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Center for Computational Systems Medicine
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FusionGeneSummary

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FusionProtFeature

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FusionGeneSequence

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FusionGenePPI

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RelatedDrugs

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RelatedDiseases

Fusion gene ID: 36200

FusionGeneSummary for SSRP1_FADS2

check button Fusion gene summary
Fusion gene informationFusion gene name: SSRP1_FADS2
Fusion gene ID: 36200
HgeneTgene
Gene symbol

SSRP1

FADS2

Gene ID

6749

9415

Gene namestructure specific recognition protein 1fatty acid desaturase 2
SynonymsFACT|FACT80|T160D6D|DES6|FADSD6|LLCDL2|SLL0262|TU13
Cytomap

11q12.1

11q12.2

Type of geneprotein-codingprotein-coding
DescriptionFACT complex subunit SSRP1FACT 80 kDa subunitFACTp80chromatin-specific transcription elongation factor 80 kDa subunitcisplatin-DNA SSRPfacilitates chromatin remodeling 80 kDa subunitfacilitates chromatin transcription complex 80 kDa subunitfacilitafatty acid desaturase 2acyl-CoA 6-desaturasedelta-6 fatty acid desaturasedelta-6-desaturaselinoleoyl-CoA desaturase (delta-6-desaturase)-like 2
Modification date2018052220180519
UniProtAcc

Q08945

O95864

Ensembl transtripts involved in fusion geneENST00000278412, ENST00000257261, 
ENST00000522056, ENST00000278840, 
ENST00000521849, ENST00000574708, 
ENST00000522639, ENST00000517839, 
Fusion gene scores* DoF score5 X 5 X 2=5016 X 7 X 7=784
# samples 517
** MAII scorelog2(5/50*10)=0log2(17/784*10)=-2.20531890797751
possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs).
DoF>8 and MAII<0
Context

PubMed: SSRP1 [Title/Abstract] AND FADS2 [Title/Abstract] AND fusion [Title/Abstract]

Functional or gene categories assigned by FusionGDB annotation
* DoF score (Degree of Frequency) = # partners X # break points X # cancer types
** MAII score (Major Active Isofusion Index) = log2(# samples/DoF score*10)

check button Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID

check button Fusion gene information from three resources
(ChiTars (NAR, 2018), tumorfusions (NAR, 2018), Gao et al. (Cell, 2018))
* All genome coordinats were lifted-over on hg19.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.
Data typeSourceCancer typeSampleHgeneHchrHbpHstrandTgeneTchrTbpTstrand
ChiTaRS3.1CX787277SSRP1chr11

57093553

-FADS2chr11

61605334

+
* LD: Li Ding group's fusion gene list
  RV: Roel Verhaak group's fusion gene list
  ChiTaRs fusion database

check button Open reading frame (ORF) analsis of fusion genes based on Ensembl gene isoform structure.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.
ORFHenstTenstHgeneHchrHbpHstrandTgeneTchrTbpTstrand
intron-3CDSENST00000278412ENST00000257261SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-3CDSENST00000278412ENST00000522056SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-3CDSENST00000278412ENST00000278840SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-3CDSENST00000278412ENST00000521849SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-intronENST00000278412ENST00000574708SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-intronENST00000278412ENST00000522639SSRP1chr11

57093553

-FADS2chr11

61605334

+
intron-intronENST00000278412ENST00000517839SSRP1chr11

57093553

-FADS2chr11

61605334

+

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FusionProtFeatures for SSRP1_FADS2


check buttonMain function of each fusion partner protein. (from UniProt)
HgeneTgene
SSRP1

Q08945

FADS2

O95864

Component of the FACT complex, a general chromatinfactor that acts to reorganize nucleosomes. The FACT complex isinvolved in multiple processes that require DNA as a template suchas mRNA elongation, DNA replication and DNA repair. Duringtranscription elongation the FACT complex acts as a histonechaperone that both destabilizes and restores nucleosomalstructure. It facilitates the passage of RNA polymerase II andtranscription by promoting the dissociation of one histone H2A-H2Bdimer from the nucleosome, then subsequently promotes thereestablishment of the nucleosome following the passage of RNApolymerase II. The FACT complex is probably also involved inphosphorylation of 'Ser-392' of p53/TP53 via its association withCK2 (casein kinase II). Binds specifically to double-stranded DNAand at low levels to DNA modified by the antitumor agentcisplatin. May potentiate cisplatin-induced cell death by blockingreplication and repair of modified DNA. Also acts as atranscriptional coactivator for p63/TP63.{ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11239457,ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12934006,ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:9489704,ECO:0000269|PubMed:9566881, ECO:0000269|PubMed:9836642}. Component of a lipid metabolic pathway that catalyzesbiosynthesis of highly unsaturated fatty acids (HUFA) fromprecursor essential polyunsaturated fatty acids (PUFA) linoleicacid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3).Catalyzes the first and rate limiting step in this pathway whichis the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3)respectively and other desaturation steps. Highly unsaturatedfatty acids (HUFA) play pivotal roles in many biologicalfunctions. It catalizes as well the introduction of a cis doublebond in palmitate to produce the mono-unsaturated fatty acidsapienate, the most abundant fatty acid in sebum.{ECO:0000269|PubMed:12713571, ECO:0000269|PubMed:9867867}.

check buttonRetention analysis result of each fusion partner protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at

download page

.

* Minus value of BPloci means that the break pointn is located before the CDS.
- In-frame and retained protein feature among the 13 regional features.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenProtein featureProtein feature note

- In-frame and not-retained protein feature among the 13 regional features.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenProtein featureProtein feature note


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FusionGeneSequence for SSRP1_FADS2


check button For in-frame fusion transcripts, we provide the fusion transcript sequences and fusion amino acid sequences.
(nt: nucleotides, aa: amino acids)

* Fusion amino acid sequences.

* Fusion transcript sequences (only coding sequence (CDS) region).

* Fusion transcript sequences (Full-length transcript).

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FusionGenePPI for SSRP1_FADS2


check button Go to ChiPPI (Chimeric Protein-Protein interactions) to see the chimeric PPI interaction in

ChiPPI page

.

check button Protein-protein interactors with each fusion partner protein in wild-type (BIOGRID-3.4.160)
HgeneHgene's interactorsTgeneTgene's interactors


check button - Retained PPIs in in-frame fusion.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenStill interaction with


check button - Lost PPIs in in-frame fusion.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenInteraction lost with


check button - Retained PPIs, but lost function due to frame-shift fusion.
PartnerGeneHbpTbpENSTStrandBPexonTotalExonProtein feature loci*BPlociTotalLenInteraction lost with


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RelatedDrugs for SSRP1_FADS2


check button Drugs targeting genes involved in this fusion gene.
(DrugBank Version 5.1.0 2018-04-02)
PartnerGeneUniProtAccDrugBank IDDrug nameDrug activityDrug typeDrug status

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RelatedDiseases for SSRP1_FADS2


check button Diseases associated with fusion partners.
(DisGeNet 4.0)
PartnerGeneDisease IDDisease name# pubmedsSource
TgeneFADS2C0005586Bipolar Disorder1PSYGENET
TgeneFADS2C0009404Colorectal Neoplasms1CTD_human
TgeneFADS2C0023794Lipoidosis1CTD_human
TgeneFADS2C0036341Schizophrenia1PSYGENET
TgeneFADS2C4277682Chemical and Drug Induced Liver Injury1CTD_human