[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Colon; 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).
[2]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).

Comments

FUNCTION: May be involved in transcriptional regulation.
INTERACTION:
P36575:ARR3; NbExp=1; IntAct=EBI-743906, EBI-718116;
SUBCELLULAR LOCATION: Nucleus (Probable).
SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.
SIMILARITY: Contains 5 C2H2-type zinc fingers.
SIMILARITY: Contains 1 KRAB domain.
SIMILARITY: Contains 1 SCAN box domain.

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

BC007263; AAH07263.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00063800; -.

NP_116141.1; -.

3D structure databases

ModBase

Q96IT1.

Protein-protein interaction databases

IntAct

Q96IT1; 2.

PTM databases

PhosphoSite

Q96IT1; -.

Organism-specific databases

GC01M245527; -.

HGNC:23713; ZNF496.

PA134888470; -.

Gene expression databases

Q96IT1; -.

Q96IT1; -.

HS_ZNF496; -.

ENSG00000162714; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003700;	Molecular function: transcription factor activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (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

IPR001909; Krueppel-associated_box.
IPR003309; Treg_SCAN.
IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
IPR013087; Znf_C2H2/integrase_DNA-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.

Pfam

PF01352; KRAB; 1.
PF02023; SCAN; 1.
PF00096; zf-C2H2; 5.
Pfam graphical view of domain structure.

ProDom

PD000003; Znf_C2H2; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00349; KRAB; 1.
SM00431; SCAN; 1.
SM00355; ZnF_C2H2; 5.
SMART graphical view of domain structure.

PROSITE

PS50805; KRAB; 1.
PS50804; SCAN_BOX; 1.
PS00028; ZINC_FINGER_C2H2_1; 4.
PS50157; ZINC_FINGER_C2H2_2; 5.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q96IT1; -.

Genome annotation databases

Ensembl

ENSG00000162714; Homo sapiens. [Contig view]

GeneID

84838; -.

KEGG

hsa:84838; -.

Phylogenomic databases

HOGENOM

Q96IT1; -.

HOVERGEN

Q96IT1; -.

Other

75061; -.

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

Keywords

DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 587`	`587`	`Zinc finger protein 496.`	`PRO_0000047617`
`DOMAIN`	`42 124`	`83`	`SCAN box.`
`DOMAIN`	`221 291`	`71`	`KRAB.`
`ZN_FING`	`406 428`	`23`	`C2H2-type 1; degenerate.`
`ZN_FING`	`435 457`	`23`	`C2H2-type 2.`
`ZN_FING`	`463 485`	`23`	`C2H2-type 3.`
`ZN_FING`	`522 545`	`24`	`C2H2-type 4.`
`ZN_FING`	`553 575`	`23`	`C2H2-type 5.`
`MOD_RES`	`185 185`		`Phosphoserine.`

Sequence information

Length: 587 AA [This is the length of the unprocessed precursor]

Molecular weight: 66908 Da [This is the MW of the unprocessed precursor]

CRC64: 72A4F4D5CD309013 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTALCPRVL APKESEEPRK MRSPPGENPS PQGELPSPES SRRLFRRFRY QEAAGPREAL 

        70         80         90        100        110        120 
QRLWDLCGGW LRPERHTKEQ ILELLVLEQF LAILPREIQS WVRAQEPESG EQAVAAVEAL 

       130        140        150        160        170        180 
EREPGRPWQW LKHCEDPVVI DDGDSPLDQE QEQLPVEPHS DLAKNQDAQP ITLAQCLGLP 

       190        200        210        220        230        240 
SRPPSQLSGD PVLQDAFLLQ EENVRDTQQV TTLQLPPSRV SPFKDMILCF SEEDWSLLDP 

       250        260        270        280        290        300 
AQTGFYGEFI IGEDYGVSMP PNDLAAQPDL SQGEENEPRV PELQDLQGKE VPQVSYLDSP 

       310        320        330        340        350        360 
SLQPFQVEER RKREELQVPE FQACPQTVVP QNTYPAGGNP RSLENSLDEE VTIEIVLSSS 

       370        380        390        400        410        420 
GDEDSQHGPY CTEELGSPTE KQRSLPASHR SSTEAGGEVQ TSKKSYVCPN CGKIFRWRVN 

       430        440        450        460        470        480 
FIRHLRSRRE QEKPHECSVC GELFSDSEDL DGHLESHEAQ KPYRCGACGK SFRLNSHLLS 

       490        500        510        520        530        540 
HRRIHLQPDR LQPVEKREQA ASEDADKGPK EPLENGKAKL SFQCCECGKA FQRHDHLARH 

       550        560        570        580 
RSHFHLKDKA RPFQCRYCVK SFTQNYDLLR HERLHMKRRS KQALNSY

Q96IT1 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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