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Q9UQR1 (ZN148_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Transcription factor ZBP-89
Zinc finger DNA-binding protein 89
Gene names
Name:ZNF148
Synonyms:ZBP89
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Subunit structure

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

Subcellular location

Nucleus.

Post-translational modification

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

Sequence similarities

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

Contains 4 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular defense response

Traceable author statement PubMed 8355710. Source: ProtInc

gamete generation

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from direct assay PubMed 12771217. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 9685330. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12771217. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

transcription from RNA polymerase II promoter

Traceable author statement PubMed 9685330. Source: ProtInc

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondouble-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding

Inferred from direct assay PubMed 12771217. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 794794Zinc finger protein 148
PRO_0000047427

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 Ref.8
Modified residue2501Phosphoserine Ref.8
Modified residue3061Phosphoserine Ref.7 Ref.8 Ref.10 Ref.12
Modified residue4121Phosphoserine Ref.8
Modified residue6071N6-acetyllysine Ref.11
Modified residue6651Phosphoserine Ref.12
Modified residue7841Phosphoserine Ref.8 Ref.10 Ref.12

Experimental info

Sequence conflict2871R → T in CAA15422. Ref.2
Sequence conflict3481L → V in CAA15422. Ref.2
Sequence conflict3791E → K in AAB57692. Ref.5
Sequence conflict4951A → R in CAA15422. Ref.2
Sequence conflict6161T → N in AAB57692. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9UQR1 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 50413723459EBD1F

FASTA79488,976
        10         20         30         40         50         60 
MNIDDKLEGL FLKCGGIDEM QSSRTMVVMG GVSGQSTVSG ELQDSVLQDR SMPHQEILAA 

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

       130        140        150        160        170        180 
TDVSEQLMRD KKQIREPVDL 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 SALDKSDLKK DKNDYLPLYS SSTKVKDEYM 

       370        380        390        400        410        420 
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQNQT ISPLSTYEES 

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

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

       550        560        570        580        590        600 
LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSEVPE VTPSENVGSS SQASSSDKAN 

       610        620        630        640        650        660 
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSIDKQV YATMPINSFR 

       670        680        690        700        710        720 
SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT STQDFLDQVT SQKKAEAQPV 

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

       790 
MTSSPDATTG QTFG 

« Hide

References

« Hide 'large scale' references
[1]"The human ZBP-89 homolog, located at chromosome 3q21, represses gastrin gene expression."
Law D.J., Tarle S.A., Merchant J.L.
Mamm. Genome 9:165-167(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human stromelysin gene promoter activity is modulated by transcription factor ZBP-89."
Ye S., Whatling C., Watkins H., Henney A.
FEBS Lett. 450:268-272(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Kidney.
[5]"The growth-regulating transcription factor ZBP-89 is located at human chromosome 3q21 and mouse chromosome 8B1."
Law D.J., Chen X.N., Korenberg J.R., Mortensen E.R., Merchant J.L.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-665.
[6]"Regulation of murine cytochrome c oxidase Vb gene expression during myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein (JKTBP1) reciprocally regulate transcription activity by physical interaction with the BERF-1/ZBP-89 factor."
Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M., Giallongo A., Avadhani N.G.
J. Biol. Chem. 279:35242-35254(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HNRNPDL.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-250; SER-306; SER-412 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-665 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039019 mRNA. Translation: AAC39926.1.
AJ236885 mRNA. Translation: CAA15422.1.
CH471052 Genomic DNA. Translation: EAW79394.1.
CH471052 Genomic DNA. Translation: EAW79395.1.
CH471052 Genomic DNA. Translation: EAW79396.1.
CH471052 Genomic DNA. Translation: EAW79398.1.
BC050260 mRNA. Translation: AAH50260.1.
U96633 Genomic DNA. Translation: AAB57692.1.
RefSeqNP_068799.2. NM_021964.2.
UniGeneHs.592591.

3D structure databases

ProteinModelPortalQ9UQR1.
SMRQ9UQR1. Positions 136-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113501. 12 interactions.
IntActQ9UQR1. 4 interactions.
STRING9606.ENSP00000353863.

PTM databases

PhosphoSiteQ9UQR1.

Polymorphism databases

DMDM12643385.

Proteomic databases

PaxDbQ9UQR1.
PRIDEQ9UQR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360647; ENSP00000353863; ENSG00000163848.
ENST00000484491; ENSP00000420335; ENSG00000163848.
ENST00000485866; ENSP00000420448; ENSG00000163848.
ENST00000492394; ENSP00000419322; ENSG00000163848.
GeneID7707.
KEGGhsa:7707.
UCSCuc003ehx.4. human.

Organism-specific databases

CTD7707.
GeneCardsGC03M124944.
HGNCHGNC:12933. ZNF148.
HPACAB017486.
HPA001656.
MIM601897. gene.
neXtProtNX_Q9UQR1.
PharmGKBPA37520.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000293204.
HOVERGENHBG054247.
InParanoidQ9UQR1.
OMANDAYLNN.
OrthoDBEOG76QFGM.
PhylomeDBQ9UQR1.
TreeFamTF331779.

Enzyme and pathway databases

SignaLinkQ9UQR1.

Gene expression databases

ArrayExpressQ9UQR1.
BgeeQ9UQR1.
CleanExHS_ZNF148.
GenevestigatorQ9UQR1.

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

GeneWikiZNF148.
GenomeRNAi7707.
NextBio29880.
PROQ9UQR1.
SOURCESearch...

Entry information

Entry nameZN148_HUMAN
AccessionPrimary (citable) accession number: Q9UQR1
Secondary accession number(s): D3DN27 expand/collapse secondary AC list , O00389, O43591, Q58EY5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: April 16, 2014
This is version 124 of the entry and version 2 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

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM