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Q2M1K9 (ZN423_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1284 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12841284Zinc finger protein 423
PRO_0000308595

Regions

Zinc finger67 – 9327C2H2-type 1; degenerate
Zinc finger138 – 16023C2H2-type 2
Zinc finger166 – 18823C2H2-type 3
Zinc finger194 – 21623C2H2-type 4
Zinc finger222 – 24423C2H2-type 5
Zinc finger263 – 28624C2H2-type 6
Zinc finger295 – 31824C2H2-type 7
Zinc finger323 – 34523C2H2-type 8
Zinc finger409 – 43325C2H2-type 9; degenerate
Zinc finger441 – 46424C2H2-type 10
Zinc finger480 – 50324C2H2-type 11
Zinc finger517 – 54024C2H2-type 12
Zinc finger563 – 58826C2H2-type 13; atypical
Zinc finger632 – 65423C2H2-type 14
Zinc finger662 – 68423C2H2-type 15
Zinc finger692 – 71524C2H2-type 16
Zinc finger720 – 74324C2H2-type 17
Zinc finger750 – 77324C2H2-type 18
Zinc finger781 – 80323C2H2-type 19
Zinc finger807 – 83024C2H2-type 20
Zinc finger886 – 90823C2H2-type 21; degenerate
Zinc finger930 – 95223C2H2-type 22
Zinc finger959 – 98123C2H2-type 23
Zinc finger1020 – 104223C2H2-type 24
Zinc finger1064 – 108219C2H2-type 25; degenerate
Zinc finger1120 – 114324C2H2-type 26
Zinc finger1168 – 119023C2H2-type 27
Zinc finger1198 – 122023C2H2-type 28
Zinc finger1229 – 125224C2H2-type 29
Zinc finger1259 – 128224C2H2-type 30

Amino acid modifications

Modified residue471Phosphoserine Ref.5
Modified residue501Phosphoserine Ref.5
Modified residue6041Phosphoserine Ref.5
Modified residue10541Phosphoserine Ref.5

Natural variations

Natural variant6291N → S.
Corresponds to variant rs34214571 [ dbSNP | Ensembl ].
VAR_036844
Natural variant9131P → 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 variant12771H → Y in JBTS19. Ref.6
VAR_068502

Experimental info

Mutagenesis4201N → 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
Mutagenesis4261E → 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
Mutagenesis4521T → 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
Mutagenesis4581E → 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
Mutagenesis4911D → 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
Mutagenesis4971E → 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
Mutagenesis5281T → 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
Mutagenesis5341E → 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
Mutagenesis5741F → 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
Mutagenesis5811T → 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

Secondary structure

.............. 1284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2M1K9 [UniParc].

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

FASTA1,284144,605
        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' 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., 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.
RefSeqNP_001258549.1. NM_001271620.1.
NP_055884.2. NM_015069.3.
XP_005255913.1. XM_005255856.2.
UniGeneHs.530930.
Hs.744482.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MDGNMR-A928-981[»]
ProteinModelPortalQ2M1K9.
SMRQ2M1K9. Positions 32-352, 641-827, 928-981, 1062-1284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116718. 9 interactions.
IntActQ2M1K9. 9 interactions.
MINTMINT-2819859.
STRING9606.ENSP00000262383.

PTM databases

PhosphoSiteQ2M1K9.

Polymorphism databases

DMDM121941357.

Proteomic databases

PaxDbQ2M1K9.
PRIDEQ2M1K9.

Protocols and materials databases

DNASU23090.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262383; ENSP00000262383; ENSG00000102935.
ENST00000561648; ENSP00000455426; ENSG00000102935.
ENST00000562520; ENSP00000457664; ENSG00000102935.
ENST00000562871; ENSP00000457928; ENSG00000102935.
ENST00000563137; ENSP00000455588; ENSG00000102935.
GeneID23090.
KEGGhsa:23090.
UCSCuc010vgn.3. human.

Organism-specific databases

CTD23090.
GeneCardsGC16M049524.
HGNCHGNC:16762. ZNF423.
HPAHPA015258.
MIM604557. gene.
614844. phenotype.
neXtProtNX_Q2M1K9.
Orphanet2318. Joubert syndrome with oculorenal defect.
PharmGKBPA134903681.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000155793.
HOVERGENHBG052773.
OMAFIEHCQM.
OrthoDBEOG7NGQB0.
PhylomeDBQ2M1K9.
TreeFamTF331504.

Gene expression databases

ArrayExpressQ2M1K9.
BgeeQ2M1K9.
CleanExHS_ZNF423.
GenevestigatorQ2M1K9.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 4 hits.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 30 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 27 hits.
PS50157. ZINC_FINGER_C2H2_2. 23 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiZNF423.
GenomeRNAi23090.
NextBio44239.
PROQ2M1K9.
SOURCESearch...

Entry information

Entry nameZN423_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 91 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 16

Human chromosome 16: entries, gene names and cross-references to MIM