HUNB_DROME
ID HUNB_DROME Reviewed; 758 AA.
AC P05084; Q24018; Q29R06; Q960U7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Protein hunchback {ECO:0000303|PubMed:1438276};
GN Name=hb {ECO:0000303|PubMed:1438276, ECO:0000312|FlyBase:FBgn0001180};
GN ORFNames=CG9786 {ECO:0000312|FlyBase:FBgn0001180};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RA Tautz D., Lehmann R., Schnuerch H., Schuh R., Seifert E., Kienlin A.,
RA Jones K., Jaeckle H.;
RT "Finger protein of novel structure encoded by hunchback, a second member of
RT the gap class of Drosophila segmentation genes.";
RL Nature 327:383-389(1987).
RN [2]
RP SEQUENCE REVISION TO 525.
RA Tautz D.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8200478; DOI=10.1006/dbio.1994.1156;
RA Margolis J.S., Borowsky M., Shim C.W., Posakony J.W.;
RT "A small region surrounding the distal promoter of the hunchback gene
RT directs maternal expression.";
RL Dev. Biol. 163:381-388(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-349.
RX PubMed=1438276; DOI=10.1073/pnas.89.22.10782;
RA Sommer R.J., Retzlaff M., Goerlich K., Sander K., Tautz D.;
RT "Evolutionary conservation pattern of zinc-finger domains of Drosophila
RT segmentation genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10782-10786(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-758.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [9]
RP POLYMORPHISM.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178; SER-188; SER-207;
RP SER-209; SER-210; SER-537 AND SER-540, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Gap class segmentation protein that controls development of
CC head structures.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: In embryo, expression of maternal transcript is
CC highest in anterior region. Zygotic transcript is expressed in anterior
CC region until the beginning of gastrulation and in posterior region
CC until early gastrulation. After this, it is expressed in developing
CC nervous system. {ECO:0000269|PubMed:8200478}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. Expression
CC of the maternal transcript decreases until embryonic stage 14, zygotic
CC transcript is first detected at stage 11.
CC -!- SIMILARITY: Belongs to the hunchback C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Y00274; CAA68377.1; -; Genomic_DNA.
DR EMBL; U17742; AAB60232.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13395.1; -; Genomic_DNA.
DR EMBL; BT024234; ABC86296.1; -; mRNA.
DR EMBL; AY051838; AAK93262.1; -; mRNA.
DR PIR; A93395; A29253.
DR RefSeq; NP_731267.1; NM_169233.2.
DR RefSeq; NP_731268.1; NM_169234.2.
DR AlphaFoldDB; P05084; -.
DR BioGRID; 66207; 18.
DR DIP; DIP-17417N; -.
DR IntAct; P05084; 7.
DR STRING; 7227.FBpp0081431; -.
DR iPTMnet; P05084; -.
DR PaxDb; P05084; -.
DR DNASU; 41032; -.
DR EnsemblMetazoa; FBtr0081950; FBpp0081431; FBgn0001180.
DR EnsemblMetazoa; FBtr0081951; FBpp0081432; FBgn0001180.
DR GeneID; 41032; -.
DR KEGG; dme:Dmel_CG9786; -.
DR UCSC; CG9786-RA; d. melanogaster.
DR CTD; 15120; -.
DR FlyBase; FBgn0001180; hb.
DR VEuPathDB; VectorBase:FBgn0001180; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000171732; -.
DR HOGENOM; CLU_021336_0_0_1; -.
DR InParanoid; P05084; -.
DR OMA; QNSLQHF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P05084; -.
DR SignaLink; P05084; -.
DR BioGRID-ORCS; 41032; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41032; -.
DR PRO; PR:P05084; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001180; Expressed in cleaving embryo and 59 other tissues.
DR ExpressionAtlas; P05084; baseline and differential.
DR Genevisible; P05084; DM.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0007402; P:ganglion mother cell fate determination; TAS:FlyBase.
DR GO; GO:0048699; P:generation of neurons; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0035289; P:posterior head segmentation; TAS:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; TAS:FlyBase.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:FlyBase.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007431; P:salivary gland development; TAS:FlyBase.
DR GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR GO; GO:0007419; P:ventral cord development; NAS:FlyBase.
DR GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; TAS:FlyBase.
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 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Gap protein; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..758
FT /note="Protein hunchback"
FT /id="PRO_0000046948"
FT ZN_FING 240..262
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 269..291
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..319
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 325..349
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 705..727
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 733..757
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 172..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 437
FT /note="A -> P"
FT VARIANT 649
FT /note="V -> M"
SQ SEQUENCE 758 AA; 83114 MW; AD74802EB856ACD7 CRC64;
MQNWETTATT NYEQHNAWYN SMFAANIKQE PGHHLDGNSV ASSPRQSPIP STNHLEQFLK
QQQQQLQQQP MDTLCAMTPS PSQNDQNSLQ HYDANLQQQL LQQQQYQQHF QAAQQQHHHH
HHLMGGFNPL TPPGLPNPMQ HFYGGNLRPS PQPTPTSAST IAPVAVATGS SEKLQALTPP
MDVTPPKSPA KSSQSNIEPE KEHDQMSNSS EDMKYMAESE DDDTNIRMPI YNSHGKMKNY
KCKTCGVVAI TKVDFWAHTR THMKPDKILQ CPKCPFVTEF KHHLEYHIRK HKNQKPFQCD
KCSYTCVNKS MLNSHRKSHS SVYQYRCADC DYATKYCHSF KLHLRKYGHK PGMVLDEDGT
PNPSLVIDVY GTRRGPKSKN GGPIASGGSG SGSRKSNVAA VAPQQQQSQP AQPVATSQLS
AALQGFPLVQ GNSAPPAASP VLPLPASPAK SVASVEQTPS LPSPANLLPP LASLLQQNRN
MAFFPYWNLN LQMLAAQQQA AVLAQLSPRM REQLQQQNQQ QSDNEEEEQD DEYERKSVDS
AMDLSQGTPV KEDEQQQQPQ QPLAMNLKVE EEATPLMSSS NASRRKGRVL KLDTLLQLRS
EAMTSPEQLK VPSTPMPTAS SPIAGRKPMP EEHCSGTSSA DESMETAHVP QANTSASSTA
SSSGNSSNAS SNSNGNSSSN SSSNGTTSAV AAPPSGTPAA AGAIYECKYC DIFFKDAVLY
TIHMGYHSCD DVFKCNMCGE KCDGPVGLFV HMARNAHS
