NRBP_PONAB
ID NRBP_PONAB Reviewed; 535 AA.
AC Q5RBH9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Nuclear receptor-binding protein;
GN Name=NRBP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH90881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH90881.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in subcellular trafficking between the
CC endoplasmic reticulum and Golgi apparatus through interactions with the
CC Rho-type GTPases. {ECO:0000250|UniProtKB:Q9UHY1}.
CC -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase which
CC phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ
CC and is retained in the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}.
CC Endomembrane system {ECO:0000250}. Cell projection, lamellipodium
CC {ECO:0000250}. Note=Colocalizes with activated RAC3 to endomembranes
CC and at the cell periphery in lamellipodia. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
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; CR858669; CAH90881.1; -; mRNA.
DR RefSeq; NP_001125503.1; NM_001132031.1.
DR RefSeq; XP_009235713.1; XM_009237438.1.
DR AlphaFoldDB; Q5RBH9; -.
DR SMR; Q5RBH9; -.
DR STRING; 9601.ENSPPYP00000014013; -.
DR Ensembl; ENSPPYT00000014580; ENSPPYP00000014013; ENSPPYG00000012546.
DR GeneID; 100172412; -.
DR KEGG; pon:100172412; -.
DR CTD; 29959; -.
DR eggNOG; KOG1266; Eukaryota.
DR GeneTree; ENSGT00940000155605; -.
DR HOGENOM; CLU_024273_0_0_1; -.
DR InParanoid; Q5RBH9; -.
DR OrthoDB; 695382at2759; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT CHAIN 2..535
FT /note="Nuclear receptor-binding protein"
FT /id="PRO_0000086452"
FT DOMAIN 68..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99J45"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
SQ SEQUENCE 535 AA; 59818 MW; 398078660F6EEDD0 CRC64;
MSEGESQTVL SSGSDPKVES SSSAPGLTSV SPPVTSTTSA ASPEEEEESE DESEILEESP
CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ FSERKNYKLQ EEKVRAVFDN
LIQLEHLNIV KFHKYWADIK ENKARVIFIT EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW
CTQILSALSY LHSCDPPIIH GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL
HFFAPEYGEV TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDPLQ
REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE NALEEITKNM
DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG IYPLTAFGLP RPQQPQQEEV
TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN IESVEEGVKH HLTLLLKLED KLNRHLSCDL
MPNENIPELA AELVQLGFIS EADQSRLTSL LEETLNKFNF ARSSTLNSAA VTVSS