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Protein

Protein fem-1 homolog B

Gene

Fem1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • branching involved in prostate gland morphogenesis Source: MGI
  • epithelial cell maturation Source: MGI
  • epithelial cell maturation involved in prostate gland development Source: MGI
  • protein ubiquitination Source: MGI
  • regulation of DNA damage checkpoint Source: UniProtKB
  • regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • regulation of ubiquitin-protein transferase activity Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein fem-1 homolog B
Short name:
FEM1b
Alternative name(s):
FEM1-beta
Fem-1-like death receptor-binding protein alpha
Fem-1-like in apoptotic pathway protein alpha
Short name:
F1A-alpha
mt-Fem
Gene namesi
Name:Fem1b
Synonyms:F1aa, Kiaa0396
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1335087. Fem1b.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus By similarity

  • Note: Associated with chromatin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Abnormal glucose tolerance predominantly due to defective glucose-stimulated insulin secretion.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 627627Protein fem-1 homolog BPRO_0000324531Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei342 – 3432Cleavage; by a caspase-3-like proteaseBy similarity

Proteomic databases

MaxQBiQ9Z2G0.
PaxDbiQ9Z2G0.
PeptideAtlasiQ9Z2G0.
PRIDEiQ9Z2G0.

PTM databases

iPTMnetiQ9Z2G0.
PhosphoSiteiQ9Z2G0.

Expressioni

Tissue specificityi

Expressed in pancreatic islets, within both beta cells and non-beta cells (at protein level). Highly expressed in adult testis.1 Publication

Gene expression databases

BgeeiQ9Z2G0.
CleanExiMM_FEM1B.
GenevisibleiQ9Z2G0. MM.

Interactioni

Subunit structurei

Homooligomer. Component of a probable ECS E3 ubiquitin-protein ligase complex containing CUL2, RBX1, TCEB1, TCEB2 and FEM1B. Interacts with PPM1F and PHTF1. Interacts with the death domain of FAS/TNFRSF6 and TNFRSF1A (By similarity). Interacts with CHEK1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199631. 3 interactions.
STRINGi10090.ENSMUSP00000034775.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2G0.
SMRiQ9Z2G0. Positions 8-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati45 – 7430ANK 1Add
BLAST
Repeati87 – 11630ANK 2Add
BLAST
Repeati120 – 14930ANK 3Add
BLAST
Repeati153 – 18230ANK 4Add
BLAST
Repeati186 – 21530ANK 5Add
BLAST
Repeati218 – 24831ANK 6Add
BLAST
Repeati344 – 37734TPRAdd
BLAST
Repeati483 – 52745ANK 7Add
BLAST
Repeati531 – 56838ANK 8Add
BLAST

Sequence similaritiesi

Belongs to the fem-1 family.Curated
Contains 8 ANK repeats.PROSITE-ProRule annotation
Contains 1 TPR repeat.Curated

Keywords - Domaini

ANK repeat, Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0508. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129781.
HOVERGENiHBG057774.
InParanoidiQ9Z2G0.
KOiK10349.
OMAiERYRDSE.
OrthoDBiEOG7T4MJT.
PhylomeDBiQ9Z2G0.
TreeFamiTF351376.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2G0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGLAGYVYK AASEGKVLTL AALLLNRSES DIRYLLGYVS QQGGQRSTPL
60 70 80 90 100
IIAARNGHAK VVRLLLEHYR VQTQQTGTVR FDGYVIDGAT ALWCAAGAGH
110 120 130 140 150
FEVVKLLVSH GANVNHTTVT NSTPLRAACF DGRLDIVKYL VENNANISIA
160 170 180 190 200
NKYDNTCLMI AAYKGHTDVV RYLLEQRADP NAKAHCGATA LHFAAEAGHI
210 220 230 240 250
DIVKELIKWR AAIVVNGHGM TPLKVAAESC KADVVELLLS HADCDRRSRI
260 270 280 290 300
EALELLGASF ANDRENYDIM KTYHYLYLAM LERFQDGDNI LEKEVLPPIH
310 320 330 340 350
AYGNRTECRN PQELEAIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR
360 370 380 390 400
GAVYADNMEF EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE
410 420 430 440 450
AVKAPDIECV LRCSVLEIEQ SMNRVKNISD ADVHSAMDNY ECNLYTFLYL
460 470 480 490 500
VCISTKTQCS EEDQCRINKQ IYNLIHLDPR TREGFSLLHL AVNSNTPVDD
510 520 530 540 550
FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV QYNRPISDFL
560 570 580 590 600
TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL
610 620
AARAVRANDI NYQDQIPRTL EEFVGFH
Length:627
Mass (Da):70,223
Last modified:May 1, 1999 - v1
Checksum:i72D4ABA2D4576F1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841A → V in BAE21305 (PubMed:16141072).Curated
Sequence conflicti201 – 2011D → G in AAF05315 (PubMed:10542291).Curated
Sequence conflicti513 – 5131L → R in BAB33298 (Ref. 3) Curated
Sequence conflicti540 – 5401V → A in AAF05315 (PubMed:10542291).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064448 mRNA. Translation: AAC82373.1.
AF178633 mRNA. Translation: AAF05315.1.
AB022863 mRNA. Translation: BAB33298.1.
AK032338 mRNA. Translation: BAC27822.1.
AK132692 mRNA. Translation: BAE21305.1.
AK145371 mRNA. Translation: BAE26395.1.
AK149329 mRNA. Translation: BAE28816.1.
AK154060 mRNA. Translation: BAE32347.1.
AK160393 mRNA. Translation: BAE35763.1.
BC068236 mRNA. Translation: AAH68236.1.
AK122272 mRNA. Translation: BAC65554.1.
CCDSiCCDS23266.1.
RefSeqiNP_034323.1. NM_010193.4.
UniGeneiMm.24069.

Genome annotation databases

EnsembliENSMUST00000034775; ENSMUSP00000034775; ENSMUSG00000032244.
GeneIDi14155.
KEGGimmu:14155.
UCSCiuc009qam.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064448 mRNA. Translation: AAC82373.1.
AF178633 mRNA. Translation: AAF05315.1.
AB022863 mRNA. Translation: BAB33298.1.
AK032338 mRNA. Translation: BAC27822.1.
AK132692 mRNA. Translation: BAE21305.1.
AK145371 mRNA. Translation: BAE26395.1.
AK149329 mRNA. Translation: BAE28816.1.
AK154060 mRNA. Translation: BAE32347.1.
AK160393 mRNA. Translation: BAE35763.1.
BC068236 mRNA. Translation: AAH68236.1.
AK122272 mRNA. Translation: BAC65554.1.
CCDSiCCDS23266.1.
RefSeqiNP_034323.1. NM_010193.4.
UniGeneiMm.24069.

3D structure databases

ProteinModelPortaliQ9Z2G0.
SMRiQ9Z2G0. Positions 8-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199631. 3 interactions.
STRINGi10090.ENSMUSP00000034775.

PTM databases

iPTMnetiQ9Z2G0.
PhosphoSiteiQ9Z2G0.

Proteomic databases

MaxQBiQ9Z2G0.
PaxDbiQ9Z2G0.
PeptideAtlasiQ9Z2G0.
PRIDEiQ9Z2G0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034775; ENSMUSP00000034775; ENSMUSG00000032244.
GeneIDi14155.
KEGGimmu:14155.
UCSCiuc009qam.3. mouse.

Organism-specific databases

CTDi10116.
MGIiMGI:1335087. Fem1b.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0508. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129781.
HOVERGENiHBG057774.
InParanoidiQ9Z2G0.
KOiK10349.
OMAiERYRDSE.
OrthoDBiEOG7T4MJT.
PhylomeDBiQ9Z2G0.
TreeFamiTF351376.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9Z2G0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2G0.
CleanExiMM_FEM1B.
GenevisibleiQ9Z2G0. MM.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 8 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The murine fem1 gene family: homologs of the Caenorhabditis elegans sex-determination protein FEM-1."
    Ventura-Holman T., Seldin M.F., Li W., Maher J.F.
    Genomics 54:221-230(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: CD-1.
    Tissue: Testis.
  2. "F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosis."
    Chan S.-L., Tan K.-O., Zhang L., Yee K.S.Y., Ronca F., Chan M.-Y., Yu V.C.
    J. Biol. Chem. 274:32461-32468(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Haploid germ cell specific gene."
    Tanaka H., Koga M., Nishimune Y.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Olfactory bulb, Retina, Testis and Thymus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "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."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-627.
  7. "Putative homeodomain transcription factor 1 interacts with the feminization factor homolog fem1b in male germ cells."
    Oyhenart J., Benichou S., Raich N.
    Biol. Reprod. 72:780-787(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PHTF1.
  8. "Abnormal glucose homeostasis and pancreatic islet function in mice with inactivation of the Fem1b gene."
    Lu D., Ventura-Holman T., Li J., McMurray R.W., Subauste J.S., Maher J.F.
    Mol. Cell. Biol. 25:6570-6577(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiFEM1B_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2G0
Secondary accession number(s): Q3TV57
, Q3ULQ3, Q3V148, Q80U13, Q99NC9, Q9QZL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.