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HDGR2_XENTR
ID   HDGR2_XENTR             Reviewed;         643 AA.
AC   Q6P4K1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE            Short=HRP-2;
GN   Name=hdgfl2; Synonyms=hdgfrp2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a regulator of myogenesis (By similarity).
CC       Promotes the repair of DNA double-strand breaks (DSBs) through the
CC       homologous recombination pathway by facilitating the recruitment of the
CC       DNA endonuclease RBBP8 to the DSBs (By similarity).
CC       {ECO:0000250|UniProtKB:Q7Z4V5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3UMU9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q925G1}.
CC   -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR   EMBL; BC063366; AAH63366.1; -; mRNA.
DR   RefSeq; NP_989176.1; NM_203845.1.
DR   AlphaFoldDB; Q6P4K1; -.
DR   SMR; Q6P4K1; -.
DR   STRING; 8364.ENSXETP00000052142; -.
DR   PaxDb; Q6P4K1; -.
DR   DNASU; 394783; -.
DR   GeneID; 394783; -.
DR   KEGG; xtr:394783; -.
DR   CTD; 84717; -.
DR   Xenbase; XB-GENE-6456056; hdgfl2.
DR   eggNOG; KOG1904; Eukaryota.
DR   InParanoid; Q6P4K1; -.
DR   OMA; AVHRKTY; -.
DR   OrthoDB; 530959at2759; -.
DR   TreeFam; TF105385; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd05834; HDGF_related; 1.
DR   Gene3D; 1.20.930.10; -; 1.
DR   InterPro; IPR035496; HDGF-rel_PWWP.
DR   InterPro; IPR036218; HIVI-bd_sf.
DR   InterPro; IPR021567; LEDGF_IBD.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   Pfam; PF11467; LEDGF; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF140576; SSF140576; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   Myogenesis; Nucleus; Reference proteome.
FT   CHAIN           1..643
FT                   /note="Hepatoma-derived growth factor-related protein 2"
FT                   /id="PRO_0000317648"
FT   DOMAIN          7..64
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          88..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          295..345
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        88..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..580
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  72266 MW;  2FB2D91D1490A868 CRC64;
     MPLNFKPGDL VFAKMKGYPH WPARIDDVKD GAVKPPPNKY PIFFYGTHET AFLAPKDLFP
     YEKCKDKYGK PNKRKGFNEG LWEIQNNPQA SYSLPPASVS SSDSDVPEEK STARSDGEEE
     QETGQAILPT AGVSSSDEEG SDKGGVKRKG RTTTPPSAKR TKHSSSEQEP DSASSSEEEN
     SDSDQDFTPE KSTPRIQRRT TNLGKKNKIF AESDSKSDES EDEKKEEEQK KSPSSSSASS
     PSLSSSDSEA PVKKTPRGRR PAEKPAPKPR GRGRKAEPIP SSDSSDSDSS VDRISEWKKR
     DEERRRELEE RRKKEQEEQL RRLREEEREE EERKKREKAE KGDKSDSDSD SSKSEVIAPP
     KPKKSSSSSD SEEDKKPVKE VKPVASEIKK GKKEKVRAIS DDSDSDKKVK KTIKKTRPSE
     SARKTNQKEK RGERPRGRPS KVEKEKKKPE VITARKVVKK EPTVEEKLQK LHSEIKFALK
     VDNPDIQKCL DALEELGGLQ VTSQILQKNT DVVATLKKIR RYKANQSVMD KAAEVYSRIK
     ARILGPKLES QQKTVQKVNT AEKDPEEEKQ TGKVEEDMDA SVNGDFLSQR IETAGDKEQD
     GEGQNLDNKT EMETKQNNHA EHNSNPTEET IECRLISSEN QTS
 
 
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