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

Prothymosin alpha

Gene

PTMA

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

Functioni

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

GO - Biological processi

  1. transcription, DNA-templated Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Prothymosin alpha
Cleaved into the following 2 chains:
Gene namesi
Name:PTMA
Synonyms:TMSA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9623. PTMA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33966.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Prothymosin alphaPRO_0000423255Add
BLAST
Initiator methioninei1 – 11Removed; alternate9 Publications
Chaini2 – 111110Prothymosin alpha, N-terminally processedPRO_0000299250Add
BLAST
Peptidei2 – 2928Thymosin alpha-1PRO_0000029865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylserine; in Prothymosin alpha, N-terminally processed9 Publications
Modified residuei2 – 21Phosphoserine6 Publications
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei13 – 131PhosphothreonineBy similarity
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei15 – 151N6-acetyllysine; alternate1 Publication
Modified residuei15 – 151N6-succinyllysine; alternateBy similarity
Modified residuei102 – 1021Phosphothreonine1 Publication
Modified residuei103 – 1031N6-acetyllysineBy similarity
Modified residuei107 – 1071Phosphothreonine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06454.
PaxDbiP06454.
PRIDEiP06454.

PTM databases

PhosphoSiteiP06454.

Miscellaneous databases

PMAP-CutDBP06454.

Expressioni

Gene expression databases

BgeeiP06454.
CleanExiHS_PTMA.
ExpressionAtlasiP06454. baseline and differential.
GenevestigatoriP06454.

Organism-specific databases

HPAiHPA047183.

Interactioni

Protein-protein interaction databases

BioGridi111724. 66 interactions.
DIPiDIP-40743N.
IntActiP06454. 6 interactions.
MINTiMINT-138772.
STRINGi9606.ENSP00000344547.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi9 – 2820Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9INMR-A2-29[»]
ProteinModelPortaliP06454.
SMRiP06454. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 10160Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the pro/parathymosin family.Curated

Phylogenomic databases

eggNOGiNOG259527.
GeneTreeiENSGT00730000111051.
HOGENOMiHOG000089972.
InParanoidiP06454.
KOiK13784.
TreeFamiTF350357.

Family and domain databases

InterProiIPR004931. Pro/parathymosin.
[Graphical view]
PANTHERiPTHR22745. PTHR22745. 1 hit.
PfamiPF03247. Prothymosin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06454-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAE NEENGEQEAD
60 70 80 90 100
NEVDEEEEEG GEEEEEEEEG DGEEEDGDED EEAESATGKR AAEDDEDDDV
110
DTKKQKTDED D
Length:111
Mass (Da):12,203
Last modified:January 23, 2007 - v2
Checksum:i910BBF9D8D14B8E7
GO
Isoform 2 (identifier: P06454-2) [UniParc]FASTAAdd to basket

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

Show »
Length:110
Mass (Da):12,074
Checksum:i3A76436E79930993
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei40 – 401Missing in isoform 2. 4 PublicationsVSP_011508

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42833.1. [P06454-1]
CCDS46541.1. [P06454-2]
PIRiA42004. TNHUA.
C33356.
RefSeqiNP_001092755.1. NM_001099285.1. [P06454-1]
NP_002814.3. NM_002823.4. [P06454-2]
UniGeneiHs.459927.

Genome annotation databases

EnsembliENST00000341369; ENSP00000344547; ENSG00000187514. [P06454-1]
ENST00000409115; ENSP00000386819; ENSG00000187514. [P06454-2]
GeneIDi5757.
KEGGihsa:5757.
UCSCiuc002vsc.4. human. [P06454-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42833.1. [P06454-1]
CCDS46541.1. [P06454-2]
PIRiA42004. TNHUA.
C33356.
RefSeqiNP_001092755.1. NM_001099285.1. [P06454-1]
NP_002814.3. NM_002823.4. [P06454-2]
UniGeneiHs.459927.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L9INMR-A2-29[»]
ProteinModelPortaliP06454.
SMRiP06454. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111724. 66 interactions.
DIPiDIP-40743N.
IntActiP06454. 6 interactions.
MINTiMINT-138772.
STRINGi9606.ENSP00000344547.

PTM databases

PhosphoSiteiP06454.

Proteomic databases

MaxQBiP06454.
PaxDbiP06454.
PRIDEiP06454.

Protocols and materials databases

DNASUi5757.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341369; ENSP00000344547; ENSG00000187514. [P06454-1]
ENST00000409115; ENSP00000386819; ENSG00000187514. [P06454-2]
GeneIDi5757.
KEGGihsa:5757.
UCSCiuc002vsc.4. human. [P06454-1]

Organism-specific databases

CTDi5757.
GeneCardsiGC02P232571.
HGNCiHGNC:9623. PTMA.
HPAiHPA047183.
MIMi188390. gene.
neXtProtiNX_P06454.
PharmGKBiPA33966.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG259527.
GeneTreeiENSGT00730000111051.
HOGENOMiHOG000089972.
InParanoidiP06454.
KOiK13784.
TreeFamiTF350357.

Miscellaneous databases

ChiTaRSiPTMA. human.
GeneWikiiThymosin_%CE%B11.
GenomeRNAii5757.
NextBioi22406.
PMAP-CutDBP06454.
PROiP06454.
SOURCEiSearch...

Gene expression databases

BgeeiP06454.
CleanExiHS_PTMA.
ExpressionAtlasiP06454. baseline and differential.
GenevestigatoriP06454.

Family and domain databases

InterProiIPR004931. Pro/parathymosin.
[Graphical view]
PANTHERiPTHR22745. PTHR22745. 1 hit.
PfamiPF03247. Prothymosin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. 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(1988) [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(1988) [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 (JAN-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(2003) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
  8. Cited for: PARTIAL PROTEIN SEQUENCE.
  9. 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. 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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2008) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2009) [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. 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(2010) [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], CLEAVAGE OF INITIATOR METHIONINE [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. Cited for: STRUCTURE BY NMR OF 2-29, ACETYLATION AT SER-2.

Entry informationi

Entry nameiPTMA_HUMAN
AccessioniPrimary (citable) accession number: P06454
Secondary accession number(s): Q15249, Q15592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 146 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.