G3BP2_PONAB
ID G3BP2_PONAB Reviewed; 482 AA.
AC Q5R9L3; Q5RAH4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Ras GTPase-activating protein-binding protein 2;
DE Short=G3BP-2;
DE AltName: Full=GAP SH3 domain-binding protein 2;
GN Name=G3BP2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scaffold protein that plays an essential role in cytoplasmic
CC stress granule formation which acts as a platform for antiviral
CC signaling. {ECO:0000250|UniProtKB:Q9UN86}.
CC -!- SUBUNIT: Forms homooligomers. Forms heterodimers with G3BP1. Interacts
CC with NFKBIA (via N-terminus). Interacts with USP10. Interacts with
CC PABPC1. {ECO:0000250|UniProtKB:Q9UN86}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UN86}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UN86}.
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DR EMBL; CR859041; CAH91236.1; -; mRNA.
DR EMBL; CR859374; CAH91547.1; -; mRNA.
DR RefSeq; NP_001125730.1; NM_001132258.1.
DR RefSeq; XP_009238363.1; XM_009240088.1.
DR RefSeq; XP_009238364.1; XM_009240089.1.
DR RefSeq; XP_009238366.1; XM_009240091.1.
DR AlphaFoldDB; Q5R9L3; -.
DR SMR; Q5R9L3; -.
DR STRING; 9601.ENSPPYP00000016578; -.
DR Ensembl; ENSPPYT00000034523; ENSPPYP00000025619; ENSPPYG00000014846.
DR GeneID; 100172655; -.
DR KEGG; pon:100172655; -.
DR CTD; 9908; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; Q5R9L3; -.
DR OMA; PHQIGSE; -.
DR OrthoDB; 1526879at2759; -.
DR TreeFam; TF325464; -.
DR Proteomes; UP000001595; Chromosome 4.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IEA:InterPro.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd12464; RRM_G3BP2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034377; G3BP2.
DR InterPro; IPR034376; G3BP2_RRM.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039539; Ras_GTPase_bind_prot.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10693; PTHR10693; 1.
DR PANTHER; PTHR10693:SF10; PTHR10693:SF10; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Immunity; Innate immunity; Isopeptide bond; Methylation;
KW mRNA transport; Phosphoprotein; Reference proteome; RNA-binding; Transport;
KW Ubl conjugation.
FT CHAIN 1..482
FT /note="Ras GTPase-activating protein-binding protein 2"
FT /id="PRO_0000271372"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 331..409
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 140..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97379"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97379"
FT MOD_RES 457
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 468
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P97379"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT CONFLICT 310
FT /note="G -> D (in Ref. 1; CAH91236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54121 MW; 74B8EA43C0560229 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND
IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV
PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEER QPSPEPVQEN ANSGYYEAHP
VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKNLEE LEEKSTTPPP AEPVSLPQEP
PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVEA KPEVQSQPPR VREQRPRERP
GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL
RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG
GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM AQKLGSGRGT GQMEGRFTGQ
RR
