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Q8N5A5 (ZGPAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger CCCH-type with G patch domain-containing protein
Alternative name(s):
G patch domain-containing protein 6
Zinc finger CCCH domain-containing protein 9
Zinc finger and G patch domain-containing protein
Gene names
Name:ZGPAT
Synonyms:GPATC6, GPATCH6, KIAA1847, ZC3H9, ZC3HDC9, ZIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription repressor that specifically binds the 5'-GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by recruiting the chromatin multiprotein complex NuRD to target promoters. Negatively regulates expression of EGFR, a gene involved in cell proliferation, survival and migration. Its ability to repress genes of the EGFR pathway suggest it may act as a tumor suppressor. Able to suppress breast carcinogenesis. Ref.7 Ref.8

Isoform 4:Antagonizes the transcription repression by isoform 1 by competing for the binding of the NuRD complex. Does not bind DNA. Ref.7 Ref.8

Subunit structure

Interacts with CHD4/Mi-2; the interaction is direct. Ref.7

Subcellular location

Nucleus Ref.7 Ref.8.

Isoform 4: Nucleus Ref.7 Ref.8.

Tissue specificity

Widely expressed. Ref.7

Induction

Down-regulated in breast carcinomas.

Post-translational modification

Ubiquitinated in case of infection by HIV-1, leading to its degradation. Ubiquitination is mediated by the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex that is hijacked by HIV-1 via interaction between HIV-1 Vpr and DCAF1/VPRBP. Ref.11

Sequence similarities

Contains 1 C3H1-type zinc finger.

Contains 1 G-patch domain.

Sequence caution

The sequence BAB47476.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAC11317.1 differs from that shown. Reason: Frameshift at position 290.

The sequence CAI95713.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N5A5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q8N5A5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     291-310: Missing.
Isoform 3 (identifier: Q8N5A5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     282-310: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8N5A5-4)

Also known as: sZIP;

The sequence of this isoform differs from the canonical sequence as follows:
     1-343: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Zinc finger CCCH-type with G patch domain-containing protein
PRO_0000213894

Regions

Domain333 – 37947G-patch
Zinc finger175 – 20127C3H1-type
Compositional bias119 – 12810Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10

Natural variations

Alternative sequence1 – 343343Missing in isoform 4.
VSP_053599
Alternative sequence282 – 31029Missing in isoform 3.
VSP_038121
Alternative sequence291 – 31020Missing in isoform 2.
VSP_007754
Natural variant611S → R. Ref.1 Ref.3 Ref.5 Ref.6
Corresponds to variant rs1291212 [ dbSNP | Ensembl ].
VAR_025539

Experimental info

Sequence conflict1841L → Q in BAB55426. Ref.3
Sequence conflict1881C → R in BAC11317. Ref.3
Sequence conflict3441M → V in BAB55426. Ref.3
Sequence conflict4331G → R in AAH19338. Ref.6
Sequence conflict5191Q → R in BAB55426. Ref.3

Secondary structure

.......................... 531
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 15, 2007. Version 3.
Checksum: 36572156BABDA876

FASTA53157,359
        10         20         30         40         50         60 
MDEESLESAL QTYRAQLQQV ELALGAGLDS SEQADLRQLQ GDLKELIELT EASLVSVRKS 

        70         80         90        100        110        120 
SLLAALDEER PGRQEDAEYQ AFREAITEAV EAPAAARGSG SETVPKAEAG PESAAGGQEE 

       130        140        150        160        170        180 
EEGEDEEELS GTKVSAPYYS SWGTLEYHNA MVVGTEEAED GSAGVRVLYL YPTHKSLKPC 

       190        200        210        220        230        240 
PFFLEGKCRF KENCRFSHGQ VVSLDELRPF QDPDLSSLQA GSACLAKHQD GLWHAARITD 

       250        260        270        280        290        300 
VDNGYYTVKF DSLLLREAVV EGDGILPPLR TEATESDSDS DGTGDSSYAR VVGSDAVDSA 

       310        320        330        340        350        360 
QSSALCPSLA VVGSDAVDSG TCSSAFAGWE VHTRGIGSRL LTKMGYEFGK GLGRHAEGRV 

       370        380        390        400        410        420 
EPIHAVVLPR GKSLDQCVET LQKQTRVGKA GTNKPPRCRG RGARPGGRPA PRNVFDFLNE 

       430        440        450        460        470        480 
KLQGQAPGAL EAGAAPAGRR SKDMYHASKS AKRALSLRLF QTEEKIERTQ RDIRSIQEAL 

       490        500        510        520        530 
ARNAGRHSVA SAQLQEKLAG AQRQLGQLRA QEAGLQQEQR KADTHKKMTE F 

« Hide

Isoform 2 [UniParc].

Checksum: 5007C362ECC2CD79
Show »

FASTA51155,500
Isoform 3 [UniParc].

Checksum: 8DD60FEEDB37D2F9
Show »

FASTA50254,605
Isoform 4 (sZIP) [UniParc].

Checksum: 00ABC2D9BC65E7C9
Show »

FASTA18820,697

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ARG-61.
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-61.
Tissue: Thyroid.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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], VARIANT ARG-61.
[6]"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] (ISOFORMS 2 AND 3), VARIANT ARG-61.
Tissue: Placenta and Uterus.
[7]"ZIP: a novel transcription repressor, represses EGFR oncogene and suppresses breast carcinogenesis."
Li R., Zhang H., Yu W., Chen Y., Gui B., Liang J., Wang Y., Sun L., Yang X., Zhang Y., Shi L., Li Y., Shang Y.
EMBO J. 28:2763-2776(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, TISSUE SPECIFICITY, INTERACTION WITH CHD4.
[8]"sZIP, an alternative splice variant of ZIP, antagonizes transcription repression and growth inhibition by ZIP."
Yu W., Li R., Gui B., Shang Y.
J. Biol. Chem. 285:14301-14307(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 4), FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"HIV-1 Vpr Induces the Degradation of ZIP and sZIP, Adaptors of the NuRD Chromatin Remodeling Complex, by Hijacking DCAF1/VprBP."
Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C., Bouaziz S., Ramirez B.C., Margottin-Goguet F.
PLoS ONE 8:E77320-E77320(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[12]"Crystal structure of the zinc finger of ZGPAT."
Structural genomics consortium (SGC)
Submitted (FEB-2013) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 120-268 IN COMPLEX WITH ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB058750 mRNA. Translation: BAB47476.3. Different initiation.
AK027878 mRNA. Translation: BAB55426.1.
AK074961 mRNA. Translation: BAC11317.1. Frameshift.
AL121845 Genomic DNA. Translation: CAC03670.1.
AL121845 Genomic DNA. Translation: CAI21879.1.
AL121845 Genomic DNA. Translation: CAI21880.1.
AL121845 Genomic DNA. Translation: CAI95713.1. Sequence problems.
CH471077 Genomic DNA. Translation: EAW75223.1.
CH471077 Genomic DNA. Translation: EAW75226.1.
BC019338 mRNA. Translation: AAH19338.1.
BC032612 mRNA. Translation: AAH32612.1.
CCDSCCDS13534.1. [Q8N5A5-1]
CCDS13535.1. [Q8N5A5-2]
CCDS56203.1. [Q8N5A5-3]
RefSeqNP_001076582.1. NM_001083113.1. [Q8N5A5-2]
NP_001182582.1. NM_001195653.1. [Q8N5A5-2]
NP_001182583.1. NM_001195654.1. [Q8N5A5-3]
NP_115916.3. NM_032527.4. [Q8N5A5-1]
NP_852150.2. NM_181485.2. [Q8N5A5-2]
UniGeneHs.590868.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4II1X-ray2.65A/B/C/D120-268[»]
ProteinModelPortalQ8N5A5.
SMRQ8N5A5. Positions 127-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124150. 8 interactions.
IntActQ8N5A5. 19 interactions.
MINTMINT-2810381.

PTM databases

PhosphoSiteQ8N5A5.

Polymorphism databases

DMDM147744602.

Proteomic databases

MaxQBQ8N5A5.
PaxDbQ8N5A5.
PRIDEQ8N5A5.

Protocols and materials databases

DNASU84619.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328969; ENSP00000332013; ENSG00000197114. [Q8N5A5-1]
ENST00000355969; ENSP00000348242; ENSG00000197114. [Q8N5A5-2]
ENST00000357119; ENSP00000349634; ENSG00000197114. [Q8N5A5-3]
ENST00000369967; ENSP00000358984; ENSG00000197114. [Q8N5A5-2]
ENST00000448100; ENSP00000391176; ENSG00000197114. [Q8N5A5-2]
GeneID84619.
KEGGhsa:84619.
UCSCuc002ygi.2. human. [Q8N5A5-2]
uc002ygk.3. human. [Q8N5A5-1]
uc002ygm.3. human. [Q8N5A5-3]

Organism-specific databases

CTD84619.
GeneCardsGC20P062338.
H-InvDBHIX0138076.
HGNCHGNC:15948. ZGPAT.
HPAHPA043248.
neXtProtNX_Q8N5A5.
PharmGKBPA134881248.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241375.
HOVERGENHBG056371.
InParanoidQ8N5A5.
OMAKEIYHAS.
OrthoDBEOG71RXK5.
PhylomeDBQ8N5A5.
TreeFamTF105970.

Gene expression databases

BgeeQ8N5A5.
CleanExHS_ZGPAT.
GenevestigatorQ8N5A5.

Family and domain databases

Gene3D4.10.1000.10. 1 hit.
InterProIPR000467. G_patch_dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamPF01585. G-patch. 1 hit.
[Graphical view]
SMARTSM00443. G_patch. 1 hit.
SM00356. ZnF_C3H1. 1 hit.
[Graphical view]
PROSITEPS50174. G_PATCH. 1 hit.
PS50103. ZF_C3H1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZGPAT. human.
GeneWikiZGPAT.
GenomeRNAi84619.
NextBio74496.
PROQ8N5A5.

Entry information

Entry nameZGPAT_HUMAN
AccessionPrimary (citable) accession number: Q8N5A5
Secondary accession number(s): E1P5K1 expand/collapse secondary AC list , Q4VXN9, Q5JWI9, Q5JWJ0, Q8NC55, Q8WUV4, Q96JI0, Q96JU4, Q9H401
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: May 15, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 3 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

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 20

Human chromosome 20: entries, gene names and cross-references to MIM