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P26350 (PTMA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prothymosin alpha
Gene names
Name:Ptma
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

Sequence similarities

Belongs to the pro/parathymosin family.

Ontologies

Keywords
   Cellular componentNucleus
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processhistone exchange

Inferred from direct assay PubMed 20434447. Source: MGI

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone binding

Inferred from direct assay PubMed 20434447. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 111111Prothymosin alpha
PRO_0000423256
Initiator methionine11Removed; alternate Ref.4 Ref.7
Chain2 – 111110Prothymosin alpha, N-terminally processed
PRO_0000299251
Peptide2 – 2928Thymosin alpha
PRO_0000029866

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylserine; in Prothymosin alpha, N-terminally processed Ref.7
Modified residue21Phosphoserine By similarity
Modified residue81Phosphothreonine By similarity
Modified residue91Phosphoserine By similarity
Modified residue101Phosphoserine By similarity
Modified residue131Phosphothreonine By similarity
Modified residue141Phosphothreonine By similarity
Modified residue151N6-acetyllysine; alternate Ref.7
Modified residue151N6-succinyllysine; alternate Ref.7
Modified residue1021Phosphothreonine By similarity
Modified residue1031N6-acetyllysine Ref.7
Modified residue1071Phosphothreonine By similarity

Experimental info

Sequence conflict1061K → KK AA sequence Ref.4

Secondary structure

... 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26350 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 345FACE953A3E8FA

FASTA11112,254
        10         20         30         40         50         60 
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAQ NEENGEQEAD NEVDEEEEEG 

        70         80         90        100        110 
GEEEEEEEEG DGEEEDGDED EEAEAPTGKR VAEDDEDDDV DTKKQKTEED D 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the murine prothymosin alpha cDNA and its deduced primary and secondary protein structure."
Schmidt G., Werner D.
Biochim. Biophys. Acta 1088:442-444(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Eye and Thymus.
[3]"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].
Strain: C57BL/6.
Tissue: Brain and Limb.
[4]"Depression of prothymosin alpha production in murine thymus correlates with staphylococcal enterotoxin-B-induced immunosuppression."
Low T.L.K., Pan T.L., Lin Y.S.
FEBS Lett. 273:1-5(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-111.
[5]"Prothymosin alpha is an evolutionary conserved protein covalently linked to a small RNA."
Makarova T., Grebenshikov N., Egorov C., Vartapetian A., Bogdanov A.
FEBS Lett. 257:247-250(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-18; 22-68 AND 91-103.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-15 AND LYS-103, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56135 mRNA. Translation: CAA39601.1.
AK037980 mRNA. Translation: BAC29913.1.
AK084218 mRNA. Translation: BAC39141.1.
AK132003 mRNA. Translation: BAE20932.1.
AK142076 mRNA. Translation: BAE24932.1.
AK145650 mRNA. Translation: BAE26566.1.
AK153953 mRNA. Translation: BAE32276.1.
BC081453 mRNA. Translation: AAH81453.1.
BC083135 mRNA. Translation: AAH83135.1.
CCDSCCDS35649.1.
PIRS15073.
RefSeqNP_032998.1. NM_008972.2.
UniGeneMm.19187.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z32X-ray2.00B39-54[»]
ProteinModelPortalP26350.
SMRP26350. Positions 2-29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202469. 4 interactions.

PTM databases

PhosphoSiteP26350.

Proteomic databases

MaxQBP26350.
PaxDbP26350.
PRIDEP26350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045897; ENSMUSP00000044188; ENSMUSG00000026238.
GeneID19231.
KEGGmmu:19231.
UCSCuc007bvp.1. mouse.

Organism-specific databases

CTD5757.
MGIMGI:97803. Ptma.

Phylogenomic databases

eggNOGNOG44821.
HOVERGENHBG078507.
InParanoidP26350.
KOK13784.
OMASERCHIS.
OrthoDBEOG70PC27.
TreeFamTF350357.

Gene expression databases

BgeeP26350.
CleanExMM_PTMA.
GenevestigatorP26350.

Family and domain databases

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

Other

ChiTaRSPTMA. mouse.
EvolutionaryTraceP26350.
NextBio296040.
PMAP-CutDBP26350.
PROP26350.
SOURCESearch...

Entry information

Entry namePTMA_MOUSE
AccessionPrimary (citable) accession number: P26350
Secondary accession number(s): Q3UQV6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot