ID   ZN496_HUMAN             Reviewed;         587 AA.
AC   Q96IT1;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   19-JAN-2010, entry version 61.
DE   RecName: Full=Zinc finger protein 496;
DE   AltName: Full=Zinc finger protein with KRAB and SCAN domains 17;
GN   Name=ZNF496; Synonyms=ZKSCAN17;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       P36575:ARR3; NbExp=1; IntAct=EBI-743906, EBI-718116;
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 KRAB domain.
CC   -!- SIMILARITY: Contains 1 SCAN box domain.
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DR   EMBL; BC007263; AAH07263.1; -; mRNA.
DR   IPI; IPI00063800; -.
DR   RefSeq; NP_116141.1; -.
DR   UniGene; Hs.654803; -.
DR   SMR; Q96IT1; 33-126, 403-575.
DR   IntAct; Q96IT1; 2.
DR   STRING; Q96IT1; -.
DR   PhosphoSite; Q96IT1; -.
DR   PRIDE; Q96IT1; -.
DR   Ensembl; ENST00000294753; ENSP00000294753; ENSG00000162714; Homo sapiens.
DR   GeneID; 84838; -.
DR   KEGG; hsa:84838; -.
DR   UCSC; uc001ico.1; human.
DR   CTD; 84838; -.
DR   GeneCards; GC01M245527; -.
DR   HGNC; HGNC:23713; ZNF496.
DR   PharmGKB; PA134888470; -.
DR   HOVERGEN; Q96IT1; -.
DR   OrthoDB; EOG9M683T; -.
DR   PhylomeDB; Q96IT1; -.
DR   NextBio; 75061; -.
DR   ArrayExpress; Q96IT1; -.
DR   Bgee; Q96IT1; -.
DR   CleanEx; HS_ZNF496; -.
DR   Genevestigator; Q96IT1; -.
DR   GermOnline; ENSG00000162714; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR003309; Treg_SCAN.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    587       Zinc finger protein 496.
FT                                /FTId=PRO_0000047617.
FT   DOMAIN       42    124       SCAN box.
FT   DOMAIN      221    291       KRAB.
FT   ZN_FING     406    428       C2H2-type 1; degenerate.
FT   ZN_FING     435    457       C2H2-type 2.
FT   ZN_FING     463    485       C2H2-type 3.
FT   ZN_FING     522    545       C2H2-type 4.
FT   ZN_FING     553    575       C2H2-type 5.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
SQ   SEQUENCE   587 AA;  66908 MW;  72A4F4D5CD309013 CRC64;
     MPTALCPRVL APKESEEPRK MRSPPGENPS PQGELPSPES SRRLFRRFRY QEAAGPREAL
     QRLWDLCGGW LRPERHTKEQ ILELLVLEQF LAILPREIQS WVRAQEPESG EQAVAAVEAL
     EREPGRPWQW LKHCEDPVVI DDGDSPLDQE QEQLPVEPHS DLAKNQDAQP ITLAQCLGLP
     SRPPSQLSGD PVLQDAFLLQ EENVRDTQQV TTLQLPPSRV SPFKDMILCF SEEDWSLLDP
     AQTGFYGEFI IGEDYGVSMP PNDLAAQPDL SQGEENEPRV PELQDLQGKE VPQVSYLDSP
     SLQPFQVEER RKREELQVPE FQACPQTVVP QNTYPAGGNP RSLENSLDEE VTIEIVLSSS
     GDEDSQHGPY CTEELGSPTE KQRSLPASHR SSTEAGGEVQ TSKKSYVCPN CGKIFRWRVN
     FIRHLRSRRE QEKPHECSVC GELFSDSEDL DGHLESHEAQ KPYRCGACGK SFRLNSHLLS
     HRRIHLQPDR LQPVEKREQA ASEDADKGPK EPLENGKAKL SFQCCECGKA FQRHDHLARH
     RSHFHLKDKA RPFQCRYCVK SFTQNYDLLR HERLHMKRRS KQALNSY
//