FA83D_MOUSE
ID FA83D_MOUSE Reviewed; 585 AA.
AC Q9D7I8; A2AC91; Q3TXE0; Q6P396; Q8BYC0;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein FAM83D {ECO:0000305};
GN Name=Fam83d {ECO:0000312|MGI:MGI:1919128};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, Thymus, and Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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.
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 (By
CC similarity). May play also a role in cell proliferation through
CC activation of the ERK1/ERK2 signaling cascade (By similarity). May also
CC be important for proper chromosome congression and alignment during
CC mitosis through its interaction with KIF22 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4H8}.
CC -!- SUBUNIT: Interacts with FBXW7; promotes FBXW7 degradation (By
CC similarity). May interact with RAF1 (By similarity). Interacts with
CC KIF22; recruits KIF22 to mitotic spindle microtubules (By similarity).
CC Interacts (via C-terminus) with DYNLL1 (By similarity). Interacts with
CC HMMR (By similarity). Interacts (via N-terminus) with CSNK1A1/CK1a; in
CC mitotic cells (By similarity). {ECO:0000250|UniProtKB:Q9H4H8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H4H8}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9H4H8}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9H4H8}.
CC Note=Primarily cytoplasmic during interphase, but at prophase,
CC associates with spindle microtubules, with a clear concentration toward
CC the spindle poles. It persists on spindle microtubules through
CC metaphase and anaphase. {ECO:0000250|UniProtKB:Q9H4H8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9D7I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D7I8-2; Sequence=VSP_036447;
CC Name=3;
CC IsoId=Q9D7I8-3; Sequence=VSP_039768;
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:31338967}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; AK009199; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK040615; BAC30645.1; -; mRNA.
DR EMBL; AK156048; BAE33562.1; -; mRNA.
DR EMBL; AK159308; BAE34976.1; -; mRNA.
DR EMBL; AL663077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064129; AAH64129.1; -; mRNA.
DR EMBL; BC068129; AAH68129.1; -; mRNA.
DR CCDS; CCDS50788.1; -. [Q9D7I8-1]
DR RefSeq; NP_082251.2; NM_027975.2. [Q9D7I8-1]
DR RefSeq; XP_006500260.1; XM_006500197.1. [Q9D7I8-2]
DR AlphaFoldDB; Q9D7I8; -.
DR SMR; Q9D7I8; -.
DR BioGRID; 215001; 13.
DR IntAct; Q9D7I8; 13.
DR STRING; 10090.ENSMUSP00000029183; -.
DR iPTMnet; Q9D7I8; -.
DR PhosphoSitePlus; Q9D7I8; -.
DR EPD; Q9D7I8; -.
DR MaxQB; Q9D7I8; -.
DR PaxDb; Q9D7I8; -.
DR PeptideAtlas; Q9D7I8; -.
DR PRIDE; Q9D7I8; -.
DR ProteomicsDB; 267698; -. [Q9D7I8-1]
DR ProteomicsDB; 267699; -. [Q9D7I8-2]
DR ProteomicsDB; 267700; -. [Q9D7I8-3]
DR Antibodypedia; 57303; 83 antibodies from 17 providers.
DR Ensembl; ENSMUST00000029183; ENSMUSP00000029183; ENSMUSG00000027654. [Q9D7I8-1]
DR GeneID; 71878; -.
DR KEGG; mmu:71878; -.
DR UCSC; uc008nqq.2; mouse. [Q9D7I8-1]
DR CTD; 81610; -.
DR MGI; MGI:1919128; Fam83d.
DR VEuPathDB; HostDB:ENSMUSG00000027654; -.
DR eggNOG; ENOG502RC3Z; Eukaryota.
DR GeneTree; ENSGT00940000158405; -.
DR HOGENOM; CLU_040298_0_0_1; -.
DR InParanoid; Q9D7I8; -.
DR OMA; HFLDMCM; -.
DR OrthoDB; 433035at2759; -.
DR PhylomeDB; Q9D7I8; -.
DR TreeFam; TF330777; -.
DR BioGRID-ORCS; 71878; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9D7I8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7I8; protein.
DR Bgee; ENSMUSG00000027654; Expressed in dorsal pancreas and 136 other tissues.
DR Genevisible; Q9D7I8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:1902480; P:protein localization to mitotic spindle; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0032006; P:regulation of TOR signaling; ISS: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 Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Mitosis; Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..585
FT /note="Protein FAM83D"
FT /id="PRO_0000079461"
FT REGION 334..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..585
FT /note="Required for interaction with KIF22 and function in
FT chromosome congression"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT REGION 425..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT VAR_SEQ 1..328
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039768"
FT VAR_SEQ 1..215
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036447"
FT CONFLICT 255
FT /note="Y -> F (in Ref. 3; AAH64129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 64324 MW; E3528EDAAE13FBEF CRC64;
MAARFELLDD LPAACLSPCG PPNPTELFSE ARRLALEQLL AGGPDAWAAF LRRERLGRFL
NADEVREVLG AAERPGEDGA AVAEDSFGSS HECSSGTYFP EQSDLEPPAL ELGWPSFYQG
AYRGATRVEA HFQPRGAGAG GPYGCKDALR QQLRSAREVI AVVMDVFSDI DIFRDLQESC
RKRGVAVYIL LDQTLLPHFL DMCMDLRVHP EQEKLMTVRT ITGNIYYARS GTKVVGKVHE
KFTLIDGIRV ATGSYSFTWT DGKLNSSNLV ILSGQVVEHF DLEFRILYAQ SEPISSKLLS
NFQINSKFDH LADRKPQSKE PTLGNLLRMR LARLSSTPRK SNLGPEEPPK DRAKPKRPDS
EASTISDEDY FHSHKDQLED SKVADAATQT EPREEMAAVS LSEVGTQTSS SMMCVGTQTT
VVTRAASSQA TVWSKSTTTQ TEADESFLPQ GAQSKEGSPA SKMSVSRSSS VRSSSSVSSQ
GSLASSVSSH VSLTAADLHT PAYPKYLGLG TPHLDLCLRD SFRNLSKERQ VHFTGIRSRL
TQMLTVLSRR TLFTEHYLSY SPGSFTRAST NLVSVRDIAL YPPYQ
