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!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
- MyHits
| Description | RecName: Full=Zinc finger protein 532; |
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| MyHits synonyms | ZN532_MOUSE , Q6NXK2 , Q504Z6 , Q6ZPL1 , 9A3B6E1F7803627B |
 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, ismart:ZnF_C2H2 [T]; 13, iprf:ZINC_FINGER_C2H2_2 [T]; 14, ipat:ZINC_FINGER_C2H2_1 [T].
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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 30-NOV-2016, entry version 109.
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; Sciurognathi;
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 -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC {ECO:0000255|PROSITE-ProRule:PRU00042}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98220.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; -; 2.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF16622; zf-C2H2_11; 1.
DR Pfam; PF13912; zf-C2H2_6; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
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 751 772 ismart:ZnF_C2H2 [T]
FT MYHIT 938 961 ismart:ZnF_C2H2 [T]
FT MYHIT 615 635 ismart:ZnF_C2H2 [T]
FT MYHIT 784 812 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 615 633 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 999 1021 ismart:ZnF_C2H2 [T]
FT MYHIT 999 1021 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 940 961 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 643 667 ismart:ZnF_C2H2 [T]
FT MYHIT 909 931 ismart:ZnF_C2H2 [T]
FT MYHIT 938 966 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 1001 1021 ipat:ZINC_FINGER_C2H2_1 [T]
FT MYHIT 784 807 ismart:ZnF_C2H2 [T]
FT MYHIT 814 840 ismart:ZnF_C2H2 [T]
FT MYHIT 814 845 iprf:ZINC_FINGER_C2H2_2 [T]
FT MYHIT 786 807 ipat:ZINC_FINGER_C2H2_1 [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
//
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