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Nucleophosmin (NPM) (Nucleolar phosphoprotein B23) (Nucleolar protein NO38) (Numatrin)

 NPM_RAT                 Reviewed;         292 AA.
P13084; Q63698; Q64269;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
12-SEP-2018, entry version 160.
RecName: Full=Nucleophosmin;
Short=NPM;
AltName: Full=Nucleolar phosphoprotein B23;
AltName: Full=Nucleolar protein NO38;
AltName: Full=Numatrin;
Name=Npm1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B23.1 AND B23.2), AND PARTIAL
PROTEIN SEQUENCE.
PubMed=3417636;
Chang J.-H., Dumbar T.S., Olson M.O.J.;
"cDNA and deduced primary structure of rat protein B23, a nucleolar
protein containing highly conserved sequences.";
J. Biol. Chem. 263:12824-12827(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B23.2).
PubMed=2745414;
Chang J.-H., Olson M.O.J.;
"A single gene codes for two forms of rat nucleolar protein B23
mRNA.";
J. Biol. Chem. 264:11732-11737(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS B23.1 AND B23.2).
PubMed=2211699;
Chang J.-H., Olson M.O.J.;
"Structure of the gene for rat nucleolar protein B23.";
J. Biol. Chem. 265:18227-18233(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B23.1).
TISSUE=Pituitary, and Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 55-101; 238-246 AND 266-271, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[6]
INTERACTION WITH CEBPA.
PubMed=20075868; DOI=10.1038/emboj.2009.404;
Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.;
"Nucleolar retention of a translational C/EBPalpha isoform stimulates
rDNA transcription and cell size.";
EMBO J. 29:897-909(2010).
-!- FUNCTION: Involved in diverse cellular processes such as ribosome
biogenesis, centrosome duplication, protein chaperoning, histone
assembly, cell proliferation, and regulation of tumor suppressors
p53/TP53 and ARF. Binds ribosome presumably to drive ribosome
nuclear export. Associated with nucleolar ribonucleoprotein
structures and bind single-stranded nucleic acids. Acts as a
chaperonin for the core histones H3, H2B and H4. Stimulates APEX1
endonuclease activity on apurinic/apyrimidinic (AP) double-
stranded DNA but inhibits APEX1 endonuclease activity on AP
single-stranded RNA. May exert a control of APEX1 endonuclease
activity within nucleoli devoted to repair AP on rDNA and the
removal of oxidized rRNA molecules. In concert with BRCA2,
regulates centrosome duplication. Regulates centriole duplication:
phosphorylation by PLK2 is able to trigger centriole replication.
Negatively regulates the activation of EIF2AK2/PKR and suppresses
apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.
Antagonizes the inhibitory effect of ATF5 on cell proliferation
and relieves ATF5-induced G2/M blockade. In complex with MYC
enhances the transcription of MYC target genes.
{ECO:0000250|UniProtKB:P06748}.
-!- SUBUNIT: Decamer formed by two pentameric rings associated in a
head-to-head fashion. Disulfide-linked dimers under certain
conditions. The SWAP complex consists of NPM1, NCL, PARP1 and
SWAP70. Interacts with NSUN2 and SENP3. Interacts with the
methylated form of RPS10. Interacts (via N-terminal domain) with
APEX1; the interaction is RNA-dependent and decreases in hydrogen
peroxide-damaged cells. Interacts with NEK2. Interacts with ROCK2
and BRCA2 (By similarity). Interacts with RPGR. Interacts with
CENPW (By similarity). Interacts with EIF2AK2/PKR (By similarity).
Interacts with CEBPA (isoform 4) (PubMed:20075868). Interacts with
DDX31; this interaction prevents interaction between NPM1 and HDM2
(By similarity). Interacts with MYC; competitive with NOP53.
Interacts with NOP53; the interaction is direct and competitive
with MYC (By similarity). Interacts with LRRC34 (By similarity).
Interacts with RRP1B (By similarity).
{ECO:0000250|UniProtKB:P06748, ECO:0000250|UniProtKB:Q61937,
ECO:0000269|PubMed:20075868}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P06748}. Note=Generally nucleolar, but is
translocated to the nucleoplasm in case of serum starvation or
treatment with anticancer drugs. Colocalizes with the methylated
form of RPS10 in the granular component (GC) region of the
nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2
is required for its localization to the centrosome during mitosis
(By similarity). {ECO:0000250|UniProtKB:P06748}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B23.1;
IsoId=P13084-1; Sequence=Displayed;
Name=B23.2;
IsoId=P13084-2; Sequence=VSP_003617;
-!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
affinity to histones. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at
Ser-4 by PLK2 in S phase is required for centriole duplication and
is sufficient to trigger centriole replication. Phosphorylation at
Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2
at Ser-125 and Thr-198. Phosphorylation at Thr-198 may trigger
initiation of centrosome duplication. Phosphorylated by CDK1 at
Thr-198, Thr-217, Thr-232 and Thr-235 during cell mitosis. When
these four sites are phosphorated, RNA-binding activity seem to be
abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-198
phosphorylated form has higher affinity for ROCK2 (By similarity).
{ECO:0000250|UniProtKB:P06748}.
-!- PTM: Sumoylated by ARF. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P06748}.
-!- PTM: May be ubiquitinated. Ubiquitination leads to proteasomal
degradation. Deubiquitinated by USP36 (By similarity).
{ECO:0000250|UniProtKB:P06748}.
-!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J03969; AAA40796.1; -; mRNA.
EMBL; M37039; AAA41730.1; -; Genomic_DNA.
EMBL; M37035; AAA41730.1; JOINED; Genomic_DNA.
EMBL; M37036; AAA41730.1; JOINED; Genomic_DNA.
EMBL; M37037; AAA41730.1; JOINED; Genomic_DNA.
EMBL; M37038; AAA41730.1; JOINED; Genomic_DNA.
EMBL; M37041; AAA41731.1; -; Genomic_DNA.
EMBL; M37035; AAA41731.1; JOINED; Genomic_DNA.
EMBL; M37036; AAA41731.1; JOINED; Genomic_DNA.
EMBL; M37037; AAA41731.1; JOINED; Genomic_DNA.
EMBL; M37038; AAA41731.1; JOINED; Genomic_DNA.
EMBL; M37040; AAA41731.1; JOINED; Genomic_DNA.
EMBL; M25062; AAA40795.1; -; Genomic_DNA.
EMBL; J04943; AAA40794.1; -; mRNA.
EMBL; J04944; AAA40793.1; -; Genomic_DNA.
EMBL; BC060579; AAH60579.1; -; mRNA.
EMBL; BC088088; AAH88088.1; -; mRNA.
PIR; A28939; A28939.
PIR; A36089; A36089.
PIR; B36089; A34168.
RefSeq; NP_037124.1; NM_012992.4. [P13084-1]
UniGene; Rn.54537; -.
ProteinModelPortal; P13084; -.
SMR; P13084; -.
BioGrid; 247531; 3.
IntAct; P13084; 2.
MINT; P13084; -.
STRING; 10116.ENSRNOP00000006591; -.
iPTMnet; P13084; -.
PhosphoSitePlus; P13084; -.
SwissPalm; P13084; -.
World-2DPAGE; 0004:P13084; -.
PaxDb; P13084; -.
PRIDE; P13084; -.
Ensembl; ENSRNOT00000006591; ENSRNOP00000006591; ENSRNOG00000004616. [P13084-1]
Ensembl; ENSRNOT00000064744; ENSRNOP00000062356; ENSRNOG00000004616. [P13084-2]
GeneID; 25498; -.
KEGG; rno:25498; -.
UCSC; RGD:3192; rat. [P13084-1]
CTD; 4869; -.
RGD; 3192; Npm1.
eggNOG; ENOG410IHZM; Eukaryota.
eggNOG; ENOG4111IKX; LUCA.
GeneTree; ENSGT00440000034554; -.
HOGENOM; HOG000013061; -.
HOVERGEN; HBG001860; -.
InParanoid; P13084; -.
KO; K11276; -.
OMA; KMQASVD; -.
OrthoDB; EOG091G0NLY; -.
PhylomeDB; P13084; -.
TreeFam; TF327704; -.
PRO; PR:P13084; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000004616; Expressed in 10 organ(s), highest expression level in spleen.
Genevisible; P13084; RN.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0001652; C:granular component; IEA:Ensembl.
GO; GO:0015934; C:large ribosomal subunit; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IDA:RGD.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0015935; C:small ribosomal subunit; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IMP:RGD.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IDA:RGD.
GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:RGD.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IPI:RGD.
GO; GO:0043422; F:protein kinase B binding; IDA:RGD.
GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0019843; F:rRNA binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
GO; GO:0003300; P:cardiac muscle hypertrophy; IEP:RGD.
GO; GO:0007569; P:cell aging; ISS:UniProtKB.
GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IDA:RGD.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:RGD.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:RGD.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:Ensembl.
GO; GO:0051054; P:positive regulation of DNA metabolic process; IDA:RGD.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:RGD.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB.
GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IEA:Ensembl.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:Ensembl.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IEA:Ensembl.
GO; GO:0006407; P:rRNA export from nucleus; IEA:Ensembl.
GO; GO:0009303; P:rRNA transcription; IMP:RGD.
Gene3D; 1.10.10.2100; -; 1.
InterPro; IPR032569; NPM1_C.
InterPro; IPR038101; NPM1_C_sf.
InterPro; IPR004301; Nucleoplasmin.
InterPro; IPR024057; Nucleoplasmin_core_dom.
InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
PANTHER; PTHR22747; PTHR22747; 1.
Pfam; PF16276; NPM1-C; 1.
Pfam; PF03066; Nucleoplasmin; 1.
SUPFAM; SSF69203; SSF69203; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Alternative splicing; Chaperone;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Disulfide bond; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Ubl conjugation.
CHAIN 1 292 Nucleophosmin.
/FTId=PRO_0000219483.
REGION 1 185 Required for interaction with SENP3.
{ECO:0000250}.
REGION 1 117 Necessary for interaction with APEX1.
{ECO:0000250}.
REGION 241 292 Required for nucleolar localization.
{ECO:0000250}.
MOTIF 152 157 Nuclear localization signal.
{ECO:0000255}.
MOTIF 190 196 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 1 9 Met-rich.
COMPBIAS 120 132 Asp/Glu-rich (acidic).
COMPBIAS 158 187 Asp/Glu-rich (highly acidic).
SITE 55 55 Interaction between pentamers.
{ECO:0000250}.
SITE 80 80 Interaction between pentamers.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 4 4 Phosphoserine; by PLK1 and PLK2.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 32 32 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61937}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 95 95 Phosphothreonine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 125 125 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 150 150 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 154 154 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 198 198 Phosphothreonine; by CDK1 and CDK2.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 206 206 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 211 211 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 217 217 Phosphothreonine; by CDK1. {ECO:0000250}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 228 228 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 232 232 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 235 235 Phosphothreonine; by CDK1.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 248 248 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 255 255 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 265 265 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 265 265 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q61937}.
MOD_RES 271 271 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 277 277 Phosphothreonine.
{ECO:0000250|UniProtKB:P06748}.
MOD_RES 290 290 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 141 141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 255 255 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P06748}.
VAR_SEQ 256 292 GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL ->
AH (in isoform B23.2).
{ECO:0000303|PubMed:2745414,
ECO:0000303|PubMed:3417636}.
/FTId=VSP_003617.
SEQUENCE 292 AA; 32560 MW; 1372A474F9ED2457 CRC64;
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDDEDDEDDE DDEDDDDDDF
DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS
SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL


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201-20-6690 NPM1{nucleophosmin (nucleolar phosphoprotein B23, numatrin)}mouse.mAb 0.2ml
EIAAB27510 140 kDa nucleolar phosphoprotein,Nolc1,Nopp140,Nucleolar 130 kDa protein,Nucleolar and coiled-body phosphoprotein 1,Nucleolar phosphoprotein p130,Rat,Rattus norvegicus
GWB-4ADFEC Anti- NPM1 (nucleophosmin (nucleolar phosphoprotein B23. numatrin)) Antibody
GWB-249772 Anti- NPM1 (nucleophosmin (nucleolar phosphoprotein B23. numatrin)) Antibody
GWB-81E3B8 Anti- NPM1 (nucleophosmin (nucleolar phosphoprotein B23. numatrin)) Antibody
GS-1472a nucleophosmin (nucleolar phosphoprotein B23, numatrin) primary antibody, Host: Rabbit 200ul
CSB-EL015996RA Rat nucleophosmin (nucleolar phosphoprotein B23, numatrin) (NPM1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL015996MO Mouse nucleophosmin (nucleolar phosphoprotein B23, numatrin) (NPM1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL015996HU Human nucleophosmin (nucleolar phosphoprotein B23, numatrin) (NPM1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015996BO Bovine nucleophosmin (nucleolar phosphoprotein B23, numatrin) (NPM1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL015996CH Chicken nucleophosmin (nucleolar phosphoprotein B23, numatrin) (NPM1) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-PA015996GA01HU Rabbit anti-human nucleophosmin (nucleolar phosphoprotein B23, numatrin) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA015996GA01HU Rabbit anti-human nucleophosmin (nucleolar phosphoprotein B23, numatrin) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
18-003-44233 MKI67 FHA domain-interacting nucleolar phosphoprotein - Nucleolar protein interacting with the FHA domain of pKI-67; hNIFK; Nucleolar phosphoprotein Nopp34 Polyclonal 0.05 mg Aff Pur


 

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