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HES2_XENLA
ID   HES2_XENLA              Reviewed;         191 AA.
AC   Q00P32; Q5XHC4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Transcription factor HES-2 {ECO:0000250|UniProtKB:O54792, ECO:0000303|PubMed:17008450};
DE            Short=XHes2 {ECO:0000250|UniProtKB:O54792, ECO:0000303|PubMed:17008450};
DE   AltName: Full=Hairy and enhancer of split 2 {ECO:0000303|PubMed:17008450};
GN   Name=hes2;
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] {ECO:0000305, ECO:0000312|EMBL:ABA40833.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, HOMODIMERIZATION, INTERACTION WITH
RP   NEUROD1; NEUROD4; HES1 AND HES6R, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:17008450};
RX   PubMed=17008450; DOI=10.1242/dev.02567;
RA   Soelter M., Locker M., Boy S., Taelman V., Bellefroid E.J., Perron M.,
RA   Pieler T.;
RT   "Characterization and function of the bHLH-O protein XHes2: insight into
RT   the mechanisms controlling retinal cell fate decision.";
RL   Development 133:4097-4108(2006).
RN   [2] {ECO:0000312|EMBL:AAH84134.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH92348.1}, and
RC   Kidney {ECO:0000312|EMBL:AAH84134.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH HEY1.
RX   PubMed=15531363; DOI=10.1016/j.ydbio.2004.08.019;
RA   Taelman V., Van Wayenbergh R., Soelter M., Pichon B., Pieler T.,
RA   Christophe D., Bellefroid E.J.;
RT   "Sequences downstream of the bHLH domain of the Xenopus hairy-related
RT   transcription factor-1 act as an extended dimerization domain that
RT   contributes to the selection of the partners.";
RL   Dev. Biol. 276:47-63(2004).
CC   -!- FUNCTION: Transcriptional repressor. Essential in the retina to govern
CC       glial versus neuronal differentiation. Promotes gliogenesis through the
CC       inhibition of neuronal differentiation by at least two distinct
CC       mechanisms; represses proneural gene transcription, and also physically
CC       interacts with proneural proteins, including neurod1.
CC       {ECO:0000269|PubMed:17008450}.
CC   -!- SUBUNIT: Transcription repression requires formation of a complex with
CC       a corepressor protein of the Groucho/TLE family (By similarity).
CC       Homodimer, and heterodimer with the other bHLH proteins neurod1,
CC       neurod4/ath3, hes1/hairy1 and hes6r. Weakly interacts with the bHLH
CC       protein hey1/hrt1. {ECO:0000250, ECO:0000269|PubMed:15531363,
CC       ECO:0000269|PubMed:17008450}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54792,
CC       ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- TISSUE SPECIFICITY: Expressed in the animal half of the early cleavage
CC       stage embryo. During neurulation and organogenesis, the otic vesicles
CC       and retina are the main sites of expression; expression in otic
CC       placodes begins as early as stage 13.5, persisting in the otic vesicles
CC       at stage 30 and beyond. Also transiently expressed in the olfactory
CC       placodes. In addition, weakly expressed in primary neurons. Expression
CC       in the retina begins at stage 21, and is seen throughout the neural
CC       retina by stage 30. From stage 35 onwards, expression progressively
CC       declines in the central retina, while remaining high in the margins. At
CC       stage 41, expression becomes restricted to the ciliary marginal zone
CC       (CMZ) of the retina, the only region where retinogenesis is still
CC       occurring. {ECO:0000269|PubMed:17008450}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:17008450}.
CC   -!- INDUCTION: Differentially regulated in the ectoderm and neuroectoderm
CC       by notch and neurog2/ngnr1. {ECO:0000269|PubMed:17008450}.
CC   -!- DOMAIN: Has a particular type of basic domain (presence of a helix-
CC       interrupting proline) that binds to the N-box (CACNAG), rather than the
CC       canonical E-box (CANNTG). {ECO:0000250|UniProtKB:P14003}.
CC   -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC       domain necessary for the interaction with Groucho/TLE family members,
CC       transcriptional corepressors recruited to specific target DNA by Hairy-
CC       related proteins. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH84134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH92348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DQ156231; ABA40833.1; -; mRNA.
DR   EMBL; BC084134; AAH84134.1; ALT_INIT; mRNA.
DR   EMBL; BC092348; AAH92348.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001116354.1; NM_001122882.1.
DR   AlphaFoldDB; Q00P32; -.
DR   SMR; Q00P32; -.
DR   GeneID; 495039; -.
DR   KEGG; xla:495039; -.
DR   CTD; 495039; -.
DR   Xenbase; XB-GENE-865581; hes2.L.
DR   OMA; YHSDCES; -.
DR   OrthoDB; 1427802at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 495039; Expressed in egg cell and 9 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0014015; P:positive regulation of gliogenesis; IMP:UniProtKB.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..191
FT                   /note="Transcription factor HES-2"
FT                   /id="PRO_0000370232"
FT   DOMAIN          28..85
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   DOMAIN          97..130
FT                   /note="Orange"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           188..191
FT                   /note="WRPW motif"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        93
FT                   /note="Q -> P (in Ref. 1; ABA40833)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   191 AA;  21823 MW;  CB27C48F56708578 CRC64;
     MAPNVALADS MHNYQPKPGK RNQEASELRK TLKPLMEKRR RARINESLNQ LKTLILPLIG
     KDNSRYSKLE KADILEMTVR FLRDIPPVQA QNQADRYKEG YRACVERLSA ILGKSHVLTG
     EASNRLLEYL QRSPELCSSD CNHPPKPQRP RIVLQVSPRT SQFGSPLQNQ PSSHRPAPCP
     PQLNSSIWRP W
 
 
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