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TYB10_HUMAN
ID   TYB10_HUMAN             Reviewed;          44 AA.
AC   P63313; P13472; Q596K9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Thymosin beta-10;
GN   Name=TMSB10; Synonyms=PTMB10, THYB10;
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].
RC   TISSUE=Kidney;
RX   PubMed=3365256; DOI=10.1016/s0006-291x(88)80118-9;
RA   McCreary V., Kartha S., Bell G.I., Toback F.G.;
RT   "Sequence of a human kidney cDNA clone encoding thymosin beta 10.";
RL   Biochem. Biophys. Res. Commun. 152:862-866(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=2169566; DOI=10.1016/0169-328x(90)90057-k;
RA   Hall A.K., Hempstead J., Morgan J.I.;
RT   "Thymosin beta 10 levels in developing human brain and its regulation by
RT   retinoic acid in the HTB-10 neuroblastoma.";
RL   Brain Res. Mol. Brain Res. 8:129-135(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8425765; DOI=10.1002/ijc.2910530218;
RA   Weterman M.A., van Muijen G.N.P., Ruiter D.J., Bloemers H.P.J.;
RT   "Thymosin beta-10 expression in melanoma cell lines and melanocytic
RT   lesions: a new progression marker for human cutaneous melanoma.";
RL   Int. J. Cancer 53:278-284(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Condon M.R., Hall A.K.;
RT   "Human thymosin beta 10 gene: its characterization and nucleotide
RT   sequence.";
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of a migration inducing gene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Uterus;
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-15 AND LYS-39, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND THR-34, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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   -!- INTERACTION:
CC       P63313; P13196: ALAS1; NbExp=6; IntAct=EBI-2688673, EBI-3905054;
CC       P63313; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-2688673, EBI-1044640;
CC       P63313; Q9NUX5: POT1; NbExp=2; IntAct=EBI-2688673, EBI-752420;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DEVELOPMENTAL STAGE: Found to decrease dramatically after birth.
CC       {ECO:0000269|PubMed:2169566}.
CC   -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA36746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAC41691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/TMSB10ID42595ch2p11.html";
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DR   EMBL; M20259; AAA36744.1; -; mRNA.
DR   EMBL; M92381; AAC41691.1; ALT_INIT; mRNA.
DR   EMBL; S54005; AAB25225.1; -; mRNA.
DR   EMBL; M92383; AAA36746.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY453400; AAS47517.1; -; mRNA.
DR   EMBL; AK311952; BAG34892.1; -; mRNA.
DR   EMBL; AC022210; AAY24191.1; -; Genomic_DNA.
DR   EMBL; BC016025; AAH16025.1; -; mRNA.
DR   EMBL; BC016731; AAH16731.1; -; mRNA.
DR   CCDS; CCDS1970.1; -.
DR   PIR; A27704; A27704.
DR   RefSeq; NP_066926.1; NM_021103.3.
DR   AlphaFoldDB; P63313; -.
DR   SMR; P63313; -.
DR   BioGRID; 114609; 46.
DR   IntAct; P63313; 20.
DR   STRING; 9606.ENSP00000233143; -.
DR   iPTMnet; P63313; -.
DR   MetOSite; P63313; -.
DR   PhosphoSitePlus; P63313; -.
DR   BioMuta; TMSB10; -.
DR   DMDM; 54039778; -.
DR   EPD; P63313; -.
DR   jPOST; P63313; -.
DR   MassIVE; P63313; -.
DR   PaxDb; P63313; -.
DR   PeptideAtlas; P63313; -.
DR   PRIDE; P63313; -.
DR   ProteomicsDB; 57519; -.
DR   TopDownProteomics; P63313; -.
DR   Antibodypedia; 16880; 110 antibodies from 19 providers.
DR   DNASU; 9168; -.
DR   Ensembl; ENST00000233143.6; ENSP00000233143.4; ENSG00000034510.6.
DR   GeneID; 9168; -.
DR   KEGG; hsa:9168; -.
DR   MANE-Select; ENST00000233143.6; ENSP00000233143.4; NM_021103.4; NP_066926.1.
DR   UCSC; uc002sow.2; human.
DR   CTD; 9168; -.
DR   DisGeNET; 9168; -.
DR   GeneCards; TMSB10; -.
DR   HGNC; HGNC:11879; TMSB10.
DR   HPA; ENSG00000034510; Low tissue specificity.
DR   MIM; 188399; gene.
DR   neXtProt; NX_P63313; -.
DR   OpenTargets; ENSG00000034510; -.
DR   PharmGKB; PA36580; -.
DR   VEuPathDB; HostDB:ENSG00000034510; -.
DR   eggNOG; KOG4794; Eukaryota.
DR   GeneTree; ENSGT00940000163007; -.
DR   HOGENOM; CLU_208046_0_1_1; -.
DR   InParanoid; P63313; -.
DR   OrthoDB; 1632292at2759; -.
DR   PhylomeDB; P63313; -.
DR   PathwayCommons; P63313; -.
DR   SignaLink; P63313; -.
DR   BioGRID-ORCS; 9168; 235 hits in 1075 CRISPR screens.
DR   ChiTaRS; TMSB10; human.
DR   GeneWiki; TMSB10; -.
DR   GenomeRNAi; 9168; -.
DR   Pharos; P63313; Tbio.
DR   PRO; PR:P63313; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000034510; Expressed in cortical plate and 211 other tissues.
DR   Genevisible; P63313; 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   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..44
FT                   /note="Thymosin beta-10"
FT                   /id="PRO_0000045931"
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:0007744|PubMed:19413330"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         21
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZWY8"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63312"
FT   VARIANT         7
FT                   /note="M -> R (in dbSNP:rs1804515)"
FT                   /id="VAR_052304"
SQ   SEQUENCE   44 AA;  5026 MW;  5485277C275A1C70 CRC64;
     MADKPDMGEI ASFDKAKLKK TETQEKNTLP TKETIEQEKR SEIS
 
 
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