PTMS_HUMAN
ID PTMS_HUMAN Reviewed; 102 AA.
AC P20962;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Parathymosin;
GN Name=PTMS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 IDENTIFICATION BY 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 LYS-4; LYS-15 AND LYS-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-5, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. {ECO:0000305}.
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DR EMBL; M24398; AAA61185.1; -; mRNA.
DR CCDS; CCDS8560.1; -.
DR PIR; A32264; A32264.
DR RefSeq; NP_002815.3; NM_002824.5.
DR AlphaFoldDB; P20962; -.
DR SMR; P20962; -.
DR BioGRID; 111730; 77.
DR IntAct; P20962; 21.
DR MINT; P20962; -.
DR STRING; 9606.ENSP00000478828; -.
DR iPTMnet; P20962; -.
DR PhosphoSitePlus; P20962; -.
DR SwissPalm; P20962; -.
DR BioMuta; PTMS; -.
DR CPTAC; CPTAC-1532; -.
DR CPTAC; CPTAC-1533; -.
DR EPD; P20962; -.
DR jPOST; P20962; -.
DR MassIVE; P20962; -.
DR MaxQB; P20962; -.
DR PaxDb; P20962; -.
DR PeptideAtlas; P20962; -.
DR PRIDE; P20962; -.
DR ProteomicsDB; 53832; -.
DR TopDownProteomics; P20962; -.
DR Antibodypedia; 22672; 160 antibodies from 22 providers.
DR DNASU; 5763; -.
DR Ensembl; ENST00000309083.8; ENSP00000310088.7; ENSG00000159335.18.
DR GeneID; 5763; -.
DR KEGG; hsa:5763; -.
DR MANE-Select; ENST00000309083.8; ENSP00000310088.7; NM_002824.6; NP_002815.3.
DR UCSC; uc001qqq.3; human.
DR CTD; 5763; -.
DR DisGeNET; 5763; -.
DR GeneCards; PTMS; -.
DR HGNC; HGNC:9629; PTMS.
DR HPA; ENSG00000159335; Tissue enhanced (liver).
DR MIM; 168440; gene.
DR neXtProt; NX_P20962; -.
DR OpenTargets; ENSG00000159335; -.
DR PharmGKB; PA33973; -.
DR VEuPathDB; HostDB:ENSG00000159335; -.
DR eggNOG; ENOG502SSXW; Eukaryota.
DR GeneTree; ENSGT01030000234816; -.
DR HOGENOM; CLU_087174_1_0_1; -.
DR InParanoid; P20962; -.
DR OMA; ACDDCEG; -.
DR PathwayCommons; P20962; -.
DR SignaLink; P20962; -.
DR SIGNOR; P20962; -.
DR BioGRID-ORCS; 5763; 155 hits in 1085 CRISPR screens.
DR ChiTaRS; PTMS; human.
DR GeneWiki; PTMS_(gene); -.
DR GenomeRNAi; 5763; -.
DR Pharos; P20962; Tbio.
DR PRO; PR:P20962; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P20962; protein.
DR Bgee; ENSG00000159335; Expressed in tendon of biceps brachii and 172 other tissues.
DR ExpressionAtlas; P20962; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; TAS:ProtInc.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004931; Pro/parathymosin.
DR PANTHER; PTHR22745; PTHR22745; 1.
DR Pfam; PF03247; Prothymosin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Immunity; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..102
FT /note="Parathymosin"
FT /id="PRO_0000191632"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0J8"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04550"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 102 AA; 11530 MW; 1B169F911B37B856 CRC64;
MSEKSVEAAA ELSAKDLKEK KEKVEEKASR KERKKEVVEE EENGAEEEEE ETAEDGEEED
EGEEEDEEEE EEDDEGPALK RAAEEEDEAD PKRQKTENGA SA
