GRAP_MOUSE
ID GRAP_MOUSE Reviewed; 217 AA.
AC Q9CX99; Q0VBE3; Q3U545;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=GRB2-related adapter protein {ECO:0000305};
GN Name=Grap {ECO:0000312|MGI:MGI:1918770};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=30610177; DOI=10.1073/pnas.1810951116;
RA Li C., Bademci G., Subasioglu A., Diaz-Horta O., Zhu Y., Liu J.,
RA Mitchell T.G., Abad C., Seyhan S., Duman D., Cengiz F.B., Tokgoz-Yilmaz S.,
RA Blanton S.H., Farooq A., Walz K., Zhai R.G., Tekin M.;
RT "Dysfunction of GRAP, encoding the GRB2-related adaptor protein, is linked
RT to sensorineural hearing loss.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:1347-1352(2019).
CC -!- FUNCTION: Couples signals from receptor and cytoplasmic tyrosine
CC kinases to the Ras signaling pathway. Plays a role in the inner ear and
CC in hearing. {ECO:0000250|UniProtKB:Q13588}.
CC -!- SUBUNIT: Associates through its SH2 domain with ligand-activated
CC receptors for stem cell factor (KIT) and erythropoietin (EPOR). Also
CC forms a stable complex with the Bcr-Abl oncoprotein. GRAP is associated
CC with the Ras guanine nucleotide exchange factor SOS1, primarily through
CC its N-terminal SH3 domain. Interacts with phosphorylated LAT upon TCR
CC activation. Interacts with SHB (By similarity).
CC {ECO:0000250|UniProtKB:Q13588}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q08012};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q08012}. Synapse
CC {ECO:0000250|UniProtKB:Q08012}. Note=Localizes at the presynaptic
CC terminal. {ECO:0000250|UniProtKB:Q08012}.
CC -!- TISSUE SPECIFICITY: Expressed in inner ear, in neruonal fibers
CC innervating cochlear and utricular auditory hair cells (at protein
CC level). {ECO:0000269|PubMed:30610177}.
CC -!- SIMILARITY: Belongs to the GRB2/sem-5/DRK family. {ECO:0000305}.
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DR EMBL; AK018457; BAB31222.1; -; mRNA.
DR EMBL; AK153888; BAE32235.1; -; mRNA.
DR EMBL; AL596209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120674; AAI20675.1; -; mRNA.
DR EMBL; BC120676; AAI20677.1; -; mRNA.
DR CCDS; CCDS24817.1; -.
DR RefSeq; NP_082093.1; NM_027817.3.
DR AlphaFoldDB; Q9CX99; -.
DR SMR; Q9CX99; -.
DR IntAct; Q9CX99; 4.
DR STRING; 10090.ENSMUSP00000004959; -.
DR iPTMnet; Q9CX99; -.
DR PhosphoSitePlus; Q9CX99; -.
DR EPD; Q9CX99; -.
DR MaxQB; Q9CX99; -.
DR PaxDb; Q9CX99; -.
DR PRIDE; Q9CX99; -.
DR ProteomicsDB; 271290; -.
DR DNASU; 71520; -.
DR Ensembl; ENSMUST00000004959; ENSMUSP00000004959; ENSMUSG00000004837.
DR GeneID; 71520; -.
DR KEGG; mmu:71520; -.
DR UCSC; uc007jhz.1; mouse.
DR CTD; 10750; -.
DR MGI; MGI:1918770; Grap.
DR VEuPathDB; HostDB:ENSMUSG00000004837; -.
DR eggNOG; KOG3601; Eukaryota.
DR GeneTree; ENSGT00940000156254; -.
DR HOGENOM; CLU_073617_1_0_1; -.
DR InParanoid; Q9CX99; -.
DR OMA; GRCHGHV; -.
DR OrthoDB; 1091250at2759; -.
DR PhylomeDB; Q9CX99; -.
DR TreeFam; TF354288; -.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR BioGRID-ORCS; 71520; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Grap; mouse.
DR PRO; PR:Q9CX99; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CX99; protein.
DR Bgee; ENSMUSG00000004837; Expressed in mesenteric lymph node and 114 other tissues.
DR Genevisible; Q9CX99; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd11948; SH3_GRAP_N; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR035645; GRAP_N_SH3.
DR InterPro; IPR043539; Grb2-like.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46037; PTHR46037; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Repeat; SH2 domain; SH3 domain; Synapse.
FT CHAIN 1..217
FT /note="GRB2-related adapter protein"
FT /id="PRO_0000088207"
FT DOMAIN 1..58
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 60..152
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 158..217
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
SQ SEQUENCE 217 AA; 25277 MW; 1AF124C3D2773DD2 CRC64;
MESVALYSFQ ATESDELAFN KGDTLKILNM EDDQNWYKAE LRGAEGFVPK NYIRVKPHPW
YSGRISRQLA EETLMKRNHL GAFLIRESES SPGEFSVSVN YGDQVQHFKV LREASGKYFL
WEEKFNSLNE LVDFYRTTTI AKRRQIFLCD EQPLIKPSRA CFAQAQFDFS AQDPSQLSLR
RGDIVEVVER EDPHWWRGRA GGRLGFFPRS YVQPVHL
