ZN131_MOUSE
ID ZN131_MOUSE Reviewed; 619 AA.
AC Q8K3J5; Q3UYZ4; Q80UU7; Q8C8D0; Q9D042;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger protein 131;
GN Name=Znf131; Synonyms=Zfp131;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=12163020; DOI=10.1016/s0006-291x(02)00850-1;
RA Trappe R., Buddenberg P., Uedelhoven J., Glaser B., Buck A., Engel W.,
RA Burfeind P.;
RT "The murine BTB/POZ zinc finger gene Znf131: predominant expression in the
RT developing central nervous system, in adult brain, testis, and thymus.";
RL Biochem. Biophys. Res. Commun. 296:319-327(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
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 MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 92-619 (ISOFORM 2).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
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: May be involved in transcriptional regulation as a repressor
CC of ESR1/ER-alpha signaling (By similarity). Plays a role during
CC development and organogenesis as well as in the function of the adult
CC central nervous system. {ECO:0000250, ECO:0000269|PubMed:12163020}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K3J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3J5-2; Sequence=VSP_016924;
CC Name=3;
CC IsoId=Q8K3J5-3; Sequence=VSP_016925, VSP_016926;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Predominant expression is
CC found in the developing central nervous system with strongest signals
CC in the forebrain, midbrain, and hindbrain areas and in the neural tube.
CC {ECO:0000269|PubMed:12163020}.
CC -!- DEVELOPMENTAL STAGE: Expression found as early as 8.5 dpc. High
CC expression is found in the developing limb buds of embryos.
CC {ECO:0000269|PubMed:12163020}.
CC -!- PTM: Monosumoylated at Lys-598 by CBX4 and UHRF2. Sumoylation may
CC potentiate ZNF131 inhibition of estrogen signaling. Sumoylation does
CC not interfere with ubiquitination (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY092766; AAM18207.1; -; mRNA.
DR EMBL; AK011832; BAB27867.1; -; mRNA.
DR EMBL; AK030398; BAC26943.1; -; mRNA.
DR EMBL; AK047429; BAC33056.1; -; mRNA.
DR EMBL; AK134257; BAE22067.1; -; mRNA.
DR EMBL; AK135723; BAE22629.1; -; mRNA.
DR EMBL; AK162903; BAE37106.1; -; mRNA.
DR EMBL; BC048839; AAH48839.1; -; mRNA.
DR EMBL; BC057991; AAH57991.1; -; mRNA.
DR CCDS; CCDS56903.1; -. [Q8K3J5-2]
DR CCDS; CCDS79245.1; -. [Q8K3J5-1]
DR RefSeq; NP_001289476.1; NM_001302547.1. [Q8K3J5-1]
DR RefSeq; NP_001289477.1; NM_001302548.1. [Q8K3J5-2]
DR RefSeq; NP_001289478.1; NM_001302549.1. [Q8K3J5-1]
DR RefSeq; NP_001289479.1; NM_001302550.1. [Q8K3J5-1]
DR RefSeq; NP_082521.1; NM_028245.4. [Q8K3J5-2]
DR RefSeq; XP_006517829.1; XM_006517766.1. [Q8K3J5-1]
DR RefSeq; XP_006517832.1; XM_006517769.3. [Q8K3J5-1]
DR RefSeq; XP_017171099.1; XM_017315610.1. [Q8K3J5-2]
DR AlphaFoldDB; Q8K3J5; -.
DR SMR; Q8K3J5; -.
DR STRING; 10090.ENSMUSP00000136867; -.
DR iPTMnet; Q8K3J5; -.
DR PhosphoSitePlus; Q8K3J5; -.
DR EPD; Q8K3J5; -.
DR MaxQB; Q8K3J5; -.
DR PeptideAtlas; Q8K3J5; -.
DR PRIDE; Q8K3J5; -.
DR ProteomicsDB; 302073; -. [Q8K3J5-1]
DR ProteomicsDB; 302074; -. [Q8K3J5-2]
DR ProteomicsDB; 302075; -. [Q8K3J5-3]
DR Antibodypedia; 23236; 280 antibodies from 23 providers.
DR DNASU; 72465; -.
DR Ensembl; ENSMUST00000177916; ENSMUSP00000136867; ENSMUSG00000094870. [Q8K3J5-1]
DR Ensembl; ENSMUST00000178271; ENSMUSP00000136019; ENSMUSG00000094870. [Q8K3J5-2]
DR Ensembl; ENSMUST00000223722; ENSMUSP00000153044; ENSMUSG00000094870. [Q8K3J5-1]
DR Ensembl; ENSMUST00000223813; ENSMUSP00000152941; ENSMUSG00000094870. [Q8K3J5-2]
DR Ensembl; ENSMUST00000224946; ENSMUSP00000153517; ENSMUSG00000094870. [Q8K3J5-3]
DR GeneID; 72465; -.
DR KEGG; mmu:72465; -.
DR UCSC; uc007rzn.2; mouse. [Q8K3J5-1]
DR UCSC; uc007rzo.2; mouse. [Q8K3J5-2]
DR UCSC; uc007rzq.2; mouse. [Q8K3J5-3]
DR CTD; 72465; -.
DR MGI; MGI:1919715; Zfp131.
DR VEuPathDB; HostDB:ENSMUSG00000094870; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000154668; -.
DR HOGENOM; CLU_031851_0_0_1; -.
DR InParanoid; Q8K3J5; -.
DR OMA; KEHLMCH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8K3J5; -.
DR TreeFam; TF331428; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR BioGRID-ORCS; 72465; 25 hits in 73 CRISPR screens.
DR ChiTaRS; Zfp131; mouse.
DR PRO; PR:Q8K3J5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8K3J5; protein.
DR Bgee; ENSMUSG00000094870; Expressed in cleaving embryo and 264 other tissues.
DR ExpressionAtlas; Q8K3J5; baseline and differential.
DR Genevisible; Q8K3J5; MM.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor 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:0043565; F:sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR027758; Zfp131.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24399:SF35; PTHR24399:SF35; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..619
FT /note="Zinc finger protein 131"
FT /id="PRO_0000047414"
FT DOMAIN 34..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 261..283
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..311
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..381
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..414
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 420..443
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 574..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..148
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 317..328
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 574..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52739"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52739"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 244..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12163020,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_016924"
FT VAR_SEQ 353
FT /note="E -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016925"
FT VAR_SEQ 354..619
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016926"
FT CONFLICT 80
FT /note="M -> V (in Ref. 2; BAE22067)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="V -> E (in Ref. 2; BAE22067)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> A (in Ref. 2; BAE22067)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="W -> R (in Ref. 3; AAH48839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 71022 MW; 932A6B9EF62AE5DB CRC64;
MEAEETMECL QEFPEHHKMI LDRLNEQREQ DRFTDITLIV DGHHFKAHKA VLAACSKFFY
KFFQEFTQEP LVEIEGVSKM AFRHLIEFTY TAKLMIQGEE EANDVWKAAE FLQMLEAIKA
LEVRNKENSA PLEENTTGKN EAKKRKIAET SNVITESLPS AESEPVEIEV EIAEGTIEVE
DEGIEALEEM ASAKQSIKYI QSTGSSDDSA LALLADITSK YRQGESKGQI SEDDCASDPI
SKQVEGIEIV ELQLSHVKDL FHCEKCNRSF KLFYHFKEHM KSHSTESFKC EICNKRYLRE
SAWKQHLNCY HLEEGGVSKK QRTGKKIHIC QYCDKQFDHF GHFKEHLRKH TGEKPFECSN
CHERFARNST LKCHLTACQT GVGAKKGRKK LYECQVCNSV FNSWDQFKDH LVIHTGDKPN
HCTLCDLWFM QGNELRRHLS DAHNISERIV TEEVLSVETH LQTEPVTSMT IIEQVGKVHV
LPLLQVQVDS AQVTVEQVHP DLLQDSQVHD SQMTGLPEQV QVSYLEVGRI QTEEGTEVHV
EELHVERVNQ MPVEVQTELL EADLDHMTPE IMSQEEREPN HADAAMEEHE DAEGLETKPS
EYSQARKTEN DRTSLPVLE
