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MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Zinc finger protein 532;
MyHits logo
MyHits synonymsZN532_MOUSE , Q6NXK2 , Q504Z6 , Q6ZPL1 , 9A3B6E1F7803627B
match map segment
iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 ismart:ZnF_C2H2 ipat:ZINC_FINGER_C2H2_1 ipat:ZINC_FINGER_C2H2_1 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2 ismart:ZnF_C2H2 iprf:ZINC_FINGER_C2H2_2  
Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:Q9HCE3}; 2, N6-acetyllysine. {ECO:0000244|PubMed:23806337}; 3, Phosphoserine. {ECO:0000244|PubMed:21183079}; 4, ZN_FING C2H2-type 1; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 5, ZN_FING C2H2-type 2; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 6, ZN_FING C2H2-type 3. {ECO:0000255|PROSITE- ProRule:PRU00042}; 7, ZN_FING C2H2-type 4; degenerate. {ECO:0000255|PROSITE-ProRule:PRU00042}; 8, ZN_FING C2H2-type 5. {ECO:0000255|PROSITE- ProRule:PRU00042}; 9, ZN_FING C2H2-type 6. {ECO:0000255|PROSITE- ProRule:PRU00042}; 10, COMPBIAS Poly-Glu; 11, VAR_SEQ QMKKHPCRQCDKSFSSSHSLCRHNRIKHKGIRKVYACSHCP DSRRTFTKRLMLERHIQLMHGIKDPDVKELSDDAGDVTNDE EEEAEIKEDAKVPSPKRKLEEPVLEFRPPRGAITQPLKKLK INVFKVHKCAVCGFTTENLLQFHEHIPQHRSDGSSHQCREC GLCYTSHGSLARHLFIVHKLKEPQPVSKQNGAGEDSQQENK PSPEDEAAEGAASDRKCKVCAKTFETEAALNTHMRTHGMAF IKSKRMSSAEK -> KTCTVCQMLLPNQCSYASHQRIHQHK SPYTCPECGAICRSVHFQNHITKNCLHYTRRVGFRCVHCNV VYSDVAALKSHIQGSHCEVFYKCPICPMAFKSAPSTHSHAY TQHPGVKIGEPNK (in isoform 2). {ECO:0000303|PubMed:15489334}; 12, iprf:ZINC_FINGER_C2H2_2 [T]; 13, ismart:ZnF_C2H2 [T]; 14, ipat:ZINC_FINGER_C2H2_1 [T].
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   10-MAY-2017, entry version 113.
DE   RecName: Full=Zinc finger protein 532;
GN   Name=Znf532; Synonyms=Kiaa1629, Zfp532;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND IDENTIFICATION
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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         Note=No experimental confirmation available. May be produced at
CC         very low levels due to a premature stop codon in the mRNA,
CC         leading to nonsense-mediated mRNA decay.;
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=Translation N-terminally shortened.; 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. [Q6NXK2-1]
DR   RefSeq; XP_017173418.1; XM_017317929.1. [Q6NXK2-1]
DR   RefSeq; XP_017173419.1; XM_017317930.1. [Q6NXK2-1]
DR   UniGene; Mm.286232; -.
DR   UniGene; Mm.419081; -.
DR   ProteinModelPortal; Q6NXK2; -.
DR   STRING; 10090.ENSMUSP00000036582; -.
DR   iPTMnet; Q6NXK2; -.
DR   PhosphoSitePlus; Q6NXK2; -.
DR   PaxDb; Q6NXK2; -.
DR   PeptideAtlas; Q6NXK2; -.
DR   PRIDE; Q6NXK2; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00530000063261; -.
DR   HOGENOM; HOG000010306; -.
DR   HOVERGEN; HBG062228; -.
DR   InParanoid; Q6NXK2; -.
DR   PhylomeDB; Q6NXK2; -.
DR   TreeFam; TF329009; -.
DR   PRO; PR:Q6NXK2; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   Bgee; ENSMUSG00000042439; -.
DR   CleanEx; MM_ZFP532; -.
DR   ExpressionAtlas; Q6NXK2; baseline and differential.
DR   Genevisible; Q6NXK2; MM.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; Complete proteome; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1036       Zinc finger protein 532.
FT                                /FTId=PRO_0000299553.
FT   ZN_FING     615    634       C2H2-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     751    775       C2H2-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     784    807       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     814    840       C2H2-type 4; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   ZN_FING     938    961       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     999   1021       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    861    866       Poly-Glu.
FT   MOD_RES     130    130       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   MOD_RES     133    133       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   MOD_RES     134    134       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   MOD_RES     175    175       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     306    306       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   MOD_RES     313    313       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     433    433       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   MOD_RES     875    875       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9HCE3}.
FT   VAR_SEQ     780   1036       QMKKHPCRQCDKSFSSSHSLCRHNRIKHKGIRKVYACSHCP
FT                                DSRRTFTKRLMLERHIQLMHGIKDPDVKELSDDAGDVTNDE
FT                                EEEAEIKEDAKVPSPKRKLEEPVLEFRPPRGAITQPLKKLK
FT                                INVFKVHKCAVCGFTTENLLQFHEHIPQHRSDGSSHQCREC
FT                                GLCYTSHGSLARHLFIVHKLKEPQPVSKQNGAGEDSQQENK
FT                                PSPEDEAAEGAASDRKCKVCAKTFETEAALNTHMRTHGMAF
FT                                IKSKRMSSAEK -> KTCTVCQMLLPNQCSYASHQRIHQHK
FT                                SPYTCPECGAICRSVHFQNHITKNCLHYTRRVGFRCVHCNV
FT                                VYSDVAALKSHIQGSHCEVFYKCPICPMAFKSAPSTHSHAY
FT                                TQHPGVKIGEPNK (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_027745.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       615    633       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       909    931       ismart:ZnF_C2H2 [T]
FT   MYHIT       784    812       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       814    845       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       751    772       ismart:ZnF_C2H2 [T]
FT   MYHIT       784    807       ismart:ZnF_C2H2 [T]
FT   MYHIT       938    961       ismart:ZnF_C2H2 [T]
FT   MYHIT       940    961       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       999   1021       ismart:ZnF_C2H2 [T]
FT   MYHIT       615    635       ismart:ZnF_C2H2 [T]
FT   MYHIT       786    807       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT      1001   1021       ipat:ZINC_FINGER_C2H2_1 [T]
FT   MYHIT       814    840       ismart:ZnF_C2H2 [T]
FT   MYHIT       999   1021       iprf:ZINC_FINGER_C2H2_2 [T]
FT   MYHIT       643    667       ismart:ZnF_C2H2 [T]
FT   MYHIT       938    966       iprf:ZINC_FINGER_C2H2_2 [T]
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
//