GGYF1_HUMAN
ID GGYF1_HUMAN Reviewed; 1035 AA.
AC O75420; Q6Y7W7; Q8WZ38;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=GRB10-interacting GYF protein 1;
DE AltName: Full=PERQ amino acid-rich with GYF domain-containing protein 1;
GN Name=GIGYF1; Synonyms=CDS2, PERQ1; ORFNames=PP3360;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA Tsui L.-C., Rosenthal A.;
RT "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT genes.";
RL Genome Res. 8:1060-1073(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=12771153; DOI=10.1074/jbc.m211572200;
RA Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A., Smith R.J.;
RT "Two novel proteins that are linked to insulin-like growth factor (IGF-I)
RT receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL J. Biol. Chem. 278:31564-31573(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 729-1035.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-28, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-137; SER-157;
RP SER-406; SER-538; SER-638 AND SER-862, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP INTERACTION WITH DDX6, AND MUTAGENESIS OF TRP-294; PHE-306 AND PHE-312.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
CC -!- FUNCTION: May act cooperatively with GRB10 to regulate tyrosine kinase
CC receptor signaling. May increase IGF1 receptor phosphorylation under
CC IGF1 stimulation as well as phosphorylation of IRS1 and SHC1 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12771153}.
CC -!- SUBUNIT: Interacts with GRB10 (By similarity). This transient binding
CC is increased under IGF1 stimulation and leads to recruitment of
CC GIGYF1/GRB10 complex to IGF1 receptor (By similarity). Interacts with
CC DDX6 (PubMed:31439631). {ECO:0000250|UniProtKB:Q99MR1,
CC ECO:0000269|PubMed:31439631}.
CC -!- INTERACTION:
CC O75420; Q9NXR5-2: ANKRD10; NbExp=3; IntAct=EBI-947774, EBI-12102070;
CC O75420; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-947774, EBI-742909;
CC O75420; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-947774, EBI-8643161;
CC O75420; Q9HC52: CBX8; NbExp=3; IntAct=EBI-947774, EBI-712912;
CC O75420; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-947774, EBI-10961624;
CC O75420; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-947774, EBI-739773;
CC O75420; P26196: DDX6; NbExp=3; IntAct=EBI-947774, EBI-351257;
CC O75420; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-947774, EBI-744099;
CC O75420; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-947774, EBI-11986315;
CC O75420; Q92993: KAT5; NbExp=3; IntAct=EBI-947774, EBI-399080;
CC O75420; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-947774, EBI-14069005;
CC O75420; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-947774, EBI-348259;
CC O75420; Q8NEH6: MNS1; NbExp=3; IntAct=EBI-947774, EBI-743811;
CC O75420; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-947774, EBI-11750983;
CC O75420; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-947774, EBI-10271199;
CC O75420; P54646: PRKAA2; NbExp=3; IntAct=EBI-947774, EBI-1383852;
CC O75420; P0CG20: PRR35; NbExp=3; IntAct=EBI-947774, EBI-11986293;
CC O75420; Q9NW64: RBM22; NbExp=3; IntAct=EBI-947774, EBI-2602260;
CC O75420; Q9UPN6: SCAF8; NbExp=3; IntAct=EBI-947774, EBI-7954236;
CC O75420; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-947774, EBI-748391;
CC O75420; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-947774, EBI-358489;
CC O75420; P09012: SNRPA; NbExp=3; IntAct=EBI-947774, EBI-607085;
CC O75420; P14678-2: SNRPB; NbExp=3; IntAct=EBI-947774, EBI-372475;
CC O75420; P09234: SNRPC; NbExp=3; IntAct=EBI-947774, EBI-766589;
CC O75420; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-947774, EBI-11959123;
CC O75420; Q96MF2: STAC3; NbExp=3; IntAct=EBI-947774, EBI-745680;
CC O75420; Q15560: TCEA2; NbExp=3; IntAct=EBI-947774, EBI-710310;
CC O75420; Q08117-2: TLE5; NbExp=3; IntAct=EBI-947774, EBI-11741437;
CC O75420; Q12815: TROAP; NbExp=3; IntAct=EBI-947774, EBI-2349743;
CC O75420; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-947774, EBI-10687282;
CC -!- DOMAIN: The GYF domain interacts with GRB10. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GIGYF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78792.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL55738.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF053356; AAC78792.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY176044; AAO46888.1; -; mRNA.
DR EMBL; AF289554; AAL55738.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34708.1; -.
DR RefSeq; NP_072096.2; NM_022574.4.
DR RefSeq; XP_005250589.1; XM_005250532.1.
DR PDB; 5NVK; X-ray; 2.90 A; B/D/F/H=33-103.
DR PDBsum; 5NVK; -.
DR AlphaFoldDB; O75420; -.
DR SMR; O75420; -.
DR BioGRID; 122218; 171.
DR IntAct; O75420; 51.
DR STRING; 9606.ENSP00000275732; -.
DR GlyGen; O75420; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75420; -.
DR PhosphoSitePlus; O75420; -.
DR BioMuta; GIGYF1; -.
DR EPD; O75420; -.
DR jPOST; O75420; -.
DR MassIVE; O75420; -.
DR MaxQB; O75420; -.
DR PaxDb; O75420; -.
DR PeptideAtlas; O75420; -.
DR PRIDE; O75420; -.
DR ProteomicsDB; 49992; -.
DR Antibodypedia; 16628; 88 antibodies from 17 providers.
DR DNASU; 64599; -.
DR Ensembl; ENST00000275732.5; ENSP00000275732.4; ENSG00000146830.11.
DR Ensembl; ENST00000646601.1; ENSP00000494292.1; ENSG00000146830.11.
DR Ensembl; ENST00000678049.1; ENSP00000503354.1; ENSG00000146830.11.
DR MANE-Select; ENST00000678049.1; ENSP00000503354.1; NM_001375765.1; NP_001362694.1.
DR UCSC; uc003uwg.2; human.
DR DisGeNET; 64599; -.
DR GeneCards; GIGYF1; -.
DR HGNC; HGNC:9126; GIGYF1.
DR HPA; ENSG00000146830; Low tissue specificity.
DR MIM; 612064; gene.
DR neXtProt; NX_O75420; -.
DR OpenTargets; ENSG00000146830; -.
DR PharmGKB; PA162389554; -.
DR VEuPathDB; HostDB:ENSG00000146830; -.
DR eggNOG; KOG1862; Eukaryota.
DR GeneTree; ENSGT00940000159845; -.
DR HOGENOM; CLU_007300_0_0_1; -.
DR InParanoid; O75420; -.
DR OMA; FHNTGEC; -.
DR OrthoDB; 412069at2759; -.
DR PhylomeDB; O75420; -.
DR TreeFam; TF325513; -.
DR PathwayCommons; O75420; -.
DR SignaLink; O75420; -.
DR SIGNOR; O75420; -.
DR BioGRID-ORCS; 64599; 26 hits in 1075 CRISPR screens.
DR ChiTaRS; GIGYF1; human.
DR GenomeRNAi; 64599; -.
DR Pharos; O75420; Tbio.
DR PRO; PR:O75420; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75420; protein.
DR Bgee; ENSG00000146830; Expressed in sural nerve and 168 other tissues.
DR Genevisible; O75420; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..1035
FT /note="GRB10-interacting GYF protein 1"
FT /id="PRO_0000058314"
FT DOMAIN 474..522
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 105..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MR1"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 294
FT /note="W->A: Abolishes interaction with DDX6."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 306
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-312."
FT /evidence="ECO:0000269|PubMed:31439631"
FT MUTAGEN 312
FT /note="F->A: Abolishes interaction with DDX6; when
FT associated with A-306."
FT /evidence="ECO:0000269|PubMed:31439631"
FT CONFLICT 729..730
FT /note="RK -> DE (in Ref. 3; AAL55738)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="S -> T (in Ref. 3; AAL55738)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="L -> V (in Ref. 3; AAL55738)"
FT /evidence="ECO:0000305"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:5NVK"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5NVK"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5NVK"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5NVK"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5NVK"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:5NVK"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5NVK"
SQ SEQUENCE 1035 AA; 114601 MW; 7DACB6F80EBEA7D0 CRC64;
MAAETLNFGP EWLRALSGGG SVASPPPSPA MPKYKLADYR YGREEMLALY VKENKVPEEL
QDKEFAAVLQ DEPLQPLALE PLTEEEQRNF SLSVNSVAVL RLMGKGAGPP LAGTSRGRGS
TRSRGRGRGD SCFYQRSIEE GDGAFGRSPR EIQRSQSWDD RGERRFEKSA RRDGARCGFE
EGGAGPRKEH ARSDSENWRS LREEQEEEEE GSWRLGAGPR RDGDRWRSAS PDGGPRSAGW
REHGERRRKF EFDLRGDRGG CGEEEGRGGG GSSHLRRCRA PEGFEEDKDG LPEWCLDDED
EEMGTFDASG AFLPLKKGPK EPIPEEQELD FQGLEEEEEP SEGLEEEGPE AGGKELTPLP
PQEEKSSSPS PLPTLGPLWG TNGDGDETAE KEPPAAEDDI RGIQLSPGVG SSAGPPGDLE
DDEGLKHLQQ EAEKLVASLQ DSSLEEEQFT AAMQTQGLRH SAAATALPLS HGAARKWFYK
DPQGEIQGPF TTQEMAEWFQ AGYFSMSLLV KRGCDEGFQP LGEVIKMWGR VPFAPGPSPP
PLLGNMDQER LKKQQELAAA ALYQQLQHQQ FLQLVSSRQL PQCALREKAA LGDLTPPPPP
PPQQQQQQLT AFLQQLQALK PPRGGDQNLL PTMSRSLSVP DSGRLWDVHT SASSQSGGEA
SLWDIPINSS TQGPILEQLQ LQHKFQERRE VELRAKREEE ERKRREEKRR QQQQEEQKRR
QEEEELFRRK HVRQQELLLK LLQQQQAVPV PPAPSSPPPL WAGLAKQGLS MKTLLELQLE
GERQLHKQPP PREPARAQAP NHRVQLGGLG TAPLNQWVSE AGPLWGGPDK SGGGSSGLGL
WEDTPKSGGS LVRGLGLKNS RSSPSLSDSY SHLSGRPIRK KTEEEEKLLK LLQGIPRPQD
GFTQWCEQML HTLSATGSLD VPMAVAILKE VESPYDVHDY IRSCLGDTLE AKEFAKQFLE
RRAKQKASQQ RQQQQEAWLS SASLQTAFQA NHSTKLGPGE GSKAKRRALM LHSDPSILGY
SLHGSSGEIE SVDDY
