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HUNB_DROYA
ID   HUNB_DROYA              Reviewed;         759 AA.
AC   O62541; B4PT90;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein hunchback {ECO:0000250|UniProtKB:P05084};
GN   Name=hb {ECO:0000250|UniProtKB:P05084};
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12572604; DOI=10.1093/oxfordjournals.molbev.a025868;
RA   Tautz D., Nigro L.;
RT   "Microevolutionary divergence pattern of the segmentation gene hunchback in
RT   Drosophila.";
RL   Mol. Biol. Evol. 15:1403-1411(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Gap class segmentation protein that controls development of
CC       head structures. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; AJ005376; CAA06506.1; -; Genomic_DNA.
DR   EMBL; CM000160; EDW96551.1; -; Genomic_DNA.
DR   RefSeq; XP_002096839.1; XM_002096803.2.
DR   AlphaFoldDB; O62541; -.
DR   SMR; O62541; -.
DR   STRING; 7245.FBpp0269844; -.
DR   EnsemblMetazoa; FBtr0271352; FBpp0269844; FBgn0022824.
DR   GeneID; 6536253; -.
DR   KEGG; dya:Dyak_GE24834; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_021336_0_0_1; -.
DR   OMA; QNSLQHF; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IEA:EnsemblMetazoa.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR   GO; GO:0007400; P:neuroblast fate determination; IEA:EnsemblMetazoa.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR   GO; GO:0040034; P:regulation of development, heterochronic; IEA:InterPro.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0050767; P:regulation of neurogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0035282; P:segmentation; IEA:UniProtKB-KW.
DR   InterPro; IPR027742; Hunchback.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24392:SF33; PTHR24392:SF33; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   3: Inferred from homology;
KW   Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..759
FT                   /note="Protein hunchback"
FT                   /id="PRO_0000046966"
FT   ZN_FING         241..263
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         270..292
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         298..320
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         326..350
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         706..728
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         734..758
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         179
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05084"
FT   CONFLICT        495
FT                   /note="A -> L (in Ref. 1; CAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="Q -> H (in Ref. 1; CAA06506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="P -> A (in Ref. 1; CAA06506)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   759 AA;  83262 MW;  1C9920F0C8F29985 CRC64;
     MQNWETTATT NYEQHNAWYN SMFAANIKQE PGHHLDGNSV ASSPRQSPIP STNHLEQFLK
     QQQQQQHQQQ PMDTLCAMTP SPSQNDQNSL QHYDASLQQQ LLQQQQYQQH FQAAQQQHHH
     HHHLMGGFNP LTPPGLPNPM QHFYGGNLRP SPQPTPTSAS TVAPVAVATG SSEKLQALTP
     PMDVTPPKSP AKSSQSNIEP EKEHDQMSNS SEDMKYMAES EDDDTNIRMP IYNSHGKMKN
     YKCKTCGVVA ITKVDFWAHT RTHMKPDKIL QCPKCPFVTE FKHHLEYHIR KHKNQKPFQC
     DKCSYTCVNK SMLNSHRKSH SSVYQYRCAD CDYATKYCHS FKLHLRKYGH KPGMVLDEDG
     TPNPSLVIDV YGTRRGPKSK NGGPIASGGS GSGSRKPNVA AVAPQQQQSQ PAQPATSQLS
     AALQGFPLVQ SNSAPPAASP VLPLPASPAK SVASVEQTPS LPSPANLLPP LASLLQQNRN
     MAFFPYWNLN LQMLAAQQQA AVLAQLSPRM REQLQQQNQQ QSDNEEEEQD DEYERKSVDS
     AMDLSQGTPV KEDDQHQQQQ QPQQPLAMNL KVEEEATPLM SSSNASRRKG RVLKLDTLLQ
     LRSEAMTSPE QLKVPSTPMP TASSPIAGRK PMPEDHCSGT SSADESMETA HVPQANTSAS
     STASSSGNSS NASSNGNSSS NSSSNGTSSA AAAPASGTPA AAGAIYECKY CDIFFKDAVL
     YTIHMGYHSC DDVFKCNMCG EKCDGPVGLF VHMARNAHS
 
 
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