FA83H_MOUSE
ID FA83H_MOUSE Reviewed; 1209 AA.
AC Q148V8; Q8BZF6; Q8CI79; Q8R5C2; Q8R5D0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein FAM83H {ECO:0000305};
GN Name=Fam83h {ECO:0000312|MGI:MGI:2145900};
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; TISSUE=Urinary bladder;
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 MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18252228; DOI=10.1016/j.ajhg.2007.09.020;
RA Kim J.-W., Lee S.-K., Lee Z.H., Park J.-C., Lee K.-E., Lee M.-H.,
RA Park J.-T., Seo B.-M., Hu J.C.-C., Simmer J.P.;
RT "FAM83H mutations in families with autosomal-dominant hypocalcified
RT amelogenesis imperfecta.";
RL Am. J. Hum. Genet. 82:489-494(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-882 AND SER-893, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-904; SER-915;
RP SER-948; SER-959 AND SER-970, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-904; SER-915;
RP THR-917; SER-926; THR-928; SER-948; SER-959; SER-970 AND SER-1041, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Testis;
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).
CC -!- FUNCTION: May play a major role in the structural organization and
CC calcification of developing enamel. May play a role in keratin
CC cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments.
CC Thereby, it may regulate epithelial cell migration.
CC {ECO:0000250|UniProtKB:Q6ZRV2}.
CC -!- SUBUNIT: Interacts with CSNK1A1; recruits CSNK1A1 to keratin filaments.
CC Interacts with KRT18 and probably other keratins.
CC {ECO:0000250|UniProtKB:Q6ZRV2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q6ZRV2}. Note=Colocalizes with keratin
CC filaments. {ECO:0000250|UniProtKB:Q6ZRV2}.
CC -!- TISSUE SPECIFICITY: Expressed in tooth follicle, eye, liver and kidney.
CC {ECO:0000269|PubMed:18252228}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36149.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK035531; BAC29093.1; -; mRNA.
DR EMBL; BC022937; AAH22937.1; -; mRNA.
DR EMBL; BC023045; AAH23045.1; -; mRNA.
DR EMBL; BC036149; AAH36149.1; ALT_INIT; mRNA.
DR EMBL; BC117947; AAI17948.1; -; mRNA.
DR EMBL; BC117948; AAI17949.1; -; mRNA.
DR CCDS; CCDS27559.1; -.
DR RefSeq; NP_001161725.1; NM_001168253.1.
DR RefSeq; NP_598848.2; NM_134087.2.
DR RefSeq; XP_006520299.2; XM_006520236.3.
DR RefSeq; XP_006520300.1; XM_006520237.3.
DR AlphaFoldDB; Q148V8; -.
DR SMR; Q148V8; -.
DR BioGRID; 222906; 5.
DR IntAct; Q148V8; 3.
DR MINT; Q148V8; -.
DR STRING; 10090.ENSMUSP00000126453; -.
DR iPTMnet; Q148V8; -.
DR PhosphoSitePlus; Q148V8; -.
DR SwissPalm; Q148V8; -.
DR jPOST; Q148V8; -.
DR MaxQB; Q148V8; -.
DR PaxDb; Q148V8; -.
DR PeptideAtlas; Q148V8; -.
DR PRIDE; Q148V8; -.
DR ProteomicsDB; 275843; -.
DR Antibodypedia; 14675; 44 antibodies from 12 providers.
DR Ensembl; ENSMUST00000060807; ENSMUSP00000059839; ENSMUSG00000046761.
DR Ensembl; ENSMUST00000170153; ENSMUSP00000126453; ENSMUSG00000046761.
DR GeneID; 105732; -.
DR KEGG; mmu:105732; -.
DR UCSC; uc007wic.2; mouse.
DR CTD; 286077; -.
DR MGI; MGI:2145900; Fam83h.
DR VEuPathDB; HostDB:ENSMUSG00000046761; -.
DR eggNOG; ENOG502QW7K; Eukaryota.
DR GeneTree; ENSGT00940000159342; -.
DR HOGENOM; CLU_009734_0_0_1; -.
DR InParanoid; Q148V8; -.
DR OrthoDB; 84242at2759; -.
DR PhylomeDB; Q148V8; -.
DR TreeFam; TF330777; -.
DR BioGRID-ORCS; 105732; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Fam83h; mouse.
DR PRO; PR:Q148V8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q148V8; protein.
DR Bgee; ENSMUSG00000046761; Expressed in lip and 101 other tissues.
DR ExpressionAtlas; Q148V8; baseline and differential.
DR Genevisible; Q148V8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045095; C:keratin filament; ISO:MGI.
DR GO; GO:1990254; F:keratin filament binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0044380; P:protein localization to cytoskeleton; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09188; PLDc_FAM83H_N; 1.
DR InterPro; IPR012461; FAM83_N.
DR InterPro; IPR041996; PLDc_FAM83H_N.
DR Pfam; PF07894; FAM83; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1209
FT /note="Protein FAM83H"
FT /id="PRO_0000324489"
FT REGION 1..286
FT /note="Mediates interaction with CSNK1A1 and is required
FT for FAM83H activity in keratin cytoskeleton organization"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT REGION 512..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 749
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 873
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 917
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 928
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1072
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZRV2"
FT CONFLICT 873
FT /note="T -> A (in Ref. 1; BAC29093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1209 AA; 131115 MW; 1954B609EA75EF25 CRC64;
MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALTEGGP EAYNRFLASE GAPDFLCPEE
LEHVSRHLQP PQYVAREPPE GTPSDVDMDG SSGTYWPVNS DQAVPELDLG WPLTFGFQGT
EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV VAVVMDMFTD VDLLSEVLEA AARRVPVYIL
LDEMNAQHFL DMADKCRVNL HHVDFLRVRT VAGPTYYCRT GKSFKGHLKE KFLLVDCAVV
MSGSYSFMWS FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAGA LARMDAYALA
PYSGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF LSAFRREELQ
RMPGGALEPH TGLRPLARPT EAGPFGELAG PRGFFQSRHL EMDAFKRHSY ATPDGAGAVE
NFAAARQVSR QTFLSHGDDF RFQTSHFQRD QLYQQHYQWD PQFAPARPQG LFEKLRAGRP
GFADPDDFAL GAGHRFPELG ADVHQRLEYV PSSASREVRH GSDPAFGPSP RGLEPSGASR
PNLGQRFPCQ ATLRQGLDTA SEAEPERRGG PEGRAGLRHW RLASYLSGCH GDGGEEGLPM
EAEACEDEVL APGGRDLLPS AFRTPAAFPA KGPKPGSGSG GGDSSEREGP EETSLAKQDS
FRSRLNPLIQ RSSRLRSSLI FASQAEGAVG TAAATTEKVQ LMHKEQTVSE TLGPSGEAVR
SSASAKVAEL LEKYKGPARD PGGAGGAVTS SSHSKAVVSQ AWREEVVAPG GAGTERRSLE
SCLLDLRDSF AQQLHQEAER HPGAASLTAA QLLDTLGGTD RLPSRFLSAQ GRSLSPQGRD
SPPPEGLGTH QLPYSEPKGN PTPAYPERKG SPTPAYPERK GSPTPAYPER KGSPTPAYPE
RKGSPTQAYP ERKGSPTSGF PNRRGSPTTG LMEQKGSPTS TYPDRRGSPV PPVPERRGSP
VPPVPERRGS LTFAGESSKT GPTEEVSSGP MEVLRKGSLR LRQLLSPKNE RRGEDEGSFP
TPQENGQPES PRRPSLSRGD STEAAAEERG SRVRLASATA NALYSSNLRD DTKAILEQIS
AHGQKHRGVP APGPAHSSPD VGRPTTAGDL APDMSDKDKC SAIFRSDSLG TQGRLSRTLP
GSAEERDRLL RRMESMRKEK RVYSRFEVFC KKDEAGSSGA GDNLADEDTR DSKMGKFVPK
ILGTFKSKK
