P06454 (PTMA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prothymosin alpha

Cleaved into the following chain:

1. Thymosin alpha-1

Gene names

Name:	PTMA
Synonyms:	TMSA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	111 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Nucleus
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Traceable author statement PubMed 10854063. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 111

110

Prothymosin alpha

PRO_0000299250

Peptide

2 – 29

28

Thymosin alpha-1

PRO_0000029865

Regions

Compositional bias

42 – 101

60

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.9 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18

Modified residue

2

1

Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.17

Modified residue

8

1

Phosphothreonine By similarity

Modified residue

9

1

Phosphoserine Ref.15

Modified residue

10

1

Phosphoserine Ref.17

Modified residue

13

1

Phosphothreonine By similarity

Modified residue

14

1

Phosphothreonine By similarity

Modified residue

15

1

N6-acetyllysine Ref.14

Modified residue

102

1

Phosphothreonine Ref.13

Modified residue

107

1

Phosphothreonine Ref.11

Natural variations

Alternative sequence

40

1

Missing in isoform 2.

VSP_011508

Secondary structure

1

.

.

.

.

.

111

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

9 – 28

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 910BBF9D8D14B8E7	FASTA	111	12,203
	10 20 30 40 50 60 MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAE NEENGEQEAD NEVDEEEEEG 70 80 90 100 110 GEEEEEEEEG DGEEEDGDED EEAESATGKR AAEDDEDDDV DTKKQKTDED D
	Isoform 2 [UniParc]. Checksum: 3A76436E79930993	FASTA	110	12,074
	10 20 30 40 50 60 MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAN EENGEQEADN EVDEEEEEGG 70 80 90 100 110 EEEEEEEEGD GEEEDGDEDE EAESATGKRA AEDDEDDDVD TKKQKTDEDD

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[15]	"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 SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
[18]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00455510.
IPI00827535.

PIR

TNHUA. A42004.
C33356.

RefSeq

NP_001092755.1. NM_001099285.1.
NP_002814.3. NM_002823.4.

UniGene

Hs.459927.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2L9I	NMR	-	A	2-29	[»]

ProteinModelPortal

P06454.

SMR

P06454. Positions 2-29.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06454. 3 interactions.

MINT

MINT-138772.

STRING

9606.ENSP00000344547.

PTM databases

PhosphoSite

P06454.

Polymorphism databases

DMDM

135834.

Proteomic databases

PaxDb

P06454.

PRIDE

P06454.

Protocols and materials databases

DNASU

5757.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341369; ENSP00000344547; ENSG00000187514.
ENST00000409115; ENSP00000386819; ENSG00000187514.

GeneID

5757.

KEGG

hsa:5757.

UCSC

uc002vsc.4. human.

Organism-specific databases

CTD

5757.

GeneCards

GC02P232536.

HGNC

HGNC:9623. PTMA.

HPA

HPA047183.

MIM

188390. gene.

neXtProt

NX_P06454.

PharmGKB

PA33966.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG259527.

HOGENOM

HOG000089972.

KO

K13784.

Gene expression databases

ArrayExpress

P06454.

Bgee

P06454.

CleanEx

HS_PTMA.

Genevestigator

P06454.

GermOnline

ENSG00000187514. Homo sapiens.

Family and domain databases

InterPro

IPR004931. Pro/parathymosin.
[Graphical view]

PANTHER

PTHR22745. PTHR22745. 1 hit.

Pfam

PF03247. Prothymosin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PTMA. human.

GenomeRNAi

5757.

NextBio

22406.

PMAP-CutDB

P06454.

SOURCE

Search...

Entry information

Entry name

PTMA_HUMAN

Accession

Primary (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 3, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.