TYB10_MOUSE
ID TYB10_MOUSE Reviewed; 44 AA.
AC Q6ZWY8; Q3V2M3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thymosin beta-10;
GN Name=Tmsb10; Synonyms=Ptmb10;
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;
RC TISSUE=Placenta, Small intestine, Testis, and Wolffian duct;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Plays an important role in the organization of the
CC cytoskeleton. Binds to and sequesters actin monomers (G actin) and
CC therefore inhibits actin polymerization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; AK003178; BAB22622.1; -; mRNA.
DR EMBL; AK005512; BAB24091.1; -; mRNA.
DR EMBL; AK008557; BAB25742.1; -; mRNA.
DR EMBL; AK012361; BAB28189.1; -; mRNA.
DR EMBL; AK019212; BAB31603.1; -; mRNA.
DR EMBL; AK019232; BAB31614.1; -; mRNA.
DR EMBL; AK131711; BAE20774.1; -; mRNA.
DR EMBL; AK161987; BAE36668.1; -; mRNA.
DR CCDS; CCDS39519.1; -.
DR RefSeq; NP_001034481.1; NM_001039392.2.
DR RefSeq; NP_001177256.1; NM_001190327.1.
DR RefSeq; NP_079560.1; NM_025284.4.
DR AlphaFoldDB; Q6ZWY8; -.
DR SMR; Q6ZWY8; -.
DR BioGRID; 202470; 2.
DR STRING; 10090.ENSMUSP00000109683; -.
DR iPTMnet; Q6ZWY8; -.
DR PhosphoSitePlus; Q6ZWY8; -.
DR jPOST; Q6ZWY8; -.
DR MaxQB; Q6ZWY8; -.
DR PaxDb; Q6ZWY8; -.
DR PRIDE; Q6ZWY8; -.
DR ProteomicsDB; 297760; -.
DR Antibodypedia; 16880; 110 antibodies from 19 providers.
DR DNASU; 19240; -.
DR Ensembl; ENSMUST00000114048; ENSMUSP00000109682; ENSMUSG00000079523.
DR Ensembl; ENSMUST00000114049; ENSMUSP00000109683; ENSMUSG00000079523.
DR Ensembl; ENSMUST00000114050; ENSMUSP00000109684; ENSMUSG00000079523.
DR Ensembl; ENSMUST00000170837; ENSMUSP00000137210; ENSMUSG00000091955.
DR GeneID; 19240; -.
DR KEGG; mmu:19240; -.
DR UCSC; uc009cjf.2; mouse.
DR CTD; 9168; -.
DR MGI; MGI:109146; Tmsb10.
DR VEuPathDB; HostDB:ENSMUSG00000079523; -.
DR VEuPathDB; HostDB:ENSMUSG00000091955; -.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000163007; -.
DR GeneTree; ENSGT01050000245361; -.
DR HOGENOM; CLU_208046_0_1_1; -.
DR InParanoid; Q6ZWY8; -.
DR OrthoDB; 1632292at2759; -.
DR PhylomeDB; Q6ZWY8; -.
DR BioGRID-ORCS; 19240; 2 hits in 68 CRISPR screens.
DR ChiTaRS; Tmsb10; mouse.
DR PRO; PR:Q6ZWY8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000079523; Expressed in embryonic brain and 102 other tissues.
DR ExpressionAtlas; Q6ZWY8; baseline and differential.
DR Genevisible; Q6ZWY8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR Gene3D; 1.20.5.520; -; 1.
DR InterPro; IPR001152; Beta-thymosin.
DR InterPro; IPR038386; Beta-thymosin_sf.
DR PANTHER; PTHR12021; PTHR12021; 1.
DR Pfam; PF01290; Thymosin; 1.
DR PIRSF; PIRSF001828; Thymosin_beta; 1.
DR SMART; SM00152; THY; 1.
DR PROSITE; PS00500; THYMOSIN_B4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21752"
FT CHAIN 2..44
FT /note="Thymosin beta-10"
FT /id="PRO_0000045932"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P21752"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63312"
SQ SEQUENCE 44 AA; 5026 MW; 5485277C275A1C70 CRC64;
MADKPDMGEI ASFDKAKLKK TETQEKNTLP TKETIEQEKR SEIS
