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Q61624 (ZN148_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Znf148
Synonyms:Zbp89, Zfp148
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

Interacts with HNRNPDL By similarity. Interacts with the 5FMC complex; the interaction requires association with CHTOP. Ref.6

Subcellular location

Nucleus.

Tissue specificity

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

Developmental stage

Detected in embryos from E7 to E17. Expression decreases in developing skeletal muscles. Ref.1 Ref.4

Post-translational modification

Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the stimulation of transcription of its target genes. Ref.6

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 4 C2H2-type zinc fingers.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 794794Zinc finger protein 148
PRO_0000047428

Regions

Zinc finger171 – 19323C2H2-type 1
Zinc finger199 – 22123C2H2-type 2
Zinc finger227 – 24923C2H2-type 3
Zinc finger255 – 27824C2H2-type 4

Amino acid modifications

Modified residue1941Phosphothreonine By similarity
Modified residue2501Phosphoserine By similarity
Modified residue3061Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Modified residue6071N6-acetyllysine By similarity
Modified residue6651Phosphoserine By similarity
Modified residue7841Phosphoserine By similarity

Experimental info

Sequence conflict2831K → N in AAB38507. Ref.3
Sequence conflict3141K → P in AAB38507. Ref.3
Sequence conflict3191K → Q in AAB38507. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q61624 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 4CB1C2A1822703FD

FASTA79488,751
        10         20         30         40         50         60 
MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSAVSG ELQESVLQDR SLPHQEILAA 

        70         80         90        100        110        120 
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMDTHERL PQGLQYALNV PISVKQEITF 

       130        140        150        160        170        180 
TDVSEQLMRD KKQVREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF 

       190        200        210        220        230        240 
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY 

       250        260        270        280        290        300 
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED 

       310        320        330        340        350        360 
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SVLDKSDLKK DKNDYLPLYS SSTKVKDEYM 

       370        380        390        400        410        420 
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQSQT ISPLSSYEDS 

       430        440        450        460        470        480 
KVSKYAFELV DKQALLDSEG SADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA 

       490        500        510        520        530        540 
SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILDS QALNVEIKSN HDKNVIPDEV 

       550        560        570        580        590        600 
LQTLLDHYSH KPNGQHEISF SVADTEVTSS ISINSSDVPE VTQSENVGSS SQASSSDKAN 

       610        620        630        640        650        660 
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNP PAFSSIDKQV YAAMPINSFR 

       670        680        690        700        710        720 
SGMNSPLRTT PDKSHFGLIV GDSQHPFPFS GDETNHASAT STADFLDQVT SQKKAEAQPV 

       730        740        750        760        770        780 
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG 

       790 
MTSSPDATTG QTFG 

« Hide

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98096 mRNA. Translation: CAA66725.1.
BC026144 mRNA. Translation: AAH26144.1.
U80078 mRNA. Translation: AAB38507.1.
CCDSCCDS28130.1.
RefSeqNP_035879.1. NM_011749.4.
XP_006522165.1. XM_006522102.1.
UniGeneMm.392667.

3D structure databases

ProteinModelPortalQ61624.
SMRQ61624. Positions 138-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204640. 1 interaction.
IntActQ61624. 1 interaction.
MINTMINT-4140637.
STRING10090.ENSMUSP00000087106.

PTM databases

PhosphoSiteQ61624.

Proteomic databases

PaxDbQ61624.
PRIDEQ61624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089677; ENSMUSP00000087106; ENSMUSG00000022811.
ENSMUST00000165418; ENSMUSP00000126338; ENSMUSG00000022811.
GeneID22661.
KEGGmmu:22661.
UCSCuc007zab.1. mouse.

Organism-specific databases

CTD22661.
MGIMGI:1332234. Zfp148.

Phylogenomic databases

eggNOGCOG5048.
GeneTreeENSGT00530000063238.
HOGENOMHOG000293204.
HOVERGENHBG054247.
InParanoidQ61624.
OMANDAYLNN.
OrthoDBEOG76QFGM.
PhylomeDBQ61624.
TreeFamTF331779.

Gene expression databases

ArrayExpressQ61624.
BgeeQ61624.
CleanExMM_ZFP148.
GenevestigatorQ61624.

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]
SMARTSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZNF148. mouse.
NextBio303071.
PROQ61624.
SOURCESearch...

Entry information

Entry nameZN148_MOUSE
AccessionPrimary (citable) accession number: Q61624
Secondary accession number(s): P97475
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot