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Q61624

- ZN148_MOUSE

UniProt

Q61624 - ZN148_MOUSE

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Protein
Zinc finger protein 148
Gene
Znf148, Zbp89, Zfp148
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri171 – 19323C2H2-type 1
Add
BLAST
Zinc fingeri199 – 22123C2H2-type 2
Add
BLAST
Zinc fingeri227 – 24923C2H2-type 3
Add
BLAST
Zinc fingeri255 – 27824C2H2-type 4
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. double-stranded DNA binding Source: Ensembl
  3. metal ion binding Source: UniProtKB-KW
  4. sequence-specific DNA binding transcription factor activity Source: MGI
  5. transcription regulatory region sequence-specific DNA binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. gamete generation Source: MGI
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  4. protein complex assembly Source: Ensembl
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 148
Alternative name(s):
Beta enolase repressor factor 1
G-rich box-binding protein
Transcription factor BFCOL1
Transcription factor ZBP-89
Zinc finger DNA-binding protein 89
Gene namesi
Name:Znf148
Synonyms:Zbp89, Zfp148
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1332234. Zfp148.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 794794Zinc finger protein 148
PRO_0000047428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Phosphothreonine By similarity
Modified residuei250 – 2501Phosphoserine By similarity
Modified residuei306 – 3061Phosphoserine By similarity
Modified residuei412 – 4121Phosphoserine By similarity
Modified residuei607 – 6071N6-acetyllysine By similarity
Modified residuei665 – 6651Phosphoserine By similarity
Modified residuei784 – 7841Phosphoserine By similarity

Post-translational modificationi

Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ61624.
PRIDEiQ61624.

PTM databases

PhosphoSiteiQ61624.

Expressioni

Tissue specificityi

Strong expression detected in brain, lung, liver and kidney, with lower levels detected in spleen, skeletal muscle, testis and heart.1 Publication

Developmental stagei

Detected in embryos from E7 to E17. Expression decreases in developing skeletal muscles.2 Publications

Gene expression databases

ArrayExpressiQ61624.
BgeeiQ61624.
CleanExiMM_ZFP148.
GenevestigatoriQ61624.

Interactioni

Subunit structurei

Interacts with HNRNPDL By similarity. Interacts with the 5FMC complex; the interaction requires association with CHTOP.1 Publication

Protein-protein interaction databases

BioGridi204640. 1 interaction.
IntActiQ61624. 1 interaction.
MINTiMINT-4140637.
STRINGi10090.ENSMUSP00000087106.

Structurei

3D structure databases

ProteinModelPortaliQ61624.
SMRiQ61624. Positions 138-296.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063238.
HOGENOMiHOG000293204.
HOVERGENiHBG054247.
InParanoidiQ61624.
OMAiNDAYLNN.
OrthoDBiEOG76QFGM.
PhylomeDBiQ61624.
TreeFamiTF331779.

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]
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61624-1 [UniParc]FASTAAdd to Basket

« Hide

MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSAVSG ELQESVLQDR    50
SLPHQEILAA DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMDTHERL 100
PQGLQYALNV PISVKQEITF TDVSEQLMRD KKQVREPVDL QKKKKRKQRS 150
PAKILTINED GSLGLKTPKS HVCEHCNAAF RTNYHLQRHV FIHTGEKPFQ 200
CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY HMERHKRTHS 250
GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED 300
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SVLDKSDLKK DKNDYLPLYS 350
SSTKVKDEYM VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS 400
LKQPLEQSQT ISPLSSYEDS KVSKYAFELV DKQALLDSEG SADIDQVDNL 450
QEGPSKPVHS STNYDDAMQF LKKKRYLQAA SNNSREYALN VGTIASQPSV 500
TQAAVASVID ESTTASILDS QALNVEIKSN HDKNVIPDEV LQTLLDHYSH 550
KPNGQHEISF SVADTEVTSS ISINSSDVPE VTQSENVGSS SQASSSDKAN 600
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNP PAFSSIDKQV 650
YAAMPINSFR SGMNSPLRTT PDKSHFGLIV GDSQHPFPFS GDETNHASAT 700
STADFLDQVT SQKKAEAQPV HQAYQMSSFE QPFRAPYHGS RAGIATQFST 750
ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG MTSSPDATTG QTFG 794
Length:794
Mass (Da):88,751
Last modified:June 1, 1998 - v2
Checksum:i4CB1C2A1822703FD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti283 – 2831K → N in AAB38507. 1 Publication
Sequence conflicti314 – 3141K → P in AAB38507. 1 Publication
Sequence conflicti319 – 3191K → Q in AAB38507. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98096 mRNA. Translation: CAA66725.1.
BC026144 mRNA. Translation: AAH26144.1.
U80078 mRNA. Translation: AAB38507.1.
CCDSiCCDS28130.1.
RefSeqiNP_035879.1. NM_011749.4.
XP_006522165.1. XM_006522102.1.
UniGeneiMm.392667.

Genome annotation databases

EnsembliENSMUST00000089677; ENSMUSP00000087106; ENSMUSG00000022811.
ENSMUST00000165418; ENSMUSP00000126338; ENSMUSG00000022811.
GeneIDi22661.
KEGGimmu:22661.
UCSCiuc007zab.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98096 mRNA. Translation: CAA66725.1 .
BC026144 mRNA. Translation: AAH26144.1 .
U80078 mRNA. Translation: AAB38507.1 .
CCDSi CCDS28130.1.
RefSeqi NP_035879.1. NM_011749.4.
XP_006522165.1. XM_006522102.1.
UniGenei Mm.392667.

3D structure databases

ProteinModelPortali Q61624.
SMRi Q61624. Positions 138-296.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204640. 1 interaction.
IntActi Q61624. 1 interaction.
MINTi MINT-4140637.
STRINGi 10090.ENSMUSP00000087106.

PTM databases

PhosphoSitei Q61624.

Proteomic databases

PaxDbi Q61624.
PRIDEi Q61624.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089677 ; ENSMUSP00000087106 ; ENSMUSG00000022811 .
ENSMUST00000165418 ; ENSMUSP00000126338 ; ENSMUSG00000022811 .
GeneIDi 22661.
KEGGi mmu:22661.
UCSCi uc007zab.1. mouse.

Organism-specific databases

CTDi 22661.
MGIi MGI:1332234. Zfp148.

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00530000063238.
HOGENOMi HOG000293204.
HOVERGENi HBG054247.
InParanoidi Q61624.
OMAi NDAYLNN.
OrthoDBi EOG76QFGM.
PhylomeDBi Q61624.
TreeFami TF331779.

Miscellaneous databases

ChiTaRSi ZNF148. mouse.
NextBioi 303071.
PROi Q61624.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61624.
Bgeei Q61624.
CleanExi MM_ZFP148.
Genevestigatori Q61624.

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 ]
SMARTi SM00355. ZnF_C2H2. 4 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Negative regulation of beta enolase gene transcription in embryonic muscle is dependent upon a zinc finger factor that binds to the G-rich box within the muscle-specific enhancer."
    Passantino R., Antona V., Barbieri G., Rubino P., Melchionna R., Cossu G., Feo S., Giallongo A.
    J. Biol. Chem. 273:484-494(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: CD-1.
    Tissue: Limb.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. "Cloning and characterization of a transcription factor that binds to the proximal promoters of the two mouse type I collagen genes."
    Hasegawa T., Takeuchi A., Miyaishi O., Isobe K., de Crombrugghe B.
    J. Biol. Chem. 272:4915-4923(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-794.
  4. "ZBP-89, a Kruppel-like zinc finger protein, inhibits epidermal growth factor induction of the gastrin promoter."
    Merchant J.L., Iyer G.R., Taylor B.R., Kitchen J.R., Mortensen E.R., Wang Z., Flintoft R.J., Michel J., Bassel-Duby R.
    Mol. Cell. Biol. 16:6644-6653(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
    Tissue: Pituitary adenoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."
    Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.
    Mol. Cell. Proteomics 11:1263-1273(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE 5FMC COMPLEX AND CHTOP, SUMOYLATION, DESUMOYLATION BY SENP3.

Entry informationi

Entry nameiZN148_MOUSE
AccessioniPrimary (citable) accession number: Q61624
Secondary accession number(s): P97475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi