ZN532_MOUSE
ID ZN532_MOUSE Reviewed; 1036 AA.
AC Q6NXK2; Q504Z6; Q6ZPL1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Zinc finger protein 532;
GN Name=Znf532; Synonyms=Kiaa1629, Zfp532;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-643 (ISOFORM 1/2).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, 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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NXK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXK2-2; Sequence=VSP_027745;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98220.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC067032; AAH67032.1; -; mRNA.
DR EMBL; BC094671; AAH94671.1; -; mRNA.
DR EMBL; AK129410; BAC98220.1; ALT_INIT; mRNA.
DR CCDS; CCDS29307.1; -. [Q6NXK2-1]
DR RefSeq; NP_997138.1; NM_207255.2. [Q6NXK2-1]
DR RefSeq; XP_011245259.1; XM_011246957.1.
DR RefSeq; XP_017173418.1; XM_017317929.1.
DR RefSeq; XP_017173419.1; XM_017317930.1.
DR AlphaFoldDB; Q6NXK2; -.
DR BioGRID; 236687; 1.
DR STRING; 10090.ENSMUSP00000036582; -.
DR iPTMnet; Q6NXK2; -.
DR PhosphoSitePlus; Q6NXK2; -.
DR jPOST; Q6NXK2; -.
DR MaxQB; Q6NXK2; -.
DR PaxDb; Q6NXK2; -.
DR PeptideAtlas; Q6NXK2; -.
DR PRIDE; Q6NXK2; -.
DR ProteomicsDB; 275295; -. [Q6NXK2-2]
DR Antibodypedia; 9795; 47 antibodies from 11 providers.
DR Ensembl; ENSMUST00000049016; ENSMUSP00000036582; ENSMUSG00000042439. [Q6NXK2-1]
DR Ensembl; ENSMUST00000169679; ENSMUSP00000129390; ENSMUSG00000042439. [Q6NXK2-1]
DR Ensembl; ENSMUST00000182478; ENSMUSP00000138315; ENSMUSG00000042439. [Q6NXK2-2]
DR GeneID; 328977; -.
DR KEGG; mmu:328977; -.
DR UCSC; uc008ffc.2; mouse. [Q6NXK2-1]
DR CTD; 328977; -.
DR MGI; MGI:3036282; Zfp532.
DR VEuPathDB; HostDB:ENSMUSG00000042439; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154437; -.
DR HOGENOM; CLU_006283_0_0_1; -.
DR InParanoid; Q6NXK2; -.
DR PhylomeDB; Q6NXK2; -.
DR TreeFam; TF329009; -.
DR BioGRID-ORCS; 328977; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Zfp532; mouse.
DR PRO; PR:Q6NXK2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6NXK2; protein.
DR Bgee; ENSMUSG00000042439; Expressed in cortical plate and 245 other tissues.
DR ExpressionAtlas; Q6NXK2; baseline and differential.
DR Genevisible; Q6NXK2; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR045914; Zn532-like.
DR InterPro; IPR041697; Znf-C2H2_11.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR47222; PTHR47222; 2.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1036
FT /note="Zinc finger protein 532"
FT /id="PRO_0000299553"
FT ZN_FING 615..634
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 751..775
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 784..807
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 814..840
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 938..961
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 999..1021
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 26..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT CROSSLNK 879
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT CROSSLNK 902
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCE3"
FT VAR_SEQ 780..1036
FT /note="QMKKHPCRQCDKSFSSSHSLCRHNRIKHKGIRKVYACSHCPDSRRTFTKRLM
FT LERHIQLMHGIKDPDVKELSDDAGDVTNDEEEEAEIKEDAKVPSPKRKLEEPVLEFRPP
FT RGAITQPLKKLKINVFKVHKCAVCGFTTENLLQFHEHIPQHRSDGSSHQCRECGLCYTS
FT HGSLARHLFIVHKLKEPQPVSKQNGAGEDSQQENKPSPEDEAAEGAASDRKCKVCAKTF
FT ETEAALNTHMRTHGMAFIKSKRMSSAEK -> KTCTVCQMLLPNQCSYASHQRIHQHKS
FT PYTCPECGAICRSVHFQNHITKNCLHYTRRVGFRCVHCNVVYSDVAALKSHIQGSHCEV
FT FYKCPICPMAFKSAPSTHSHAYTQHPGVKIGEPNK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027745"
SQ SEQUENCE 1036 AA; 110949 MW; 9A3B6E1F7803627B CRC64;
MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDHESH IKQNAHVDDD SHTPSSSDVG
VSVIVKNVRN IDSSEGVEKD GHNPTGNGLH NGFLTASSLD SYGKDGAKSL KGDTPASEVT
LKDPAFSQFS PISSAEEFED DEKIEVDDPP DKEEARAGFR SNVLTGSAPQ QDFDKLKALG
GENSSKTGVS TSGHTDKNKV KREAESNSIT LSVYEPFKVR KAEDKLKENS EKMLESRVLD
GKPSSEKSDS GIAAAASSKT KPSSKLSSCI AAIAALSAKK AASDSCKEPV ANSREASPLP
KEVNDSPKAA DKSPESQNLI DGTKKASLKP SDSPRSVSSE NSSKGSPSSP VGSTPAIPKV
RIKTIKTSSG EIKRTVTRVL PEVDLDSGKK PSEQAASVMA SVTSLLSSSA SATVLSSPPR
APLQTAMVTS AVSSAELTPK QVTIKPVATA FLPVSAVKTA GSQVINLKLA NNTTVKATVI
SAASVQSASS AIIKAANAIQ QQTVVVPASS LANAKLVPKT VHLANLNLLP QGAQATSELR
QVLTKPQQQI KQAIINAAAS QPPKKVSRVQ VVSSLQSSVV EAFNKVLSSV NPVPVYTPNL
SPPANAGITL PMRGYKCLEC GDAFALEKSL SQHYDRRSVR IEVTCNHCTK NLVFYNKCSL
LSHARGHKEK GVVMQCSHLI LKPVPADQMI VPPSSNTAAS TLQSSVGAAT HTVPKVQPGI
AGAVISAPAS TPMSPAMPLD EDPSKLCRHS LKCLECNEVF QDEPSLATHF QHAADTSGQQ
MKKHPCRQCD KSFSSSHSLC RHNRIKHKGI RKVYACSHCP DSRRTFTKRL MLERHIQLMH
GIKDPDVKEL SDDAGDVTND EEEEAEIKED AKVPSPKRKL EEPVLEFRPP RGAITQPLKK
LKINVFKVHK CAVCGFTTEN LLQFHEHIPQ HRSDGSSHQC RECGLCYTSH GSLARHLFIV
HKLKEPQPVS KQNGAGEDSQ QENKPSPEDE AAEGAASDRK CKVCAKTFET EAALNTHMRT
HGMAFIKSKR MSSAEK
