GBLP_MACFA
ID GBLP_MACFA Reviewed; 317 AA.
AC Q4R7Y4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1;
DE Contains:
DE RecName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed;
GN Name=GNB2L1; ORFNames=QtsA-14081;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the recruitment, assembly and/or regulation of a
CC variety of signaling molecules. Interacts with a wide variety of
CC proteins and plays a role in many cellular processes. Component of the
CC 40S ribosomal subunit involved in translational repression. Binds to
CC and stabilizes activated protein kinase C (PKC), increasing PKC-
CC mediated phosphorylation. May recruit activated PKC to the ribosome,
CC leading to phosphorylation of EIF6. Inhibits the activity of SRC
CC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging
CC the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by
CC PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK
CC heterodimer. Facilitates ligand-independent nuclear translocation of AR
CC following PKC activation, represses AR transactivation activity and is
CC required for phosphorylation of AR by SRC. Modulates IGF1R-dependent
CC integrin signaling and promotes cell spreading and contact with the
CC extracellular matrix. Involved in PKC-dependent translocation of ADAM12
CC to the cell membrane. Promotes the ubiquitination and proteasome-
CC mediated degradation of proteins such as CLEC1B and HIF1A. Required for
CC VANGL2 membrane localization, inhibits Wnt signaling, and regulates
CC cellular polarization and oriented cell division during gastrulation.
CC Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates
CC internalization of the muscarinic receptor CHRM2. Promotes apoptosis by
CC increasing oligomerization of BAX and disrupting the interaction of BAX
CC with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity.
CC Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a
CC role in regulation of FLT1-mediated cell migration (By similarity).
CC Involved in the transport of ABCB4 from the Golgi to the apical bile
CC canalicular membrane (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P63244}.
CC -!- SUBUNIT: Interacts with CPNE3 (By similarity). May interact with ABCB4
CC (By similarity). Component of the small (40S) ribosomal subunit. Exists
CC as a monomer and also forms oligomers. Binds SLC9A3R1. Forms a ternary
CC complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1.
CC Interacts with SRC (via SH2 domain); the interaction is enhanced by
CC tyrosine phosphorylation of RACK1. Recruited in a circadian manner into
CC a nuclear complex which also includes BMAL1 and PRKCA. Interacts with
CC AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12.
CC Interacts with CLEC1B (via N-terminal region) and with HIF1A; the
CC interaction promotes their degradation. Interacts with RHOA; this
CC enhances RHOA activation and promotes cell migration. Interacts with
CC CHRM2; the interaction regulates CHRM2 internalization. Interacts with
CC TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for
CC PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1.
CC Interacts with HRAS. Interacts with LARP4B. Interacts with PKD2L1 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63244}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63244}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000250|UniProtKB:P63244}.
CC Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P68040}. Note=Recruited to the plasma membrane
CC through interaction with KRT1 which binds to membrane-bound ITGB1. Also
CC associated with the membrane in oncogene-transformed cells. PKC
CC activation induces translocation from the perinuclear region to the
CC cell periphery (By similarity). In the brain, detected mainly in cell
CC bodies and dendrites with little expression in axonal fibers or nuclei
CC (By similarity). {ECO:0000250|UniProtKB:P63244,
CC ECO:0000250|UniProtKB:P68040}.
CC -!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required
CC for binding to SRC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC protein RACK1 subfamily. {ECO:0000305}.
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DR EMBL; AB168677; BAE00788.1; -; mRNA.
DR AlphaFoldDB; Q4R7Y4; -.
DR SMR; Q4R7Y4; -.
DR STRING; 9541.XP_005558900.1; -.
DR eggNOG; KOG0279; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Biological rhythms; Cell cycle; Cell membrane;
KW Cell projection; Cytoplasm; Developmental protein; Gastrulation;
KW Growth regulation; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosomal protein; Translation regulation;
KW WD repeat.
FT CHAIN 1..317
FT /note="Guanine nucleotide-binding protein subunit beta-2-
FT like 1"
FT /id="PRO_0000424481"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT CHAIN 2..317
FT /note="Guanine nucleotide-binding protein subunit beta-2-
FT like 1, N-terminally processed"
FT /id="PRO_0000232130"
FT REPEAT 13..44
FT /note="WD 1"
FT REPEAT 61..91
FT /note="WD 2"
FT REPEAT 103..133
FT /note="WD 3"
FT REPEAT 146..178
FT /note="WD 4"
FT REPEAT 190..220
FT /note="WD 5"
FT REPEAT 231..260
FT /note="WD 6"
FT REPEAT 281..311
FT /note="WD 7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Guanine nucleotide-binding
FT protein subunit beta-2-like 1, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 52
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68040"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63244"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68040"
SQ SEQUENCE 317 AA; 35077 MW; 257F91E369ED2044 CRC64;
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR
GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI
VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA
NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC
FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA
GYTDNLVRVW QVTIGTR
