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PTTG3_HUMAN
ID   PTTG3_HUMAN             Reviewed;         202 AA.
AC   Q9NZH4; O95356;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Putative pituitary tumor-transforming gene 3 protein;
DE            Short=hPTTG3;
DE   AltName: Full=Securin-3;
DE   AltName: Full=rcPTTG1;
GN   Name=PTTG3P; Synonyms=PTTG3;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=10806349; DOI=10.1016/s0378-1119(00)00096-2;
RA   Chen L., Puri R., Lefkowitz E.J., Kakar S.S.;
RT   "Identification of the human pituitary tumor transforming gene (hPTTG)
RT   family: molecular structure, expression, and chromosomal localization.";
RL   Gene 248:41-50(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA   Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT   "Emergence of young human genes after a burst of retroposition in
RT   primates.";
RL   PLoS Biol. 3:E357-E357(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary adenoma;
RA   Mu Y.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Prezant T.R., Heaney A.P., Yu R., Kim K.W., Gutman S.F., Wang Z.,
RA   Melmed S.;
RT   "Distinct expression patterns and functions of the human pituitary tumor
RT   transforming gene (PTTG) family.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in ovarian tumor and tumor cell lines
CC       (SK-OV-3 and PA1). {ECO:0000269|PubMed:10806349}.
CC   -!- DOMAIN: The N-terminal destruction box (D-box) acts as a recognition
CC       signal for degradation via the ubiquitin-proteasome pathway.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the securin family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AF200720; AAF72580.1; -; Genomic_DNA.
DR   EMBL; DQ120700; ABC40663.1; -; Genomic_DNA.
DR   EMBL; AF095289; AAC64411.1; -; mRNA.
DR   EMBL; AY028471; AAK40241.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NZH4; -.
DR   iPTMnet; Q9NZH4; -.
DR   PhosphoSitePlus; Q9NZH4; -.
DR   BioMuta; HGNC:13422; -.
DR   DMDM; 74719651; -.
DR   jPOST; Q9NZH4; -.
DR   MassIVE; Q9NZH4; -.
DR   MaxQB; Q9NZH4; -.
DR   PeptideAtlas; Q9NZH4; -.
DR   PRIDE; Q9NZH4; -.
DR   ProteomicsDB; 83387; -.
DR   GeneCards; PTTG3P; -.
DR   HGNC; HGNC:13422; PTTG3P.
DR   neXtProt; NX_Q9NZH4; -.
DR   InParanoid; Q9NZH4; -.
DR   PhylomeDB; Q9NZH4; -.
DR   Pharos; Q9NZH4; Tdark.
DR   PRO; PR:Q9NZH4; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q9NZH4; protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   GO; GO:0045143; P:homologous chromosome segregation; IBA:GO_Central.
DR   GO; GO:2000816; P:negative regulation of mitotic sister chromatid separation; IBA:GO_Central.
DR   InterPro; IPR006940; Securin_separation_inhibitor.
DR   PANTHER; PTHR10418; PTHR10418; 1.
DR   Pfam; PF04856; Securin; 1.
PE   5: Uncertain;
KW   Cytoplasm; Nucleus; Proto-oncogene; Reference proteome; SH3-binding.
FT   CHAIN           1..202
FT                   /note="Putative pituitary tumor-transforming gene 3
FT                   protein"
FT                   /id="PRO_0000333860"
FT   REGION          69..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           61..64
FT                   /note="D-box"
FT                   /evidence="ECO:0000250"
FT   MOTIF           163..173
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        70..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        198
FT                   /note="S -> C (in Ref. 3; AAC64411)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  22064 MW;  C19E6E9FE344A539 CRC64;
     MATLIYVDKE NEEPGILVAT KDGLKLGSGP SIKALDGRSQ VSISCFGKTF DAPTSLPKAT
     RKALGTVNRA TEKSVKTNGP LKQKQPSFSA KKMTEKTVKA KNSVPASDDG YPEIEKLFPF
     NPLGFESFDL PEEHQIAHLP LSEVPLMILD EERELEKLFQ LGPPSPLKMP SPPWKSNLLQ
     SPLSILLTLD VELPPVCSDI DI
 
 
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