.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG291744.

HOVERGEN

HBG051335.

InParanoid

O75398.

OMA

QSCVNCG.

Gene expression databases

ArrayExpress

O75398.

Bgee

O75398.

CleanEx

HS_SPN.

Genevestigator

O75398.

GermOnline

ENSG00000177030. Homo sapiens.

Family and domain databases

Gene3D

3.10.390.10. 1 hit.

InterPro

IPR000770. SAND_dom.
IPR010919. SAND_dom-like.
IPR024119. TF_DEAF-1.
IPR002893. Znf_MYND.
[Graphical view]

PANTHER

PTHR10237. PTHR10237. 1 hit.

Pfam

PF01342. SAND. 1 hit.
PF01753. zf-MYND. 1 hit.
[Graphical view]

SMART

SM00258. SAND. 1 hit.
[Graphical view]

SUPFAM

SSF63763. SAND_like. 1 hit.

PROSITE

PS50864. SAND. 1 hit.
PS01360. ZF_MYND_1. 1 hit.
PS50865. ZF_MYND_2. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

O75398.

GenomeRNAi

10522.

NextBio

39912.

SOURCE

Search...

Entry information

Entry name

DEAF1_HUMAN

Accession

Primary (citable) accession number: O75398
Secondary accession number(s): A8K1F8 , 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:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.