FA83H_HUMAN
ID FA83H_HUMAN Reviewed; 1179 AA.
AC Q6ZRV2; A0JLS2; Q8N4W0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein FAM83H {ECO:0000305};
GN Name=FAM83H {ECO:0000312|HGNC:HGNC:24797};
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1179.
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1179.
RC TISSUE=Placenta, and Prostate;
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-1003, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN AI3A.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-647; SER-785 AND
RP SER-1003, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-881; THR-883;
RP SER-892; SER-903; SER-936; SER-945; SER-1003; SER-1024 AND SER-1025, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-914 AND SER-1003,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465; SER-523; SER-647;
RP SER-759; SER-785; SER-870; SER-881; SER-892; SER-903; SER-914; SER-936;
RP SER-945; SER-1003; THR-1040 AND SER-1048, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, INTERACTION WITH CSNK1A1 AND KRT18, SUBCELLULAR LOCATION, REGION,
RP AND MUTAGENESIS OF PHE-251 AND PHE-274.
RX PubMed=23902688; DOI=10.1242/jcs.129684;
RA Kuga T., Kume H., Kawasaki N., Sato M., Adachi J., Shiromizu T.,
RA Hoshino I., Nishimori T., Matsubara H., Tomonaga T.;
RT "A novel mechanism of keratin cytoskeleton organization through casein
RT kinase Ialpha and FAM83H in colorectal cancer.";
RL J. Cell Sci. 126:4721-4731(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-514; SER-516;
RP SER-523; SER-647; SER-667; SER-785; SER-870; SER-881; SER-892; SER-903;
RP SER-914; SER-925; SER-936; SER-1003; SER-1025 AND SER-1147, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; THR-756; SER-813;
RP SER-914; SER-1003 AND SER-1068, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP VARIANT AI3A CYS-557.
RX PubMed=26142250; DOI=10.1016/j.archoralbio.2015.06.016;
RA Urzua B., Martinez C., Ortega-Pinto A., Adorno D., Morales-Bozo I.,
RA Riadi G., Jara L., Plaza A., Lefimil C., Lozano C., Reyes M.;
RT "Novel missense mutation of the FAM83H gene causes retention of amelogenin
RT and a mild clinical phenotype of hypocalcified enamel.";
RL Arch. Oral Biol. 60:1356-1367(2015).
CC -!- FUNCTION: May play a major role in the structural organization and
CC calcification of developing enamel (PubMed:18252228). May play a role
CC in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin
CC filaments. Thereby, it may regulate epithelial cell migration
CC (PubMed:23902688). {ECO:0000269|PubMed:18252228,
CC ECO:0000269|PubMed:23902688}.
CC -!- SUBUNIT: Interacts with CSNK1A1; recruits CSNK1A1 to keratin filaments.
CC Interacts with KRT18 and probably other keratins.
CC {ECO:0000269|PubMed:23902688}.
CC -!- INTERACTION:
CC Q6ZRV2; P48729: CSNK1A1; NbExp=11; IntAct=EBI-2556538, EBI-1383726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23902688}. Note=Colocalizes with keratin filaments.
CC {ECO:0000269|PubMed:23902688}.
CC -!- TISSUE SPECIFICITY: Expressed in the tooth follicle.
CC {ECO:0000269|PubMed:18252228}.
CC -!- DISEASE: Amelogenesis imperfecta 3A (AI3A) [MIM:130900]: An autosomal
CC dominant hypomineralized form of amelogenesis imperfecta, a defect of
CC enamel formation. AI3A is characterized by enamel of normal thickness
CC but soft and with cheesy consistency. Enamel is lost from tooth soon
CC after eruption. {ECO:0000269|PubMed:18252228,
CC ECO:0000269|PubMed:26142250}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87207.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC105219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK127960; BAC87207.1; ALT_INIT; mRNA.
DR EMBL; BC007264; AAH07264.1; -; mRNA.
DR EMBL; BC033256; AAH33256.1; -; mRNA.
DR CCDS; CCDS6410.2; -.
DR RefSeq; NP_940890.3; NM_198488.3.
DR RefSeq; XP_005250946.1; XM_005250889.3.
DR AlphaFoldDB; Q6ZRV2; -.
DR SMR; Q6ZRV2; -.
DR BioGRID; 130292; 148.
DR IntAct; Q6ZRV2; 63.
DR MINT; Q6ZRV2; -.
DR STRING; 9606.ENSP00000373565; -.
DR iPTMnet; Q6ZRV2; -.
DR PhosphoSitePlus; Q6ZRV2; -.
DR SwissPalm; Q6ZRV2; -.
DR BioMuta; FAM83H; -.
DR DMDM; 296439349; -.
DR CPTAC; CPTAC-367; -.
DR CPTAC; CPTAC-368; -.
DR EPD; Q6ZRV2; -.
DR jPOST; Q6ZRV2; -.
DR MassIVE; Q6ZRV2; -.
DR MaxQB; Q6ZRV2; -.
DR PaxDb; Q6ZRV2; -.
DR PeptideAtlas; Q6ZRV2; -.
DR PRIDE; Q6ZRV2; -.
DR ProteomicsDB; 68170; -.
DR Antibodypedia; 14675; 44 antibodies from 12 providers.
DR DNASU; 286077; -.
DR Ensembl; ENST00000388913.4; ENSP00000373565.3; ENSG00000180921.7.
DR Ensembl; ENST00000612192.2; ENSP00000478790.1; ENSG00000273889.2.
DR GeneID; 286077; -.
DR KEGG; hsa:286077; -.
DR MANE-Select; ENST00000388913.4; ENSP00000373565.3; NM_198488.5; NP_940890.4.
DR UCSC; uc064rej.1; human.
DR CTD; 286077; -.
DR DisGeNET; 286077; -.
DR GeneCards; FAM83H; -.
DR HGNC; HGNC:24797; FAM83H.
DR HPA; ENSG00000180921; Tissue enhanced (esophagus, skin).
DR MalaCards; FAM83H; -.
DR MIM; 130900; phenotype.
DR MIM; 611927; gene.
DR neXtProt; NX_Q6ZRV2; -.
DR OpenTargets; ENSG00000180921; -.
DR Orphanet; 100032; Hypocalcified amelogenesis imperfecta.
DR PharmGKB; PA144596434; -.
DR VEuPathDB; HostDB:ENSG00000180921; -.
DR eggNOG; ENOG502QW7K; Eukaryota.
DR GeneTree; ENSGT00940000159342; -.
DR HOGENOM; CLU_009734_0_0_1; -.
DR InParanoid; Q6ZRV2; -.
DR OMA; MESEAYN; -.
DR OrthoDB; 84242at2759; -.
DR PhylomeDB; Q6ZRV2; -.
DR TreeFam; TF330777; -.
DR PathwayCommons; Q6ZRV2; -.
DR SignaLink; Q6ZRV2; -.
DR BioGRID-ORCS; 286077; 42 hits in 1079 CRISPR screens.
DR GeneWiki; FAM83H; -.
DR GenomeRNAi; 286077; -.
DR Pharos; Q6ZRV2; Tbio.
DR PRO; PR:Q6ZRV2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6ZRV2; protein.
DR Bgee; ENSG00000180921; Expressed in lower esophagus mucosa and 93 other tissues.
DR ExpressionAtlas; Q6ZRV2; baseline and differential.
DR Genevisible; Q6ZRV2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:1990254; F:keratin filament binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0044380; P:protein localization to cytoskeleton; IMP: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 Amelogenesis imperfecta; Biomineralization; Cytoplasm; Cytoskeleton;
KW Disease variant; Phosphoprotein; Reference proteome.
FT CHAIN 1..1179
FT /note="Protein FAM83H"
FT /id="PRO_0000324488"
FT REGION 1..286
FT /note="Mediates interaction with CSNK1A1 and is required
FT for FAM83H activity in keratin cytoskeleton organization"
FT /evidence="ECO:0000269|PubMed:23902688"
FT REGION 484..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 756
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 883
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q148V8"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q148V8"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1040
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 201
FT /note="Q -> H (in dbSNP:rs9969600)"
FT /id="VAR_062189"
FT VARIANT 557
FT /note="G -> C (in AI3A; mild form; dbSNP:rs312262803)"
FT /evidence="ECO:0000269|PubMed:26142250"
FT /id="VAR_073954"
FT MUTAGEN 251
FT /note="F->A: No effect on interaction with CSNK1A1 and
FT function in keratin cytoskeleton organization."
FT /evidence="ECO:0000269|PubMed:23902688"
FT MUTAGEN 274
FT /note="F->A: Decreased interaction with CSNK1A1 and loss of
FT function in keratin cytoskeleton organization."
FT /evidence="ECO:0000269|PubMed:23902688"
FT CONFLICT 605
FT /note="E -> V (in Ref. 2; BAC87207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1179 AA; 127122 MW; D35A1822D8E517F0 CRC64;
MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALAEGGS EAYSRFLATE GAPDFLCPEE
LEHVSRHLRP PQYVTREPPE GSLLDVDMDG SSGTYWPVNS DQAVPELDLG WPLTFGFQGT
EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV VAVVMDMFTD VDLLSEVLEA AARRVPVYIL
LDEMNAQHFL DMADKCRVNL QHVDFLRVRT VAGPTYYCRT GKSFKGHVKE KFLLVDCAVV
MSGSYSFMWS FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAAA LARMDAYALA
PYAGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF LSAFRREEPP
RMPGGALEPH AGLRPLSRRL EAEAGPAGEL AGARGFFQAR HLEMDAFKRH SFATEGAGAV
ENFAAARQVS RQTFLSHGDD FRFQTSHFHR DQLYQQQYQW DPQLTPARPQ GLFEKLRGGR
AGFADPDDFT LGAGPRFPEL GPDGHQRLDY VPSSASREVR HGSDPAFAPG PRGLEPSGAP
RPNLTQRFPC QAAARPGPDP APEAEPERRG GPEGRAGLRR WRLASYLSGC HGEDGGDDGL
PAPMEAEAYE DDVLAPGGRA PAGDLLPSAF RVPAAFPTKV PVPGPGSGGN GPEREGPEEP
GLAKQDSFRS RLNPLVQRSS RLRSSLIFST SQAEGAAGAA AATEKVQLLH KEQTVSETLG
PGGEAVRSAA STKVAELLEK YKGPARDPGG GAGAITVASH SKAVVSQAWR EEVAAPGAVG
GERRSLESCL LDLRDSFAQQ LHQEAERQPG AASLTAAQLL DTLGRSGSDR LPSRFLSAQS
HSTSPQGLDS PLPLEGSGAH QVLHNESKGS PTSAYPERKG SPTPGFSTRR GSPTTGFIEQ
KGSPTSAYPE RRGSPVPPVP ERRSSPVPPV PERRGSLTLT ISGESPKAGP AEEGPSGPME
VLRKGSLRLR QLLSPKGERR MEDEGGFPVP QENGQPESPR RLSLGQGDST EAATEERGPR
ARLSSATANA LYSSNLRDDT KAILEQISAH GQKHRAVPAP SPGPTHNSPE LGRPPAAGVL
APDMSDKDKC SAIFRSDSLG TQGRLSRTLP ASAEERDRLL RRMESMRKEK RVYSRFEVFC
KKEEASSPGA GEGPAEEGTR DSKVGKFVPK ILGTFKSKK
