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MPND_MOUSE
ID   MPND_MOUSE              Reviewed;         487 AA.
AC   Q3TV65; Q3T9P5; Q3UIC8; Q8VEN1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=MPN domain-containing protein {ECO:0000305};
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q5VVJ2};
GN   Name=Mpnd {ECO:0000312|MGI:MGI:1915297};
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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Heart, and Spleen;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-487.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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).
CC   -!- FUNCTION: Probable protease (By similarity). Acts as a sensor of N(6)-
CC       methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA,
CC       leading to its degradation (By similarity).
CC       {ECO:0000250|UniProtKB:Q5VVJ2, ECO:0000250|UniProtKB:Q8N594}.
CC   -!- DOMAIN: The RAMA domain recognizes and binds N(6)-methyladenosine
CC       methylation on DNA (m6A). {ECO:0000250|UniProtKB:Q8N594}.
CC   -!- PTM: Degraded following binding to N(6)-methyladenosine methylated DNA
CC       (m6A). {ECO:0000250|UniProtKB:Q8N594}.
CC   -!- SIMILARITY: Belongs to the peptidase M67 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE35755.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK146973; BAE27578.1; ALT_INIT; mRNA.
DR   EMBL; AK160356; BAE35755.1; ALT_FRAME; mRNA.
DR   EMBL; AK172381; BAE42975.1; -; mRNA.
DR   EMBL; BC017625; AAH17625.2; -; mRNA.
DR   CCDS; CCDS50150.1; -.
DR   RefSeq; NP_080806.4; NM_026530.5.
DR   AlphaFoldDB; Q3TV65; -.
DR   BioGRID; 212626; 1.
DR   STRING; 10090.ENSMUSP00000119745; -.
DR   iPTMnet; Q3TV65; -.
DR   PhosphoSitePlus; Q3TV65; -.
DR   MaxQB; Q3TV65; -.
DR   PaxDb; Q3TV65; -.
DR   PRIDE; Q3TV65; -.
DR   ProteomicsDB; 291396; -.
DR   Antibodypedia; 23593; 146 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000149441; ENSMUSP00000119745; ENSMUSG00000003199.
DR   GeneID; 68047; -.
DR   KEGG; mmu:68047; -.
DR   UCSC; uc008dap.1; mouse.
DR   CTD; 84954; -.
DR   MGI; MGI:1915297; Mpnd.
DR   VEuPathDB; HostDB:ENSMUSG00000003199; -.
DR   eggNOG; KOG1555; Eukaryota.
DR   GeneTree; ENSGT00940000160191; -.
DR   HOGENOM; CLU_037792_0_0_1; -.
DR   InParanoid; Q3TV65; -.
DR   OMA; MMLVEFY; -.
DR   OrthoDB; 590811at2759; -.
DR   PhylomeDB; Q3TV65; -.
DR   TreeFam; TF324811; -.
DR   BioGRID-ORCS; 68047; 5 hits in 73 CRISPR screens.
DR   ChiTaRS; Mpnd; mouse.
DR   PRO; PR:Q3TV65; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3TV65; protein.
DR   Bgee; ENSMUSG00000003199; Expressed in dorsal pancreas and 252 other tissues.
DR   ExpressionAtlas; Q3TV65; baseline and differential.
DR   Genevisible; Q3TV65; MM.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR040843; RAMA.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF18755; RAMA; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW   Protease; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N594"
FT   CHAIN           2..487
FT                   /note="MPN domain-containing protein"
FT                   /id="PRO_0000278805"
FT   DOMAIN          61..156
FT                   /note="RAMA"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          258..393
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           335..348
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   COMPBIAS        14..28
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N594"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N594"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N594"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N594"
FT   CONFLICT        228
FT                   /note="M -> I (in Ref. 1; BAE27578)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   487 AA;  53376 MW;  647B07573D33FAB4 CRC64;
     MAAPESLSPG ATAEEAPEED EDDAEAEDPE RGTGSGGRSG SLGGSGGGTA GPGMALGGAL
     TRRAVTLRVL LKDELLEPGE GVLSIYYLGR KFTGDLQLDG RIVWQETGQV FNSPSAWATH
     CKKLVNPAKK SGCGWASVKY KGQKLDKYKA AWLRRHQLHM PVATADESPT SEGEEEELLL
     EEEEEDVLAG VSSEDKGHRP PGKGSLEPEA TPPGKRMDKV PVPIRYCMLG SRDSARNPHT
     LVEVTSFAAI NKFQPFNVAV SSNVLFLLDF HCHLTRSEVV GYLGGRWDIN NQMLTVLRAF
     PCRSRLGDTD TAATVEEEIY QVLFLRGLSL VGWYHSHPHS PAVPSLQDID AQMEYQLRLQ
     GSSNGFQPCL ALLCSPYYSG NPGPESKICP FWVMPPPEQR PSDYGIPMDV EMAYVQDSFL
     TNDVLQEMVM LAEFYKGAPD LVKFQEAWSP EHTYLDKLKM SLASRTPKDQ GMCHVLEQVC
     SVLKQGS
 
 
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