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Protein

Fas apoptotic inhibitory molecule 1

Gene

Faim

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Fas apoptotic inhibitory molecule 1
Gene namesi
Name:Faim
Synonyms:Faim1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1344387. Faim.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 179178Fas apoptotic inhibitory molecule 1PRO_0000087174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WUD8.
MaxQBiQ9WUD8.
PaxDbiQ9WUD8.
PRIDEiQ9WUD8.

Expressioni

Tissue specificityi

Widely expressed, with the highest levels in brain, thymus, kidney, and spleen.1 Publication

Gene expression databases

BgeeiQ9WUD8.
CleanExiMM_FAIM.
ExpressionAtlasiQ9WUD8. baseline and differential.
GenevisibleiQ9WUD8. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108532.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi97 – 1048Combined sources
Beta strandi107 – 1148Combined sources
Turni115 – 1184Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi147 – 17125Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KD2NMR-A91-179[»]
ProteinModelPortaliQ9WUD8.
SMRiQ9WUD8. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WUD8.

Family & Domainsi

Sequence similaritiesi

Belongs to the FAIM1 family.Curated

Phylogenomic databases

eggNOGiKOG4352. Eukaryota.
ENOG410XRNP. LUCA.
GeneTreeiENSGT00390000007364.
HOGENOMiHOG000007913.
HOVERGENiHBG051543.
InParanoidiQ9WUD8.
PhylomeDBiQ9WUD8.

Family and domain databases

InterProiIPR010695. FAIM1.
[Graphical view]
PANTHERiPTHR13088. PTHR13088. 1 hit.
PfamiPF06905. FAIM1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WUD8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDLVAVWDV ALSDGVHKIE FEHGTTSGKR VVYVDGKEEI RREWMFKLVG
60 70 80 90 100
KETFFVGAAK TKATINIDAI SGFAYEYTLE IDGKSLKKYM ENRSKTTSTW
110 120 130 140 150
VLRLDGEDLR VVLEKDTMDV WCNGQKMETA GEFVDDGTET HFSVGNHGCY
160 170
IKAVSSGKRK EGIIHTLIVD NREIPELTQ
Length:179
Mass (Da):20,201
Last modified:November 1, 1999 - v1
Checksum:i10E49A8E65926556
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571G → R in BAB24225 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130367 mRNA. Translation: AAD23879.1.
AK005762 mRNA. Translation: BAB24225.1.
BC079662 mRNA. Translation: AAH79662.1.
CCDSiCCDS23431.1.
RefSeqiNP_001116323.1. NM_001122851.1.
NP_035940.3. NM_011810.3.
UniGeneiMm.74605.

Genome annotation databases

EnsembliENSMUST00000035038; ENSMUSP00000035038; ENSMUSG00000032463.
GeneIDi23873.
KEGGimmu:23873.
UCSCiuc009rdt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130367 mRNA. Translation: AAD23879.1.
AK005762 mRNA. Translation: BAB24225.1.
BC079662 mRNA. Translation: AAH79662.1.
CCDSiCCDS23431.1.
RefSeqiNP_001116323.1. NM_001122851.1.
NP_035940.3. NM_011810.3.
UniGeneiMm.74605.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KD2NMR-A91-179[»]
ProteinModelPortaliQ9WUD8.
SMRiQ9WUD8. Positions 1-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108532.

Proteomic databases

EPDiQ9WUD8.
MaxQBiQ9WUD8.
PaxDbiQ9WUD8.
PRIDEiQ9WUD8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035038; ENSMUSP00000035038; ENSMUSG00000032463.
GeneIDi23873.
KEGGimmu:23873.
UCSCiuc009rdt.2. mouse.

Organism-specific databases

CTDi55179.
MGIiMGI:1344387. Faim.

Phylogenomic databases

eggNOGiKOG4352. Eukaryota.
ENOG410XRNP. LUCA.
GeneTreeiENSGT00390000007364.
HOGENOMiHOG000007913.
HOVERGENiHBG051543.
InParanoidiQ9WUD8.
PhylomeDBiQ9WUD8.

Miscellaneous databases

EvolutionaryTraceiQ9WUD8.
NextBioi303587.
PROiQ9WUD8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUD8.
CleanExiMM_FAIM.
ExpressionAtlasiQ9WUD8. baseline and differential.
GenevisibleiQ9WUD8. MM.

Family and domain databases

InterProiIPR010695. FAIM1.
[Graphical view]
PANTHERiPTHR13088. PTHR13088. 1 hit.
PfamiPF06905. FAIM1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene coding for a Fas apoptosis inhibitory molecule (FAIM) isolated from inducibly Fas-resistant B lymphocytes."
    Schneider T.J., Fischer G.M., Donohoe T.J., Colarusso T.P., Rothstein T.L.
    J. Exp. Med. 189:949-956(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Thymus.
  2. "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.
    Tissue: Testis.
  3. "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.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  5. "Fas apoptosis inhibitory molecule contains a novel beta-sandwich in contact with a partially ordered domain."
    Hemond M., Rothstein T.L., Wagner G.
    J. Mol. Biol. 386:1024-1037(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 91-179, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFAIM1_MOUSE
AccessioniPrimary (citable) accession number: Q9WUD8
Secondary accession number(s): Q9DAK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: November 1, 1999
Last modified: March 16, 2016
This is version 94 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.