Full text data of PTMS
PTMS
[Confidence: low (only semi-automatic identification from reviews)]
Parathymosin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Parathymosin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P20962
ID PTMS_HUMAN Reviewed; 102 AA.
AC P20962;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Parathymosin;
GN Name=PTMS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2537638; DOI=10.1016/0006-291X(89)92801-5;
RA Clinton M., Frangou-Lazaridis M., Panneerselvam C., Horecker B.L.;
RT "The sequence of human parathymosin deduced from a cloned human kidney
RT cDNA.";
RL Biochem. Biophys. Res. Commun. 158:855-862(1989).
RN [2]
RP PROTEIN SEQUENCE OF 5-15, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-4; LYS-15 AND LYS-92,
RP MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Parathymosin may mediate immune function by blocking the
CC effect of prothymosin alpha which confers resistance to certain
CC opportunistic infections.
CC -!- SIMILARITY: Belongs to the pro/parathymosin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M24398; AAA61185.1; -; mRNA.
DR PIR; A32264; A32264.
DR RefSeq; NP_002815.3; NM_002824.4.
DR UniGene; Hs.504613; -.
DR ProteinModelPortal; P20962; -.
DR IntAct; P20962; 11.
DR MINT; MINT-5000299; -.
DR STRING; 9606.ENSP00000310088; -.
DR PhosphoSite; P20962; -.
DR DMDM; 135846; -.
DR PaxDb; P20962; -.
DR PRIDE; P20962; -.
DR DNASU; 5763; -.
DR Ensembl; ENST00000309083; ENSP00000310088; ENSG00000159335.
DR GeneID; 5763; -.
DR KEGG; hsa:5763; -.
DR UCSC; uc001qqq.3; human.
DR CTD; 5763; -.
DR GeneCards; GC12P006875; -.
DR HGNC; HGNC:9629; PTMS.
DR HPA; HPA038186; -.
DR MIM; 168440; gene.
DR neXtProt; NX_P20962; -.
DR PharmGKB; PA33973; -.
DR eggNOG; NOG85883; -.
DR HOGENOM; HOG000115773; -.
DR InParanoid; P20962; -.
DR OMA; VEEPRSC; -.
DR ChiTaRS; PTMS; human.
DR GeneWiki; PTMS_(gene); -.
DR GenomeRNAi; 5763; -.
DR NextBio; 22422; -.
DR PRO; PR:P20962; -.
DR ArrayExpress; P20962; -.
DR Bgee; P20962; -.
DR CleanEx; HS_PTMS; -.
DR Genevestigator; P20962; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; Immunity;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 102 Parathymosin.
FT /FTId=PRO_0000191632.
FT COMPBIAS 36 90 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 4 4 N6-acetyllysine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 15 15 N6-acetyllysine.
FT MOD_RES 92 92 N6-acetyllysine.
SQ SEQUENCE 102 AA; 11530 MW; 1B169F911B37B856 CRC64;
MSEKSVEAAA ELSAKDLKEK KEKVEEKASR KERKKEVVEE EENGAEEEEE ETAEDGEEED
EGEEEDEEEE EEDDEGPALK RAAEEEDEAD PKRQKTENGA SA
//
ID PTMS_HUMAN Reviewed; 102 AA.
AC P20962;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Parathymosin;
GN Name=PTMS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2537638; DOI=10.1016/0006-291X(89)92801-5;
RA Clinton M., Frangou-Lazaridis M., Panneerselvam C., Horecker B.L.;
RT "The sequence of human parathymosin deduced from a cloned human kidney
RT cDNA.";
RL Biochem. Biophys. Res. Commun. 158:855-862(1989).
RN [2]
RP PROTEIN SEQUENCE OF 5-15, AND MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-4; LYS-15 AND LYS-92,
RP MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Parathymosin may mediate immune function by blocking the
CC effect of prothymosin alpha which confers resistance to certain
CC opportunistic infections.
CC -!- SIMILARITY: Belongs to the pro/parathymosin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M24398; AAA61185.1; -; mRNA.
DR PIR; A32264; A32264.
DR RefSeq; NP_002815.3; NM_002824.4.
DR UniGene; Hs.504613; -.
DR ProteinModelPortal; P20962; -.
DR IntAct; P20962; 11.
DR MINT; MINT-5000299; -.
DR STRING; 9606.ENSP00000310088; -.
DR PhosphoSite; P20962; -.
DR DMDM; 135846; -.
DR PaxDb; P20962; -.
DR PRIDE; P20962; -.
DR DNASU; 5763; -.
DR Ensembl; ENST00000309083; ENSP00000310088; ENSG00000159335.
DR GeneID; 5763; -.
DR KEGG; hsa:5763; -.
DR UCSC; uc001qqq.3; human.
DR CTD; 5763; -.
DR GeneCards; GC12P006875; -.
DR HGNC; HGNC:9629; PTMS.
DR HPA; HPA038186; -.
DR MIM; 168440; gene.
DR neXtProt; NX_P20962; -.
DR PharmGKB; PA33973; -.
DR eggNOG; NOG85883; -.
DR HOGENOM; HOG000115773; -.
DR InParanoid; P20962; -.
DR OMA; VEEPRSC; -.
DR ChiTaRS; PTMS; human.
DR GeneWiki; PTMS_(gene); -.
DR GenomeRNAi; 5763; -.
DR NextBio; 22422; -.
DR PRO; PR:P20962; -.
DR ArrayExpress; P20962; -.
DR Bgee; P20962; -.
DR CleanEx; HS_PTMS; -.
DR Genevestigator; P20962; -.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; Immunity;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 102 Parathymosin.
FT /FTId=PRO_0000191632.
FT COMPBIAS 36 90 Asp/Glu-rich (acidic).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 4 4 N6-acetyllysine.
FT MOD_RES 5 5 Phosphoserine.
FT MOD_RES 15 15 N6-acetyllysine.
FT MOD_RES 92 92 N6-acetyllysine.
SQ SEQUENCE 102 AA; 11530 MW; 1B169F911B37B856 CRC64;
MSEKSVEAAA ELSAKDLKEK KEKVEEKASR KERKKEVVEE EENGAEEEEE ETAEDGEEED
EGEEEDEEEE EEDDEGPALK RAAEEEDEAD PKRQKTENGA SA
//
MIM
168440
*RECORD*
*FIELD* NO
168440
*FIELD* TI
*168440 PARATHYMOSIN; PTMS
*FIELD* TX
CLONING
Parathymosin is a polypeptide similar in size and amino acid composition
read moreto prothymosin-alpha (188390). It has a high content of dicarboxylic
amino acids and a complete absence of aromatic and sulfur-containing
amino acids. It has 101 amino acid residues as compared to 111 for
prothymosin. Clinton et al. (1989) reported the isolation of a cDNA
clone for human kidney parathymosin containing the complete coding
region and extending into the 5-prime and 3-prime flanking sequences.
The open reading frame contains 306 nucleotides, including the codon for
the initiator methionine. Analysis of the 5-prime flanking sequence
excluded the presence of a hydrophobic signal peptide in the translated
sequence. This permitted the conclusion that parathymosin, like
prothymosin-alpha, is synthesized without formation of a larger
precursor polypeptide. Parathymosin and prothymosin show a reciprocal
relationship: the highest levels of parathymosin and its mRNA are
present in liver, kidney, and brain (with lowest levels in thymus and
spleen), whereas prothymosin-alpha and its mRNA are present in highest
concentrations in thymus and spleen (with lower levels in kidney, brain,
and liver).
MAPPING
By in situ hybridization of rat parathymosin cDNA to human metaphase
chromosomes, Szabo et al. (1989) localized the gene for human
parathymosin to chromosome 17q12-q22. However, Gross (2011) mapped the
PTMS gene to chromosome 12p13.31 based on an alignment of the PTMS
sequence (GenBank GENBANK BC017025) with the genomic sequence (GRCh37).
*FIELD* RF
1. Clinton, M.; Frangou-Lazaridis, M.; Panneerselvam, C.; Horecker,
B. L.: The sequence of human parathymosin deduced from a cloned human
kidney cDNA. Biochem. Biophys. Res. Commun. 158: 855-862, 1989.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/3/2011.
3. Szabo, P.; Clinton, M.; Macera, M.; Horecker, B. L.: Localization
of the gene coding for parathymosin to chromosome 17 in humans. Cytogenet.
Cell Genet. 50: 91-92, 1989.
*FIELD* CN
Matthew B. Gross - updated: 2/3/2011
*FIELD* CD
Victor A. McKusick: 5/13/1989
*FIELD* ED
carol: 02/11/2011
mgross: 2/3/2011
supermim: 3/16/1992
carol: 10/5/1990
supermim: 3/20/1990
ddp: 10/27/1989
root: 10/17/1989
root: 5/18/1989
*RECORD*
*FIELD* NO
168440
*FIELD* TI
*168440 PARATHYMOSIN; PTMS
*FIELD* TX
CLONING
Parathymosin is a polypeptide similar in size and amino acid composition
read moreto prothymosin-alpha (188390). It has a high content of dicarboxylic
amino acids and a complete absence of aromatic and sulfur-containing
amino acids. It has 101 amino acid residues as compared to 111 for
prothymosin. Clinton et al. (1989) reported the isolation of a cDNA
clone for human kidney parathymosin containing the complete coding
region and extending into the 5-prime and 3-prime flanking sequences.
The open reading frame contains 306 nucleotides, including the codon for
the initiator methionine. Analysis of the 5-prime flanking sequence
excluded the presence of a hydrophobic signal peptide in the translated
sequence. This permitted the conclusion that parathymosin, like
prothymosin-alpha, is synthesized without formation of a larger
precursor polypeptide. Parathymosin and prothymosin show a reciprocal
relationship: the highest levels of parathymosin and its mRNA are
present in liver, kidney, and brain (with lowest levels in thymus and
spleen), whereas prothymosin-alpha and its mRNA are present in highest
concentrations in thymus and spleen (with lower levels in kidney, brain,
and liver).
MAPPING
By in situ hybridization of rat parathymosin cDNA to human metaphase
chromosomes, Szabo et al. (1989) localized the gene for human
parathymosin to chromosome 17q12-q22. However, Gross (2011) mapped the
PTMS gene to chromosome 12p13.31 based on an alignment of the PTMS
sequence (GenBank GENBANK BC017025) with the genomic sequence (GRCh37).
*FIELD* RF
1. Clinton, M.; Frangou-Lazaridis, M.; Panneerselvam, C.; Horecker,
B. L.: The sequence of human parathymosin deduced from a cloned human
kidney cDNA. Biochem. Biophys. Res. Commun. 158: 855-862, 1989.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 2/3/2011.
3. Szabo, P.; Clinton, M.; Macera, M.; Horecker, B. L.: Localization
of the gene coding for parathymosin to chromosome 17 in humans. Cytogenet.
Cell Genet. 50: 91-92, 1989.
*FIELD* CN
Matthew B. Gross - updated: 2/3/2011
*FIELD* CD
Victor A. McKusick: 5/13/1989
*FIELD* ED
carol: 02/11/2011
mgross: 2/3/2011
supermim: 3/16/1992
carol: 10/5/1990
supermim: 3/20/1990
ddp: 10/27/1989
root: 10/17/1989
root: 5/18/1989