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MYNN_MOUSE
ID   MYNN_MOUSE              Reviewed;         610 AA.
AC   Q99MD8; Q6P1G7; Q8BT55; Q922I4; Q9CSA0; Q9CXJ8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Myoneurin;
GN   Name=Mynn;
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), AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=10873615; DOI=10.1006/bbrc.2000.2862;
RA   Alliel P.M., Seddiqi N., Goudou D., Cifuentes-Diaz C., Romero N.,
RA   Velasco E., Rieger F., Perin J.-P.;
RT   "Myoneurin, a novel member of the BTB/POZ-zinc finger family highly
RT   expressed in human muscle.";
RL   Biochem. Biophys. Res. Commun. 273:385-391(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
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] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and 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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=14694499; DOI=10.1002/mus.10526;
RA   Cifuentes-Diaz C., Bitoun M., Goudou D., Seddiqi N., Romero N., Rieger F.,
RA   Perin J.-P., Alliel P.M.;
RT   "Neuromuscular expression of the BTB/POZ and zinc finger protein
RT   myoneurin.";
RL   Muscle Nerve 29:59-65(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14694499}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99MD8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99MD8-2; Sequence=VSP_020220;
CC       Name=3;
CC         IsoId=Q99MD8-3; Sequence=VSP_020218, VSP_020219;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the neuromuscular system.
CC       Located in and around synaptic myonuclei in adult muscle. Expression is
CC       dysregulated after nerve injury. Also found in the cerebellum, testis,
CC       heart, brain and liver. {ECO:0000269|PubMed:10873615,
CC       ECO:0000269|PubMed:14694499}.
CC   -!- DEVELOPMENTAL STAGE: Expression is developmentally regulated in muscle
CC       and is associated with neuromuscular junctions during the late
CC       embryonic period. {ECO:0000269|PubMed:14694499}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF349561; AAK18605.1; -; mRNA.
DR   EMBL; AK014315; BAB29266.1; -; mRNA.
DR   EMBL; AK019238; BAC25584.2; -; mRNA.
DR   EMBL; AK013445; BAB28858.1; -; mRNA.
DR   EMBL; AK136107; BAE22823.1; -; mRNA.
DR   EMBL; BC007477; AAH07477.1; -; mRNA.
DR   EMBL; BC065084; AAH65084.1; -; mRNA.
DR   CCDS; CCDS17284.1; -. [Q99MD8-1]
DR   CCDS; CCDS79891.1; -. [Q99MD8-2]
DR   RefSeq; NP_001276550.1; NM_001289621.1. [Q99MD8-2]
DR   RefSeq; NP_001276551.1; NM_001289622.1.
DR   RefSeq; NP_001276552.1; NM_001289623.1.
DR   RefSeq; NP_085034.2; NM_030557.3. [Q99MD8-1]
DR   AlphaFoldDB; Q99MD8; -.
DR   SMR; Q99MD8; -.
DR   BioGRID; 219802; 24.
DR   IntAct; Q99MD8; 1.
DR   STRING; 10090.ENSMUSP00000041034; -.
DR   iPTMnet; Q99MD8; -.
DR   PhosphoSitePlus; Q99MD8; -.
DR   EPD; Q99MD8; -.
DR   MaxQB; Q99MD8; -.
DR   PaxDb; Q99MD8; -.
DR   PeptideAtlas; Q99MD8; -.
DR   PRIDE; Q99MD8; -.
DR   ProteomicsDB; 293599; -. [Q99MD8-1]
DR   ProteomicsDB; 293600; -. [Q99MD8-2]
DR   Antibodypedia; 18640; 254 antibodies from 26 providers.
DR   DNASU; 80732; -.
DR   Ensembl; ENSMUST00000047502; ENSMUSP00000041034; ENSMUSG00000037730. [Q99MD8-2]
DR   Ensembl; ENSMUST00000192715; ENSMUSP00000141951; ENSMUSG00000037730. [Q99MD8-1]
DR   Ensembl; ENSMUST00000195396; ENSMUSP00000141623; ENSMUSG00000037730. [Q99MD8-3]
DR   Ensembl; ENSMUST00000195751; ENSMUSP00000141450; ENSMUSG00000037730. [Q99MD8-3]
DR   GeneID; 80732; -.
DR   KEGG; mmu:80732; -.
DR   UCSC; uc008oux.2; mouse. [Q99MD8-1]
DR   UCSC; uc008ouz.2; mouse. [Q99MD8-2]
DR   CTD; 55892; -.
DR   MGI; MGI:1931415; Mynn.
DR   VEuPathDB; HostDB:ENSMUSG00000037730; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161266; -.
DR   HOGENOM; CLU_022540_1_0_1; -.
DR   InParanoid; Q99MD8; -.
DR   OMA; TNCDAKF; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q99MD8; -.
DR   TreeFam; TF330787; -.
DR   BioGRID-ORCS; 80732; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Mynn; mouse.
DR   PRO; PR:Q99MD8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q99MD8; protein.
DR   Bgee; ENSMUSG00000037730; Expressed in metanephric loop of Henle and 249 other tissues.
DR   Genevisible; Q99MD8; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
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; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 5.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..610
FT                   /note="Myoneurin"
FT                   /id="PRO_0000248218"
FT   DOMAIN          24..89
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         302..324
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         330..352
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         358..381
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         387..409
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         415..437
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         443..465
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         471..493
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         499..522
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          156..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           174..190
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           257..262
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        157..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         46..60
FT                   /note="SEYFGAIYRSTSENN -> IGMLKKSIRLLTISK (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020218"
FT   VAR_SEQ         61..610
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020219"
FT   VAR_SEQ         468..495
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020220"
FT   CONFLICT        127
FT                   /note="T -> A (in Ref. 2; BAB28858)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="S -> I (in Ref. 2; BAC25584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="K -> Q (in Ref. 2; BAB29266)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="A -> G (in Ref. 2; BAB29266)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        440
FT                   /note="E -> G (in Ref. 1; AAK18605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        512
FT                   /note="K -> E (in Ref. 2; BAC25584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="K -> E (in Ref. 2; BAC25584)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   610 AA;  68593 MW;  0FB8DC19C0501935 CRC64;
     MQYSHHCEHL LERLNKQREA GFLCDCTVVI GEFQFKAHRN VLASFSEYFG AIYRSTSENN
     VFLDQSQVKA DGFQKLLEFI YTGTLNLDSW NVKEIHQAAD YLKVEEVVTK CKIKMEDFAF
     IASPSSTEIS SITGNIELNQ QACLLTLRDY NNREKSEVST DSVQANPKPR ALTKKSSQSK
     KKKKAFSSQK PGQSKAVQYP SDVLESASVE LFLETSKLSS PVVEQIIQGN DSSELELTSV
     VENTFPTQDI VQTVTVKRKR RKSQSHCALK EHSMSNIASV KSPYELENAG EELDARFSKA
     KPMCNTCGKV FSEASSLRRH MRIHKGVKPY VCHLCGKAFT QCNQLKTHVR THTGERPYKC
     ELCDKGFAQK CQLVFHSRMH HGEEKPYKCD VCNLQFATSS NLKIHARKHS GEKPYVCDRC
     GQRFAQASTL TYHVRRHTGE KPYVCDTCGK AFAVSSSLIT HSRKHTGEKP YICGICGKSF
     ISSGELNKHF RSHTGERPFI CELCGNSYTD IKNLKKHKTK VHSGTDKNPD CSVDDHAVSE
     QDSVQRSPLS ETLDVKPSDM TLPLALPLGT EDHQMLLPVT DSQSPASDTL LRSTVNGYSE
     PQLIFLQQLY
 
 
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