HIBN_XENLA
ID HIBN_XENLA Reviewed; 590 AA.
AC P06180;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone-binding protein N1/N2;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Oocyte;
RX PubMed=3549279; DOI=10.1002/j.1460-2075.1986.tb04681.x;
RA Kleinschmidt J.A., Dingwall C., Maier G., Franke W.W.;
RT "Molecular characterization of a karyophilic, histone-binding protein: cDNA
RT cloning, amino acid sequence and expression of nuclear protein N1/N2 of
RT Xenopus laevis.";
RL EMBO J. 5:3547-3552(1986).
CC -!- FUNCTION: This protein is involved in nucleosome assembly. It is bound
CC to H3 and H4 in the absence of DNA, but released from H3 and H4 in the
CC presence of DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; X04712; CAA28419.1; -; mRNA.
DR PIR; A25680; A25680.
DR RefSeq; NP_001081537.1; NM_001088068.1.
DR PDB; 1PJN; X-ray; 2.50 A; A=532-552.
DR PDBsum; 1PJN; -.
DR AlphaFoldDB; P06180; -.
DR SMR; P06180; -.
DR DNASU; 397901; -.
DR GeneID; 397901; -.
DR KEGG; xla:397901; -.
DR CTD; 397901; -.
DR Xenbase; XB-GENE-980259; nasp.S.
DR OrthoDB; 1176629at2759; -.
DR EvolutionaryTrace; P06180; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 397901; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:CAFA.
DR Gene3D; 1.25.40.10; -; 1.
DR IDEAL; IID50002; -.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome;
KW Repeat; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..590
FT /note="Histone-binding protein N1/N2"
FT /id="PRO_0000083971"
FT REPEAT 36..69
FT /note="TPR 1"
FT REPEAT 357..390
FT /note="TPR 2"
FT REPEAT 399..432
FT /note="TPR 3"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 531..537
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 105..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 65029 MW; C4F072577665E180 CRC64;
MAEETAALST EKTEDTSTAP STSAEKADGI DIDTEAKRLM GAGQKHLVMK DVRSAVNLFQ
EASSLLAKQY GETADECAEA FYSYGMSLLE LARLENGVLG NALEGMPEDD EEEAEKEEDP
NIPSADNLDE KEREQLREQV YDAMAEDQRA PDDTSESEAK GKPEGDSKDK EADEKMKNGQ
KETEKVTDDL KIDSASRDVP MDKSGKGEPP ESKDAETLVE QKESKPETLK EKSIETKEKD
LSKEKTDAKE TANQSPDSTE VAEEKMDSEA SESKESTSIP PTENEANKPD DPEKMEEEEE
GEDSEENEDG TEENEGTEEK ETEEEDVGNL QLAWEMLDLC KTIFKRQQSK EAQLKAAQAH
QKLGEVCIES ENYSQAVEDF LACLNIQKEH LEEHDRLLAE THYHLGLAYQ YSSKHEEAIS
HFTQSIGVIE KRMDVLTKQL EASVGELVDE VKKEMDELKD LLPDIKEKIE DSKEAQKNAT
VTEKALKETL VGGSSGFSKE NGSTSSSSAV EKSGDSTVPV TNCVSDISHL VRKKRKTEEE
SPLKDKDAKK SKQEPVANGA GNGDAVVPTN EEAEKAEEAS METATVESTA