FA83D_HUMAN
ID FA83D_HUMAN Reviewed; 585 AA.
AC Q9H4H8; B4E1I7; Q5THR2; Q68EN1; Q6P457; Q7Z6H0; Q96DF5; Q96N89; Q9BVM8;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein FAM83D {ECO:0000305};
DE AltName: Full=Spindle protein CHICA {ECO:0000305|PubMed:18485706};
GN Name=FAM83D {ECO:0000312|HGNC:HGNC:16122};
GN Synonyms=C20orf129 {ECO:0000312|HGNC:HGNC:16122};
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] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Trachea;
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Placenta, and Uterus;
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15561729; DOI=10.1074/mcp.m400158-mcp200;
RA Sauer G., Koerner R., Hanisch A., Ries A., Nigg E.A., Sillje H.H.W.;
RT "Proteome analysis of the human mitotic spindle.";
RL Mol. Cell. Proteomics 4:35-43(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF22, REGION,
RP PHOSPHORYLATION, AND INDUCTION.
RX PubMed=18485706; DOI=10.1016/j.cub.2008.04.041;
RA Santamaria A., Nagel S., Sillje H.H.W., Nigg E.A.;
RT "The spindle protein CHICA mediates localization of the chromokinesin Kid
RT to the mitotic spindle.";
RL Curr. Biol. 18:723-729(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513, AND IDENTIFICATION BY
RP MASS 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 INTERACTION WITH DYNLL1 AND HMMR, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 391-THR--THR-393; 409-THR--THR-411 AND 442-THR--THR-444.
RX PubMed=22965910; DOI=10.1083/jcb.201202112;
RA Dunsch A.K., Hammond D., Lloyd J., Schermelleh L., Gruneberg U., Barr F.A.;
RT "Dynein light chain 1 and a spindle-associated adaptor promote dynein
RT asymmetry and spindle orientation.";
RL J. Cell Biol. 198:1039-1054(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-568, 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 [12]
RP FUNCTION, INTERACTION WITH FBXW7, AND INVOLVEMENT IN BREAST CANCER.
RX PubMed=24344117; DOI=10.18632/oncotarget.1581;
RA Wang Z., Liu Y., Zhang P., Zhang W., Wang W., Curr K., Wei G., Mao J.H.;
RT "FAM83D promotes cell proliferation and motility by downregulating tumor
RT suppressor gene FBXW7.";
RL Oncotarget 4:2476-2486(2013).
RN [13]
RP INTERACTION WITH RAF1, AND INVOLVEMENT IN CANCER.
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 [14]
RP FUNCTION, AND INVOLVEMENT IN HEPATOCELLULAR CARCINOMA.
RX PubMed=25646692; DOI=10.1016/j.bbrc.2015.01.108;
RA Wang D., Han S., Peng R., Wang X., Yang X.X., Yang R.J., Jiao C.Y.,
RA Ding D., Ji G.W., Li X.C.;
RT "FAM83D activates the MEK/ERK signaling pathway and promotes cell
RT proliferation in hepatocellular carcinoma.";
RL Biochem. Biophys. Res. Commun. 458:313-320(2015).
RN [15]
RP INTERACTION WITH CSNK1A1.
RX PubMed=31338967; DOI=10.15252/embr.201847495;
RA Fulcher L.J., He Z., Mei L., Macartney T.J., Wood N.T., Prescott A.R.,
RA Whigham A.J., Varghese J., Gourlay R., Ball G., Clarke R., Campbell D.G.,
RA Maxwell C.A., Sapkota G.P.;
RT "FAM83D directs protein kinase CK1alpha to the mitotic spindle for proper
RT spindle positioning.";
RL EMBO Rep. 20:e47495-e47495(2019).
CC -!- FUNCTION: Through the degradation of FBXW7, may act indirectly on the
CC expression and downstream signaling of MTOR, JUN and MYC
CC (PubMed:24344117). May play also a role in cell proliferation through
CC activation of the ERK1/ERK2 signaling cascade (PubMed:25646692). May
CC also be important for proper chromosome congression and alignment
CC during mitosis through its interaction with KIF22 (PubMed:18485706).
CC {ECO:0000269|PubMed:18485706, ECO:0000269|PubMed:24344117,
CC ECO:0000269|PubMed:25646692}.
CC -!- SUBUNIT: Interacts with FBXW7; promotes FBXW7 degradation
CC (PubMed:24344117). May interact with RAF1 (PubMed:24736947). Interacts
CC with KIF22; recruits KIF22 to mitotic spindle microtubules
CC (PubMed:18485706). Interacts (via C-terminus) with DYNLL1
CC (PubMed:22965910). Interacts with HMMR (PubMed:22965910). Interacts
CC (via N-terminus) with CSNK1A1/CK1a; in mitotic cells (PubMed:31338967).
CC {ECO:0000269|PubMed:18485706, ECO:0000269|PubMed:22965910,
CC ECO:0000269|PubMed:24344117, ECO:0000269|PubMed:24736947,
CC ECO:0000269|PubMed:31338967}.
CC -!- INTERACTION:
CC Q9H4H8; P48729: CSNK1A1; NbExp=5; IntAct=EBI-2556127, EBI-1383726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18445686}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15561729,
CC ECO:0000269|PubMed:18485706}. Note=Primarily cytoplasmic during
CC interphase, but at prophase, associates with spindle microtubules, with
CC a clear concentration toward the spindle poles. It persists on spindle
CC microtubules through metaphase and anaphase.
CC {ECO:0000269|PubMed:18485706}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H4H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H4H8-2; Sequence=VSP_036446;
CC -!- TISSUE SPECIFICITY: Expressed in the testis.
CC {ECO:0000269|PubMed:22965910}.
CC -!- INDUCTION: Up-regulated during mitosis. {ECO:0000269|PubMed:18485706}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:18485706}.
CC -!- DISEASE: Note=Probable proto-oncogene that regulates cell
CC proliferation, growth, migration and epithelial to mesenchymal
CC transition (PubMed:24344117, PubMed:24736947, PubMed:25646692).
CC Expression increased in hepatocellular carcinoma, promotes
CC proliferation and cell colony formation via activation of MEK/ERK
CC signaling (PubMed:25646692). Expression increased in breast cancer; may
CC be a prognostic indicator of poor disease-free survival
CC (PubMed:24344117). {ECO:0000269|PubMed:24344117,
CC ECO:0000269|PubMed:24736947, ECO:0000269|PubMed:25646692}.
CC -!- MISCELLANEOUS: Was named CHICA (girl in Spanish) because it interacts
CC with KID.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01068.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH06553.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH53683.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH63661.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH80188.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71016.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71016.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK055793; BAB71016.1; ALT_SEQ; mRNA.
DR EMBL; AK303860; BAG64799.1; -; mRNA.
DR EMBL; AL023803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001068; AAH01068.2; ALT_INIT; mRNA.
DR EMBL; BC006553; AAH06553.3; ALT_INIT; mRNA.
DR EMBL; BC053683; AAH53683.1; ALT_INIT; mRNA.
DR EMBL; BC063661; AAH63661.1; ALT_INIT; mRNA.
DR EMBL; BC080188; AAH80188.1; ALT_INIT; mRNA.
DR CCDS; CCDS42872.2; -. [Q9H4H8-1]
DR RefSeq; NP_112181.3; NM_030919.2. [Q9H4H8-1]
DR PDB; 5E0L; X-ray; 1.31 A; C=384-394.
DR PDB; 5E0M; X-ray; 1.65 A; C=436-446.
DR PDBsum; 5E0L; -.
DR PDBsum; 5E0M; -.
DR AlphaFoldDB; Q9H4H8; -.
DR SMR; Q9H4H8; -.
DR BioGRID; 123547; 92.
DR IntAct; Q9H4H8; 32.
DR MINT; Q9H4H8; -.
DR STRING; 9606.ENSP00000481110; -.
DR iPTMnet; Q9H4H8; -.
DR PhosphoSitePlus; Q9H4H8; -.
DR BioMuta; FAM83D; -.
DR DMDM; 25452904; -.
DR EPD; Q9H4H8; -.
DR jPOST; Q9H4H8; -.
DR MassIVE; Q9H4H8; -.
DR MaxQB; Q9H4H8; -.
DR PaxDb; Q9H4H8; -.
DR PeptideAtlas; Q9H4H8; -.
DR PRIDE; Q9H4H8; -.
DR ProteomicsDB; 80838; -. [Q9H4H8-1]
DR ProteomicsDB; 80839; -. [Q9H4H8-2]
DR Antibodypedia; 57303; 83 antibodies from 17 providers.
DR DNASU; 81610; -.
DR Ensembl; ENST00000619850.2; ENSP00000481465.1; ENSG00000101447.15. [Q9H4H8-1]
DR GeneID; 81610; -.
DR KEGG; hsa:81610; -.
DR MANE-Select; ENST00000619850.2; ENSP00000481465.1; NM_030919.3; NP_112181.3.
DR UCSC; uc061wzh.1; human. [Q9H4H8-1]
DR CTD; 81610; -.
DR DisGeNET; 81610; -.
DR GeneCards; FAM83D; -.
DR HGNC; HGNC:16122; FAM83D.
DR HPA; ENSG00000101447; Tissue enhanced (esophagus, intestine, smooth muscle).
DR MIM; 618380; gene.
DR neXtProt; NX_Q9H4H8; -.
DR OpenTargets; ENSG00000101447; -.
DR PharmGKB; PA25670; -.
DR VEuPathDB; HostDB:ENSG00000101447; -.
DR eggNOG; ENOG502RC3Z; Eukaryota.
DR GeneTree; ENSGT00940000158405; -.
DR HOGENOM; CLU_040298_0_0_1; -.
DR InParanoid; Q9H4H8; -.
DR OMA; HFLDMCM; -.
DR OrthoDB; 433035at2759; -.
DR PhylomeDB; Q9H4H8; -.
DR TreeFam; TF330777; -.
DR PathwayCommons; Q9H4H8; -.
DR SignaLink; Q9H4H8; -.
DR BioGRID-ORCS; 81610; 37 hits in 1084 CRISPR screens.
DR ChiTaRS; FAM83D; human.
DR GenomeRNAi; 81610; -.
DR Pharos; Q9H4H8; Tbio.
DR PRO; PR:Q9H4H8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H4H8; protein.
DR Bgee; ENSG00000101447; Expressed in esophagus squamous epithelium and 138 other tissues.
DR ExpressionAtlas; Q9H4H8; baseline and differential.
DR Genevisible; Q9H4H8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; IMP:UniProtKB.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:1902480; P:protein localization to mitotic spindle; IMP:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; 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; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..585
FT /note="Protein FAM83D"
FT /id="PRO_0000079460"
FT REGION 338..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..585
FT /note="Required for interaction with KIF22 and function in
FT chromosome congression"
FT /evidence="ECO:0000269|PubMed:18485706"
FT REGION 439..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 123..138
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036446"
FT MUTAGEN 391..393
FT /note="TQT->AAA: Abolishes interaction with DYNLL1 and no
FT effect on interaction with HMMR; when associated with 409-
FT A--A-411 and 442-A--A-444."
FT /evidence="ECO:0000269|PubMed:22965910"
FT MUTAGEN 409..411
FT /note="TQT->AAA: Abolishes interaction with DYNLL1 and no
FT effect on interaction with HMMR; when associated with 391-
FT A--A-393 and 442-A--A-444."
FT /evidence="ECO:0000269|PubMed:22965910"
FT MUTAGEN 442..444
FT /note="TQT->AAA: Abolishes interaction with DYNLL1 and no
FT effect on interaction with HMMR; when associated with 391-
FT A--A-393 and 409-A--A-411."
FT /evidence="ECO:0000269|PubMed:22965910"
FT CONFLICT 11
FT /note="V -> L (in Ref. 3; AAH01068/AAH06553/AAH63661)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="G -> GA (in Ref. 3; AAH53683)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="H -> R (in Ref. 2; BAG64799)"
FT /evidence="ECO:0000305"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:5E0L"
SQ SEQUENCE 585 AA; 64424 MW; 9D1C86F0BFE47B10 CRC64;
MALLSEGLDE VPAACLSPCG PPNPTELFSE SRRLALEELV AGGPEAFAAF LRRERLARFL
NPDEVHAILR AAERPGEEGA AAAAAAEDSF GSSHDCSSGT YFPEQSDLEP PLLELGWPAF
YQGAYRGATR VETHFQPRGA GEGGPYGCKD ALRQQLRSAR EVIAVVMDVF TDIDIFRDLQ
EICRKQGVAV YILLDQALLS QFLDMCMDLK VHPEQEKLMT VRTITGNIYY ARSGTKIIGK
VHEKFTLIDG IRVATGSYSF TWTDGKLNSS NLVILSGQVV EHFDLEFRIL YAQSKPISPK
LLSHFQSSNK FDHLTNRKPQ SKELTLGNLL RMRLARLSST PRKADLDPEM PAEGKAERKP
HDCESSTVSE EDYFSSHRDE LQSRKAIDAA TQTEPGEEMP GLSVSEVGTQ TSITTACAGT
QTAVITRIAS SQTTIWSRST TTQTDMDENI LFPRGTQSTE GSPVSKMSVS RSSSLKSSSS
VSSQGSVASS TGSPASIRTT DFHNPGYPKY LGTPHLELYL SDSLRNLNKE RQFHFAGIRS
RLNHMLAMLS RRTLFTENHL GLHSGNFSRV NLLAVRDVAL YPSYQ
