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Protein

FAS-associated factor 2

Gene

FAF2

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

Functioni

Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:18711132, PubMed:24215460). Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis (PubMed:23297223).3 Publications

GO - Molecular functioni

  • lipase binding Source: MGI
  • lipase inhibitor activity Source: MGI
  • ubiquitin binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • lipid particle organization Source: MGI
  • negative regulation of catalytic activity Source: GOC
  • response to unfolded protein Source: UniProtKB-KW
  • retrograde protein transport, ER to cytosol Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Biological processi

Unfolded protein response

Names & Taxonomyi

Protein namesi
Recommended name:
FAS-associated factor 2
Alternative name(s):
Protein ETEA
UBX domain-containing protein 3B
UBX domain-containing protein 8
Gene namesi
Name:FAF2
Synonyms:ETEA, KIAA0887, UBXD8, UBXN3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:24666. FAF2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: MGI
  • lipid particle Source: UniProtKB
  • VCP-NPL4-UFD1 AAA ATPase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Lipid droplet

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385570.

Polymorphism and mutation databases

BioMutaiFAF2.
DMDMi74731375.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 445444FAS-associated factor 2PRO_0000244064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei167 – 1671N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ96CS3.
MaxQBiQ96CS3.
PaxDbiQ96CS3.
PeptideAtlasiQ96CS3.
PRIDEiQ96CS3.

PTM databases

iPTMnetiQ96CS3.
PhosphoSiteiQ96CS3.
SwissPalmiQ96CS3.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in brain.1 Publication

Gene expression databases

BgeeiQ96CS3.
CleanExiHS_FAF2.
ExpressionAtlasiQ96CS3. baseline and differential.
GenevisibleiQ96CS3. HS.

Interactioni

Subunit structurei

Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8, UBE2J1/UBC6E and AUP1 (PubMed:18711132). Interacts with YOD1 (PubMed:19818707). Interacts (via N-terminus) with UBQLN2 (via C-terminus) (PubMed:24215460). Interacts with PNPLA2 and UBAC2 (PubMed:23297223).4 Publications

GO - Molecular functioni

  • lipase binding Source: MGI
  • ubiquitin binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116806. 187 interactions.
DIPiDIP-46261N.
IntActiQ96CS3. 47 interactions.
STRINGi9606.ENSP00000261942.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2414Combined sources
Helixi29 – 3911Combined sources
Helixi43 – 5210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAMNMR-A3-56[»]
ProteinModelPortaliQ96CS3.
SMRiQ96CS3. Positions 2-56, 136-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96CS3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4837UBAAdd
BLAST
Domaini357 – 43983UBXPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili275 – 35076Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.Curated
Contains 1 UBX domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1363. Eukaryota.
ENOG410XSFS. LUCA.
GeneTreeiENSGT00530000063422.
HOGENOMiHOG000007539.
HOVERGENiHBG101311.
InParanoidiQ96CS3.
KOiK18726.
OMAiPCLPTEE.
PhylomeDBiQ96CS3.
TreeFamiTF314172.

Family and domain databases

InterProiIPR012336. Thioredoxin-like_fold.
IPR006577. UAS.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00594. UAS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q96CS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPEERDLT QEQTEKLLQF QDLTGIESMD QCRHTLEQHN WNIEAAVQDR
60 70 80 90 100
LNEQEGVPSV FNPPPSRPLQ VNTADHRIYS YVVSRPQPRG LLGWGYYLIM
110 120 130 140 150
LPFRFTYYTI LDIFRFALRF IRPDPRSRVT DPVGDIVSFM HSFEEKYGRA
160 170 180 190 200
HPVFYQGTYS QALNDAKREL RFLLVYLHGD DHQDSDEFCR NTLCAPEVIS
210 220 230 240 250
LINTRMLFWA CSTNKPEGYR VSQALRENTY PFLAMIMLKD RRMTVVGRLE
260 270 280 290 300
GLIQPDDLIN QLTFIMDANQ TYLVSERLER EERNQTQVLR QQQDEAYLAS
310 320 330 340 350
LRADQEKERK KREERERKRR KEEEVQQQKL AEERRRQNLQ EEKERKLECL
360 370 380 390 400
PPEPSPDDPE SVKIIFKLPN DSRVERRFHF SQSLTVIHDF LFSLKESPEK
410 420 430 440
FQIEANFPRR VLPCIPSEEW PNPPTLQEAG LSHTEVLFVQ DLTDE
Length:445
Mass (Da):52,623
Last modified:March 1, 2004 - v2
Checksum:iD5510BCB0623096B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088120 mRNA. Translation: BAC22491.1.
BC001069 mRNA. Translation: AAH01069.2.
BC006145 mRNA. Translation: AAH06145.2.
BC014001 mRNA. Translation: AAH14001.2.
AB020694 mRNA. Translation: BAA74910.1.
CCDSiCCDS34296.1.
RefSeqiNP_055428.1. NM_014613.2.
UniGeneiHs.484242.

Genome annotation databases

EnsembliENST00000261942; ENSP00000261942; ENSG00000113194.
GeneIDi23197.
KEGGihsa:23197.
UCSCiuc003mej.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB088120 mRNA. Translation: BAC22491.1.
BC001069 mRNA. Translation: AAH01069.2.
BC006145 mRNA. Translation: AAH06145.2.
BC014001 mRNA. Translation: AAH14001.2.
AB020694 mRNA. Translation: BAA74910.1.
CCDSiCCDS34296.1.
RefSeqiNP_055428.1. NM_014613.2.
UniGeneiHs.484242.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAMNMR-A3-56[»]
ProteinModelPortaliQ96CS3.
SMRiQ96CS3. Positions 2-56, 136-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116806. 187 interactions.
DIPiDIP-46261N.
IntActiQ96CS3. 47 interactions.
STRINGi9606.ENSP00000261942.

PTM databases

iPTMnetiQ96CS3.
PhosphoSiteiQ96CS3.
SwissPalmiQ96CS3.

Polymorphism and mutation databases

BioMutaiFAF2.
DMDMi74731375.

Proteomic databases

EPDiQ96CS3.
MaxQBiQ96CS3.
PaxDbiQ96CS3.
PeptideAtlasiQ96CS3.
PRIDEiQ96CS3.

Protocols and materials databases

DNASUi23197.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261942; ENSP00000261942; ENSG00000113194.
GeneIDi23197.
KEGGihsa:23197.
UCSCiuc003mej.4. human.

Organism-specific databases

CTDi23197.
GeneCardsiFAF2.
HGNCiHGNC:24666. FAF2.
neXtProtiNX_Q96CS3.
PharmGKBiPA162385570.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1363. Eukaryota.
ENOG410XSFS. LUCA.
GeneTreeiENSGT00530000063422.
HOGENOMiHOG000007539.
HOVERGENiHBG101311.
InParanoidiQ96CS3.
KOiK18726.
OMAiPCLPTEE.
PhylomeDBiQ96CS3.
TreeFamiTF314172.

Miscellaneous databases

ChiTaRSiFAF2. human.
EvolutionaryTraceiQ96CS3.
GenomeRNAii23197.
PROiQ96CS3.

Gene expression databases

BgeeiQ96CS3.
CleanExiHS_FAF2.
ExpressionAtlasiQ96CS3. baseline and differential.
GenevisibleiQ96CS3. HS.

Family and domain databases

InterProiIPR012336. Thioredoxin-like_fold.
IPR006577. UAS.
IPR009060. UBA-like.
IPR029071. Ubiquitin-rel_dom.
IPR001012. UBX_dom.
[Graphical view]
PfamiPF00789. UBX. 1 hit.
[Graphical view]
SMARTiSM00594. UAS. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50033. UBX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the highly expressed ETEA gene from blood cells of atopic dermatitis patients."
    Imai Y., Nakada A., Hashida R., Sugita Y., Tanaka T., Tsujimoto G., Matsumoto K., Akasawa A., Saito H., Oshida T.
    Biochem. Biophys. Res. Commun. 297:1282-1290(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: T-cell.
  2. "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: Lung and Muscle.
  3. "Prediction of the coding sequences of unidentified human genes. XII. 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. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-445.
    Tissue: Brain.
  4. "SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins."
    Mueller B., Klemm E.J., Spooner E., Claessen J.H., Ploegh H.L.
    Proc. Natl. Acad. Sci. U.S.A. 105:12325-12330(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH SEL1L, SUBCELLULAR LOCATION, FUNCTION.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct role in the emergence and regression of lipid droplets."
    Zehmer J.K., Bartz R., Bisel B., Liu P., Seemann J., Anderson R.G.W.
    J. Cell Sci. 122:3694-3702(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
    Ernst R., Mueller B., Ploegh H.L., Schlieker C.
    Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YOD1.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover."
    Olzmann J.A., Richter C.M., Kopito R.R.
    Proc. Natl. Acad. Sci. U.S.A. 110:1345-1350(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PNPLA2 AND UBAC2, SUBCELLULAR LOCATION.
  11. "Pathogenic mutation of UBQLN2 impairs its interaction with UBXD8 and disrupts endoplasmic reticulum-associated protein degradation."
    Xia Y., Yan L.H., Huang B., Liu M., Liu X., Huang C.
    J. Neurochem. 129:99-106(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBQLN2.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of the novel identified UBA-like domain in the N-terminal of human ETEA protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 3-56.

Entry informationi

Entry nameiFAF2_HUMAN
AccessioniPrimary (citable) accession number: Q96CS3
Secondary accession number(s): O94963
, Q8IUF2, Q9BRP2, Q9BVM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2004
Last modified: June 8, 2016
This is version 128 of the entry and version 2 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

Miscellaneous

Up-regulated in T-cells and eosinophils from patients with atopic dermatitis.

Caution

It seems odd to name this protein FAS-associated factor, but not have any mention of this in the CC lines.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  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.