ID   FBX43_HUMAN             Reviewed;         708 AA.
AC   Q4G163;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=F-box only protein 43;
DE   AltName: Full=Endogenous meiotic inhibitor 2;
GN   Name=FBXO43; Synonyms=EMI2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   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.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=15520277; DOI=10.1101/gad.1255304;
RA   Jin J., Cardozo T., Lovering R.C., Elledge S.J., Pagano M.,
RA   Harper J.W.;
RT   "Systematic analysis and nomenclature of mammalian F-box proteins.";
RL   Genes Dev. 18:2573-2580(2004).
RN   [3]
RP   UBIQUITINATION, PHOSPHORYLATION AT SER-76 AND SER-334, AND MUTAGENESIS
RP   OF 75-ASP-SER-76 AND 333-ASP-SER-334.
RX   PubMed=15753281; DOI=10.1073/pnas.0501108102;
RA   Tung J.J., Hansen D.V., Ban K.H., Loktev A.V., Summers M.K.,
RA   Adler J.R. III, Jackson P.K.;
RT   "A role for the anaphase-promoting complex inhibitor Emi2/XErp1, a
RT   homolog of early mitotic inhibitor 1, in cytostatic factor arrest of
RT   Xenopus eggs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4318-4323(2005).
RN   [4]
RP   PHOSPHORYLATION AT THR-234.
RX   PubMed=16407128; DOI=10.1073/pnas.0509549102;
RA   Hansen D.V., Tung J.J., Jackson P.K.;
RT   "CaMKII and polo-like kinase 1 sequentially phosphorylate the
RT   cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic
RT   exit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:608-613(2006).
CC   -!- FUNCTION: Required to establish and maintain the arrest of oocytes
CC       at the second meiotic metaphase until fertilization. Probably acts
CC       by inhibiting the anaphase-promoting complex/cyclosome (APC/C)
CC       ubiquitin ligase. Probably recognizes and binds to some
CC       phosphorylated proteins and promotes their ubiquitination and
CC       degradation (Probable).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       May interact with CDC20 (By similarity).
CC   -!- PTM: Phosphorylated on Ser-76, Thr-234 and Ser-334 in reponse to
CC       calcium, which is a prerequisite for ubiquitination and
CC       proteasomal degradation (Probable).
CC   -!- PTM: Ubiquitinated in response to calcium, which promotes
CC       proteasomal degradation.
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC021590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00175439; -.
DR   RefSeq; NP_001025031.2; -.
DR   UniGene; Hs.339577; -.
DR   PhosphoSite; Q4G163; -.
DR   PRIDE; Q4G163; -.
DR   Ensembl; ENSG00000156509; Homo sapiens.
DR   GeneID; 286151; -.
DR   KEGG; hsa:286151; -.
DR   GeneCards; GC08M101214; -.
DR   HGNC; HGNC:28521; FBXO43.
DR   MIM; 609110; gene.
DR   PharmGKB; PA134913061; -.
DR   HOGENOM; Q4G163; -.
DR   HOVERGEN; Q4G163; -.
DR   NextBio; 96042; -.
DR   ArrayExpress; Q4G163; -.
DR   Bgee; Q4G163; -.
DR   CleanEx; HS_FBXO43; -.
DR   GermOnline; ENSG00000156509; Homo sapiens.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   InterPro; IPR001810; F-box.
DR   InterPro; IPR002867; Znf_C6HC.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF01485; IBR; 1.
DR   SMART; SM00647; IBR; 1.
DR   PROSITE; PS50181; FBOX; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Meiosis; Metal-binding; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    708       F-box only protein 43.
FT                                /FTId=PRO_0000247233.
FT   DOMAIN      490    547       F-box.
FT   ZN_FING     622    681       IBR-type.
FT   MOD_RES      76     76       Phosphoserine (Probable).
FT   MOD_RES     234    234       Phosphothreonine.
FT   MOD_RES     334    334       Phosphoserine (Probable).
FT   MOD_RES     503    503       Phosphotyrosine (By similarity).
FT   MUTAGEN      75     76       DS->AA: Impairs ubiquitination and
FT                                degradation in response to calcium.
FT   MUTAGEN     333    334       DS->AA: Impairs ubiquitination and
FT                                degradation in response to calcium.
SQ   SEQUENCE   708 AA;  78402 MW;  E42A358AE7BD29D1 CRC64;
     MSFKDKDERI SCLEAYVTLT SKSSRFTDET EILKMSQRHS GQAGTEAGNG ADSPPIVNSK
     YSTFRDFCST SSFQDSGYNE LKSCSFDNID KEYLGKKEKG PTLLYEHPET SGLGLTHPLE
     SPTQKKKCIL PRKEKDKTPE LCETPKISGK KCLPRRRLNV SFALLKGDFE SQNSSLESSI
     SQVINLEKNI PSSASGFSRA NNFSPLVTST LKTEEVTSCS QKLRLNFSQQ KTSTIDDSKD
     DCSLFEVECI SPIQGNNFKD SITHDFSDSS LCINDENACP ELLGSSVSGT TCGTDEDIFV
     TPISNLVANI RFNASQILSP SPEVRGSIST PEDSGFNSLS LEKSEDSLSD QEGSFQELLQ
     KHKGTPKVGD TIRKTRHLGR SRRLSTLREQ SSQSETEEEK QIVHPDSEKR AAAASAISEG
     QLSSDESGDL TFSLKNLSKT PALQLVHELF MKSKRKRLQE NSGHEFLEQG DGEKIAVLQC
     ILAGLIGKKM GIEKLDILTE LKYRNLKHIL AMVLESLTAE SLCSVWKVSR NWREIVVQDK
     NANRRRKFYI TQLKTDSEGA VLNVEDAATR LQLLNRSALR SVQAQARIPG SQREQGSTLS
     PWGEVLTPLA SSSVTHLSSK QEEYVKVAKT LFTDEALKPC PRCQSPAKYQ PYKKRGLCSR
     TACGFDFCVL CLCAYHGSEE CSRGAAKPRN RKDALPGSAQ SKRNLKRL
//