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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) (mt-Fem)

 FEM1B_MOUSE             Reviewed;         627 AA.
Q9Z2G0; Q3TV57; Q3ULQ3; Q3V148; Q80U13; Q99NC9; Q9QZL3;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
13-NOV-2019, entry version 151.
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;
AltName: Full=mt-Fem;
Name=Fem1b; Synonyms=F1aa, Kiaa0396;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=CD-1; TISSUE=Testis;
PubMed=9828124; DOI=10.1006/geno.1998.5569;
Ventura-Holman T., Seldin M.F., Li W., Maher J.F.;
"The murine fem1 gene family: homologs of the Caenorhabditis elegans
sex-determination protein FEM-1.";
Genomics 54:221-230(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
Tanaka H., Koga M., Nishimune Y.;
"Haploid germ cell specific gene.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Olfactory bulb, Retina, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-627.
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH PHTF1.
PubMed=15601915; DOI=10.1095/biolreprod.104.035964;
Oyhenart J., Benichou S., Raich N.;
"Putative homeodomain transcription factor 1 interacts with the
feminization factor homolog fem1b in male germ cells.";
Biol. Reprod. 72:780-787(2005).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16024793; DOI=10.1128/mcb.25.15.6570-6577.2005;
Lu D., Ventura-Holman T., Li J., McMurray R.W., Subauste J.S.,
Maher J.F.;
"Abnormal glucose homeostasis and pancreatic islet function in mice
with inactivation of the Fem1b gene.";
Mol. Cell. Biol. 25:6570-6577(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:16024793}.
-!- 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 (By similarity). Interacts with
CHEK1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15601915}.
Nucleus {ECO:0000250}. Note=Associated with chromatin.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in pancreatic islets, within both
beta cells and non-beta cells (at protein level). Highly expressed
in adult testis. {ECO:0000269|PubMed:9828124}.
-!- DISRUPTION PHENOTYPE: Abnormal glucose tolerance predominantly due
to defective glucose-stimulated insulin secretion.
{ECO:0000269|PubMed:16024793}.
-!- SIMILARITY: Belongs to the fem-1 family. {ECO:0000305}.
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EMBL; AF064448; AAC82373.1; -; mRNA.
EMBL; AF178633; AAF05315.1; -; mRNA.
EMBL; AB022863; BAB33298.1; -; mRNA.
EMBL; AK032338; BAC27822.1; -; mRNA.
EMBL; AK132692; BAE21305.1; -; mRNA.
EMBL; AK145371; BAE26395.1; -; mRNA.
EMBL; AK149329; BAE28816.1; -; mRNA.
EMBL; AK154060; BAE32347.1; -; mRNA.
EMBL; AK160393; BAE35763.1; -; mRNA.
EMBL; BC068236; AAH68236.1; -; mRNA.
EMBL; AK122272; BAC65554.1; -; mRNA.
CCDS; CCDS23266.1; -.
RefSeq; NP_034323.1; NM_010193.4.
BioGrid; 199631; 3.
IntAct; Q9Z2G0; 1.
STRING; 10090.ENSMUSP00000034775; -.
iPTMnet; Q9Z2G0; -.
PhosphoSitePlus; Q9Z2G0; -.
EPD; Q9Z2G0; -.
MaxQB; Q9Z2G0; -.
PaxDb; Q9Z2G0; -.
PeptideAtlas; Q9Z2G0; -.
PRIDE; Q9Z2G0; -.
Ensembl; ENSMUST00000034775; ENSMUSP00000034775; ENSMUSG00000032244.
GeneID; 14155; -.
KEGG; mmu:14155; -.
UCSC; uc009qam.3; mouse.
CTD; 10116; -.
MGI; MGI:1335087; Fem1b.
eggNOG; KOG0508; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000161115; -.
InParanoid; Q9Z2G0; -.
KO; K10349; -.
OMA; MEGLMIR; -.
OrthoDB; 252380at2759; -.
PhylomeDB; Q9Z2G0; -.
TreeFam; TF351376; -.
Reactome; R-MMU-8951664; Neddylation.
UniPathway; UPA00143; -.
ChiTaRS; Fem1b; mouse.
PRO; PR:Q9Z2G0; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032244; Expressed in 294 organ(s), highest expression level in primitive streak.
Genevisible; Q9Z2G0; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005123; F:death receptor binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
GO; GO:2000001; P:regulation of DNA damage checkpoint; ISS:UniProtKB.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; ISO:MGI.
Gene3D; 1.25.40.20; -; 4.
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; S