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HUMAN:FAF1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) FAF1 (synonyms: UBXD12, UBXN3A)
Protein Name(s) FAS-associated factor 1

hFAF1 UBX domain-containing protein 12 UBX domain-containing protein 3A

External Links
UniProt Q9UNN5
EMBL AF106798
AF094700
AF136173
AJ271408
AF132938
AL359977
AC091610
AC118557
AL049637
AL603746
AL603746
AC091610
AC118557
AL049637
AL359977
CH471059
BC004970
BC067100
AL133631
CCDS CCDS554.1
PIR JC7093
T43466
RefSeq NP_008982.1
UniGene Hs.530402
PDB 1H8C
2DZM
2EC4
3E21
3QC8
3QCA
3QQ8
3QWZ
3QX1
3R3M
PDBsum 1H8C
2DZM
2EC4
3E21
3QC8
3QCA
3QQ8
3QWZ
3QX1
3R3M
ProteinModelPortal Q9UNN5
SMR Q9UNN5
BioGrid 116298
DIP DIP-38245N
IntAct Q9UNN5
MINT MINT-88745
STRING 9606.ENSP00000379457
PhosphoSite Q9UNN5
DMDM 20454906
MaxQB Q9UNN5
PaxDb Q9UNN5
PRIDE Q9UNN5
DNASU 11124
Ensembl ENST00000396153
GeneID 11124
KEGG hsa:11124
UCSC uc001cse.1
CTD 11124
GeneCards GC01M050905
HGNC HGNC:3578
HPA HPA018253
HPA019008
MIM 604460
neXtProt NX_Q9UNN5
PharmGKB PA27976
eggNOG NOG288188
GeneTree ENSGT00530000063422
HOGENOM HOG000043073
HOVERGEN HBG002876
InParanoid Q9UNN5
OMA VLSNVFC
OrthoDB EOG72NRPV
PhylomeDB Q9UNN5
TreeFam TF314172
SignaLink Q9UNN5
ChiTaRS FAF1
EvolutionaryTrace Q9UNN5
GeneWiki FAF1
GenomeRNAi 11124
NextBio 42280
PRO PR:Q9UNN5
Proteomes UP000005640
Bgee Q9UNN5
CleanEx HS_FAF1
ExpressionAtlas Q9UNN5
Genevestigator Q9UNN5
GO GO:0031265
GO:0034098
GO:0005829
GO:0005635
GO:0005634
GO:0048471
GO:0031072
GO:0051059
GO:0019901
GO:0019887
GO:0043130
GO:0031625
GO:0006915
GO:0008219
GO:0007253
GO:0043065
GO:1902043
GO:0031334
GO:0043161
GO:0030155
GO:0042176
GO:0045859
InterPro IPR012336
IPR006577
IPR029071
IPR001012
Pfam PF00789
SMART SM00594
SM00166
SUPFAM SSF52833
SSF54236
PROSITE PS50033

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0010942

positive regulation of cell death

PMID:15596450[1]

ECO:0000314

P

Figure 9 demonstrates hFAF1 ability to induce apoptosis, specifically through heat shock. The graph in figure 9 shows that HSP+ hFAF1 had the lowest cell viability of all samples proposed and cell viability was confirmed through 3-2, 5-diphenyltetrazolium bromide assay.

complete
CACAO 9754

GO:0008219

cell death

PMID:22876279[2]

ECO:0000315

P

Figure 4 B & C shows the pro-apoptosis abilities of hFAF1. The plates show that in those cells where hFAF1 was knocked out there was a significant increase in cell growth, in contrast those plates where the hFAF1 was left functioning properly there was a lack of cell growth, which was due to hFAF1 ability to break down HSP 70. This is again shown in the table, which specifically points out the amount of colonies.

complete
CACAO 9784

involved_in

GO:0010942

positive regulation of cell death

PMID:15596450[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1903364

positive regulation of cellular protein catabolic process

PMID:26842564[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:Q9H211)

Seeded From UniProt

complete

involved_in

GO:0045740

positive regulation of DNA replication

PMID:26842564[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:26842564[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0043130

ubiquitin binding

PMID:18775313[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0034098

VCP-NPL4-UFD1 AAA ATPase complex

PMID:18775313[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0031625

ubiquitin protein ligase binding

PMID:18775313[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051059

NF-kappaB binding

PMID:14600157[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q04206

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:11713579[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0043161

proteasome-mediated ubiquitin-dependent protein catabolic process

PMID:15743842[7]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043065

positive regulation of apoptotic process

PMID:10462485[8]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042176

regulation of protein catabolic process

PMID:15743842[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031334

positive regulation of protein complex assembly

PMID:15688372[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0031265

CD95 death-inducing signaling complex

PMID:12702723[10]

ECO:0000303

author statement without traceable support used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:15596450[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019901

protein kinase binding

PMID:11713579[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019887

protein kinase regulator activity

PMID:11713579[6]

ECO:0000303

author statement without traceable support used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0008219

cell death

PMID:15743842[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007253

cytoplasmic sequestering of NF-kappaB

PMID:14600157[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15596450[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:15596450[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045859

regulation of protein kinase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0019887

P

Seeded From UniProt

complete

involved_in

GO:1902043

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P54731
ensembl:ENSMUSP00000099785

P

Seeded From UniProt

complete

involved_in

GO:0030155

regulation of cell adhesion

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P54731
ensembl:ENSMUSP00000099785

P

Seeded From UniProt

complete

enables

GO:0019904

protein domain specific binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P54731
ensembl:ENSMUSP00000099785

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P54731
ensembl:ENSMUSP00000099785

C

Seeded From UniProt

complete

part_of

GO:0005635

nuclear envelope

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P54731
ensembl:ENSMUSP00000099785

C

Seeded From UniProt

complete

involved_in

GO:0008219

cell death

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033043

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0006915

apoptotic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0053

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 Kim, HJ et al. (2005) Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity. J. Biol. Chem. 280 8125-33 PubMed GONUTS page
  2. Lee, JJ et al. (2012) Ubiquitin-associated (UBA) domain in human Fas associated factor 1 inhibits tumor formation by promoting Hsp70 degradation. PLoS ONE 7 e40361 PubMed GONUTS page
  3. 3.0 3.1 3.2 Franz, A et al. (2016) Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard DNA replication fork progression. Nat Commun 7 10612 PubMed GONUTS page
  4. 4.0 4.1 4.2 Alexandru, G et al. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134 804-16 PubMed GONUTS page
  5. 5.0 5.1 Park, MY et al. (2004) Fas-associated factor-1 inhibits nuclear factor-kappaB (NF-kappaB) activity by interfering with nuclear translocation of the RelA (p65) subunit of NF-kappaB. J. Biol. Chem. 279 2544-9 PubMed GONUTS page
  6. 6.0 6.1 6.2 Guerra, B et al. (2001) FAS-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction. Int. J. Oncol. 19 1117-26 PubMed GONUTS page
  7. 7.0 7.1 7.2 Song, EJ et al. (2005) Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway. Mol. Cell. Biol. 25 2511-24 PubMed GONUTS page
  8. Ryu, SW et al. (1999) Identification and characterization of human Fas associated factor 1, hFAF1. Biochem. Biophys. Res. Commun. 262 388-94 PubMed GONUTS page
  9. Park, MY et al. (2005) Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation. Int. J. Cancer 115 412-8 PubMed GONUTS page
  10. Ryu, SW et al. (2003) Fas-associated factor 1, FAF1, is a member of Fas death-inducing signaling complex. J. Biol. Chem. 278 24003-10 PubMed GONUTS page