TB15A_HUMAN
ID TB15A_HUMAN Reviewed; 45 AA.
AC P0CG34; A8K614; Q99406;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Thymosin beta-15A;
DE AltName: Full=NB thymosin beta;
DE AltName: Full=Thymosin-like protein 8;
GN Name=TMSB15A; Synonyms=TMSL8, TMSNB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9039501; DOI=10.1093/dnares/3.5.311;
RA Yokoyama M., Nishi Y., Yoshii J., Okubo K., Matsubara K.;
RT "Identification and cloning of neuroblastoma-specific and nerve tissue-
RT specific genes through compiled expression profiles.";
RL DNA Res. 3:311-320(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP PROTEIN SEQUENCE OF 2-15.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP INDUCTION.
RX PubMed=19296525; DOI=10.1002/gcc.20659;
RA Banyard J., Barrows C., Zetter B.R.;
RT "Differential regulation of human thymosin beta 15 isoforms by transforming
RT growth factor beta 1.";
RL Genes Chromosomes Cancer 48:502-509(2009).
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 -!- TISSUE SPECIFICITY: Neuroblastoma-specific.
CC {ECO:0000269|PubMed:9039501}.
CC -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:19296525}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; D82345; BAA11556.1; -; mRNA.
DR EMBL; AL035609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471190; EAW54739.1; -; Genomic_DNA.
DR EMBL; BC000183; AAH00183.1; -; mRNA.
DR CCDS; CCDS14498.1; -.
DR PIR; JC5274; JC5274.
DR RefSeq; NP_068832.1; NM_021992.2.
DR RefSeq; NP_919305.2; NM_194324.2.
DR AlphaFoldDB; P0CG34; -.
DR SMR; P0CG34; -.
DR BioGRID; 130400; 1.
DR STRING; 9606.ENSP00000289373; -.
DR iPTMnet; P0CG34; -.
DR PhosphoSitePlus; P0CG34; -.
DR BioMuta; TMSB15A; -.
DR DMDM; 300681171; -.
DR EPD; P0CG34; -.
DR jPOST; P0CG34; -.
DR MassIVE; P0CG34; -.
DR PaxDb; P0CG34; -.
DR PeptideAtlas; P0CG34; -.
DR PRIDE; P0CG34; -.
DR Antibodypedia; 28923; 46 antibodies from 15 providers.
DR DNASU; 286527; -.
DR Ensembl; ENST00000289373.5; ENSP00000289373.4; ENSG00000158164.7.
DR GeneID; 11013; -.
DR GeneID; 286527; -.
DR KEGG; hsa:11013; -.
DR KEGG; hsa:286527; -.
DR MANE-Select; ENST00000289373.5; ENSP00000289373.4; NM_021992.3; NP_068832.1.
DR MANE-Select; ENST00000540220.6; ENSP00000455371.1; NM_194324.4; NP_919305.2.
DR MANE-Select; ENST00000598087.4; ENSP00000472749.1; NM_001395930.1; NP_001382859.1.
DR CTD; 11013; -.
DR CTD; 286527; -.
DR DisGeNET; 11013; -.
DR DisGeNET; 286527; -.
DR GeneCards; TMSB15A; -.
DR HGNC; HGNC:30744; TMSB15A.
DR HPA; ENSG00000158164; Tissue enhanced (lymphoid tissue, prostate).
DR MIM; 300939; gene.
DR neXtProt; NX_P0CG34; -.
DR OpenTargets; ENSG00000158164; -.
DR OpenTargets; ENSG00000158427; -.
DR OpenTargets; ENSG00000269226; -.
DR PharmGKB; PA164726584; -.
DR VEuPathDB; HostDB:ENSG00000158164; -.
DR eggNOG; KOG4794; Eukaryota.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P0CG34; -.
DR PhylomeDB; P0CG34; -.
DR PathwayCommons; P0CG34; -.
DR BioGRID-ORCS; 11013; 44 hits in 581 CRISPR screens.
DR BioGRID-ORCS; 286527; 14 hits in 240 CRISPR screens.
DR ChiTaRS; TMSB15A; human.
DR GeneWiki; TMSB15A; -.
DR GeneWiki; TMSB15B; -.
DR Pharos; P0CG34; Tbio.
DR PRO; PR:P0CG34; -.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000158164; Expressed in embryo and 129 other tissues.
DR Genevisible; P0CG34; HS.
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: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 Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..45
FT /note="Thymosin beta-15A"
FT /id="PRO_0000185159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 45 AA; 5229 MW; B1182868530D59C2 CRC64;
MSDKPDLSEV EKFDRSKLKK TNTEEKNTLP SKETIQQEKE CVQTS
