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THUM1_MOUSE
ID   THUM1_MOUSE             Reviewed;         350 AA.
AC   Q99J36; Q3U6Y3;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=THUMP domain-containing protein 1;
GN   Name=Thumpd1;
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; TISSUE=Bone marrow, and Medulla oblongata;
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].
RC   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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-8; SER-86 AND SER-88, CLEAVAGE OF INITIATOR METHIONINE
RP   [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, 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: Functions as a tRNA-binding adapter to mediate NAT10-
CC       dependent tRNA acetylation. {ECO:0000250|UniProtKB:Q9NXG2}.
CC   -!- SUBUNIT: Interacts with NAT10. {ECO:0000250|UniProtKB:Q9NXG2}.
CC   -!- SIMILARITY: Belongs to the THUMPD1 family. {ECO:0000305}.
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DR   EMBL; AK032078; BAC27685.1; -; mRNA.
DR   EMBL; AK152912; BAE31591.1; -; mRNA.
DR   EMBL; BC004776; AAH04776.1; -; mRNA.
DR   CCDS; CCDS21785.1; -.
DR   RefSeq; NP_663560.1; NM_145585.2.
DR   RefSeq; XP_017177688.1; XM_017322199.1.
DR   AlphaFoldDB; Q99J36; -.
DR   SMR; Q99J36; -.
DR   BioGRID; 231447; 3.
DR   STRING; 10090.ENSMUSP00000033236; -.
DR   iPTMnet; Q99J36; -.
DR   PhosphoSitePlus; Q99J36; -.
DR   EPD; Q99J36; -.
DR   jPOST; Q99J36; -.
DR   MaxQB; Q99J36; -.
DR   PaxDb; Q99J36; -.
DR   PeptideAtlas; Q99J36; -.
DR   PRIDE; Q99J36; -.
DR   ProteomicsDB; 262982; -.
DR   Antibodypedia; 25603; 134 antibodies from 23 providers.
DR   DNASU; 233802; -.
DR   Ensembl; ENSMUST00000033236; ENSMUSP00000033236; ENSMUSG00000030942.
DR   GeneID; 233802; -.
DR   KEGG; mmu:233802; -.
DR   UCSC; uc009jlo.2; mouse.
DR   CTD; 55623; -.
DR   MGI; MGI:2444479; Thumpd1.
DR   VEuPathDB; HostDB:ENSMUSG00000030942; -.
DR   eggNOG; KOG3943; Eukaryota.
DR   GeneTree; ENSGT00390000002365; -.
DR   HOGENOM; CLU_039352_0_0_1; -.
DR   InParanoid; Q99J36; -.
DR   OMA; ECVFFMK; -.
DR   OrthoDB; 1478461at2759; -.
DR   PhylomeDB; Q99J36; -.
DR   TreeFam; TF313884; -.
DR   BioGRID-ORCS; 233802; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Thumpd1; mouse.
DR   PRO; PR:Q99J36; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q99J36; protein.
DR   Bgee; ENSMUSG00000030942; Expressed in ileal epithelium and 252 other tissues.
DR   Genevisible; Q99J36; MM.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR   CDD; cd11717; THUMP_THUMPD1_like; 1.
DR   InterPro; IPR004114; THUMP_dom.
DR   InterPro; IPR040183; THUMPD1-like.
DR   PANTHER; PTHR13452; PTHR13452; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   SMART; SM00981; THUMP; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   CHAIN           2..350
FT                   /note="THUMP domain-containing protein 1"
FT                   /id="PRO_0000072531"
FT   DOMAIN          147..254
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXG2"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NXG2"
SQ   SEQUENCE   350 AA;  38885 MW;  AD24B88A009749F8 CRC64;
     MATTAQQSPQ PVAGKRKGKS QFLPAKRARR GDAGGPRQLE PGLQGILITC NMNERKCVEE
     AYSLLNEYGD DMYGPEKFID KDQQPSGSEG EDDDAEAALK KEVGDIKAST EKRLRRFQSV
     ESGANNVVFI RTLGIEPEKL VHHILQDMYK TKKKKTRVIL RMLPISGTCK AFLEDMKKYA
     ETFLEPWFKA PNKGTFQIVY KSRNNSHMNR EEVIKELAGI VGSLNSENKV DLTNPEYTVV
     VEIIKAVCCL SVVKDYVLFR KYNLQEVVKS AKDSQPHPKL GNGKEAKLEP DSKLSQSDPP
     EGNQVAPESI EELGQTEPGS ETQAGSEGDA KPEPESQVSE VPKTNENELS
 
 
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