FA83D_BOVIN
ID FA83D_BOVIN Reviewed; 581 AA.
AC A3KN19;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Protein FAM83D {ECO:0000305};
GN Name=FAM83D {ECO:0000250|UniProtKB:Q9H4H8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9H4H8}.
CC -!- SIMILARITY: Belongs to the FAM83 family. {ECO:0000305}.
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DR EMBL; BC133491; AAI33492.1; -; mRNA.
DR RefSeq; NP_001076862.1; NM_001083393.1.
DR AlphaFoldDB; A3KN19; -.
DR SMR; A3KN19; -.
DR STRING; 9913.ENSBTAP00000000862; -.
DR PaxDb; A3KN19; -.
DR PRIDE; A3KN19; -.
DR GeneID; 508561; -.
DR KEGG; bta:508561; -.
DR CTD; 81610; -.
DR eggNOG; ENOG502RC3Z; Eukaryota.
DR InParanoid; A3KN19; -.
DR OrthoDB; 433035at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..581
FT /note="Protein FAM83D"
FT /id="PRO_0000365008"
FT REGION 75..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..581
FT /note="Required for interaction with KIF22 and function in
FT chromosome congression"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT REGION 366..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4H8"
SQ SEQUENCE 581 AA; 63396 MW; F170D36268D93A37 CRC64;
MALRYDGLDE LPAACLSPCG PPNPAELYSE ERRLALEELL AGGPGAFSAF LRRERLGRFL
NPDEVRSILR AAERPGEEGA AAGAEDSFGS SHDCSSGTYF PEQSDLEPPL LELGWPAFYQ
GAYRGATRVE AHFQPRGAGA GGPYGCKDAL RQQLRLAREV IAVVMDVFTD IDIFRDLQEI
SRKQGVAVYI LLDQALLSQF LDMCMDLKVH PEEEKLMTVR TITGNIYYAR SGTKIVGKVH
EKFTLIDGIR VATGSYSFTW TDGKLNSSNL VILSGQVVEH FDLEFRILYA QSKPISSKLL
SSFRISGRFD HLVDQKPLSK ELTLGNLLRL RLARLSSTPR KVELGGEEGR AEAVCGASKT
STISEEDYFS SRKDRLEGRR VTDAATQTEP GETPAVSMSD VGTQASAATA CTGTQTTVAT
RVVSSQTVVP TTSATTQTDV DEGVLASPGS QSKEGSPVSK MSVSRSSSLR SSSSLSSQGS
VASSIGSQTS FRSTDFATPG PPKYQSTPHF DLCFRDSLRN LNKERQFHFA GIRSRLNHML
AMLSRKTFLT ENYLSFNSGS FARSSANLLA VREIMLYPSY Q
