FAIM1_HUMAN
ID FAIM1_HUMAN Reviewed; 179 AA.
AC Q9NVQ4; Q6IAN2;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Fas apoptotic inhibitory molecule 1;
GN Name=FAIM; Synonyms=FAIM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-130 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-117.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-151 (ISOFORM 3), AND VARIANTS THR-117 AND
RP SER-127.
RC TISSUE=Retina;
RX PubMed=12107411;
RA Wistow G., Berstein S.L., Wyatt M.K., Ray S., Behal A., Touchman J.W.,
RA Bouffard G., Smith D., Peterson K.;
RT "Expressed sequence tag analysis of human retina for the NEIBank project:
RT retbindin, an abundant, novel retinal cDNA and alternative splicing of
RT other retina-preferred gene transcripts.";
RL Mol. Vis. 8:196-204(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Plays a role as an inducible effector molecule that mediates
CC Fas resistance produced by surface Ig engagement in B cells.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NVQ4; O43597: SPRY2; NbExp=3; IntAct=EBI-10314711, EBI-742487;
CC Q9NVQ4-2; Q86X02: CDR2L; NbExp=6; IntAct=EBI-12039347, EBI-11063830;
CC Q9NVQ4-2; Q9UN19: DAPP1; NbExp=3; IntAct=EBI-12039347, EBI-3918199;
CC Q9NVQ4-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12039347, EBI-6509505;
CC Q9NVQ4-2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-12039347, EBI-12039345;
CC Q9NVQ4-2; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-12039347, EBI-6929619;
CC Q9NVQ4-2; P17020: ZNF16; NbExp=3; IntAct=EBI-12039347, EBI-3921553;
CC Q9NVQ4-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-12039347, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=FAIM-S;
CC IsoId=Q9NVQ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVQ4-2; Sequence=VSP_008991;
CC Name=3; Synonyms=FAIM-L;
CC IsoId=Q9NVQ4-3; Sequence=VSP_038095;
CC -!- SIMILARITY: Belongs to the FAIM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86174.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FAIMID43251ch3q22.html";
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DR EMBL; AK001444; BAA91695.1; -; mRNA.
DR EMBL; AK125477; BAC86174.1; ALT_SEQ; mRNA.
DR EMBL; CR457122; CAG33403.1; -; mRNA.
DR EMBL; AC020890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012478; AAH12478.1; -; mRNA.
DR EMBL; BQ638715; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS3103.1; -. [Q9NVQ4-1]
DR CCDS; CCDS33864.1; -. [Q9NVQ4-2]
DR CCDS; CCDS33865.1; -. [Q9NVQ4-3]
DR RefSeq; NP_001028202.1; NM_001033030.1. [Q9NVQ4-2]
DR RefSeq; NP_001028203.1; NM_001033031.1. [Q9NVQ4-3]
DR RefSeq; NP_001028204.1; NM_001033032.1. [Q9NVQ4-1]
DR RefSeq; NP_060617.1; NM_018147.3. [Q9NVQ4-1]
DR PDB; 2KW1; NMR; -; A=91-179.
DR PDB; 3MX7; X-ray; 1.76 A; A=1-90.
DR PDBsum; 2KW1; -.
DR PDBsum; 3MX7; -.
DR AlphaFoldDB; Q9NVQ4; -.
DR BMRB; Q9NVQ4; -.
DR SMR; Q9NVQ4; -.
DR BioGRID; 120478; 34.
DR IntAct; Q9NVQ4; 13.
DR STRING; 9606.ENSP00000342805; -.
DR GlyGen; Q9NVQ4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVQ4; -.
DR PhosphoSitePlus; Q9NVQ4; -.
DR BioMuta; FAIM; -.
DR DMDM; 38503210; -.
DR EPD; Q9NVQ4; -.
DR jPOST; Q9NVQ4; -.
DR MassIVE; Q9NVQ4; -.
DR MaxQB; Q9NVQ4; -.
DR PaxDb; Q9NVQ4; -.
DR PeptideAtlas; Q9NVQ4; -.
DR PRIDE; Q9NVQ4; -.
DR ProteomicsDB; 82844; -. [Q9NVQ4-1]
DR ProteomicsDB; 82845; -. [Q9NVQ4-2]
DR ProteomicsDB; 82846; -. [Q9NVQ4-3]
DR Antibodypedia; 33444; 353 antibodies from 39 providers.
DR DNASU; 55179; -.
DR Ensembl; ENST00000338446.8; ENSP00000342805.4; ENSG00000158234.13. [Q9NVQ4-2]
DR Ensembl; ENST00000360570.8; ENSP00000353775.3; ENSG00000158234.13. [Q9NVQ4-3]
DR Ensembl; ENST00000393034.6; ENSP00000376754.2; ENSG00000158234.13. [Q9NVQ4-1]
DR Ensembl; ENST00000393035.6; ENSP00000376755.2; ENSG00000158234.13. [Q9NVQ4-1]
DR Ensembl; ENST00000464668.5; ENSP00000417642.1; ENSG00000158234.13. [Q9NVQ4-1]
DR GeneID; 55179; -.
DR KEGG; hsa:55179; -.
DR MANE-Select; ENST00000360570.8; ENSP00000353775.3; NM_001033031.2; NP_001028203.1. [Q9NVQ4-3]
DR UCSC; uc003esp.4; human. [Q9NVQ4-1]
DR CTD; 55179; -.
DR DisGeNET; 55179; -.
DR GeneCards; FAIM; -.
DR HGNC; HGNC:18703; FAIM.
DR HPA; ENSG00000158234; Tissue enriched (retina).
DR MIM; 617535; gene.
DR neXtProt; NX_Q9NVQ4; -.
DR OpenTargets; ENSG00000158234; -.
DR PharmGKB; PA38647; -.
DR VEuPathDB; HostDB:ENSG00000158234; -.
DR eggNOG; KOG4352; Eukaryota.
DR GeneTree; ENSGT00390000007364; -.
DR InParanoid; Q9NVQ4; -.
DR OrthoDB; 1301275at2759; -.
DR PhylomeDB; Q9NVQ4; -.
DR TreeFam; TF314971; -.
DR PathwayCommons; Q9NVQ4; -.
DR SignaLink; Q9NVQ4; -.
DR BioGRID-ORCS; 55179; 42 hits in 1077 CRISPR screens.
DR ChiTaRS; FAIM; human.
DR GenomeRNAi; 55179; -.
DR Pharos; Q9NVQ4; Tbio.
DR PRO; PR:Q9NVQ4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NVQ4; protein.
DR Bgee; ENSG00000158234; Expressed in bronchial epithelial cell and 200 other tissues.
DR ExpressionAtlas; Q9NVQ4; baseline and differential.
DR Genevisible; Q9NVQ4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IBA:GO_Central.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IBA:GO_Central.
DR Gene3D; 2.40.128.180; -; 2.
DR InterPro; IPR010695; FAIM1.
DR InterPro; IPR038513; FAIM1_dom_sf.
DR PANTHER; PTHR13088; PTHR13088; 1.
DR Pfam; PF06905; FAIM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..179
FT /note="Fas apoptotic inhibitory molecule 1"
FT /id="PRO_0000087173"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1
FT /note="M -> MLLPFIRTLPLLCYNHLLVSPDSATLSPPYSLEKM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008991"
FT VAR_SEQ 1
FT /note="M -> MASGDDSPIFEDDESPPYSLEKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12107411"
FT /id="VSP_038095"
FT VARIANT 117
FT /note="A -> T (in dbSNP:rs641320)"
FT /evidence="ECO:0000269|PubMed:12107411, ECO:0000269|Ref.2"
FT /id="VAR_024314"
FT VARIANT 127
FT /note="L -> S (in dbSNP:rs13043)"
FT /evidence="ECO:0000269|PubMed:12107411"
FT /id="VAR_024315"
FT CONFLICT 32
FT /note="V -> L (in Ref. 5; BQ638715)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="N -> S (in Ref. 2; CAG33403)"
FT /evidence="ECO:0000305"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:3MX7"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3MX7"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:3MX7"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3MX7"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2KW1"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2KW1"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2KW1"
SQ SEQUENCE 179 AA; 20215 MW; 129E7E4525535C72 CRC64;
MTDLVAVWDV ALSDGVHKIE FEHGTTSGKR VVYVDGKEEI RKEWMFKLVG KETFYVGAAK
TKATINIDAI SGFAYEYTLE INGKSLKKYM EDRSKTTNTW VLHMDGENFR IVLEKDAMDV
WCNGKKLETA GEFVDDGTET HFSIGNHDCY IKAVSSGKRK EGIIHTLIVD NREIPEIAS
