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Q2M1K9

- ZN423_HUMAN

UniProt

Q2M1K9 - ZN423_HUMAN

Protein

Zinc finger protein 423

Gene

ZNF423

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri67 – 9327C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri138 – 16023C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri166 – 18823C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri194 – 21623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri222 – 24423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri263 – 28624C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri295 – 31824C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri323 – 34523C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 43325C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri441 – 46424C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri480 – 50324C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri517 – 54024C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri563 – 58826C2H2-type 13; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri632 – 65423C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri662 – 68423C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri692 – 71524C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri720 – 74324C2H2-type 17PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri750 – 77324C2H2-type 18PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri781 – 80323C2H2-type 19PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri807 – 83024C2H2-type 20PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri886 – 90823C2H2-type 21; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri930 – 95223C2H2-type 22PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri959 – 98123C2H2-type 23PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1020 – 104223C2H2-type 24PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1064 – 108219C2H2-type 25; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1120 – 114324C2H2-type 26PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1168 – 119023C2H2-type 27PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1198 – 122023C2H2-type 28PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1229 – 125224C2H2-type 29PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1259 – 128224C2H2-type 30PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. nervous system development Source: UniProtKB-KW
    4. Notch signaling pathway Source: UniProtKB
    5. positive regulation of BMP signaling pathway Source: UniProtKB
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Developmental protein, Repressor

    Keywords - Biological processi

    Differentiation, Neurogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:ZNF423
    Synonyms:KIAA0760, NPHP14, OAZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16762. ZNF423.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti913 – 9131P → L in NPHP14; found at homozygosity in two siblings with nephronophthisis, cerebellar vermis hypoplasia and situs inversus. 1 Publication
    Corresponds to variant rs200585917 [ dbSNP | Ensembl ].
    VAR_068501
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1277 – 12771H → Y in JBTS19. 1 Publication
    VAR_068502

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi420 – 4201N → 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. 1 Publication
    Mutagenesisi426 – 4261E → 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. 1 Publication
    Mutagenesisi452 – 4521T → 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. 1 Publication
    Mutagenesisi458 – 4581E → 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. 1 Publication
    Mutagenesisi491 – 4911D → 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. 1 Publication
    Mutagenesisi497 – 4971E → 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. 1 Publication
    Mutagenesisi528 – 5281T → 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. 1 Publication
    Mutagenesisi534 – 5341E → 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. 1 Publication
    Mutagenesisi574 – 5741F → 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. 1 Publication
    Mutagenesisi581 – 5811T → 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. 1 Publication

    Keywords - Diseasei

    Ciliopathy, Disease mutation, Joubert syndrome, Nephronophthisis

    Organism-specific databases

    MIMi614844. phenotype.
    Orphaneti2318. Joubert syndrome with oculorenal defect.
    PharmGKBiPA134903681.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12841284Zinc finger protein 423PRO_0000308595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 471Phosphoserine1 Publication
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei604 – 6041Phosphoserine1 Publication
    Modified residuei1054 – 10541Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ2M1K9.
    PRIDEiQ2M1K9.

    PTM databases

    PhosphoSiteiQ2M1K9.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ2M1K9.
    BgeeiQ2M1K9.
    CleanExiHS_ZNF423.
    GenevestigatoriQ2M1K9.

    Organism-specific databases

    HPAiHPA015258.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with EBF1 By similarity. Interacts with SMAD1 and SMAD4. Interacts with PARP1. Interacts with CEP290.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CEP290O150783EBI-950016,EBI-1811944
    PARP1P098742EBI-950016,EBI-355676
    RARAP102762EBI-950016,EBI-413374

    Protein-protein interaction databases

    BioGridi116718. 9 interactions.
    IntActiQ2M1K9. 9 interactions.
    MINTiMINT-2819859.
    STRINGi9606.ENSP00000262383.

    Structurei

    Secondary structure

    1
    1284
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi933 – 9375
    Helixi942 – 9498
    Helixi950 – 9523
    Beta strandi958 – 9603
    Beta strandi962 – 9643
    Beta strandi967 – 9704
    Helixi973 – 9797

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MDGNMR-A928-981[»]
    ProteinModelPortaliQ2M1K9.
    SMRiQ2M1K9. Positions 32-352, 641-827, 928-981, 1115-1142, 1168-1284.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Contains 30 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri67 – 9327C2H2-type 1; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri138 – 16023C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri166 – 18823C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri194 – 21623C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri222 – 24423C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri263 – 28624C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri295 – 31824C2H2-type 7PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri323 – 34523C2H2-type 8PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 43325C2H2-type 9; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri441 – 46424C2H2-type 10PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri480 – 50324C2H2-type 11PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri517 – 54024C2H2-type 12PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri563 – 58826C2H2-type 13; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri632 – 65423C2H2-type 14PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri662 – 68423C2H2-type 15PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri692 – 71524C2H2-type 16PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri720 – 74324C2H2-type 17PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri750 – 77324C2H2-type 18PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri781 – 80323C2H2-type 19PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri807 – 83024C2H2-type 20PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri886 – 90823C2H2-type 21; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri930 – 95223C2H2-type 22PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri959 – 98123C2H2-type 23PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1020 – 104223C2H2-type 24PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1064 – 108219C2H2-type 25; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1120 – 114324C2H2-type 26PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1168 – 119023C2H2-type 27PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1198 – 122023C2H2-type 28PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1229 – 125224C2H2-type 29PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1259 – 128224C2H2-type 30PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000155793.
    HOVERGENiHBG052773.
    OMAiFIEHCQM.
    OrthoDBiEOG7NGQB0.
    PhylomeDBiQ2M1K9.
    TreeFamiTF331504.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 4 hits.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 30 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 27 hits.
    PS50157. ZINC_FINGER_C2H2_2. 23 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2M1K9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHKKRVEEGE ASDFSLAWDS SVTAAGGLEG EPECDQKTSR ALEDRNSVTS     50
    QEERNEDDED MEDESIYTCD HCQQDFESLA DLTDHRAHRC PGDGDDDPQL 100
    SWVASSPSSK DVASPTQMIG DGCDLGLGEE EGGTGLPYPC QFCDKSFIRL 150
    SYLKRHEQIH SDKLPFKCTY CSRLFKHKRS RDRHIKLHTG DKKYHCHECE 200
    AAFSRSDHLK IHLKTHSSSK PFKCTVCKRG FSSTSSLQSH MQAHKKNKEH 250
    LAKSEKEAKK DDFMCDYCED TFSQTEELEK HVLTRHPQLS EKADLQCIHC 300
    PEVFVDENTL LAHIHQAHAN QKHKCPMCPE QFSSVEGVYC HLDSHRQPDS 350
    SNHSVSPDPV LGSVASMSSA TPDSSASVER GSTPDSTLKP LRGQKKMRDD 400
    GQGWTKVVYS CPYCSKRDFN SLAVLEIHLK TIHADKPQQS HTCQICLDSM 450
    PTLYNLNEHV RKLHKNHAYP VMQFGNISAF HCNYCPEMFA DINSLQEHIR 500
    VSHCGPNANP SDGNNAFFCN QCSMGFLTES SLTEHIQQAH CSVGSAKLES 550
    PVVQPTQSFM EVYSCPYCTN SPIFGSILKL TKHIKENHKN IPLAHSKKSK 600
    AEQSPVSSDV EVSSPKRQRL SASANSISNG EYPCNQCDLK FSNFESFQTH 650
    LKLHLELLLR KQACPQCKED FDSQESLLQH LTVHYMTTST HYVCESCDKQ 700
    FSSVDDLQKH LLDMHTFVLY HCTLCQEVFD SKVSIQVHLA VKHSNEKKMY 750
    RCTACNWDFR KEADLQVHVK HSHLGNPAKA HKCIFCGETF STEVELQCHI 800
    TTHSKKYNCK FCSKAFHAII LLEKHLREKH CVFDAATENG TANGVPPMAT 850
    KKAEPADLQG MLLKNPEAPN SHEASEDDVD ASEPMYGCDI CGAAYTMEVL 900
    LQNHRLRDHN IRPGEDDGSR KKAEFIKGSH KCNVCSRTFF SENGLREHLQ 950
    THRGPAKHYM CPICGERFPS LLTLTEHKVT HSKSLDTGTC RICKMPLQSE 1000
    EEFIEHCQMH PDLRNSLTGF RCVVCMQTVT STLELKIHGT FHMQKLAGSS 1050
    AASSPNGQGL QKLYKCALCL KEFRSKQDLV KLDVNGLPYG LCAGCMARSA 1100
    NGQVGGLAPP EPADRPCAGL RCPECSVKFE SAEDLESHMQ VDHRDLTPET 1150
    SGPRKGTQTS PVPRKKTYQC IKCQMTFENE REIQIHVANH MIEEGINHEC 1200
    KLCNQMFDSP AKLLCHLIEH SFEGMGGTFK CPVCFTVFVQ ANKLQQHIFA 1250
    VHGQEDKIYD CSQCPQKFFF QTELQNHTMS QHAQ 1284
    Length:1,284
    Mass (Da):144,605
    Last modified:February 21, 2006 - v1
    Checksum:iF34CB87161738321
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti629 – 6291N → S.
    Corresponds to variant rs34214571 [ dbSNP | Ensembl ].
    VAR_036844
    Natural varianti913 – 9131P → L in NPHP14; found at homozygosity in two siblings with nephronophthisis, cerebellar vermis hypoplasia and situs inversus. 1 Publication
    Corresponds to variant rs200585917 [ dbSNP | Ensembl ].
    VAR_068501
    Natural varianti1277 – 12771H → Y in JBTS19. 1 Publication
    VAR_068502

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC112315 mRNA. Translation: AAI12316.1.
    BC112317 mRNA. Translation: AAI12318.1.
    AF221712 mRNA. Translation: AAF28354.1.
    AB018303 mRNA. Translation: BAA34480.2.
    CCDSiCCDS32445.1.
    RefSeqiNP_001258549.1. NM_001271620.1.
    NP_055884.2. NM_015069.3.
    XP_005255913.1. XM_005255856.2.
    UniGeneiHs.530930.
    Hs.744482.

    Genome annotation databases

    EnsembliENST00000262383; ENSP00000262383; ENSG00000102935.
    ENST00000561648; ENSP00000455426; ENSG00000102935.
    ENST00000562520; ENSP00000457664; ENSG00000102935.
    ENST00000562871; ENSP00000457928; ENSG00000102935.
    ENST00000563137; ENSP00000455588; ENSG00000102935.
    GeneIDi23090.
    KEGGihsa:23090.
    UCSCiuc010vgn.3. human.

    Polymorphism databases

    DMDMi121941357.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC112315 mRNA. Translation: AAI12316.1 .
    BC112317 mRNA. Translation: AAI12318.1 .
    AF221712 mRNA. Translation: AAF28354.1 .
    AB018303 mRNA. Translation: BAA34480.2 .
    CCDSi CCDS32445.1.
    RefSeqi NP_001258549.1. NM_001271620.1.
    NP_055884.2. NM_015069.3.
    XP_005255913.1. XM_005255856.2.
    UniGenei Hs.530930.
    Hs.744482.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MDG NMR - A 928-981 [» ]
    ProteinModelPortali Q2M1K9.
    SMRi Q2M1K9. Positions 32-352, 641-827, 928-981, 1115-1142, 1168-1284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116718. 9 interactions.
    IntActi Q2M1K9. 9 interactions.
    MINTi MINT-2819859.
    STRINGi 9606.ENSP00000262383.

    PTM databases

    PhosphoSitei Q2M1K9.

    Polymorphism databases

    DMDMi 121941357.

    Proteomic databases

    PaxDbi Q2M1K9.
    PRIDEi Q2M1K9.

    Protocols and materials databases

    DNASUi 23090.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262383 ; ENSP00000262383 ; ENSG00000102935 .
    ENST00000561648 ; ENSP00000455426 ; ENSG00000102935 .
    ENST00000562520 ; ENSP00000457664 ; ENSG00000102935 .
    ENST00000562871 ; ENSP00000457928 ; ENSG00000102935 .
    ENST00000563137 ; ENSP00000455588 ; ENSG00000102935 .
    GeneIDi 23090.
    KEGGi hsa:23090.
    UCSCi uc010vgn.3. human.

    Organism-specific databases

    CTDi 23090.
    GeneCardsi GC16M049524.
    HGNCi HGNC:16762. ZNF423.
    HPAi HPA015258.
    MIMi 604557. gene.
    614844. phenotype.
    neXtProti NX_Q2M1K9.
    Orphaneti 2318. Joubert syndrome with oculorenal defect.
    PharmGKBi PA134903681.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000155793.
    HOVERGENi HBG052773.
    OMAi FIEHCQM.
    OrthoDBi EOG7NGQB0.
    PhylomeDBi Q2M1K9.
    TreeFami TF331504.

    Miscellaneous databases

    GeneWikii ZNF423.
    GenomeRNAii 23090.
    NextBioi 44239.
    PROi Q2M1K9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q2M1K9.
    Bgeei Q2M1K9.
    CleanExi HS_ZNF423.
    Genevestigatori Q2M1K9.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 4 hits.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 30 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 27 hits.
    PS50157. ZINC_FINGER_C2H2_2. 23 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiZN423_HUMAN
    AccessioniPrimary (citable) accession number: Q2M1K9
    Secondary accession number(s): O94860, Q76N04, Q9NZ13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 94 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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

    External Data

    Dasty 3