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Protein fem-1 homolog B (FEM1b) (FEM1-beta) (Fem-1-like death receptor-binding protein alpha) (Fem-1-like in apoptotic pathway protein alpha) (F1A-alpha)

 FEM1B_HUMAN             Reviewed;         627 AA.
Q9UK73; O43146;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
26-FEB-2020, entry version 166.
RecName: Full=Protein fem-1 homolog B;
Short=FEM1b;
AltName: Full=FEM1-beta;
AltName: Full=Fem-1-like death receptor-binding protein alpha;
AltName: Full=Fem-1-like in apoptotic pathway protein alpha;
Short=F1A-alpha;
Name=FEM1B; Synonyms=F1AA, KIAA0396;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CLEAVAGE, TISSUE SPECIFICITY,
INTERACTION WITH FAS AND TNFRSF1A, AND MUTAGENESIS OF ASP-342 AND ASP-356.
PubMed=10542291; DOI=10.1074/jbc.274.45.32461;
Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.;
"F1Aalpha, a death receptor-binding protein homologous to the
Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase
substrate that mediates apoptosis.";
J. Biol. Chem. 274:32461-32468(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10623617; DOI=10.1006/bbrc.1999.1942;
Ventura-Holman T., Maher J.F.;
"Sequence, organization, and expression of the human FEM1B gene.";
Biochem. Biophys. Res. Commun. 267:317-320(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII. 78
new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 4:307-313(1997).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human chromosome
15.";
Nature 440:671-675(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PPM1F.
PubMed=11559703; DOI=10.1074/jbc.m105880200;
Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.;
"The Caenorhabditis elegans sex-determining protein fem-2 and its human
homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase
phosphatases that promote apoptosis.";
J. Biol. Chem. 276:44193-44202(2001).
[10]
IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH CUL2.
PubMed=15601820; DOI=10.1101/gad.1252404;
Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C.,
Conaway J.W., Nakayama K.I.;
"VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1
and Cul5-Rbx2 modules of ubiquitin ligases.";
Genes Dev. 18:3055-3065(2004).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEK1.
PubMed=19330022; DOI=10.1038/onc.2009.58;
Sun T.P., Shieh S.Y.;
"Human FEM1B is required for Rad9 recruitment and CHK1 activation in
response to replication stress.";
Oncogene 28:1971-1981(2009).
-!- FUNCTION: Component of an E3 ubiquitin-protein ligase complex, in which
it may act as a substrate recognition subunit. Involved in apoptosis by
acting as a death receptor-associated protein that mediates apoptosis.
Also involved in glucose homeostasis in pancreatic islet. Functions as
an adapter/mediator in replication stress-induced signaling that leads
to the activation of CHEK1. {ECO:0000269|PubMed:10542291,
ECO:0000269|PubMed:19330022}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homooligomer. Component of a probable ECS E3 ubiquitin-protein
ligase complex containing CUL2, RBX1, ELOB, ELOC and FEM1B. Interacts
with PPM1F and PHTF1. Interacts with the death domain of FAS/TNFRSF6
and TNFRSF1A. Interacts with CHEK1. {ECO:0000269|PubMed:10542291,
ECO:0000269|PubMed:11559703, ECO:0000269|PubMed:15601820,
ECO:0000269|PubMed:19330022}.
-!- INTERACTION:
Q9NWT6:HIF1AN; NbExp=3; IntAct=EBI-310482, EBI-745632;
P49593:PPM1F; NbExp=2; IntAct=EBI-310482, EBI-719945;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19330022}. Nucleus
{ECO:0000269|PubMed:19330022}. Note=In the nucleus, the protein level
increased slightly after camptothecin (CPT) treatment. Associated with
chromatin.
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis.
Weakly expressed in other tissues. {ECO:0000269|PubMed:10542291}.
-!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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EMBL; AF178632; AAF05314.1; -; mRNA.
EMBL; AF204883; AAF69303.1; -; mRNA.
EMBL; AB007856; BAA23692.2; -; mRNA.
EMBL; AK290167; BAF82856.1; -; mRNA.
EMBL; AC021553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77818.1; -; Genomic_DNA.
EMBL; BC010122; AAH10122.1; -; mRNA.
EMBL; BC014558; AAH14558.1; -; mRNA.
CCDS; CCDS10228.1; -.
RefSeq; NP_056137.1; NM_015322.4.
BioGrid; 115421; 62.
DIP; DIP-31663N; -.
IntAct; Q9UK73; 47.
MINT; Q9UK73; -.
STRING; 9606.ENSP00000307298; -.
iPTMnet; Q9UK73; -.
PhosphoSitePlus; Q9UK73; -.
BioMuta; FEM1B; -.
DMDM; 74753369; -.
EPD; Q9UK73; -.
jPOST; Q9UK73; -.
MassIVE; Q9UK73; -.
MaxQB; Q9UK73; -.
PaxDb; Q9UK73; -.
PeptideAtlas; Q9UK73; -.
PRIDE; Q9UK73; -.
ProteomicsDB; 84733; -.
DNASU; 10116; -.
Ensembl; ENST00000306917; ENSP00000307298; ENSG00000169018.
GeneID; 10116; -.
KEGG; hsa:10116; -.
UCSC; uc002arg.4; human.
CTD; 10116; -.
DisGeNET; 10116; -.
GeneCards; FEM1B; -.
HGNC; HGNC:3649; FEM1B.
HPA; HPA041920; -.
HPA; HPA042192; -.
MIM; 613539; gene.
neXtProt; NX_Q9UK73; -.
OpenTargets; ENSG00000169018; -.
PharmGKB; PA28089; -.
eggNOG; KOG0508; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000161115; -.
HOGENOM; CLU_020042_1_0_1; -.
InParanoid; Q9UK73; -.
KO; K10349; -.
OMA; MEGLMIR; -.
OrthoDB; 252380at2759; -.
PhylomeDB; Q9UK73; -.
TreeFam; TF351376; -.
Reactome; R-HSA-8951664; Neddylation.
UniPathway; UPA00143; -.
ChiTaRS; FEM1B; human.
GenomeRNAi; 10116; -.
Pharos; Q9UK73; Tbio.
PRO; PR:Q9UK73; -.
Proteomes; UP000005640; Chromosome 15.
RNAct; Q9UK73; protein.
Bgee; ENSG00000169018; Expressed in forebrain and 234 other tissues.
ExpressionAtlas; Q9UK73; baseline and differential.
Genevisible; Q9UK73; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005123; F:death receptor binding; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IEA:Ensembl.
GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 2.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 8.
SUPFAM; SSF48403; SSF48403; 2.
PROSITE; PS50297; ANK_REP_REGION; 2.
PROSITE; PS50088; ANK_REPEAT; 6.
1: Evidence at protein level;
ANK repeat; Apoptosis; Cytoplasm; Nucleus; Reference proteome; Repeat;
TPR repeat; Ubl conjugation pathway.
CHAIN 1..627
/note="Protein fem-1 homolog B"
/id="PRO_0000324530"
REPEAT 45..74
/note="ANK 1"
REPEAT 87..116
/note="ANK 2"
REPEAT 120..149
/note="ANK 3"
REPEAT 153..182
/note="ANK 4"
REPEAT 186..215
/note="ANK 5"
REPEAT 218..248
/note="ANK 6"
REPEAT 344..377
/note="TPR"
REPEAT 483..527
/note="ANK 7"
REPEAT 531..568
/note="ANK 8"
SITE 342..343
/note="Cleavage; by a caspase-3-like protease"
MUTAGEN 342
/note="D->A: Prevents cleavage by a caspase-3-like
protease."
/evidence="ECO:0000269|PubMed:10542291"
MUTAGEN 356
/note="D->A: Does not affect cleavage by a caspase-3-like
protease."
/evidence="ECO:0000269|PubMed:10542291"
SEQUENCE 627 AA; 70264 MW; 85DA943663A988C1 CRC64;
MEGLAGYVYK AASEGKVLTL AALLLNRSES DIRYLLGYVS QQGGQRSTPL IIAARNGHAK
VVRLLLEHYR VQTQQTGTVR FDGYVIDGAT ALWCAAGAGH FEVVKLLVSH GANVNHTTVT
NSTPLRAACF DGRLDIVKYL VENNANISIA NKYDNTCLMI AAYKGHTDVV RYLLEQRADP
NAKAHCGATA LHFAAEAGHI DIVKELIKWR AAIVVNGHGM TPLKVAAESC KADVVELLLS
HADCDRRSRI EALELLGASF ANDRENYDII KTYHYLYLAM LERFQDGDNI LEKEVLPPIH
AYGNRTECRN PQELESIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR GAVYADNMEF
EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE TVKAPDIECV LRCSVLEIEQ
SMNRVKNISD ADVHNAMDNY ECNLYTFLYL VCISTKTQCS EEDQCKINKQ IYNLIHLDPR
TREGFTLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
AARAVRANDI NYQDQIPRTL EEFVGFH


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