ZN496_MOUSE
ID ZN496_MOUSE Reviewed; 585 AA.
AC Q5SXI5; Q3TC40; Q3UTL1; Q8BKK0; Q8CGF9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein 496;
DE AltName: Full=NSD1-interacting zinc finger protein 1;
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 17;
GN Name=Znf496; Synonyms=Nizp11, Zfp496, Zkscan17;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH NSD1.
RX PubMed=15169884; DOI=10.1128/mcb.24.12.5184-5196.2004;
RA Nielsen A.L., Jorgensen P., Lerouge T., Cervino M., Chambon P., Losson R.;
RT "Nizp1, a novel multitype zinc finger protein that interacts with the NSD1
RT histone lysine methyltransferase through a unique C2HR motif.";
RL Mol. Cell. Biol. 24:5184-5196(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH JARID2.
RX PubMed=17521633; DOI=10.1016/j.febslet.2007.05.006;
RA Mysliwiec M.R., Kim T.G., Lee Y.;
RT "Characterization of zinc finger protein 496 that interacts with
RT Jumonji/JARID2.";
RL FEBS Lett. 581:2633-2640(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA-binding transcription factor that can both act as an
CC activator and a repressor. {ECO:0000269|PubMed:15169884,
CC ECO:0000269|PubMed:17521633}.
CC -!- SUBUNIT: Interacts (via zinc-fingers) with JARID2. Interacts with NSD1.
CC {ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}.
CC -!- INTERACTION:
CC Q5SXI5; Q62315: Jarid2; NbExp=6; IntAct=EBI-7417351, EBI-493592;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:15169884, ECO:0000269|PubMed:17521633}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5SXI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SXI5-2; Sequence=VSP_038769;
CC Name=3;
CC IsoId=Q5SXI5-3; Sequence=VSP_038768;
CC -!- DOMAIN: The C2H2-type zinc finger 1, also named C2HR, mediates the
CC interaction with NSD1.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY302242; AAQ73562.1; -; mRNA.
DR EMBL; AK051711; BAC34730.1; -; mRNA.
DR EMBL; AK139346; BAE23969.1; -; mRNA.
DR EMBL; AK155196; BAE33110.1; -; mRNA.
DR EMBL; AK155490; BAE33290.1; -; mRNA.
DR EMBL; AK170924; BAE42117.1; -; mRNA.
DR EMBL; AK170989; BAE42163.1; -; mRNA.
DR EMBL; AK171190; BAE42300.1; -; mRNA.
DR EMBL; AL592522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040205; AAH40205.1; -; mRNA.
DR CCDS; CCDS24770.1; -. [Q5SXI5-1]
DR CCDS; CCDS70197.1; -. [Q5SXI5-3]
DR RefSeq; NP_001124001.1; NM_001130529.2. [Q5SXI5-2]
DR RefSeq; NP_001277943.1; NM_001291014.1. [Q5SXI5-3]
DR RefSeq; NP_766529.3; NM_172941.4. [Q5SXI5-1]
DR RefSeq; XP_006533447.1; XM_006533384.3. [Q5SXI5-1]
DR RefSeq; XP_006533449.1; XM_006533386.3. [Q5SXI5-2]
DR PDB; 2NAB; NMR; -; A=397-434.
DR PDBsum; 2NAB; -.
DR AlphaFoldDB; Q5SXI5; -.
DR SMR; Q5SXI5; -.
DR BioGRID; 234496; 1.
DR IntAct; Q5SXI5; 2.
DR MINT; Q5SXI5; -.
DR STRING; 10090.ENSMUSP00000013262; -.
DR iPTMnet; Q5SXI5; -.
DR PhosphoSitePlus; Q5SXI5; -.
DR EPD; Q5SXI5; -.
DR MaxQB; Q5SXI5; -.
DR PaxDb; Q5SXI5; -.
DR PeptideAtlas; Q5SXI5; -.
DR PRIDE; Q5SXI5; -.
DR ProteomicsDB; 299579; -. [Q5SXI5-1]
DR ProteomicsDB; 299580; -. [Q5SXI5-2]
DR ProteomicsDB; 299581; -. [Q5SXI5-3]
DR Antibodypedia; 20839; 162 antibodies from 27 providers.
DR DNASU; 268417; -.
DR Ensembl; ENSMUST00000013262; ENSMUSP00000013262; ENSMUSG00000020472. [Q5SXI5-1]
DR Ensembl; ENSMUST00000101150; ENSMUSP00000098709; ENSMUSG00000020472. [Q5SXI5-3]
DR GeneID; 268417; -.
DR KEGG; mmu:268417; -.
DR UCSC; uc007jea.2; mouse. [Q5SXI5-1]
DR CTD; 268417; -.
DR MGI; MGI:2679270; Zkscan17.
DR VEuPathDB; HostDB:ENSMUSG00000020472; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161967; -.
DR HOGENOM; CLU_002678_49_8_1; -.
DR InParanoid; Q5SXI5; -.
DR OMA; EFQTCQQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5SXI5; -.
DR TreeFam; TF350829; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 268417; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zkscan17; mouse.
DR PRO; PR:Q5SXI5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SXI5; protein.
DR Bgee; ENSMUSG00000020472; Expressed in otolith organ and 213 other tissues.
DR Genevisible; Q5SXI5; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA: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; IDA: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; 3.
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 3D-structure; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..585
FT /note="Zinc finger protein 496"
FT /id="PRO_0000391906"
FT DOMAIN 42..124
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 220..294
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 405..427
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..455
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 461..483
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 520..543
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 575..579
FT /note="Nuclear localization signal"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96IT1"
FT CROSSLNK 494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96IT1"
FT VAR_SEQ 1..156
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038768"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038769"
FT CONFLICT 499
FT /note="A -> T (in Ref. 4; AAH40205)"
FT /evidence="ECO:0000305"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:2NAB"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2NAB"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:2NAB"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:2NAB"
SQ SEQUENCE 585 AA; 66577 MW; 9F8780B785EF71FA CRC64;
MPTALCPRVL APKESEEPRK MRSPPGENPS PQGEPPSPES SRRLFRRFRY QEAAGPREAL
QRLWELCRGW LRLERHTKEQ ILELLVLEQF LAILPWEIQS WVRAQEPESG EQAVAAVEAL
EREPGRPWQW LKHCEDPVVI DDGDGPAAPQ DLEQERMSAE SQSYPDAPPG ALVQGTGLLS
RSPGQPSEDL VPQDAFVVQE QSIRDAQPVA TCQLPPNRVS PFKDMILCFS EEDWSLLDPA
QTGFYGEFII GEDYAVSMPP NEPPVQPGHS HEEENGLRVT EWTTDLQDKE IPQASCLDLS
SLQPFQGEER RKWEELQVPE LQPCPQVVLS QSPCPAGGDP PALKSSLDQE VTIEIVLSSS
GDEDSQHSPY CTEELRSPPE DLHSVPAHQS NASAEGEVQT SQKSYVCPNC GKIFRWRVNF
IRHLRSRREQ KPHKCSVCGE LFSDSEDLDG HLETHEAQKP YRCTACGKSF RLNSHLISHR
RIHLQPASQQ PMKKSEEEAL ETEGTGASDL LEKSKAKLSF QCGDCEKSFQ RHDHLVRHRR
HCHLKDETRP FQCRYCVKTF RQNYDLLRHE RLHMKRRSKQ ALNSY
