Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UK73 (FEM1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:FEM1B
Synonyms:F1AA, KIAA0396
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length627 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Interacts with CHEK1. Ref.1 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasm. Nucleus. Note: In the nucleus, the protein level increased slightly after camptothecin (CPT) treatment. Associated with chromatin. Ref.11

Tissue specificity

Widely expressed. Highly expressed in testis. Weakly expressed in other tissues. Ref.1

Sequence similarities

Belongs to the fem-1 family.

Contains 8 ANK repeats.

Contains 1 TPR repeat.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPM1FP495932EBI-310482,EBI-719945

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 627627Protein fem-1 homolog B
PRO_0000324530

Regions

Repeat45 – 7430ANK 1
Repeat87 – 11630ANK 2
Repeat120 – 14930ANK 3
Repeat153 – 18230ANK 4
Repeat186 – 21530ANK 5
Repeat218 – 24831ANK 6
Repeat344 – 37734TPR
Repeat483 – 52745ANK 7
Repeat531 – 56838ANK 8

Sites

Site342 – 3432Cleavage; by a caspase-3-like protease

Experimental info

Mutagenesis3421D → A: Prevents cleavage by a caspase-3-like protease. Ref.1
Mutagenesis3561D → A: Does not affect cleavage by a caspase-3-like protease. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UK73 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 85DA943663A988C1

FASTA62770,264
        10         20         30         40         50         60 
MEGLAGYVYK AASEGKVLTL AALLLNRSES DIRYLLGYVS QQGGQRSTPL IIAARNGHAK 

        70         80         90        100        110        120 
VVRLLLEHYR VQTQQTGTVR FDGYVIDGAT ALWCAAGAGH FEVVKLLVSH GANVNHTTVT 

       130        140        150        160        170        180 
NSTPLRAACF DGRLDIVKYL VENNANISIA NKYDNTCLMI AAYKGHTDVV RYLLEQRADP 

       190        200        210        220        230        240 
NAKAHCGATA LHFAAEAGHI DIVKELIKWR AAIVVNGHGM TPLKVAAESC KADVVELLLS 

       250        260        270        280        290        300 
HADCDRRSRI EALELLGASF ANDRENYDII KTYHYLYLAM LERFQDGDNI LEKEVLPPIH 

       310        320        330        340        350        360 
AYGNRTECRN PQELESIRQD RDALHMEGLI VRERILGADN IDVSHPIIYR GAVYADNMEF 

       370        380        390        400        410        420 
EQCIKLWLHA LHLRQKGNRN THKDLLRFAQ VFSQMIHLNE TVKAPDIECV LRCSVLEIEQ 

       430        440        450        460        470        480 
SMNRVKNISD ADVHNAMDNY ECNLYTFLYL VCISTKTQCS EEDQCKINKQ IYNLIHLDPR 

       490        500        510        520        530        540 
TREGFTLLHL AVNSNTPVDD FHTNDVCSFP NALVTKLLLD CGAEVNAVDN EGNSALHIIV 

       550        560        570        580        590        600 
QYNRPISDFL TLHSIIISLV EAGAHTDMTN KQNKTPLDKS TTGVSEILLK TQMKMSLKCL 

       610        620 
AARAVRANDI NYQDQIPRTL EEFVGFH 

« Hide

References

« Hide 'large scale' references
[1]"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], FUNCTION, CLEAVAGE, TISSUE SPECIFICITY, INTERACTION WITH FAS AND TNFRSF1A, MUTAGENESIS OF ASP-342 AND ASP-356.
[2]"Sequence, organization, and expression of the human FEM1B gene."
Ventura-Holman T., Maher J.F.
Biochem. Biophys. Res. Commun. 267:317-320(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[6]"Analysis of the DNA sequence and duplication history of human chromosome 15."
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. expand/collapse author list , 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.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Placenta.
[9]"The Caenorhabditis elegans sex-determining protein fem-2 and its human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase phosphatases that promote apoptosis."
Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.
J. Biol. Chem. 276:44193-44202(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPM1F.
[10]"VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases."
Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., Nakayama K.I.
Genes Dev. 18:3055-3065(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH CUL2.
[11]"Human FEM1B is required for Rad9 recruitment and CHK1 activation in response to replication stress."
Sun T.P., Shieh S.Y.
Oncogene 28:1971-1981(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CHEK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF178632 mRNA. Translation: AAF05314.1.
AF204883 mRNA. Translation: AAF69303.1.
AB007856 mRNA. Translation: BAA23692.2.
AK290167 mRNA. Translation: BAF82856.1.
AC021553 Genomic DNA. No translation available.
AC107871 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77818.1.
BC010122 mRNA. Translation: AAH10122.1.
BC014558 mRNA. Translation: AAH14558.1.
RefSeqNP_056137.1. NM_015322.4.
UniGeneHs.362733.
Hs.592737.

3D structure databases

ProteinModelPortalQ9UK73.
SMRQ9UK73. Positions 3-347, 483-590.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115421. 25 interactions.
IntActQ9UK73. 19 interactions.
MINTMINT-128836.
STRING9606.ENSP00000307298.

PTM databases

PhosphoSiteQ9UK73.

Polymorphism databases

DMDM74753369.

Proteomic databases

PaxDbQ9UK73.
PRIDEQ9UK73.

Protocols and materials databases

DNASU10116.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306917; ENSP00000307298; ENSG00000169018.
GeneID10116.
KEGGhsa:10116.
UCSCuc002arg.3. human.

Organism-specific databases

CTD10116.
GeneCardsGC15P068570.
HGNCHGNC:3649. FEM1B.
HPAHPA041920.
HPA042192.
MIM613539. gene.
neXtProtNX_Q9UK73.
PharmGKBPA28089.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000008180.
HOVERGENHBG057774.
InParanoidQ9UK73.
KOK10349.
OMASAMDNYE.
OrthoDBEOG7T4MJT.
PhylomeDBQ9UK73.
TreeFamTF351376.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UK73.
BgeeQ9UK73.
CleanExHS_FEM1B.
GenevestigatorQ9UK73.

Family and domain databases

Gene3D1.25.40.20. 4 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 7 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 8 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10116.
NextBio38269.
PMAP-CutDBQ9UK73.
PROQ9UK73.
SOURCESearch...

Entry information

Entry nameFEM1B_HUMAN
AccessionPrimary (citable) accession number: Q9UK73
Secondary accession number(s): O43146
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM