NPM_XENLA
ID NPM_XENLA Reviewed; 299 AA.
AC P07222;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Nucleophosmin;
DE Short=NPM;
DE AltName: Full=Nucleolar phosphoprotein B23;
DE AltName: Full=Nucleolar protein NO38;
DE AltName: Full=Numatrin;
GN Name=npm1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=3308448; DOI=10.1002/j.1460-2075.1987.tb02447.x;
RA Schmidt-Zachmann M.S., Huegle-Doerr B., Franke W.W.;
RT "A constitutive nucleolar protein identified as a member of the
RT nucleoplasmin family.";
RL EMBO J. 6:1881-1890(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 16-124, AND SUBUNIT.
RX PubMed=15576029; DOI=10.1016/j.str.2004.09.017;
RA Namboodiri V.M., Akey I.V., Schmidt-Zachmann M.S., Head J.F., Akey C.W.;
RT "The structure and function of Xenopus NO38-core, a histone chaperone in
RT the nucleolus.";
RL Structure 12:2149-2160(2004).
CC -!- FUNCTION: Acts as a chaperonin for the core histones H3, H2B and H4.
CC Associated with nucleolar ribonucleoprotein structures and bind single-
CC stranded nucleic acids. It may function in the assembly and/or
CC transport of ribosome. May stimulate endonuclease activity on
CC apurinic/apyrimidinic (AP) double-stranded DNA. May inhibit
CC endonuclease activity on AP single-stranded RNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Decamer formed by two pentameric rings associated in a head-
CC to-head fashion. {ECO:0000269|PubMed:15576029}.
CC -!- INTERACTION:
CC P07222; P07222: npm1; NbExp=2; IntAct=EBI-11607504, EBI-11607504;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleoplasmin family. {ECO:0000305}.
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DR EMBL; X05496; CAA29046.1; -; mRNA.
DR PIR; A29681; A29681.
DR PDB; 1XB9; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=16-124.
DR PDB; 1XE0; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=16-124.
DR PDBsum; 1XB9; -.
DR PDBsum; 1XE0; -.
DR AlphaFoldDB; P07222; -.
DR SMR; P07222; -.
DR DIP; DIP-48469N; -.
DR IntAct; P07222; 1.
DR EvolutionaryTrace; P07222; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
DR InterPro; IPR032569; NPM1_C.
DR InterPro; IPR004301; Nucleoplasmin.
DR InterPro; IPR024057; Nucleoplasmin_core_dom.
DR InterPro; IPR036824; Nucleoplasmin_core_dom_sf.
DR PANTHER; PTHR22747; PTHR22747; 1.
DR Pfam; PF16276; NPM1-C; 1.
DR Pfam; PF03066; Nucleoplasmin; 1.
DR SUPFAM; SSF69203; SSF69203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..299
FT /note="Nucleophosmin"
FT /id="PRO_0000219485"
FT REPEAT 218..220
FT REPEAT 221..223
FT REPEAT 237..239
FT REPEAT 240..242
FT REGION 125..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..242
FT /note="4 X 3 AA repeats of K-T-P"
FT MOTIF 153..158
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 189..195
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 162..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction between pentamers"
FT SITE 82
FT /note="Interaction between pentamers"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 39..51
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1XE0"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1XE0"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:1XE0"
SQ SEQUENCE 299 AA; 33532 MW; C16CDF9565090843 CRC64;
MEDSMDMDNI APLRPQNFLF GCELKADKKE YSFKVEDDEN EHQLSLRTVS LGASAKDELH
VVEAEGINYE GKTIKIALAS LKPSVQPTVS LGGFEITPPV ILRLKSGSGP VYVSGQHLVA
LEDLESSDDE DEEHEPSPKN AKRIAPDSAS KVPRKKTRLE EEEEDSDEDD DDDEDDDDED
DDEEEEETPV KKTDSTKSKA AQKLNHNGKA SALSTTQKTP KTPEQKGKQD TKPQTPKTPK
TPLSSEEIKA KMQTYLEKGN VLPKVEVKFA NYVKNCFRTE NQKVIEDLWK WRQSLKDGK
