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HDGR2_DANRE
ID   HDGR2_DANRE             Reviewed;         662 AA.
AC   Q5XXA7; B8A4B6; Q1LYH9; Q803X2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE            Short=HRP-2;
GN   Name=hdgfl2; Synonyms=hdgfrp2; ORFNames=si:ch211-232a14.3, zgc:66215;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15371438; DOI=10.1074/jbc.m406307200;
RA   Cherepanov P., Devroe E., Silver P.A., Engelman A.;
RT   "Identification of an evolutionarily conserved domain in human lens
RT   epithelium-derived growth factor/transcriptional co-activator p75
RT   (LEDGF/p75) that binds HIV-1 integrase.";
RL   J. Biol. Chem. 279:48883-48892(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-417.
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-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; AY728142; AAU44351.1; -; mRNA.
DR   EMBL; BX005201; CAX13226.1; -; Genomic_DNA.
DR   EMBL; CU207239; CAX13226.1; JOINED; Genomic_DNA.
DR   EMBL; BC044157; AAH44157.1; -; mRNA.
DR   RefSeq; NP_001002037.2; NM_001002037.2.
DR   AlphaFoldDB; Q5XXA7; -.
DR   SMR; Q5XXA7; -.
DR   STRING; 7955.ENSDARP00000103259; -.
DR   PaxDb; Q5XXA7; -.
DR   PRIDE; Q5XXA7; -.
DR   GeneID; 80965; -.
DR   KEGG; dre:80965; -.
DR   CTD; 84717; -.
DR   ZFIN; ZDB-GENE-040426-2104; hdgfl2.
DR   eggNOG; KOG1904; Eukaryota.
DR   InParanoid; Q5XXA7; -.
DR   OrthoDB; 530959at2759; -.
DR   PhylomeDB; Q5XXA7; -.
DR   PRO; PR:Q5XXA7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..662
FT                   /note="Hepatoma-derived growth factor-related protein 2"
FT                   /id="PRO_0000317646"
FT   DOMAIN          7..64
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          84..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          320..370
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        84..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..406
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        152
FT                   /note="L -> P (in Ref. 1; AAU44351 and 3; AAH44157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="I -> T (in Ref. 3; AAH44157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="S -> F (in Ref. 3; AAH44157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        417
FT                   /note="E -> K (in Ref. 3; AAH44157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="V -> I (in Ref. 1; AAU44351)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="A -> P (in Ref. 1; AAU44351)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   662 AA;  73488 MW;  477FAC9DBD4FC290 CRC64;
     MPHNFRPGDL VFAKMKGYPH WPARIEDVAD GAVKPPPNKI PIFFFGTHET AFLAPKDLFA
     YEKNQERFGK PNKRKGFNEG LWEIQNNPHA SYNTPAAASS SDSEDNQPAA ASDAEEEEEA
     VVPRKAETGS DDSDSGSEDQ KKPAVKRKAP ALKRPPVKKA RASSSDRDGE ESGSPSEPEP
     SPSSDSDSGK NSDQDFTPQK ESGGRGGKKP AGRGRRKKAS SGSDSDSGSQ SDQKAARSDS
     EDEKPRPAAS GSESQSGSKS DSDSEPPPPP PPTRKAPQGR KKAEKPPPKP RARKPKPAPE
     RAPSSSSDSD SDSDTDRVSE WKKRDEERRK ELEERRKREE AEELRRLRER EKEEEEKRKK
     DKETKVRRGS SSSGSSSSDD EVDDHPLKKS KKPPPPPIPA PSDSDSPPPS ELKKKKESQK
     GRQKKEKEVK EKKERPVKEK KPQRSEEKHK AKPKAEKPKR KPVRPPEKKV EKKKEPSPEE
     KLQKLHTDIK FALKVDNPDI EKCLQALDEL SSVQVTTHIL QKNADVIATL KKIRRYKASN
     AVMEKATAVY NKLKLQFIGK IETGKPKPNE KNQEEQDAQN TDDSKPVNGE SEGERKDVSE
     SESNSKPTDQ DNPDENKSPN GIRPDPDEPA DQLNDSTEAD PTADADVKED SREQDEQMSS
     ES
 
 
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