FA83B_MOUSE
ID FA83B_MOUSE Reviewed; 1012 AA.
AC Q0VBM2; Q8BWY1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein FAM83B {ECO:0000305};
GN Name=Fam83b {ECO:0000312|MGI:MGI:2685362};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-689.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
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).
CC -!- FUNCTION: Probable proto-oncogene that functions in the epidermal
CC growth factor receptor/EGFR signaling pathway. May activate both the
CC EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling
CC cascades. {ECO:0000250|UniProtKB:Q5T0W9}.
CC -!- SUBUNIT: Interacts with EGFR; the interaction is disrupted by EGF
CC stimulation. Interacts with RAF1; displaces 14-3-3 proteins from RAF1
CC and activates RAF1 within the RAS/MAPK signaling cascade. Interacts
CC with AKT1, PIK3CA and PIK3R1; activates the PI3K/AKT signaling cascade.
CC {ECO:0000250|UniProtKB:Q5T0W9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5T0W9}.
CC Membrane {ECO:0000250|UniProtKB:Q5T0W9}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; BC120577; AAI20578.1; -; mRNA.
DR EMBL; BC120579; AAI20580.1; -; mRNA.
DR EMBL; AK049628; BAC33845.1; -; mRNA.
DR CCDS; CCDS40695.1; -.
DR RefSeq; NP_001038983.1; NM_001045518.1.
DR RefSeq; XP_006511013.1; XM_006510950.3.
DR RefSeq; XP_006511015.1; XM_006510952.3.
DR RefSeq; XP_006511016.1; XM_006510953.3.
DR AlphaFoldDB; Q0VBM2; -.
DR SMR; Q0VBM2; -.
DR STRING; 10090.ENSMUSP00000139354; -.
DR iPTMnet; Q0VBM2; -.
DR PhosphoSitePlus; Q0VBM2; -.
DR MaxQB; Q0VBM2; -.
DR PaxDb; Q0VBM2; -.
DR PeptideAtlas; Q0VBM2; -.
DR PRIDE; Q0VBM2; -.
DR ProteomicsDB; 275841; -.
DR Antibodypedia; 31026; 59 antibodies from 15 providers.
DR Ensembl; ENSMUST00000098546; ENSMUSP00000096146; ENSMUSG00000032358.
DR Ensembl; ENSMUST00000183437; ENSMUSP00000139354; ENSMUSG00000032358.
DR GeneID; 208994; -.
DR KEGG; mmu:208994; -.
DR UCSC; uc009qtb.1; mouse.
DR CTD; 222584; -.
DR MGI; MGI:2685362; Fam83b.
DR VEuPathDB; HostDB:ENSMUSG00000032358; -.
DR eggNOG; ENOG502RPYE; Eukaryota.
DR GeneTree; ENSGT00940000157889; -.
DR HOGENOM; CLU_011804_0_0_1; -.
DR InParanoid; Q0VBM2; -.
DR OMA; QFQPSQI; -.
DR OrthoDB; 103194at2759; -.
DR PhylomeDB; Q0VBM2; -.
DR TreeFam; TF330777; -.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 208994; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q0VBM2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q0VBM2; protein.
DR Bgee; ENSMUSG00000032358; Expressed in jejunum and 35 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; ISO:MGI.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR012461; FAM83_N.
DR Pfam; PF07894; FAM83; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..1012
FT /note="Protein FAM83B"
FT /id="PRO_0000297563"
FT REGION 1..284
FT /note="Required for interaction with RAF1 and for the
FT function"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT REGION 410..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T0W9"
SQ SEQUENCE 1012 AA; 114676 MW; 6D268A6DBE3D877C CRC64;
MEASSMLSSL NDECRSDNYV EPHYKEWYRV AVDTLIEHGL EAYQEFLIKE RVSDFLAEEE
INYILKNVQK IAQNTEHGSD SSCDDGSSSG TYWPMQSDVE APNLDLGWPY VMPGLLGSTH
IDLLFHPPRA HLLTIKETIR KMIKEARKVV AIVMDVFTDV DIFKEIVEAS TRGISVYILL
DESNFSHFLT MTEKQGCQIQ RLRNIRIRTV KGQDYLSKTG AKFHGKMEQK FLLVDCQKVM
YGSYSYMWSF EKAHLSMVQI ITGHLVELFD EEFRTLYARS SVPSSFAQEE SVRAKPGKAL
WENGIYQRSI SSLASVSSQR NLFGRQDQIH KLDSSYFKGR GIYPLNDQDK HSMRNHGYKP
HFVPNFNGPS TIRHFQPSQL NENWKRHSYA GEQPETTPYL LLNRAMNRTN NAPGRWRRPS
DSLSVASSLR GGQGSQQNIP AQSFADRLAQ RKTTNLAERN SNVRRSFNGT DNHIRFIQQR
MPTLENTTKS FLRSWRIESY LNDNSEVPPD SNGSTLGDRF EGYENPEAVK ANALYTHSRL
RSSFVFKPTL PEQKEVNSCT TGSSNSTIIG SQGSDTPNEV PDTSTNAPPL TEKPLPEPSS
KLPTQQEEPK MHNLQVPEKQ PEALNQRTNG RAELNNCIYT NLCVNKQREN TENQQNDNLL
KRRSFPSFDH SKVNLEHGNS KNYVYSTLTR NRIRQPEKPK EVVLKSSKSM HNVTHSAEED
DDEVIERDPP SASATKSISI AALLDVNKEE PNKEPNSKKE GKASPSFLKK GSQKLRSLLS
LTPEKRESLA KNKAPAFYRM CSSSDTLVSE GEENQKPKKS EPKVDSSPRR KRSSSSNSQG
SIHKSKEDIA VSASPGISSQ AEESRRIAPS PRPVERRLSE RAGDASAPRF NTEQIQYRDS
KEISSLMTPA RRPTPSPVLK PNELLRSHST NQRVYSRFEP FCKIESSIQP ASSVTNTHVN
RPEVKSSTMG TAYGRSSPML NYKTGAYHSY APNENKFRGF MQKFGNFIHK NK
