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Protein

Protein lifeguard 2

Gene

FAIM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. May play a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lifeguard 2
Alternative name(s):
Fas apoptotic inhibitory molecule 2
Neural membrane protein 35
Transmembrane BAX inhibitor motif-containing protein 2
Gene namesi
Name:FAIM2
Synonyms:KIAA0950, LFG, LFG2, NMP35, TMBIM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17067. FAIM2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei106 – 12621HelicalSequence AnalysisAdd
BLAST
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence AnalysisAdd
BLAST
Transmembranei194 – 21421HelicalSequence AnalysisAdd
BLAST
Transmembranei225 – 24521HelicalSequence AnalysisAdd
BLAST
Transmembranei250 – 27021HelicalSequence AnalysisAdd
BLAST
Transmembranei290 – 31021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134879081.

Polymorphism and mutation databases

BioMutaiFAIM2.
DMDMi38503167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Protein lifeguard 2PRO_0000179087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9BWQ8.
PRIDEiQ9BWQ8.

PTM databases

PhosphoSiteiQ9BWQ8.

Expressioni

Tissue specificityi

Highly expressed in breast carcinoma tissues. Enhanced expression correlates with the grade of the tumor (grade II/grade III) in primary breast tumors (at protein level). Widely expressed. Expressed at high levels in the brain especially in the hippocampus.2 Publications

Inductioni

Regulated by the AKT1/LEF1 pathway in breast cancer cell lines.1 Publication

Gene expression databases

BgeeiQ9BWQ8.
CleanExiHS_FAIM2.
ExpressionAtlasiQ9BWQ8. baseline and differential.
GenevestigatoriQ9BWQ8.

Organism-specific databases

HPAiHPA018790.
HPA048800.

Interactioni

Subunit structurei

Interacts with FAS/TNFRSF6 and BAX.2 Publications

Protein-protein interaction databases

BioGridi116659. 1 interaction.
IntActiQ9BWQ8. 1 interaction.
STRINGi9606.ENSP00000321951.

Structurei

3D structure databases

ProteinModelPortaliQ9BWQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 755Poly-Ser

Sequence similaritiesi

Belongs to the BI1 family. LFG subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0670.
GeneTreeiENSGT00500000044791.
HOGENOMiHOG000060393.
HOVERGENiHBG012084.
InParanoidiQ9BWQ8.
OMAiCNIRRIF.
OrthoDBiEOG7VB2G8.
PhylomeDBiQ9BWQ8.
TreeFamiTF319996.

Family and domain databases

InterProiIPR006214. Bax_inhibitor_1-related.
[Graphical view]
PANTHERiPTHR23291. PTHR23291. 1 hit.
PfamiPF01027. Bax1-I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BWQ8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTQGKLSVAN KAPGTEGQQQ VHGEKKEAPA VPSAPPSYEE ATSGEGMKAG
60 70 80 90 100
AFPPAPTAVP LHPSWAYVDP SSSSSYDNGF PTGDHELFTT FSWDDQKVRR
110 120 130 140 150
VFVRKVYTIL LIQLLVTLAV VALFTFCDPV KDYVQANPGW YWASYAVFFA
160 170 180 190 200
TYLTLACCSG PRRHFPWNLI LLTVFTLSMA YLTGMLSSYY NTTSVLLCLG
210 220 230 240 250
ITALVCLSVT VFSFQTKFDF TSCQGVLFVL LMTLFFSGLI LAILLPFQYV
260 270 280 290 300
PWLHAVYAAL GAGVFTLFLA LDTQLLMGNR RHSLSPEEYI FGALNIYLDI
310
IYIFTFFLQL FGTNRE
Length:316
Mass (Da):35,110
Last modified:June 1, 2001 - v1
Checksum:i574128C7ADCC51C0
GO
Isoform 2 (identifier: Q9BWQ8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Note: No experimental confirmation available.

Show »
Length:270
Mass (Da):30,448
Checksum:iD2D32BE53A3E41CC
GO

Sequence cautioni

The sequence AAF06327.1 differs from that shown. Reason: Frameshift at positions 82 and 130. Curated
The sequence BAA76794.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31Q → R in AAF06327 (PubMed:10535980).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_056989Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190461 mRNA. Translation: AAF06327.1. Frameshift.
AB023167 mRNA. Translation: BAA76794.1. Different initiation.
AK090728 mRNA. Translation: BAG52220.1.
AK290031 mRNA. Translation: BAF82720.1.
AC131157 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58103.1.
CH471111 Genomic DNA. Translation: EAW58104.1.
BC000051 mRNA. Translation: AAH00051.1.
CCDSiCCDS8791.1. [Q9BWQ8-1]
RefSeqiNP_036438.2. NM_012306.3. [Q9BWQ8-1]
UniGeneiHs.567424.

Genome annotation databases

EnsembliENST00000320634; ENSP00000321951; ENSG00000135472. [Q9BWQ8-1]
ENST00000550890; ENSP00000450132; ENSG00000135472. [Q9BWQ8-2]
GeneIDi23017.
KEGGihsa:23017.
UCSCiuc001rvi.2. human. [Q9BWQ8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190461 mRNA. Translation: AAF06327.1. Frameshift.
AB023167 mRNA. Translation: BAA76794.1. Different initiation.
AK090728 mRNA. Translation: BAG52220.1.
AK290031 mRNA. Translation: BAF82720.1.
AC131157 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58103.1.
CH471111 Genomic DNA. Translation: EAW58104.1.
BC000051 mRNA. Translation: AAH00051.1.
CCDSiCCDS8791.1. [Q9BWQ8-1]
RefSeqiNP_036438.2. NM_012306.3. [Q9BWQ8-1]
UniGeneiHs.567424.

3D structure databases

ProteinModelPortaliQ9BWQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116659. 1 interaction.
IntActiQ9BWQ8. 1 interaction.
STRINGi9606.ENSP00000321951.

PTM databases

PhosphoSiteiQ9BWQ8.

Polymorphism and mutation databases

BioMutaiFAIM2.
DMDMi38503167.

Proteomic databases

PaxDbiQ9BWQ8.
PRIDEiQ9BWQ8.

Protocols and materials databases

DNASUi23017.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320634; ENSP00000321951; ENSG00000135472. [Q9BWQ8-1]
ENST00000550890; ENSP00000450132; ENSG00000135472. [Q9BWQ8-2]
GeneIDi23017.
KEGGihsa:23017.
UCSCiuc001rvi.2. human. [Q9BWQ8-1]

Organism-specific databases

CTDi23017.
GeneCardsiGC12M050260.
HGNCiHGNC:17067. FAIM2.
HPAiHPA018790.
HPA048800.
MIMi604306. gene.
neXtProtiNX_Q9BWQ8.
PharmGKBiPA134879081.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0670.
GeneTreeiENSGT00500000044791.
HOGENOMiHOG000060393.
HOVERGENiHBG012084.
InParanoidiQ9BWQ8.
OMAiCNIRRIF.
OrthoDBiEOG7VB2G8.
PhylomeDBiQ9BWQ8.
TreeFamiTF319996.

Miscellaneous databases

ChiTaRSiFAIM2. human.
GenomeRNAii23017.
NextBioi35469442.
PROiQ9BWQ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWQ8.
CleanExiHS_FAIM2.
ExpressionAtlasiQ9BWQ8. baseline and differential.
GenevestigatoriQ9BWQ8.

Family and domain databases

InterProiIPR006214. Bax_inhibitor_1-related.
[Graphical view]
PANTHERiPTHR23291. PTHR23291. 1 hit.
PfamiPF01027. Bax1-I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LFG: an anti-apoptotic gene that provides protection from fas-mediated cell death."
    Somia N.V., Schmitt M.J., Vetter D.E., Van Antwerp D., Heinemann S.F., Verma I.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:12667-12672(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH FAS/TNFRSF6, TISSUE SPECIFICITY.
    Tissue: Lung fibroblast.
  2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum and Hippocampus.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "Sequence analysis shows that Lifeguard belongs to a new evolutionarily conserved cytoprotective family."
    Reimers K., Choi C.Y., Mau-Thek E., Vogt P.M.
    Int. J. Mol. Med. 18:729-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, INTERACTION WITH BAX.
  8. "Lifeguard/neuronal membrane protein 35 regulates Fas ligand-mediated apoptosis in neurons via microdomain recruitment."
    Fernandez M., Segura M.F., Sole C., Colino A., Comella J.X., Cena V.
    J. Neurochem. 103:190-203(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "LFG: a candidate apoptosis regulatory gene family."
    Hu L., Smith T.F., Goldberger G.
    Apoptosis 14:1255-1265(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  10. "Transactivation of lifeguard (LFG) by Akt-/LEF-1 pathway in MCF-7 and MDA-MB 231 human breast cancer cells."
    Bucan V., Adili M.Y., Choi C.Y., Eddy M.T., Vogt P.M., Reimers K.
    Apoptosis 15:814-821(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  11. "The anti-apoptotic protein lifeguard is expressed in breast cancer cells and tissues."
    Bucan V., Reimers K., Choi C.Y., Eddy M.T., Vogt P.M.
    Cell. Mol. Biol. Lett. 15:296-310(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiLFG2_HUMAN
AccessioniPrimary (citable) accession number: Q9BWQ8
Secondary accession number(s): A8K1W6
, B3KR08, Q9UJY9, Q9Y2F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.