Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thymosin beta-10

Gene

TMSB10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Thymosin beta-10
Gene namesi
Name:TMSB10
Synonyms:PTMB10, THYB10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11879. TMSB10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36580.

Polymorphism and mutation databases

BioMutaiTMSB10.
DMDMi54039778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 4443Thymosin beta-10PRO_0000045931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei4 – 41N6-acetyllysineCombined sources
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei15 – 151N6-acetyllysineCombined sources
Modified residuei21 – 211PhosphothreonineBy similarity
Modified residuei23 – 231PhosphothreonineCombined sources
Modified residuei34 – 341PhosphothreonineBy similarity
Modified residuei39 – 391N6-acetyllysineCombined sources
Modified residuei41 – 411PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63313.
PaxDbiP63313.
PeptideAtlasiP63313.
PRIDEiP63313.
TopDownProteomicsiP63313.

PTM databases

iPTMnetiP63313.
PhosphoSiteiP63313.

Expressioni

Developmental stagei

Found to decrease dramatically after birth.1 Publication

Gene expression databases

BgeeiP63313.
CleanExiHS_TMSB10.
GenevisibleiP63313. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ALAS1P131963EBI-2688673,EBI-3905054
KRTAP9-2Q9BYQ43EBI-2688673,EBI-1044640
POT1Q9NUX52EBI-2688673,EBI-752420

Protein-protein interaction databases

BioGridi114609. 14 interactions.
IntActiP63313. 11 interactions.
STRINGi9606.ENSP00000233143.

Structurei

3D structure databases

ProteinModelPortaliP63313.
SMRiP63313. Positions 6-41.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the thymosin beta family.Curated

Phylogenomic databases

eggNOGiKOG4794. Eukaryota.
ENOG410Y3I4. LUCA.
GeneTreeiENSGT00390000007040.
HOVERGENiHBG012534.
InParanoidiP63313.
KOiK13785.
OrthoDBiEOG7TJ3MT.
PhylomeDBiP63313.

Family and domain databases

Gene3Di1.20.5.520. 1 hit.
InterProiIPR001152. Beta-thymosin.
[Graphical view]
PANTHERiPTHR12021. PTHR12021. 1 hit.
PfamiPF01290. Thymosin. 1 hit.
[Graphical view]
PIRSFiPIRSF001828. Thymosin_beta. 1 hit.
ProDomiPD005116. Thymosin_b4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00152. THY. 1 hit.
[Graphical view]
PROSITEiPS00500. THYMOSIN_B4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
MADKPDMGEI ASFDKAKLKK TETQEKNTLP TKETIEQEKR SEIS
Length:44
Mass (Da):5,026
Last modified:January 23, 2007 - v2
Checksum:i5485277C275A1C70
GO

Sequence cautioni

The sequence AAA36746.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAC41691.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71M → R.
Corresponds to variant rs1804515 [ dbSNP | Ensembl ].
VAR_052304

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20259 mRNA. Translation: AAA36744.1.
M92381 mRNA. Translation: AAC41691.1. Different initiation.
S54005 mRNA. Translation: AAB25225.1.
M92383 Genomic DNA. Translation: AAA36746.1. Different initiation.
AY453400 mRNA. Translation: AAS47517.1.
AK311952 mRNA. Translation: BAG34892.1.
AC022210 Genomic DNA. Translation: AAY24191.1.
BC016025 mRNA. Translation: AAH16025.1.
BC016731 mRNA. Translation: AAH16731.1.
CCDSiCCDS1970.1.
PIRiA27704.
RefSeqiNP_066926.1. NM_021103.3.
UniGeneiHs.446574.

Genome annotation databases

EnsembliENST00000233143; ENSP00000233143; ENSG00000034510.
GeneIDi9168.
KEGGihsa:9168.
UCSCiuc002sow.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20259 mRNA. Translation: AAA36744.1.
M92381 mRNA. Translation: AAC41691.1. Different initiation.
S54005 mRNA. Translation: AAB25225.1.
M92383 Genomic DNA. Translation: AAA36746.1. Different initiation.
AY453400 mRNA. Translation: AAS47517.1.
AK311952 mRNA. Translation: BAG34892.1.
AC022210 Genomic DNA. Translation: AAY24191.1.
BC016025 mRNA. Translation: AAH16025.1.
BC016731 mRNA. Translation: AAH16731.1.
CCDSiCCDS1970.1.
PIRiA27704.
RefSeqiNP_066926.1. NM_021103.3.
UniGeneiHs.446574.

3D structure databases

ProteinModelPortaliP63313.
SMRiP63313. Positions 6-41.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114609. 14 interactions.
IntActiP63313. 11 interactions.
STRINGi9606.ENSP00000233143.

PTM databases

iPTMnetiP63313.
PhosphoSiteiP63313.

Polymorphism and mutation databases

BioMutaiTMSB10.
DMDMi54039778.

Proteomic databases

EPDiP63313.
PaxDbiP63313.
PeptideAtlasiP63313.
PRIDEiP63313.
TopDownProteomicsiP63313.

Protocols and materials databases

DNASUi9168.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233143; ENSP00000233143; ENSG00000034510.
GeneIDi9168.
KEGGihsa:9168.
UCSCiuc002sow.2. human.

Organism-specific databases

CTDi9168.
GeneCardsiTMSB10.
HGNCiHGNC:11879. TMSB10.
MIMi188399. gene.
neXtProtiNX_P63313.
PharmGKBiPA36580.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4794. Eukaryota.
ENOG410Y3I4. LUCA.
GeneTreeiENSGT00390000007040.
HOVERGENiHBG012534.
InParanoidiP63313.
KOiK13785.
OrthoDBiEOG7TJ3MT.
PhylomeDBiP63313.

Miscellaneous databases

ChiTaRSiTMSB10. human.
GeneWikiiTMSB10.
GenomeRNAii9168.
NextBioi34383.
PROiP63313.
SOURCEiSearch...

Gene expression databases

BgeeiP63313.
CleanExiHS_TMSB10.
GenevisibleiP63313. HS.

Family and domain databases

Gene3Di1.20.5.520. 1 hit.
InterProiIPR001152. Beta-thymosin.
[Graphical view]
PANTHERiPTHR12021. PTHR12021. 1 hit.
PfamiPF01290. Thymosin. 1 hit.
[Graphical view]
PIRSFiPIRSF001828. Thymosin_beta. 1 hit.
ProDomiPD005116. Thymosin_b4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00152. THY. 1 hit.
[Graphical view]
PROSITEiPS00500. THYMOSIN_B4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a human kidney cDNA clone encoding thymosin beta 10."
    McCreary V., Kartha S., Bell G.I., Toback F.G.
    Biochem. Biophys. Res. Commun. 152:862-866(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Thymosin beta 10 levels in developing human brain and its regulation by retinoic acid in the HTB-10 neuroblastoma."
    Hall A.K., Hempstead J., Morgan J.I.
    Brain Res. Mol. Brain Res. 8:129-135(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Brain.
  3. "Thymosin beta-10 expression in melanoma cell lines and melanocytic lesions: a new progression marker for human cutaneous melanoma."
    Weterman M.A., van Muijen G.N.P., Ruiter D.J., Bloemers H.P.J.
    Int. J. Cancer 53:278-284(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Human thymosin beta 10 gene: its characterization and nucleotide sequence."
    Condon M.R., Hall A.K.
    Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Identification of a migration inducing gene."
    Kim J.W.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Uterus.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-15 AND LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTYB10_HUMAN
AccessioniPrimary (citable) accession number: P63313
Secondary accession number(s): P13472, Q596K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.