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LSMD1_MOUSE
ID   LSMD1_MOUSE             Reviewed;         125 AA.
AC   Q9D2U5; Q05BF7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=N-alpha-acetyltransferase 38, NatC auxiliary subunit;
DE   AltName: Full=LSM domain-containing protein 1;
GN   Name=Naa38; Synonyms=Lsmd1;
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and 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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Pancreas, and Testis;
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: Auxillary component of the N-terminal acetyltransferase C
CC       (NatC) complex which catalyzes acetylation of N-terminal methionine
CC       residues. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC       complex, which is composed of NAA35, NAA38 and NAA30. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D2U5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2U5-2; Sequence=VSP_027567;
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; AK018782; BAB31406.1; -; mRNA.
DR   EMBL; AL596125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC048499; AAH48499.1; -; mRNA.
DR   EMBL; BC062267; AAH62267.1; -; mRNA.
DR   CCDS; CCDS24893.1; -. [Q9D2U5-1]
DR   RefSeq; NP_084359.1; NM_030083.2. [Q9D2U5-1]
DR   AlphaFoldDB; Q9D2U5; -.
DR   SMR; Q9D2U5; -.
DR   STRING; 10090.ENSMUSP00000123155; -.
DR   iPTMnet; Q9D2U5; -.
DR   PhosphoSitePlus; Q9D2U5; -.
DR   EPD; Q9D2U5; -.
DR   MaxQB; Q9D2U5; -.
DR   PaxDb; Q9D2U5; -.
DR   PeptideAtlas; Q9D2U5; -.
DR   PRIDE; Q9D2U5; -.
DR   ProteomicsDB; 292119; -. [Q9D2U5-1]
DR   ProteomicsDB; 292120; -. [Q9D2U5-2]
DR   Antibodypedia; 58902; 63 antibodies from 14 providers.
DR   DNASU; 78304; -.
DR   Ensembl; ENSMUST00000144531; ENSMUSP00000123155; ENSMUSG00000059278. [Q9D2U5-1]
DR   GeneID; 78304; -.
DR   KEGG; mmu:78304; -.
DR   UCSC; uc007jqa.1; mouse. [Q9D2U5-1]
DR   CTD; 84316; -.
DR   MGI; MGI:1925554; Naa38.
DR   VEuPathDB; HostDB:ENSMUSG00000059278; -.
DR   eggNOG; KOG3168; Eukaryota.
DR   GeneTree; ENSGT00390000018418; -.
DR   HOGENOM; CLU_076902_4_3_1; -.
DR   InParanoid; Q9D2U5; -.
DR   OMA; NFRIEMT; -.
DR   OrthoDB; 1549327at2759; -.
DR   PhylomeDB; Q9D2U5; -.
DR   TreeFam; TF323867; -.
DR   BioGRID-ORCS; 78304; 17 hits in 73 CRISPR screens.
DR   ChiTaRS; Naa38; mouse.
DR   PRO; PR:Q9D2U5; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9D2U5; protein.
DR   Bgee; ENSMUSG00000059278; Expressed in spermatid and 260 other tissues.
DR   Genevisible; Q9D2U5; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031417; C:NatC complex; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005844; C:polysome; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   CDD; cd06168; LSMD1; 1.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR034110; LSMD1.
DR   PANTHER; PTHR10701:SF17; PTHR10701:SF17; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA0"
FT   CHAIN           2..125
FT                   /note="N-alpha-acetyltransferase 38, NatC auxiliary
FT                   subunit"
FT                   /id="PRO_0000299156"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA0"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA0"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRA0"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..52
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027567"
SQ   SEQUENCE   125 AA;  13430 MW;  F0A2A6A89F21E1F5 CRC64;
     MAGAGPTMLL REENGCCSRR QSSSSAGDSD GEQEDSPATR ARQQLEALLN KTMRIRMTDG
     RTLVGCFLCT DRDCNVILGS AQEFLKPSDS FSAGEPRVLG LAMVPGHHIV SIEVQRESLS
     GGPYL
 
 
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