FRY_HUMAN
ID FRY_HUMAN Reviewed; 3013 AA.
AC Q5TBA9; Q9Y3N6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein furry homolog;
GN Name=FRY; Synonyms=C13orf14;
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].
RA Rhodes S.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1936, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [5]
RP FUNCTION, INTERACTION WITH PLK1, AND SUBCELLULAR LOCATION.
RX PubMed=22753416; DOI=10.1074/jbc.m112.378968;
RA Ikeda M., Chiba S., Ohashi K., Mizuno K.;
RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation.";
RL J. Biol. Chem. 287:27670-27681(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Plays a crucial role in the structural integrity of mitotic
CC centrosomes and in the maintenance of spindle bipolarity by promoting
CC PLK1 activity at the spindle poles in early mitosis. May function as a
CC scaffold promoting the interaction between AURKA and PLK1, thereby
CC enhancing AURKA-mediated PLK1 phosphorylation.
CC {ECO:0000269|PubMed:22753416}.
CC -!- SUBUNIT: When phosphorylated by CDK1, interacts with PLK1; this
CC interaction occurs in mitotic cells, but not in interphase cells, and
CC leads to further phosphorylation by PLK1. Interacts with AURKA.
CC {ECO:0000269|PubMed:22753416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22753416}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:22753416}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:22753416}. Note=Distributed diffusely throughout
CC the cytoplasm in interphase. Localizes to the separating centrosomes in
CC prophase, to the spindle poles and spindle microtubules in prometaphase
CC to metaphase, to spindle microtubules in anaphase and to the distal
CC sections of the midbody in cytokinesis. Colocalizes with PLK1 to
CC separating centrosomes and spindle poles from prophase to metaphase in
CC mitosis, but not in other stages of the cell cycle.
CC -!- PTM: Phosphorylated by AURKA, CDK1 and PLK1.
CC -!- SIMILARITY: Belongs to the furry protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB42442.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL049784; CAB42442.1; ALT_FRAME; mRNA.
DR EMBL; AL137143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41875.1; -.
DR RefSeq; NP_075463.2; NM_023037.2.
DR BioGRID; 115433; 10.
DR IntAct; Q5TBA9; 9.
DR MINT; Q5TBA9; -.
DR STRING; 9606.ENSP00000445043; -.
DR iPTMnet; Q5TBA9; -.
DR PhosphoSitePlus; Q5TBA9; -.
DR BioMuta; FRY; -.
DR DMDM; 74745928; -.
DR EPD; Q5TBA9; -.
DR jPOST; Q5TBA9; -.
DR MassIVE; Q5TBA9; -.
DR MaxQB; Q5TBA9; -.
DR PaxDb; Q5TBA9; -.
DR PeptideAtlas; Q5TBA9; -.
DR PRIDE; Q5TBA9; -.
DR ProteomicsDB; 64893; -.
DR Antibodypedia; 63056; 40 antibodies from 8 providers.
DR DNASU; 10129; -.
DR Ensembl; ENST00000542859.6; ENSP00000445043.2; ENSG00000073910.23.
DR GeneID; 10129; -.
DR KEGG; hsa:10129; -.
DR MANE-Select; ENST00000542859.6; ENSP00000445043.2; NM_023037.3; NP_075463.2.
DR UCSC; uc001utx.4; human.
DR CTD; 10129; -.
DR DisGeNET; 10129; -.
DR GeneCards; FRY; -.
DR HGNC; HGNC:20367; FRY.
DR HPA; ENSG00000073910; Tissue enhanced (heart).
DR MIM; 614818; gene.
DR neXtProt; NX_Q5TBA9; -.
DR OpenTargets; ENSG00000073910; -.
DR PharmGKB; PA134927490; -.
DR VEuPathDB; HostDB:ENSG00000073910; -.
DR eggNOG; KOG1825; Eukaryota.
DR GeneTree; ENSGT00610000086058; -.
DR HOGENOM; CLU_000483_0_0_1; -.
DR InParanoid; Q5TBA9; -.
DR OrthoDB; 11874at2759; -.
DR PhylomeDB; Q5TBA9; -.
DR TreeFam; TF313568; -.
DR PathwayCommons; Q5TBA9; -.
DR SignaLink; Q5TBA9; -.
DR BioGRID-ORCS; 10129; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; FRY; human.
DR GenomeRNAi; 10129; -.
DR Pharos; Q5TBA9; Tbio.
DR PRO; PR:Q5TBA9; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5TBA9; protein.
DR Bgee; ENSG00000073910; Expressed in blood vessel layer and 205 other tissues.
DR ExpressionAtlas; Q5TBA9; baseline and differential.
DR Genevisible; Q5TBA9; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR025614; Cell_morpho_N.
DR InterPro; IPR025481; Cell_Morphogen_C.
DR InterPro; IPR045842; Fry_C.
DR InterPro; IPR039867; Furry/Tao3/Mor2.
DR InterPro; IPR029473; MOR2-PAG1_mid.
DR PANTHER; PTHR12295; PTHR12295; 1.
DR Pfam; PF19421; Fry_C; 1.
DR Pfam; PF14225; MOR2-PAG1_C; 1.
DR Pfam; PF14228; MOR2-PAG1_mid; 3.
DR Pfam; PF14222; MOR2-PAG1_N; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..3013
FT /note="Protein furry homolog"
FT /id="PRO_0000281674"
FT REGION 1378..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..1981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2347..2376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2501..2527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2361..2376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 1936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 1940
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 2419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 2420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 2487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 2508
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT MOD_RES 2808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q8I9"
FT VARIANT 1968
FT /note="G -> S (in dbSNP:rs2806639)"
FT /id="VAR_053831"
SQ SEQUENCE 3013 AA; 338875 MW; 2AB5EDB7D2529538 CRC64;
MASQQDSGFF EISIKYLLKS WSNTSPVGNG YIKPPVPPAS GTHREKGPPT MLPINVDPDS
KPGEYVLKSL FVNFTTQAER KIRIIMAEPL EKPLTKSLQR GEDPQFDQVI SSMSSLSEYC
LPSILRTLFD WYKRQNGIED ESHEYRPRTS NKSKSDEQQR DYLMERRDLA IDFIFSLVLI
EVLKQIPLHP VIDSLIHDVI NLAFKHFKYK EGYLGPNTGN MHIVADLYAE VIGVLAQAKF
PAVKKKFMAE LKELRHKEQN PYVVQSIISL IMGMKFFRIK MYPVEDFEAS LQFMQECAHY
FLEVKDKDIK HALAGLFVEI LVPVAAAVKN EVNVPCLRNF VESLYDTTLE LSSRKKHSLA
LYPLVTCLLC VSQKQLFLNR WHIFLNNCLS NLKNKDPKMA RVALESLYRL LWVYMIRIKC
ESNTATQSRL ITIITTLFPK GSRGVVPRDM PLNIFVKIIQ FIAQERLDFA MKEIIFDFLC
VGKPAKAFSL NPERMNIGLR AFLVIADSLQ QKDGEPPMPV TGAVLPSGNT LRVKKTYLSK
TLTEEEAKMI GMSLYYSQVR KAVDNILRHL DKEVGRCMML TNVQMLNKEP EDMITGERKP
KIDLFRTCVA AIPRLLPDGM SKLELIDLLA RLSIHMDDEL RHIAQNSLQG LLVDFSDWRE
DVLFGFTNFL LREVNDMHHT LLDSSLKLLL QLLTQWKLVI QTQGKVYEQA NKIRNSELIA
NGSSHRIQSE RGPHCSVLHA VEGFALVLLC SFQVATRKLS VLILKEIRAL FIALGQPEDD
DRPMIDVMDQ LSSSILESFI HVAVSDSATL PLTHNVDLQW LVEWNAVLVN SHYDVKSPSH
VWIFAQSVKD PWVLCLFSFL RQENLPKHCP TALSYAWPYA FTRLQSVMPL VDPNSPINAK
KTSTAGSGDN YVTLWRNYLI LCFGVAKPSI MSPGHLRAST PEIMATTPDG TVSYDNKAIG
TPSVGVLLKQ LVPLMRLESI EITESLVLGF GRTNSLVFRE LVEELHPLMK EALERRPENK
KRRERRDLLR LQLLRIFELL ADAGVISDST NGALERDTLA LGALFLEYVD LTRMLLEAEN
DKEVEILKDI RAHFSAMVAN LIQCVPVHHR RFLFPQQSLR HHLFILFSQW AGPFSIMFTP
LDRYSDRNHQ ITRYQYCALK AMSAVLCCGP VFDNVGLSPD GYLYKWLDNI LACQDLRVHQ
LGCEVVVLLL ELNPDQINLF NWAIDRCYTG SYQLASGCFK AIATVCGSRN YPFDIVTLLN
LVLFKASDTN REIYEISMQL MQILEAKLFV YSKKVAEQRP GSILYGTHGP LPPLYSVSLA
LLSCELARMY PELTLPLFSE VSQRFPTTHP NGRQIMLTYL LPWLHNIELV DSRLLLPGSS
PSSPEDEVKD REGDVTASHG LRGNGWGSPE ATSLVLNNLM YMTAKYGDEV PGPEMENAWN
ALANNEKWSN NLRITLQFLI SLCGVSSDTV LLPYIKKVAI YLCRNNTIQT MEELLFELQQ
TEPVNPIVQH CDNPPFYRFT ASSKASAAAS GTTSSSNTVV AGQENFPDAE ENKILKESDE
RFSNVIRAHT RLESRYSNSS GGSYDEDKND PISPYTGWLL TITETKQPQP LPMPCTGGCW
APLVDYLPET ITPRGPLHRC NIAVIFMTEM VVDHSVREDW ALHLPLLLHA VFLGLDHYRP
EVFEHSKKLL LHLLIALSCN SNFHSIASVL LQTREMGEAK TLTVQPAYQP EYLYTGGFDF
LREDQSSPVP DSGLSSSSTS SSISLGGSSG NLPQMTQEVE DVDTAAETDE KANKLIEFLT
TRAFGPLWCH EDITPKNQNS KSAEQLTNFL RHVVSVFKDS KSGFHLEHQL SEVALQTALA
SSSRHYAGRS FQIFRALKQP LSAHALSDLL SRLVEVIGEH GDEIQGYVME ALLTLEAAVD
NLSDCLKNSD LLTVLSRSSS PDLSSSSKLT ASRKSTGQLN MNPGTTSGNT ATAERSRHQR
SFSVPKKFGV IDRSSDPPRS ATLDRIQACT QQGLSSKTRS SSSLKDSLTD PSHINHPTNL
LATIFWVTVA LMESDFEFEY LMALRLLSRL LAHMPLDKAE NREKLEKLQA QLKWADFSGL
QQLLLKGFTS LTTTDLTLQL FSLLTPVSKI SMVDASHAIG FPLNVLCLLP QLIQHFENPN
QFCKDIAERI AQVCLEEKNP KLSNLAHVMT LYKTHSYTRD CATWVNVVCR YLHEAYADIT
LNMVTYLAEL LEKGLPSVQQ PLLQVIYSLL SYMDLSVVPV KQFNVEVLKT IEKYVQSVHW
REALNILKLV VSRSASLVLP SYQHSDLSKI EIHRVWTSAS KELPGKTLDF HFDISETPII
GRRYDELQNS SGRDGKPRAM AVTRSTSSTS SGSNSNVLVP VSWKRPQYSQ KRTKEKLVHV
LSLCGQEVGL SKNPSVIFSS CGDLDLLEHQ TSLVSSEDGA REQENMDDTN SEQQFRVFRD
FDFLDVELED GEGESMDNFN WGVRRRSLDS LDKCDMQILE ERQLSGSTPS LNKMHHEDSD
ESSEEEDLTA SQILEHSDLI MTLSPSEETN PMELLTTACD STPAEPHSFN TRMSSFDASL
PDMNNLQISE GSKAEAVREE EDTTVHEDDL SSSINELPAA FECSDSFSLD MTEGEEKGNR
ALDQFTLASF GEGDRGVSPP PSPFFSAILA AFQPAACDDA EEAWRSHINQ LMCDSDGSCA
VYTFHVFSSL FKNIQKRFCF LTCDAASYLG DNLRGIGSKF VSSSQMLTSC SECPTLFVDA
ETLLSCGLLD KLKFSVLELQ EYLDTYNNRK EATLSWLANC KATFAGGSRD GVITCQPGDS
EEKQLELCQR LYKLHFQLLL LFQSYCKLIG QVHEVSSMPE LLNMSRELSD LKKHLKEASA
VIAADPLYSD GAWSEPTFTS TEAAIQSMLE CLKNNELGKA LRQIRECRSL WPNDIFGSSS
DDEVQTLLNI YFRHQTLGQT GTYALVGSNQ SLTEICTKLM ELNMEIRDMI RRAQSYRVLT
TFLPDSSVSG TSL
