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Protein

Prothymosin alpha

Gene

Ptma

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. histone binding Source: MGI

GO - Biological processi

  1. histone exchange Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Prothymosin alpha
Cleaved into the following 2 chains:
Gene namesi
Name:Ptma
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97803. Ptma.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Prothymosin alphaPRO_0000423256Add
BLAST
Initiator methioninei1 – 11Removed; alternate2 Publications
Chaini2 – 111110Prothymosin alpha, N-terminally processedPRO_0000299251Add
BLAST
Peptidei2 – 2928Thymosin alphaPRO_0000029866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylserine; in Prothymosin alpha, N-terminally processed1 Publication
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei13 – 131PhosphothreonineBy similarity
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei15 – 151N6-acetyllysine; alternate1 Publication
Modified residuei15 – 151N6-succinyllysine; alternate1 Publication
Modified residuei102 – 1021PhosphothreonineBy similarity
Modified residuei103 – 1031N6-acetyllysine1 Publication
Modified residuei107 – 1071PhosphothreonineBy similarity

Post-translational modificationi

Covalently linked to a small RNA of about 20 nucleotides.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26350.
PaxDbiP26350.
PRIDEiP26350.

PTM databases

PhosphoSiteiP26350.

Miscellaneous databases

PMAP-CutDBP26350.

Expressioni

Gene expression databases

BgeeiP26350.
CleanExiMM_PTMA.
ExpressionAtlasiP26350. baseline.
GenevestigatoriP26350.

Interactioni

Protein-protein interaction databases

BioGridi202469. 4 interactions.

Structurei

Secondary structure

1
111
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni42 – 443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z32X-ray2.00B39-54[»]
SMRiP26350. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26350.

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

eggNOGiNOG44821.
HOVERGENiHBG078507.
InParanoidiP26350.
KOiK13784.
OMAiKVDTSSE.
OrthoDBiEOG70PC27.
TreeFamiTF350357.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P26350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAQ NEENGEQEAD
60 70 80 90 100
NEVDEEEEEG GEEEEEEEEG DGEEEDGDED EEAEAPTGKR VAEDDEDDDV
110
DTKKQKTEED D
Length:111
Mass (Da):12,254
Last modified:January 22, 2007 - v2
Checksum:i345FACE953A3E8FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061K → KK AA sequence (PubMed:2226839).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35649.1.
PIRiS15073.
RefSeqiNP_032998.1. NM_008972.2.
UniGeneiMm.19187.

Genome annotation databases

EnsembliENSMUST00000045897; ENSMUSP00000044188; ENSMUSG00000026238.
GeneIDi19231.
KEGGimmu:19231.
UCSCiuc007bvp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35649.1.
PIRiS15073.
RefSeqiNP_032998.1. NM_008972.2.
UniGeneiMm.19187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z32X-ray2.00B39-54[»]
SMRiP26350. Positions 2-29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202469. 4 interactions.

PTM databases

PhosphoSiteiP26350.

Proteomic databases

MaxQBiP26350.
PaxDbiP26350.
PRIDEiP26350.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045897; ENSMUSP00000044188; ENSMUSG00000026238.
GeneIDi19231.
KEGGimmu:19231.
UCSCiuc007bvp.1. mouse.

Organism-specific databases

CTDi5757.
MGIiMGI:97803. Ptma.

Phylogenomic databases

eggNOGiNOG44821.
HOVERGENiHBG078507.
InParanoidiP26350.
KOiK13784.
OMAiKVDTSSE.
OrthoDBiEOG70PC27.
TreeFamiTF350357.

Miscellaneous databases

ChiTaRSiPtma. mouse.
EvolutionaryTraceiP26350.
NextBioi296040.
PMAP-CutDBP26350.
PROiP26350.
SOURCEiSearch...

Gene expression databases

BgeeiP26350.
CleanExiMM_PTMA.
ExpressionAtlasiP26350. baseline.
GenevestigatoriP26350.

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. "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(1990) [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.
    , 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(2004) [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(2003) [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(1989) [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(1988) [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(2008) [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(2012) [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.

Entry informationi

Entry nameiPTMA_MOUSE
AccessioniPrimary (citable) accession number: P26350
Secondary accession number(s): Q3UQV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 1992
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.