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Protein

Protein fem-1 homolog B

Gene

Fem1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity). Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1 (By similarity).By similarity

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

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
Gene namesi
Name:Fem1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi1304569. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 627627Protein fem-1 homolog BPRO_0000324532Add
BLAST

Sites

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

Proteomic databases

PaxDbiP0C6P7.
PRIDEiP0C6P7.

Expressioni

Tissue specificityi

Present in adult testis (at protein level).1 Publication

Developmental stagei

In testis, it is first observed in leptotene and early pachytene spermatocytes. Present at high level in pachytene spermatocytes at stage IX-X and persists throughout spermiogenesis. At spermiation, most of the protein is associated with the residual bodies, but some protein persists in the queues of mature spermatids.1 Publication

Gene expression databases

GenevisibleiP0C6P7. RN.

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009368.

Structurei

3D structure databases

ProteinModelPortaliP0C6P7.
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.
HOGENOMiHOG000008180.
HOVERGENiHBG057774.
InParanoidiP0C6P7.
KOiK10349.
OMAiERYRDSE.
OrthoDBiEOG7T4MJT.
PhylomeDBiP0C6P7.
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. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C6P7-1 [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 TREGFTLLHL 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):70,237
Last modified:March 18, 2008 - v1
Checksum:iD284ABA7D404B44D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03062554 Genomic DNA. No translation available.
RefSeqiNP_001101627.1. NM_001108157.1.
UniGeneiRn.219320.

Genome annotation databases

EnsembliENSRNOT00000009368; ENSRNOP00000009368; ENSRNOG00000007077.
GeneIDi315745.
KEGGirno:315745.
UCSCiRGD:1304569. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03062554 Genomic DNA. No translation available.
RefSeqiNP_001101627.1. NM_001108157.1.
UniGeneiRn.219320.

3D structure databases

ProteinModelPortaliP0C6P7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009368.

Proteomic databases

PaxDbiP0C6P7.
PRIDEiP0C6P7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009368; ENSRNOP00000009368; ENSRNOG00000007077.
GeneIDi315745.
KEGGirno:315745.
UCSCiRGD:1304569. rat.

Organism-specific databases

CTDi10116.
RGDi1304569. Fem1b.

Phylogenomic databases

eggNOGiKOG0508. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129781.
HOGENOMiHOG000008180.
HOVERGENiHBG057774.
InParanoidiP0C6P7.
KOiK10349.
OMAiERYRDSE.
OrthoDBiEOG7T4MJT.
PhylomeDBiP0C6P7.
TreeFamiTF351376.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiP0C6P7.

Gene expression databases

GenevisibleiP0C6P7. RN.

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. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 2 hits.
PS50088. ANK_REPEAT. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiFEM1B_RAT
AccessioniPrimary (citable) accession number: P0C6P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: June 8, 2016
This is version 61 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.