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PCNP_MOUSE
ID   PCNP_MOUSE              Reviewed;         178 AA.
AC   Q6P8I4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=PEST proteolytic signal-containing nuclear protein;
DE            Short=PCNP;
DE            Short=PEST-containing nuclear protein;
GN   Name=Pcnp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND THR-139, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: May be involved in cell cycle regulation. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with UHRF2/NIRF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Ubiquitinated; mediated by UHRF2 and leading to its subsequent
CC       proteasomal degradation. {ECO:0000250}.
CC   -!- PTM: N-terminally acetylated in a HYPK-dependent manner by the NatA
CC       acetyltransferase complex which is composed of NAA10 and NAA15.
CC       {ECO:0000250}.
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DR   EMBL; BC061235; AAH61235.1; -; mRNA.
DR   CCDS; CCDS37357.1; -.
DR   RefSeq; NP_001019793.1; NM_001024622.2.
DR   AlphaFoldDB; Q6P8I4; -.
DR   BioGRID; 218068; 3.
DR   STRING; 10090.ENSMUSP00000110087; -.
DR   iPTMnet; Q6P8I4; -.
DR   PhosphoSitePlus; Q6P8I4; -.
DR   EPD; Q6P8I4; -.
DR   jPOST; Q6P8I4; -.
DR   MaxQB; Q6P8I4; -.
DR   PaxDb; Q6P8I4; -.
DR   PRIDE; Q6P8I4; -.
DR   ProteomicsDB; 288076; -.
DR   Antibodypedia; 32287; 176 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000114444; ENSMUSP00000110087; ENSMUSG00000071533.
DR   GeneID; 76302; -.
DR   KEGG; mmu:76302; -.
DR   UCSC; uc007zma.1; mouse.
DR   CTD; 57092; -.
DR   MGI; MGI:1923552; Pcnp.
DR   VEuPathDB; HostDB:ENSMUSG00000071533; -.
DR   eggNOG; ENOG502QWEZ; Eukaryota.
DR   GeneTree; ENSGT00390000010218; -.
DR   HOGENOM; CLU_118645_1_0_1; -.
DR   InParanoid; Q6P8I4; -.
DR   OMA; NVHDQEN; -.
DR   OrthoDB; 1616182at2759; -.
DR   PhylomeDB; Q6P8I4; -.
DR   TreeFam; TF333058; -.
DR   BioGRID-ORCS; 76302; 9 hits in 68 CRISPR screens.
DR   ChiTaRS; Pcnp; mouse.
DR   PRO; PR:Q6P8I4; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q6P8I4; protein.
DR   Bgee; ENSMUSG00000071533; Expressed in ureter smooth muscle and 259 other tissues.
DR   ExpressionAtlas; Q6P8I4; baseline and differential.
DR   Genevisible; Q6P8I4; MM.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:HGNC-UCL.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:HGNC-UCL.
DR   InterPro; IPR029169; PCNP.
DR   PANTHER; PTHR16523; PTHR16523; 1.
DR   Pfam; PF15473; PCNP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   CHAIN           2..178
FT                   /note="PEST proteolytic signal-containing nuclear protein"
FT                   /id="PRO_0000058254"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         64
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         87
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         139
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         150
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WW12"
SQ   SEQUENCE   178 AA;  18963 MW;  B1310E3B12BAC309 CRC64;
     MADGKAGEEK PEKPQRAGAA GGPEEEAEKP VKTKTVSSSN GGESSSRSAE KRSAEDEAAD
     LPTKPTKMSK FGFAIGSQTA RKASAISIRL GASKPKETVP TLAPKTLSVA AAFNEDEDSE
     PEEMPPEAKM RMKNIGRDTP TSAGPNSFNK GKHGFSDNQK LWERNIKSHL GNVHDQDN
 
 
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