HUS1 report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of HUS1 at tissue level.

III. Associated gene sets

GO_0044778Biological processmeiotic DNA integrity checkpoint signaling
GO_0006281Biological processDNA repair
GO_0006289Biological processnucleotide-excision repair
GO_0006974Biological processDNA damage response
GO_0009411Biological processresponse to UV
GO_0009792Biological processembryo development ending in birth or egg hatching
GO_0001932Biological processregulation of protein phosphorylation
GO_0000724Biological processdouble-strand break repair via homologous recombination
GO_0000723Biological processtelomere maintenance
GO_0033314Biological processmitotic DNA replication checkpoint signaling
GO_0031573Biological processmitotic intra-S DNA damage checkpoint signaling
GO_0071479Biological processcellular response to ionizing radiation
GO_0000077Biological processDNA damage checkpoint signaling
GO_0005730Cellular componentnucleolus
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0030896Cellular componentcheckpoint clamp complex
GO_0035861Cellular componentsite of double-strand break
GO_0005634Cellular componentnucleus
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameHUS1
Protein nameHUS1 checkpoint clamp component
Checkpoint protein HUS1 (hHUS1)
Checkpoint protein
Synonymstcag7.704
hCG_17018
DescriptionFUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair . The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex . Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) . The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates . The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase . .

AccessionsENST00000258774.10 [O60921-1]
ENST00000432325.5 [O60921-2]
F8WAW9
ENST00000442024.5
ENST00000458191.5 [O60921-2]
A4D2F2
H7C272
O60921
ENST00000432627.5
C9JA95
C9JCK8
ENST00000446009.1
ENST00000433977.5