ZN496_HUMAN
ID ZN496_HUMAN Reviewed; 587 AA.
AC Q96IT1; Q8TBS2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 112-587 (ISOFORM 2).
RC TISSUE=Colon, and Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic 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).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-403 AND LYS-496, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: DNA-binding transcription factor that can both act as an
CC activator and a repressor. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via zinc-fingers) with JARID2. Interacts with NSD1
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96IT1; P36575: ARR3; NbExp=6; IntAct=EBI-743906, EBI-718116;
CC Q96IT1; P36575-2: ARR3; NbExp=3; IntAct=EBI-743906, EBI-11977533;
CC Q96IT1; Q96JS3: PGBD1; NbExp=6; IntAct=EBI-743906, EBI-10290053;
CC Q96IT1; O76064: RNF8; NbExp=3; IntAct=EBI-743906, EBI-373337;
CC Q96IT1; P57086: SCAND1; NbExp=3; IntAct=EBI-743906, EBI-745846;
CC Q96IT1; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-743906, EBI-5235340;
CC Q96IT1; P61956: SUMO2; NbExp=3; IntAct=EBI-743906, EBI-473220;
CC Q96IT1; P55854: SUMO3; NbExp=3; IntAct=EBI-743906, EBI-474067;
CC Q96IT1; A0A0S2Z6X0: ZKSCAN4; NbExp=3; IntAct=EBI-743906, EBI-16431094;
CC Q96IT1; Q969J2: ZKSCAN4; NbExp=10; IntAct=EBI-743906, EBI-2818641;
CC Q96IT1; Q9NWS9-2: ZNF446; NbExp=7; IntAct=EBI-743906, EBI-740232;
CC Q96IT1; Q6P088: ZNF483; NbExp=3; IntAct=EBI-743906, EBI-10196963;
CC Q96IT1; O43309: ZSCAN12; NbExp=3; IntAct=EBI-743906, EBI-1210440;
CC Q96IT1; Q9Y5A6: ZSCAN21; NbExp=6; IntAct=EBI-743906, EBI-10281938;
CC Q96IT1; P10073: ZSCAN22; NbExp=7; IntAct=EBI-743906, EBI-10178224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IT1-2; Sequence=VSP_038755;
CC -!- DOMAIN: The C2H2-type zinc finger 1, also named C2HR, mediates the
CC interaction with NSD1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC104335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007263; AAH07263.1; -; mRNA.
DR EMBL; BC025794; AAH25794.1; -; mRNA.
DR CCDS; CCDS1631.1; -. [Q96IT1-1]
DR RefSeq; NP_116141.1; NM_032752.2. [Q96IT1-1]
DR RefSeq; XP_005273385.1; XM_005273328.3.
DR AlphaFoldDB; Q96IT1; -.
DR SMR; Q96IT1; -.
DR BioGRID; 124291; 56.
DR IntAct; Q96IT1; 37.
DR MINT; Q96IT1; -.
DR STRING; 9606.ENSP00000294753; -.
DR iPTMnet; Q96IT1; -.
DR PhosphoSitePlus; Q96IT1; -.
DR BioMuta; ZNF496; -.
DR DMDM; 55976755; -.
DR EPD; Q96IT1; -.
DR jPOST; Q96IT1; -.
DR MassIVE; Q96IT1; -.
DR MaxQB; Q96IT1; -.
DR PaxDb; Q96IT1; -.
DR PeptideAtlas; Q96IT1; -.
DR PRIDE; Q96IT1; -.
DR ProteomicsDB; 76850; -. [Q96IT1-1]
DR ProteomicsDB; 76851; -. [Q96IT1-2]
DR Antibodypedia; 20839; 162 antibodies from 27 providers.
DR DNASU; 84838; -.
DR Ensembl; ENST00000294753.8; ENSP00000294753.4; ENSG00000162714.13. [Q96IT1-1]
DR Ensembl; ENST00000682384.1; ENSP00000507236.1; ENSG00000162714.13. [Q96IT1-1]
DR GeneID; 84838; -.
DR KEGG; hsa:84838; -.
DR MANE-Select; ENST00000682384.1; ENSP00000507236.1; NM_032752.3; NP_116141.1.
DR UCSC; uc001ico.4; human. [Q96IT1-1]
DR CTD; 84838; -.
DR DisGeNET; 84838; -.
DR GeneCards; ZNF496; -.
DR HGNC; HGNC:23713; ZNF496.
DR HPA; ENSG00000162714; Low tissue specificity.
DR MIM; 613911; gene.
DR neXtProt; NX_Q96IT1; -.
DR OpenTargets; ENSG00000162714; -.
DR PharmGKB; PA134888470; -.
DR VEuPathDB; HostDB:ENSG00000162714; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161967; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q96IT1; -.
DR OMA; EFQTCQQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q96IT1; -.
DR TreeFam; TF350829; -.
DR PathwayCommons; Q96IT1; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q96IT1; -.
DR BioGRID-ORCS; 84838; 5 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF496; human.
DR GenomeRNAi; 84838; -.
DR Pharos; Q96IT1; Tbio.
DR PRO; PR:Q96IT1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96IT1; protein.
DR Bgee; ENSG00000162714; Expressed in sural nerve and 167 other tissues.
DR ExpressionAtlas; Q96IT1; baseline and differential.
DR Genevisible; Q96IT1; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR027767; Zfp496.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226:SF180; PTHR23226:SF180; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
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 Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..587
FT /note="Zinc finger protein 496"
FT /id="PRO_0000047617"
FT DOMAIN 42..124
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 221..291
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 406..428
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..457
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..485
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..545
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 553..575
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 496
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 217
FT /note="P -> PRIFQFNNHRSNGYILEMLGSGGKKAQIISVLSQIYV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038755"
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
