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   27-MAR-2024, entry version 163.
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}.
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; 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; 82.
DR   IntAct; P20962; 22.
DR   MINT; P20962; -.
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; 9606-ENSP00000478828; -.
DR   PeptideAtlas; P20962; -.
DR   ProteomicsDB; 53832; -.
DR   Pumba; P20962; -.
DR   TopDownProteomics; P20962; -.
DR   Antibodypedia; 22672; 168 antibodies from 22 providers.
DR   DNASU; 5763; -.
DR   Ensembl; ENST00000309083.8; ENSP00000310088.7; ENSG00000159335.19.
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   AGR; HGNC:9629; -.
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; 157 hits in 1164 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 174 other cell types or 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:SF3; PARATHYMOSIN; 1.
DR   PANTHER; PTHR22745; PROTHYMOSIN ALPHA; 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
//