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P06454 (PTMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prothymosin alpha
Gene names
Name:PTMA
Synonyms:TMSA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length111 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.

Subcellular location

Nucleus.

Post-translational modification

Covalently linked to a small RNA of about 20 nucleotides By similarity.

Sequence similarities

Belongs to the pro/parathymosin family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtranscription, DNA-templated

Traceable author statement PubMed 10854063. Source: ProtInc

   Cellular_componentnucleus

Traceable author statement PubMed 10854063. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06454-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06454-2)

The sequence of this isoform differs from the canonical sequence as follows:
     40-40: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 111111Prothymosin alpha
PRO_0000423255
Initiator methionine11Removed; alternate
Chain2 – 111110Prothymosin alpha, N-terminally processed
PRO_0000299250
Peptide2 – 2928Thymosin alpha-1
PRO_0000029865

Regions

Compositional bias42 – 10160Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16
Modified residue21N-acetylserine; in Prothymosin alpha, N-terminally processed Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21
Modified residue21Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18
Modified residue81Phosphothreonine By similarity
Modified residue91Phosphoserine Ref.16
Modified residue101Phosphoserine Ref.18
Modified residue131Phosphothreonine By similarity
Modified residue141Phosphothreonine By similarity
Modified residue151N6-acetyllysine; alternate Ref.15
Modified residue151N6-succinyllysine; alternate By similarity
Modified residue1021Phosphothreonine Ref.14
Modified residue1031N6-acetyllysine By similarity
Modified residue1071Phosphothreonine Ref.11

Natural variations

Alternative sequence401Missing in isoform 2.
VSP_011508

Secondary structure

..... 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 910BBF9D8D14B8E7

FASTA11112,203
        10         20         30         40         50         60 
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAE NEENGEQEAD NEVDEEEEEG 

        70         80         90        100        110 
GEEEEEEEEG DGEEEDGDED EEAESATGKR AAEDDEDDDV DTKKQKTDED D 

« Hide

Isoform 2 [UniParc].

Checksum: 3A76436E79930993
Show »

FASTA11012,074

References

« Hide 'large scale' references
[1]"The human prothymosin alpha gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA."
Eschenfeldt W.H., Berger S.L.
Proc. Natl. Acad. Sci. U.S.A. 83:9403-9407(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning of cDNA for human prothymosin alpha."
Goodall G.J., Dominguez F., Horecker B.L.
Proc. Natl. Acad. Sci. U.S.A. 83:8926-8928(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Isolation and partial sequencing of the human prothymosin alpha gene family. Evidence against export of the gene products."
Eschenfeldt W.H., Manrow R.E., Krug M.S., Berger S.L.
J. Biol. Chem. 264:7546-7555(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[4]"The expression of prothymosin alpha gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation."
Gomez-Marquez J., Segade F., Dosil M., Pichel J.G., Bustelo X.R., Freire M.
J. Biol. Chem. 264:8451-8454(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"A novel prothymosin alpha cDNA from thymus."
Li Z., Fan Q., Huang W., An L.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal thymus.
[6]"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] (ISOFORM 2).
Tissue: Cervix, Lung, PNS, Skin and Testis.
[7]"Prothymosin alpha gene in humans: organization of its promoter region and localization to chromosome 2."
Szabo P., Panneerselvam C., Clinton M., Frangou-Lazaridis M., Weksler D., Whittington E., Macera M.J., Grzeschik K.H., Selvakumar A., Horecker B.L.
Hum. Genet. 90:629-634(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[8]"Human prothymosin alpha: amino acid sequence and immunologic properties."
Pan L.X., Haritos A.A., Wideman J., Komiyama T., Chang M., Stein S., Salvin S.B., Horecker B.L.
Arch. Biochem. Biophys. 250:197-201(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[9]"Phosphorylation of human and bovine prothymosin alpha in vivo."
Sburlati A.R., De La Rosa A., Batey D.W., Kurys G.L., Manrow R.E., Pannell L.K., Martin B.M., Sheeley D.M., Berger S.L.
Biochemistry 32:4587-4596(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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 SER-2 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"NMR structure of human thymosin alpha-1."
Elizondo-Riojas M.A., Chamow S.M., Tuthill C.W., Gorenstein D.G., Volk D.E.
Biochem. Biophys. Res. Commun. 416:356-361(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-29, ACETYLATION AT SER-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14630 mRNA. Translation: AAA61182.1.
M14483 mRNA. Translation: AAA61183.1.
M67480, J04797 Genomic DNA. Translation: AAA63240.1.
M67480, J04797 Genomic DNA. Translation: AAA63239.1.
M26708 mRNA. Translation: AAA60213.1.
AF348514 mRNA. Translation: AAK30146.1.
BC051265 mRNA. Translation: AAH51265.1.
BC066905 mRNA. Translation: AAH66905.1.
BC070480 mRNA. Translation: AAH70480.1.
BC071647 mRNA. Translation: AAH71647.1.
BC071879 mRNA. Translation: AAH71879.1.
S56449 Genomic DNA. Translation: AAD13882.1.
PIRTNHUA. A42004.
C33356.
RefSeqNP_001092755.1. NM_001099285.1.
NP_002814.3. NM_002823.4.
UniGeneHs.459927.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9INMR-A2-29[»]
ProteinModelPortalP06454.
SMRP06454. Positions 2-29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111724. 63 interactions.
IntActP06454. 5 interactions.
MINTMINT-138772.
STRING9606.ENSP00000344547.

PTM databases

PhosphoSiteP06454.

Proteomic databases

PaxDbP06454.
PRIDEP06454.

Protocols and materials databases

DNASU5757.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341369; ENSP00000344547; ENSG00000187514. [P06454-1]
ENST00000409115; ENSP00000386819; ENSG00000187514. [P06454-2]
GeneID5757.
KEGGhsa:5757.
UCSCuc002vsc.4. human. [P06454-1]

Organism-specific databases

CTD5757.
GeneCardsGC02P232536.
HGNCHGNC:9623. PTMA.
HPAHPA047183.
MIM188390. gene.
neXtProtNX_P06454.
PharmGKBPA33966.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259527.
HOGENOMHOG000089972.
KOK13784.
TreeFamTF350357.

Gene expression databases

BgeeP06454.
CleanExHS_PTMA.
GenevestigatorP06454.

Family and domain databases

InterProIPR004931. Pro/parathymosin.
[Graphical view]
PANTHERPTHR22745. PTHR22745. 1 hit.
PfamPF03247. Prothymosin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTMA. human.
GeneWikiThymosin_%CE%B11.
GenomeRNAi5757.
NextBio22406.
PMAP-CutDBP06454.
PROP06454.
SOURCESearch...

Entry information

Entry namePTMA_HUMAN
AccessionPrimary (citable) accession number: P06454
Secondary accession number(s): Q15249, Q15592
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM