PTMA_MOUSE
ID PTMA_MOUSE Reviewed; 111 AA.
AC P26350; Q3UQV6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Prothymosin alpha;
DE Contains:
DE RecName: Full=Prothymosin alpha, N-terminally processed;
DE Contains:
DE RecName: Full=Thymosin alpha;
GN Name=Ptma;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2015308; DOI=10.1016/0167-4781(91)90141-8;
RA Schmidt G., Werner D.;
RT "Nucleotide sequence of the murine prothymosin alpha cDNA and its deduced
RT primary and secondary protein structure.";
RL Biochim. Biophys. Acta 1088:442-444(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-111.
RX PubMed=2226839; DOI=10.1016/0014-5793(90)81037-o;
RA Low T.L.K., Pan T.L., Lin Y.S.;
RT "Depression of prothymosin alpha production in murine thymus correlates
RT with staphylococcal enterotoxin-B-induced immunosuppression.";
RL FEBS Lett. 273:1-5(1990).
RN [5]
RP PROTEIN SEQUENCE OF 15-18; 22-68 AND 91-103.
RX PubMed=2479575; DOI=10.1016/0014-5793(89)81544-3;
RA Makarova T., Grebenshikov N., Egorov C., Vartapetian A., Bogdanov A.;
RT "Prothymosin alpha is an evolutionary conserved protein covalently linked
RT to a small RNA.";
RL FEBS Lett. 257:247-250(1989).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-15 AND LYS-103,
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-15, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Prothymosin alpha may mediate immune function by conferring
CC resistance to certain opportunistic infections.
CC -!- SUBUNIT: Interacts with NUPR1; regulates apoptotic process.
CC {ECO:0000250|UniProtKB:P06454}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Covalently linked to a small RNA of about 20 nucleotides.
CC -!- SIMILARITY: Belongs to the pro/parathymosin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X56135; CAA39601.1; -; mRNA.
DR EMBL; AK037980; BAC29913.1; -; mRNA.
DR EMBL; AK084218; BAC39141.1; -; mRNA.
DR EMBL; AK132003; BAE20932.1; -; mRNA.
DR EMBL; AK142076; BAE24932.1; -; mRNA.
DR EMBL; AK145650; BAE26566.1; -; mRNA.
DR EMBL; AK153953; BAE32276.1; -; mRNA.
DR EMBL; BC081453; AAH81453.1; -; mRNA.
DR EMBL; BC083135; AAH83135.1; -; mRNA.
DR CCDS; CCDS35649.1; -.
DR PIR; S15073; S15073.
DR RefSeq; NP_032998.1; NM_008972.2.
DR PDB; 2Z32; X-ray; 2.00 A; B=39-54.
DR PDBsum; 2Z32; -.
DR AlphaFoldDB; P26350; -.
DR BMRB; P26350; -.
DR SMR; P26350; -.
DR BioGRID; 202469; 19.
DR ELM; P26350; -.
DR IntAct; P26350; 1.
DR STRING; 10090.ENSMUSP00000044188; -.
DR iPTMnet; P26350; -.
DR PhosphoSitePlus; P26350; -.
DR EPD; P26350; -.
DR jPOST; P26350; -.
DR PaxDb; P26350; -.
DR PeptideAtlas; P26350; -.
DR PRIDE; P26350; -.
DR ProteomicsDB; 301957; -.
DR TopDownProteomics; P26350; -.
DR DNASU; 19231; -.
DR Ensembl; ENSMUST00000045897; ENSMUSP00000044188; ENSMUSG00000026238.
DR GeneID; 19231; -.
DR KEGG; mmu:19231; -.
DR UCSC; uc007bvp.1; mouse.
DR CTD; 5757; -.
DR MGI; MGI:97803; Ptma.
DR VEuPathDB; HostDB:ENSMUSG00000026238; -.
DR eggNOG; ENOG502S55T; Eukaryota.
DR GeneTree; ENSGT01020000232226; -.
DR InParanoid; P26350; -.
DR OMA; RTPPMND; -.
DR TreeFam; TF350357; -.
DR BioGRID-ORCS; 19231; 17 hits in 72 CRISPR screens.
DR ChiTaRS; Ptma; mouse.
DR EvolutionaryTrace; P26350; -.
DR PRO; PR:P26350; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P26350; protein.
DR Bgee; ENSMUSG00000026238; Expressed in epiblast (generic) and 123 other tissues.
DR ExpressionAtlas; P26350; baseline and differential.
DR Genevisible; P26350; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0043486; P:histone exchange; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR IDEAL; IID50035; -.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..111
FT /note="Prothymosin alpha"
FT /id="PRO_0000423256"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:2226839,
FT ECO:0007744|PubMed:23806337"
FT CHAIN 2..111
FT /note="Prothymosin alpha, N-terminally processed"
FT /id="PRO_0000299251"
FT PEPTIDE 2..29
FT /note="Thymosin alpha"
FT /id="PRO_0000029866"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 2
FT /note="N-acetylserine; in Prothymosin alpha, N-terminally
FT processed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01252"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 15
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT MOD_RES 103
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT CROSSLNK 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06454"
FT CONFLICT 106
FT /note="K -> KK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2Z32"
SQ SEQUENCE 111 AA; 12254 MW; 345FACE953A3E8FA CRC64;
MSDAAVDTSS EITTKDLKEK KEVVEEAENG RDAPANGNAQ NEENGEQEAD NEVDEEEEEG
GEEEEEEEEG DGEEEDGDED EEAEAPTGKR VAEDDEDDDV DTKKQKTEED D
