Zinc finger protein 423 - Homo sapiens (Human)

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Q2M1K9 (ZN423_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Zinc finger protein 423

Alternative name(s):
Olf1/EBF-associated zinc finger protein
Short name=hOAZ
Smad- and Olf-interacting zinc finger protein

Gene names

Name:	ZNF423
Synonyms:	KIAA0760, NPHP14, OAZ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1284 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. Ref.2
Subunit structure	Homodimer By similarity. Interacts with EBF1 By similarity. Interacts with SMAD1 and SMAD4. Interacts with PARP1. Interacts with CEP290. Ref.2 Ref.6
Subcellular location	Nucleus Ref.2.
Tissue specificity	Expressed in brain, lung, skeletal muscle, heart, pancreas and kidney but not liver or placenta. Also expressed in aorta, ovary, pituitary, small intestine, fetal brain, fetal kidney and, within the adult brain, in the substantia nigra, medulla, amygdala, thalamus and cerebellum. Ref.2
Domain	Uses different DNA- and protein-binding zinc fingers to regulate the distinct BMP-Smad and Olf signaling pathways. C2H2-type zinc fingers 14-19 mediate the interaction with SMAD1 and SMAD4, while zinc fingers 28-30 mediate the interaction with EBF1. zinc fingers 2-8 bind the 5'-CCGCCC-3' DNA sequence in concert with EBF1, while zinc fingers 9-13 bind BMP target gene promoters in concert with SMADs. Ref.2
Involvement in disease	Nephronophthisis 14 (NPHP14) [MIM:614844]: An autosomal recessive disorder manifesting as infantile-onset kidney disease, cerebellar vermis hypoplasia, and situs inversus. Nephronophthisis is a progressive tubulo-interstitial kidney disorder histologically characterized by modifications of the tubules with thickening of the basement membrane, interstitial fibrosis and, in the advanced stages, medullary cysts. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Joubert syndrome 19 (JBTS19) [MIM:614844]: A form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). JBTS19 patients have polycystic kidney disease, Leber congenital amaurosis, cerebellar vermis hypoplasia, and breathing abnormality. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 30 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Ciliopathy Disease mutation Joubert syndrome Nephronophthisis
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of BMP signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.2. Source: UniProtKB
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
CEP290	O15078	3	EBI-950016,EBI-1811944
PARP1	P09874	2	EBI-950016,EBI-355676
RARA	P10276	2	EBI-950016,EBI-413374

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1284

1284

Zinc finger protein 423

PRO_0000308595

Regions

Zinc finger

67 – 93

C2H2-type 1; degenerate

Zinc finger

138 – 160

C2H2-type 2

Zinc finger

166 – 188

C2H2-type 3

Zinc finger

194 – 216

C2H2-type 4

Zinc finger

222 – 244

C2H2-type 5

Zinc finger

263 – 286

C2H2-type 6

Zinc finger

295 – 318

C2H2-type 7

Zinc finger

323 – 345

C2H2-type 8

Zinc finger

409 – 433

C2H2-type 9; degenerate

Zinc finger

441 – 464

C2H2-type 10

Zinc finger

480 – 503

C2H2-type 11

Zinc finger

517 – 540

C2H2-type 12

Zinc finger

563 – 588

C2H2-type 13; atypical

Zinc finger

632 – 654

C2H2-type 14

Zinc finger

662 – 684

C2H2-type 15

Zinc finger

692 – 715

C2H2-type 16

Zinc finger

720 – 743

C2H2-type 17

Zinc finger

750 – 773

C2H2-type 18

Zinc finger

781 – 803

C2H2-type 19

Zinc finger

807 – 830

C2H2-type 20

Zinc finger

886 – 908

C2H2-type 21; degenerate

Zinc finger

930 – 952

C2H2-type 22

Zinc finger

959 – 981

C2H2-type 23

Zinc finger

1020 – 1042

C2H2-type 24

Zinc finger

1064 – 1082

C2H2-type 25; degenerate

Zinc finger

1120 – 1143

C2H2-type 26

Zinc finger

1168 – 1190

C2H2-type 27

Zinc finger

1198 – 1220

C2H2-type 28

Zinc finger

1229 – 1252

C2H2-type 29

Zinc finger

1259 – 1282

C2H2-type 30

Amino acid modifications

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.5

Modified residue

604

Phosphoserine Ref.5

Modified residue

1054

Phosphoserine Ref.5

Natural variations

Natural variant

629

N → S.
Corresponds to variant rs34214571 [ dbSNP | Ensembl ].

VAR_036844

Natural variant

913

P → L in NPHP14; found at homozygosity in two siblings with nephronophthisis, cerebellar vermis hypoplasia and situs inversus. Ref.6
Corresponds to variant rs200585917 [ dbSNP | Ensembl ].

VAR_068501

Natural variant

1277

H → Y in JBTS19. Ref.6

VAR_068502

Experimental info

Mutagenesis

420

N → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-426; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

426

E → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

452

T → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-458; A-491; A-497; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

458

E → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-491; A-497; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

491

D → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-497; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

497

E → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-528; A-534; A-574 and A-581. Ref.2

Mutagenesis

528

T → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-534; A-574 and A-581. Ref.2

Mutagenesis

534

E → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-574 and A-581. Ref.2

Mutagenesis

574

F → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-581. Ref.2

Mutagenesis

581

T → A: Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-574. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q2M1K9 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: F34CB87161738321
Show »

FASTA

1,284

144,605

        10         20         30         40         50         60 
MHKKRVEEGE ASDFSLAWDS SVTAAGGLEG EPECDQKTSR ALEDRNSVTS QEERNEDDED 

        70         80         90        100        110        120 
MEDESIYTCD HCQQDFESLA DLTDHRAHRC PGDGDDDPQL SWVASSPSSK DVASPTQMIG 

       130        140        150        160        170        180 
DGCDLGLGEE EGGTGLPYPC QFCDKSFIRL SYLKRHEQIH SDKLPFKCTY CSRLFKHKRS 

       190        200        210        220        230        240 
RDRHIKLHTG DKKYHCHECE AAFSRSDHLK IHLKTHSSSK PFKCTVCKRG FSSTSSLQSH 

       250        260        270        280        290        300 
MQAHKKNKEH LAKSEKEAKK DDFMCDYCED TFSQTEELEK HVLTRHPQLS EKADLQCIHC 

       310        320        330        340        350        360 
PEVFVDENTL LAHIHQAHAN QKHKCPMCPE QFSSVEGVYC HLDSHRQPDS SNHSVSPDPV 

       370        380        390        400        410        420 
LGSVASMSSA TPDSSASVER GSTPDSTLKP LRGQKKMRDD GQGWTKVVYS CPYCSKRDFN 

       430        440        450        460        470        480 
SLAVLEIHLK TIHADKPQQS HTCQICLDSM PTLYNLNEHV RKLHKNHAYP VMQFGNISAF 

       490        500        510        520        530        540 
HCNYCPEMFA DINSLQEHIR VSHCGPNANP SDGNNAFFCN QCSMGFLTES SLTEHIQQAH 

       550        560        570        580        590        600 
CSVGSAKLES PVVQPTQSFM EVYSCPYCTN SPIFGSILKL TKHIKENHKN IPLAHSKKSK 

       610        620        630        640        650        660 
AEQSPVSSDV EVSSPKRQRL SASANSISNG EYPCNQCDLK FSNFESFQTH LKLHLELLLR 

       670        680        690        700        710        720 
KQACPQCKED FDSQESLLQH LTVHYMTTST HYVCESCDKQ FSSVDDLQKH LLDMHTFVLY 

       730        740        750        760        770        780 
HCTLCQEVFD SKVSIQVHLA VKHSNEKKMY RCTACNWDFR KEADLQVHVK HSHLGNPAKA 

       790        800        810        820        830        840 
HKCIFCGETF STEVELQCHI TTHSKKYNCK FCSKAFHAII LLEKHLREKH CVFDAATENG 

       850        860        870        880        890        900 
TANGVPPMAT KKAEPADLQG MLLKNPEAPN SHEASEDDVD ASEPMYGCDI CGAAYTMEVL 

       910        920        930        940        950        960 
LQNHRLRDHN IRPGEDDGSR KKAEFIKGSH KCNVCSRTFF SENGLREHLQ THRGPAKHYM 

       970        980        990       1000       1010       1020 
CPICGERFPS LLTLTEHKVT HSKSLDTGTC RICKMPLQSE EEFIEHCQMH PDLRNSLTGF 

      1030       1040       1050       1060       1070       1080 
RCVVCMQTVT STLELKIHGT FHMQKLAGSS AASSPNGQGL QKLYKCALCL KEFRSKQDLV 

      1090       1100       1110       1120       1130       1140 
KLDVNGLPYG LCAGCMARSA NGQVGGLAPP EPADRPCAGL RCPECSVKFE SAEDLESHMQ 

      1150       1160       1170       1180       1190       1200 
VDHRDLTPET SGPRKGTQTS PVPRKKTYQC IKCQMTFENE REIQIHVANH MIEEGINHEC 

      1210       1220       1230       1240       1250       1260 
KLCNQMFDSP AKLLCHLIEH SFEGMGGTFK CPVCFTVFVQ ANKLQQHIFA VHGQEDKIYD 

      1270       1280 
CSQCPQKFFF QTELQNHTMS QHAQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"OAZ uses distinct DNA- and protein-binding zinc fingers in separate BMP-Smad and Olf signaling pathways." Hata A., Seoane J., Lagna G., Montalvo E., Hemmati-Brivanlou A., Massague J. Cell 100:229-240(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 61-1284, FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH SMAD1 AND SMAD4, MUTAGENESIS OF ASN-420; GLU-426; THR-452; GLU-458; ASP-491; GLU-497; THR-528; GLU-534; PHE-574 AND THR-581.
[3]	"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1284. Tissue: Brain.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-50; SER-604 AND SER-1054, MASS SPECTROMETRY.
[6]	"Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling." Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H. Hildebrandt F. Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PARP1 AND CEP290, VARIANT NPHP14 LEU-913, VARIANT JBTS19 TYR-1277.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC112315 mRNA. Translation: AAI12316.1. BC112317 mRNA. Translation: AAI12318.1. AF221712 mRNA. Translation: AAF28354.1. AB018303 mRNA. Translation: BAA34480.2.
IPI	IPI00100660.
RefSeq	NP_001258549.1. NM_001271620.1. NP_055884.2. NM_015069.3.
UniGene	Hs.530930.
3D structure databases
ProteinModelPortal	Q2M1K9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q2M1K9. 9 interactions.
MINT	MINT-2819859.
STRING	9606.ENSP00000262383.
PTM databases
PhosphoSite	Q2M1K9.
Polymorphism databases
DMDM	121941357.
Proteomic databases
PaxDb	Q2M1K9.
PRIDE	Q2M1K9.
Protocols and materials databases
DNASU	23090.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262383; ENSP00000262383; ENSG00000102935. ENST00000561648; ENSP00000455426; ENSG00000102935. ENST00000562520; ENSP00000457664; ENSG00000102935. ENST00000562871; ENSP00000457928; ENSG00000102935. ENST00000563137; ENSP00000455588; ENSG00000102935.
GeneID	23090.
KEGG	hsa:23090.
UCSC	uc002efs.3. human.
Organism-specific databases
CTD	23090.
GeneCards	GC16M049524.
HGNC	HGNC:16762. ZNF423.
HPA	HPA015258.
MIM	604557. gene. 614844. phenotype.
neXtProt	NX_Q2M1K9.
PharmGKB	PA134903681.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5048.
HOGENOM	HOG000155793.
HOVERGEN	HBG052773.
OMA	ECEAAFS.
OrthoDB	EOG4NP72N.
PhylomeDB	Q2M1K9.
Gene expression databases
ArrayExpress	Q2M1K9.
Bgee	Q2M1K9.
CleanEx	HS_ZNF423.
Genevestigator	Q2M1K9.
Family and domain databases
Gene3D	3.30.160.60. 4 hits.
InterPro	IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
Pfam	PF00096. zf-C2H2. 2 hits. [Graphical view]
SMART	SM00355. ZnF_C2H2. 30 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 27 hits. PS50157. ZINC_FINGER_C2H2_2. 23 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	23090.
NextBio	44239.
SOURCE	Search...

Entry information

Entry name

ZN423_HUMAN

Accession

Primary (citable) accession number: Q2M1K9
Secondary accession number(s): O94860, Q76N04, Q9NZ13

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	February 21, 2006
Last modified:	May 1, 2013
This is version 81 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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents