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PTMS_BOVIN
ID   PTMS_BOVIN              Reviewed;         102 AA.
AC   P08814;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Parathymosin;
GN   Name=PTMS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-102.
RX   PubMed=3421960; DOI=10.1016/s0006-291x(88)80528-x;
RA   Panneerselvam C., Clinton M., Wellner D., Horecker B.L.;
RT   "Bovine parathymosin: amino acid sequence and comparison with rat
RT   parathymosin.";
RL   Biochem. Biophys. Res. Commun. 155:539-545(1988).
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   AlphaFoldDB; P08814; -.
DR   SMR; P08814; -.
DR   STRING; 9913.ENSBTAP00000024555; -.
DR   PaxDb; P08814; -.
DR   PeptideAtlas; P08814; -.
DR   PRIDE; P08814; -.
DR   eggNOG; ENOG502SSXW; Eukaryota.
DR   InParanoid; P08814; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:0000250|UniProtKB:P20962,
FT                   ECO:0000269|PubMed:3421960"
FT   CHAIN           2..102
FT                   /note="Parathymosin"
FT                   /id="PRO_0000191631"
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..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
FT   MOD_RES         5
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D0J8"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
FT   MOD_RES         52
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04550"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P20962"
SQ   SEQUENCE   102 AA;  11457 MW;  D7438E901F63F99C CRC64;
     MSEKSVEAAA ELSAKDLKEK KEKVEEKAGR KERKKEVVEE EENGAEEEEE ETAEDGEEED
     DGDEEDEEEE EEEDEGPALV RAAEEEDEAD PKRQKTENGA SA
 
 
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