[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMERIZATION, HETERODIMERIZATION WITH ZHX1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH NFYA. TISSUE=Testis; DOI=10.1042/BJ20030171; PubMed=12741956 [NCBI, ExPASy, EBI, Israel, Japan] Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M., Sekiguchi T., Kajitani T., Miyamoto K.; "Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family, functions as a transcriptional repressor."; Biochem. J. 373:747-757(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1093/dnares/5.6.355; PubMed=10048485 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."; DNA Res. 5:355-364(1998).
[3]	SEQUENCE REVISION. Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.; Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lymph; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	STRUCTURE BY NMR OF 524-601. RIKEN structural genomics initiative (RSGI); "Solution structure of the third homeobox domain of zinc fingers and homeoboxes protein 2."; Submitted (OCT-2006) to the PDB data bank.

Comments

FUNCTION: Acts as a transcriptional repressor.
SUBUNIT: Forms homodimers. Also forms heterodimers with ZHX1 and ZHX3. Heterodimerization with ZHX1 is not necessary for repressor activity. Interacts with NFYA.
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Ubiquitously expressed.
SIMILARITY: Belongs to the ZHX family.
SIMILARITY: Contains 2 C2H2-type zinc fingers.
SIMILARITY: Contains 4 homeobox DNA-binding domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB083653; BAC76615.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020661; BAA74877.2; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042145; AAH42145.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00007256; -.

NP_055758.1; -.

3D structure databases

PDB

2DMP; NMR; -; A=524-599.

[ExPASy / RCSB / EBI]

PDBsum

2DMP; -.

ModBase

Q9Y6X8.

Protein-protein interaction databases

IntAct

Q9Y6X8; 1.

PTM databases

PhosphoSite

Q9Y6X8; -.

Organism-specific databases

GC08P123863; -.

HIX0007759; -.

HGNC:18513; ZHX2.

609185; gene. [NCBI / EBI]

PharmGKB

PA128394591; -.

HUGE

KIAA0854.

Gene expression databases

ArrayExpress

Q9Y6X8; -.

Bgee

Q9Y6X8; -.

CleanEx

HS_ZHX2; -.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0043565;	Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003700;	Molecular function: transcription factor activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001356; Homeobox.
IPR017970; Homeobox_CS.
IPR012287; Homeodomain-rel.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.10.60; Homeodomain-rel; 3.

Pfam

PF00046; Homeobox; 3.
Pfam graphical view of domain structure.

SMART

SM00389; HOX; 4.
SM00355; ZnF_C2H2; 2.
SMART graphical view of domain structure.

PROSITE

PS00027; HOMEOBOX_1; FALSE_NEG.
PS50071; HOMEOBOX_2; 3.
PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
PS50157; ZINC_FINGER_C2H2_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q9Y6X8; -.

Genome annotation databases

Ensembl

ENSG00000178764; Homo sapiens. [Contig view]

GeneID

22882; -.

KEGG

hsa:22882; -.

Phylogenomic databases

HOGENOM

Q9Y6X8; -.

HOVERGEN

Q9Y6X8; -.

OMA

Q9Y6X8; LNEFTEH.

Other

43461; -.

ZHX2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; DNA-binding; Homeobox; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 837`	`837`	`Zinc fingers and homeoboxes protein 2.`	`PRO_0000049391`
`ZN_FING`	`78 101`	`24`	`C2H2-type 1.`
`ZN_FING`	`110 133`	`24`	`C2H2-type 2.`
`DNA_BIND`	`263 324`	`62`	`Homeobox 1.`
`DNA_BIND`	`439 501`	`63`	`Homeobox 2.`
`DNA_BIND`	`530 591`	`62`	`Homeobox 3.`
`DNA_BIND`	`628 690`	`63`	`Homeobox 4.`
`REGION`	`195 358`	`164`	`Required for homodimerization.`
`REGION`	`263 497`	`235`	`Required for interaction with NFYA.`
`REGION`	`263 446`	`184`	`Required for repressor activity.`
`REGION`	`317 446`	`130`	`Required for nuclear localization.`
`MOD_RES`	`16 16`		`Phosphoserine (By similarity).`
`VARIANT`	`357 357`	`1`	`V -> M (in dbSNP:rs9649951 [NCBI]).`	`VAR_049594`
`VARIANT`	`649 649`	`1`	`R -> K (in dbSNP:rs35319449 [NCBI]).`	`VAR_049595`
`VARIANT`	`779 779`	`1`	`G -> S (in dbSNP:rs3802264 [NCBI]).`	`VAR_049596`

Sequence information

Length: 837 AA [This is the length of the unprocessed precursor]

Molecular weight: 92307 Da [This is the MW of the unprocessed precursor]

CRC64: BE377ADF76D987D2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASKRKSTTP CMVRTSQVVE QDVPEEVDRA KEKGIGTPQP DVAKDSWAAE LENSSKENEV 

        70         80         90        100        110        120 
IEVKSMGESQ SKKLQGGYEC KYCPYSTQNL NEFTEHVDMQ HPNVILNPLY VCAECNFTTK 

       130        140        150        160        170        180 
KYDSLSDHNS KFHPGEANFK LKLIKRNNQT VLEQSIETTN HVVSITTSGP GTGDSDSGIS 

       190        200        210        220        230        240 
VSKTPIMKPG KPKADAKKVP KKPEEITPEN HVEGTARLVT DTAEILSRLG GVELLQDTLG 

       250        260        270        280        290        300 
HVMPSVQLPP NINLVPKVPV PLNTTKYNSA LDTNATMINS FNKFPYPTQA ELSWLTAASK 

       310        320        330        340        350        360 
HPEEHIRIWF ATQRLKHGIS WSPEEVEEAR KKMFNGTIQS VPPTITVLPA QLAPTKVTQP 

       370        380        390        400        410        420 
ILQTALPCQI LGQTSLVLTQ VTSGSTTVSC SPITLAVAGV TNHGQKRPLV TPQAAPEPKR 

       430        440        450        460        470        480 
PHIAQVPEPP PKVANPPLTP ASDRKKTKEQ IAHLKASFLQ SQFPDDAEVY RLIEVTGLAR 

       490        500        510        520        530        540 
SEIKKWFSDH RYRCQRGIVH ITSESLAKDQ LAIAASRHGR TYHAYPDFAP QKFKEKTQGQ 

       550        560        570        580        590        600 
VKILEDSFLK SSFPTQAELD RLRVETKLSR REIDSWFSER RKLRDSMEQA VLDSMGSGKK 

       610        620        630        640        650        660 
GQDVGAPNGA LSRLDQLSGA QLTSSLPSPS PAIAKSQEQV HLLRSTFART QWPTPQEYDQ 

       670        680        690        700        710        720 
LAAKTGLVRT EIVRWFKENR CLLKTGTVKW MEQYQHQPMA DDHGYDAVAR KATKPMAESP 

       730        740        750        760        770        780 
KNGGDVVPQY YKDPKKLCEE DLEKLVTRVK VGSEPAKDCL PAKPSEATSD RSEGSSRDGQ 

       790        800        810        820        830 
GSDENEESSV VDYVEVTVGE EDAISDRSDS WSQAAAEGVS ELAESDSDCV PAEAGQA

Q9Y6X8 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools