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NRBP_DROPS
ID   NRBP_DROPS              Reviewed;         663 AA.
AC   Q297L2;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Nuclear receptor-binding protein homolog;
DE   AltName: Full=MLF1-adaptor molecule;
GN   Name=Madm {ECO:0000250|UniProtKB:Q9Y0Y6}; ORFNames=GA10685;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: May play a role in subcellular trafficking between the
CC       endoplasmic reticulum and Golgi apparatus. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:Q9UHY1}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CM000070; EAL28193.2; -; Genomic_DNA.
DR   RefSeq; XP_001359050.2; XM_001359013.4.
DR   AlphaFoldDB; Q297L2; -.
DR   SMR; Q297L2; -.
DR   STRING; 7237.FBpp0284176; -.
DR   PRIDE; Q297L2; -.
DR   EnsemblMetazoa; FBtr0285738; FBpp0284176; FBgn0070741.
DR   GeneID; 4802057; -.
DR   KEGG; dpo:Dpse_GA10685; -.
DR   eggNOG; KOG1266; Eukaryota.
DR   HOGENOM; CLU_024273_0_0_1; -.
DR   InParanoid; Q297L2; -.
DR   OMA; SWRRWCT; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0070741; Expressed in female reproductive system and 3 other tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR   GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR   GO; GO:0036335; P:intestinal stem cell homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IEA:EnsemblMetazoa.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0008361; P:regulation of cell size; IEA:EnsemblMetazoa.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..663
FT                   /note="Nuclear receptor-binding protein homolog"
FT                   /id="PRO_0000351197"
FT   DOMAIN          122..392
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y0Y6"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y0Y6"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y0Y6"
FT   MOD_RES         500
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y0Y6"
SQ   SEQUENCE   663 AA;  73520 MW;  8D5F50FEEA65D978 CRC64;
     MSNSQANAGS SGSADEPTLN PSGSATLVPN LTTTNASSQA TPASTIPQQQ QPQQSQPQPQ
     PQPPPHIVGA STADAGGGVG VVVAGGSEGV NLDSSPRESG DDSEDESEIL EESPCGRWLK
     RREEVDQRDV PGIDCVHLAM DTEEGVEVVW NEVQYANMQE LKSQEEKMRQ VFDNLLQLDH
     QNIVKFHRYW TDTQQAERPR VIFITEYMSS GSLKQFLKRT KRNAKRLPLE SWRRWCTQIL
     SALSYLHSCT PPIIHGNLTC DSIFIQHNGL VKIGSVVPDA VHYSVRRQWD RESAREQERE
     RGAHYFQAPE YGAAEQLTAA LDIYAFGMCA LEMAALEIQP SNSESTAINE ETIQRTICSL
     ESDLQRDLIE KCLNPQPQGR PSANDLLFHP LLFEVHSLKL LTAHCLVFSP ANRTMFSETA
     FDGLMQRYYQ PDVIMAQLMS GGQERQYRLA DVAGADKLEK FVEDVKYGVY PLITYNGKKP
     PNFRSRAASP ERADSVKSAT PEPVDTESRR IVNMMCSVKI KEDSNDIIMT ILLRMDDKMN
     RQLTCQVNEN DTAADLTSEL VRLGFVHLDD QDKIEVLLEE TLKAGVMSDG AGAESSGAGV
     TTTATMAALE QLERNWSISD ADKTMGSSMS SPATAMMYVP QDQQQYQQQQ QEADVDQSGT
     TSN
 
 
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