FA83A_HUMAN
ID FA83A_HUMAN Reviewed; 434 AA.
AC Q86UY5; Q71HL2; Q8N7I1; Q96I47;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein FAM83A {ECO:0000305};
DE AltName: Full=Tumor antigen BJ-TSA-9 {ECO:0000303|Ref.2};
DE AltName: Full=Tumor-specific gene expressed in prostate protein {ECO:0000303|Ref.1};
GN Name=FAM83A {ECO:0000312|HGNC:HGNC:28210};
GN Synonyms=TSGP {ECO:0000303|Ref.1};
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 [MRNA] (ISOFORMS 1 AND 2).
RA Yang D., Nelson C.C., Li D., Gleave M.E.;
RT "TSGP, a shared tumor specific gene expressed in prostate cancer.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT THR-237.
RA Xueyuan D., Weifeng C.;
RT "BJ-TSA-9, a tumor specific gene which was characterized from lung
RT carcinoma and colon carcinoma.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-237.
RC TISSUE=Lung, and Pancreas;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-434 (ISOFORM 1), AND VARIANT
RP THR-237.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, 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 [6]
RP FUNCTION, PHOSPHORYLATION, INTERACTION WITH PI3-KINASE AND RAF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22886303; DOI=10.1172/jci60498;
RA Lee S.Y., Meier R., Furuta S., Lenburg M.E., Kenny P.A., Xu R.,
RA Bissell M.J.;
RT "FAM83A confers EGFR-TKI resistance in breast cancer cells and in mice.";
RL J. Clin. Invest. 122:3211-3220(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-327 AND SER-357, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 INTERACTION WITH RAF1.
RX PubMed=24736947; DOI=10.1158/1541-7786.mcr-13-0289;
RA Cipriano R., Miskimen K.L., Bryson B.L., Foy C.R., Bartel C.A.,
RA Jackson M.W.;
RT "Conserved oncogenic behavior of the FAM83 family regulates MAPK signaling
RT in human cancer.";
RL Mol. Cancer Res. 12:1156-1165(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 122-304.
RA Pinkas D.M., Sanvitale C., Wang D., Krojer T., Kopec J., Chaikuad A.,
RA Dixon Clarke S., Berridge G., Burgess-Brown N., Von Delft F.,
RA Arrowsmith C., Edwards A., Bountra C., Bullock A.;
RT "Crystal structure of human Bj-Tsa-9.";
RL Submitted (JUN-2014) to the PDB data bank.
CC -!- FUNCTION: Probable proto-oncogene that functions in the epidermal
CC growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK
CC and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for
CC the RAS/MAPK signaling cascade activation upon EGFR stimulation, it
CC also activates both signaling cascades independently of EGFR
CC activation. {ECO:0000269|PubMed:22886303}.
CC -!- SUBUNIT: Interacts with the regulatory subunit p85 of PI3-kinase;
CC increased by EGFR activation (PubMed:22886303). Interacts with RAF1;
CC increased by EGFR activation it activates RAF1 (PubMed:22886303,
CC PubMed:24736947). {ECO:0000269|PubMed:22886303,
CC ECO:0000269|PubMed:24736947}.
CC -!- INTERACTION:
CC Q86UY5; O14503: BHLHE40; NbExp=6; IntAct=EBI-1384254, EBI-711810;
CC Q86UY5; P49674: CSNK1E; NbExp=4; IntAct=EBI-1384254, EBI-749343;
CC Q86UY5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1384254, EBI-3867333;
CC Q86UY5; Q15038: DAZAP2; NbExp=3; IntAct=EBI-1384254, EBI-724310;
CC Q86UY5; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-1384254, EBI-1384254;
CC Q86UY5; P22607: FGFR3; NbExp=3; IntAct=EBI-1384254, EBI-348399;
CC Q86UY5; O75593: FOXH1; NbExp=3; IntAct=EBI-1384254, EBI-1759806;
CC Q86UY5; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-1384254, EBI-12018822;
CC Q86UY5; Q96CN9: GCC1; NbExp=3; IntAct=EBI-1384254, EBI-746252;
CC Q86UY5; Q86YR5-3: GPSM1; NbExp=3; IntAct=EBI-1384254, EBI-10261098;
CC Q86UY5; P06396: GSN; NbExp=3; IntAct=EBI-1384254, EBI-351506;
CC Q86UY5; O76011: KRT34; NbExp=3; IntAct=EBI-1384254, EBI-1047093;
CC Q86UY5; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-1384254, EBI-11962084;
CC Q86UY5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-1384254, EBI-10261141;
CC Q86UY5; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1384254, EBI-716006;
CC Q86UY5; O43639: NCK2; NbExp=3; IntAct=EBI-1384254, EBI-713635;
CC Q86UY5; Q9UPG8: PLAGL2; NbExp=5; IntAct=EBI-1384254, EBI-2876622;
CC Q86UY5; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1384254, EBI-25882629;
CC Q86UY5; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-1384254, EBI-10293968;
CC Q86UY5; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-1384254, EBI-3957793;
CC Q86UY5; P25788: PSMA3; NbExp=3; IntAct=EBI-1384254, EBI-348380;
CC Q86UY5; P47897: QARS1; NbExp=3; IntAct=EBI-1384254, EBI-347462;
CC Q86UY5; Q8NB12: SMYD1; NbExp=3; IntAct=EBI-1384254, EBI-8463848;
CC Q86UY5; P36406: TRIM23; NbExp=3; IntAct=EBI-1384254, EBI-740098;
CC Q86UY5; P14373: TRIM27; NbExp=3; IntAct=EBI-1384254, EBI-719493;
CC Q86UY5; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-1384254, EBI-7353612;
CC Q86UY5; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1384254, EBI-741480;
CC Q86UY5; Q9Y649; NbExp=3; IntAct=EBI-1384254, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22886303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TSGP-L;
CC IsoId=Q86UY5-1; Sequence=Displayed;
CC Name=2; Synonyms=TSGP-S;
CC IsoId=Q86UY5-2; Sequence=VSP_025187, VSP_025190, VSP_025191;
CC Name=3;
CC IsoId=Q86UY5-3; Sequence=VSP_025188, VSP_025189;
CC -!- PTM: Phosphorylated upon EGFR activation.
CC {ECO:0000269|PubMed:22886303}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05299.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ280322; ABB91800.1; -; mRNA.
DR EMBL; DQ280323; ABB91801.1; -; mRNA.
DR EMBL; AF497803; AAQ07260.1; -; mRNA.
DR EMBL; BC007828; AAH07828.1; -; mRNA.
DR EMBL; BC052300; AAH52300.1; -; mRNA.
DR EMBL; AK098407; BAC05299.1; ALT_INIT; mRNA.
DR CCDS; CCDS6339.1; -. [Q86UY5-3]
DR CCDS; CCDS6340.1; -. [Q86UY5-1]
DR CCDS; CCDS75784.1; -. [Q86UY5-2]
DR RefSeq; NP_001275516.1; NM_001288587.2. [Q86UY5-2]
DR RefSeq; NP_116288.2; NM_032899.6. [Q86UY5-1]
DR RefSeq; NP_996889.1; NM_207006.2. [Q86UY5-3]
DR PDB; 4URJ; X-ray; 2.68 A; A/B/C/D=122-304.
DR PDBsum; 4URJ; -.
DR AlphaFoldDB; Q86UY5; -.
DR SMR; Q86UY5; -.
DR BioGRID; 124411; 43.
DR IntAct; Q86UY5; 35.
DR STRING; 9606.ENSP00000428876; -.
DR iPTMnet; Q86UY5; -.
DR PhosphoSitePlus; Q86UY5; -.
DR BioMuta; FAM83A; -.
DR DMDM; 74727505; -.
DR EPD; Q86UY5; -.
DR jPOST; Q86UY5; -.
DR MassIVE; Q86UY5; -.
DR MaxQB; Q86UY5; -.
DR PaxDb; Q86UY5; -.
DR PeptideAtlas; Q86UY5; -.
DR PRIDE; Q86UY5; -.
DR ProteomicsDB; 69935; -. [Q86UY5-1]
DR ProteomicsDB; 69936; -. [Q86UY5-2]
DR ProteomicsDB; 69937; -. [Q86UY5-3]
DR Antibodypedia; 64700; 82 antibodies from 18 providers.
DR DNASU; 84985; -.
DR Ensembl; ENST00000276699.10; ENSP00000276699.6; ENSG00000147689.17. [Q86UY5-3]
DR Ensembl; ENST00000518448.5; ENSP00000428876.1; ENSG00000147689.17. [Q86UY5-1]
DR Ensembl; ENST00000522648.5; ENSP00000427979.1; ENSG00000147689.17. [Q86UY5-2]
DR Ensembl; ENST00000536633.2; ENSP00000445218.1; ENSG00000147689.17. [Q86UY5-3]
DR Ensembl; ENST00000690554.1; ENSP00000509471.1; ENSG00000147689.17. [Q86UY5-1]
DR GeneID; 84985; -.
DR KEGG; hsa:84985; -.
DR MANE-Select; ENST00000690554.1; ENSP00000509471.1; NM_001394396.1; NP_001381325.1.
DR UCSC; uc003ypv.5; human. [Q86UY5-1]
DR CTD; 84985; -.
DR DisGeNET; 84985; -.
DR GeneCards; FAM83A; -.
DR HGNC; HGNC:28210; FAM83A.
DR HPA; ENSG00000147689; Group enriched (esophagus, vagina).
DR neXtProt; NX_Q86UY5; -.
DR OpenTargets; ENSG00000147689; -.
DR PharmGKB; PA142671851; -.
DR VEuPathDB; HostDB:ENSG00000147689; -.
DR eggNOG; ENOG502QQDU; Eukaryota.
DR GeneTree; ENSGT00940000160768; -.
DR HOGENOM; CLU_019056_3_1_1; -.
DR InParanoid; Q86UY5; -.
DR OMA; YSFSWLC; -.
DR OrthoDB; 550760at2759; -.
DR PhylomeDB; Q86UY5; -.
DR TreeFam; TF330777; -.
DR PathwayCommons; Q86UY5; -.
DR SignaLink; Q86UY5; -.
DR BioGRID-ORCS; 84985; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; FAM83A; human.
DR GeneWiki; FAM83A; -.
DR GenomeRNAi; 84985; -.
DR Pharos; Q86UY5; Tbio.
DR PRO; PR:Q86UY5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86UY5; protein.
DR Bgee; ENSG00000147689; Expressed in lower esophagus mucosa and 122 other tissues.
DR Genevisible; Q86UY5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR012461; FAM83_N.
DR Pfam; PF07894; FAM83; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Proto-oncogene; Reference proteome.
FT CHAIN 1..434
FT /note="Protein FAM83A"
FT /id="PRO_0000286813"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 161..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025187"
FT VAR_SEQ 345..367
FT /note="GTRSVSASSGPCSPAAPHPPPPP -> VPESKQNKTKTKKQTTLWFLMAF
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025188"
FT VAR_SEQ 348..350
FT /note="SVS -> TDG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025190"
FT VAR_SEQ 351..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_025191"
FT VAR_SEQ 368..434
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025189"
FT VARIANT 237
FT /note="A -> T (in dbSNP:rs7813708)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_032178"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:4URJ"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4URJ"
FT TURN 261..266
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:4URJ"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:4URJ"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4URJ"
SQ SEQUENCE 434 AA; 47458 MW; 63D09D927D452FCC CRC64;
MSRSRHLGKI RKRLEDVKSQ WVRPARADFS DNESARLATD ALLDGGSEAY WRVLSQEGEV
DFLSSVEAQY IQAQAREPPC PPDTLGGAEA GPKGLDSSSL QSGTYFPVAS EGSEPALLHS
WASAEKPYLK EKSSATVYFQ TVKHNNIRDL VRRCITRTSQ VLVILMDVFT DVEIFCDILE
AANKRGVFVC VLLDQGGVKL FQEMCDKVQI SDSHLKNISI RSVEGEIYCA KSGRKFAGQI
REKFIISDWR FVLSGSYSFT WLCGHVHRNI LSKFTGQAVE LFDEEFRHLY ASSKPVMGLK
SPRLVAPVPP GAAPANGRLS SSSGSASDRT SSNPFSGRSA GSHPGTRSVS ASSGPCSPAA
PHPPPPPRFQ PHQGPWGAPS PQAHLSPRPH DGPPAAVYSN LGAYRPTRLQ LEQLGLVPRL
TPTWRPFLQA SPHF
