FA83G_HUMAN
ID FA83G_HUMAN Reviewed; 823 AA.
AC A6ND36; Q3KQZ4; Q6ZW60;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein FAM83G;
DE AltName: Full=Protein associated with SMAD1 {ECO:0000303|PubMed:24554596};
GN Name=FAM83G; Synonyms=PAWS1 {ECO:0000303|PubMed:24554596};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 618-823 (ISOFORM 1).
RC TISSUE=Bone;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-124; SER-127 AND SER-356, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND IDENTIFICATION BY
RP MASS 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, 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 [10]
RP INTERACTION WITH SMAD1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-610;
RP SER-614 AND SER-616 BY BMPR1A, MUTAGENESIS OF SER-610, AND FUNCTION.
RX PubMed=24554596; DOI=10.1098/rsob.130210;
RA Vogt J., Dingwell K.S., Herhaus L., Gourlay R., Macartney T., Campbell D.,
RA Smith J.C., Sapkota G.P.;
RT "Protein associated with SMAD1 (PAWS1/FAM83G) is a substrate for type I
RT bone morphogenetic protein receptors and modulates bone morphogenetic
RT protein signalling.";
RL Open Biol. 4:130210-130210(2014).
RN [11]
RP VARIANTS PHE-64 AND TRP-630.
RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
RG Care4Rare Canada Consortium;
RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
CC -!- FUNCTION: May regulate the bone morphogenetic proteins (BMP) pathway.
CC {ECO:0000269|PubMed:24554596}.
CC -!- SUBUNIT: Found in a macromolecular complex with SMAD1. Interacts with
CC SMAD1 (via MH2 domain); in a SMAD4-independent manner.
CC {ECO:0000269|PubMed:24554596}.
CC -!- INTERACTION:
CC A6ND36; P48729: CSNK1A1; NbExp=13; IntAct=EBI-1047240, EBI-1383726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24554596}.
CC Nucleus {ECO:0000269|PubMed:24554596}. Note=Detected predominantly in
CC cytosolic. Upon BMP stimulation, a small portion of PAWS1 is detected
CC in the nucleus. {ECO:0000269|PubMed:24554596}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6ND36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6ND36-2; Sequence=VSP_033120, VSP_033121, VSP_033122,
CC VSP_033123;
CC -!- PTM: BMP signaling induces the phosphorylation of PAWS1 by BMPR1A at
CC Ser-610, Ser-614 and Ser-616. In response to BMP phosphorylation at
CC Ser-610 is necessary for the activation of SMAD4-independent BMP target
CC genes such as NEDD9 and ASNS. {ECO:0000269|PubMed:24554596}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; AK123558; BAC85645.1; -; mRNA.
DR EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105988; AAI05989.1; -; mRNA.
DR CCDS; CCDS42276.1; -. [A6ND36-1]
DR RefSeq; NP_001035088.2; NM_001039999.2. [A6ND36-1]
DR RefSeq; XP_016880442.1; XM_017024953.1. [A6ND36-1]
DR AlphaFoldDB; A6ND36; -.
DR SMR; A6ND36; -.
DR BioGRID; 569917; 21.
DR IntAct; A6ND36; 12.
DR STRING; 9606.ENSP00000373647; -.
DR iPTMnet; A6ND36; -.
DR PhosphoSitePlus; A6ND36; -.
DR BioMuta; FAM83G; -.
DR EPD; A6ND36; -.
DR jPOST; A6ND36; -.
DR MassIVE; A6ND36; -.
DR MaxQB; A6ND36; -.
DR PaxDb; A6ND36; -.
DR PeptideAtlas; A6ND36; -.
DR PRIDE; A6ND36; -.
DR ProteomicsDB; 879; -. [A6ND36-1]
DR ProteomicsDB; 880; -. [A6ND36-2]
DR Antibodypedia; 6816; 102 antibodies from 19 providers.
DR DNASU; 644815; -.
DR Ensembl; ENST00000345041.4; ENSP00000343279.4; ENSG00000188522.15. [A6ND36-1]
DR Ensembl; ENST00000388995.11; ENSP00000373647.5; ENSG00000188522.15. [A6ND36-1]
DR GeneID; 644815; -.
DR KEGG; hsa:644815; -.
DR MANE-Select; ENST00000388995.11; ENSP00000373647.5; NM_001039999.3; NP_001035088.2.
DR UCSC; uc002guw.4; human. [A6ND36-1]
DR CTD; 644815; -.
DR DisGeNET; 644815; -.
DR GeneCards; FAM83G; -.
DR HGNC; HGNC:32554; FAM83G.
DR HPA; ENSG00000188522; Tissue enhanced (esophagus, skin).
DR MIM; 615886; gene.
DR neXtProt; NX_A6ND36; -.
DR OpenTargets; ENSG00000188522; -.
DR PharmGKB; PA144596433; -.
DR VEuPathDB; HostDB:ENSG00000188522; -.
DR eggNOG; ENOG502QS42; Eukaryota.
DR GeneTree; ENSGT00940000157932; -.
DR HOGENOM; CLU_019056_1_0_1; -.
DR InParanoid; A6ND36; -.
DR OMA; HSEQMAN; -.
DR OrthoDB; 354494at2759; -.
DR PhylomeDB; A6ND36; -.
DR TreeFam; TF330777; -.
DR PathwayCommons; A6ND36; -.
DR SignaLink; A6ND36; -.
DR SIGNOR; A6ND36; -.
DR BioGRID-ORCS; 644815; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; FAM83G; human.
DR GenomeRNAi; 644815; -.
DR Pharos; A6ND36; Tbio.
DR PRO; PR:A6ND36; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; A6ND36; protein.
DR Bgee; ENSG00000188522; Expressed in upper arm skin and 136 other tissues.
DR ExpressionAtlas; A6ND36; baseline and differential.
DR Genevisible; A6ND36; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0030509; P:BMP 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 Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..823
FT /note="Protein FAM83G"
FT /id="PRO_0000330817"
FT REGION 75..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24554596"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24554596"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24554596"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033120"
FT VAR_SEQ 249..271
FT /note="KFKGALAQKFMFVDGDRAVCGSY -> MGARGLGGGSRVMCLTSAPSLCC
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033121"
FT VAR_SEQ 695..725
FT /note="GQQFHHHRVPASGTRDKDGFPGPPRYRSAAD -> VGQGPCTPGVTSPSLPA
FT TQELELLSSGLPCP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033122"
FT VAR_SEQ 726..823
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033123"
FT VARIANT 64
FT /note="L -> F (found in patient with Joubert syndrome;
FT unknown pathological significance; dbSNP:rs371100508)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075713"
FT VARIANT 109
FT /note="I -> T (in dbSNP:rs2074283)"
FT /id="VAR_053903"
FT VARIANT 630
FT /note="R -> W (found in patient with Joubert syndrome;
FT unknown pathological significance; dbSNP:rs201046878)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075714"
FT MUTAGEN 610
FT /note="S->A: Completely abolishes phosphorylation by ALK3
FT in vitro. NEDD9 and ASNS activation in response to BMPs is
FT abolished."
FT /evidence="ECO:0000269|PubMed:24554596"
SQ SEQUENCE 823 AA; 90835 MW; FAAF2B78CB76725F CRC64;
MAFSQVQCLD DNHVNWRSSE SKPEFFYSEE QRLALEALVA RGRDAFYEVL KRENIRDFLS
ELELKRILET IEVYDPGSED PRGTGPSQGP EDNGVGDGEE ASGADGVPIE AEPLPSLEYW
PQKSDRSIPQ LDLGWPDTIA YRGVTRASVY MQPPIDGQAH IKEVVRKMIS QAQKVIAVVM
DMFTDVDIFK DLLDAGFKRK VAVYIIVDES NVKYFLHMCE RACMHLGHLK NLRVRSSGGT
EFFTRSATKF KGALAQKFMF VDGDRAVCGS YSFTWSAART DRNVISVLSG QVVEMFDRQF
QELYLMSHSV SLKGIPMEKE PEPEPIVLPS VVPLVPAGTV AKKLVNPKYA LVKAKSVDEI
AKISSEKQEA KKPLGLKGPA LAEHPGELPE LLPPIHPGLL HLERANMFEY LPTWVEPDPE
PGSDILGYIN IIDPNIWNPQ PSQMNRIKIR DTSQASAQHQ LWKQSQDSRP RPEPCPPPEP
SAPQDGVPAE NGLPQGDPEP LPPVPKPRTV PVADVLARDS SDIGWVLELP KEEAPQNGTD
HRLPRMAGPG HAPLQRQLSV TQDDPESLGV GLPNGLDGVE EEDDDDYVTL SDQDSHSGSS
GRGPGPRRPS VASSVSEEYF EVREHSVPLR RRHSEQVANG PTPPPRRQLS APHITRGTFV
GPQGGSPWAQ SRGREEADAL KRMQAQRSTD KEAQGQQFHH HRVPASGTRD KDGFPGPPRY
RSAADSVQSS TRNAGPAMAG PHHWQAKGGQ VPRLLPDPGS PRLAQNARPM TDGRATEEHP
SPFGIPYSKL SQSKHLKART GGSQWASSDS KRRAQAPRDR KDP
