RAD9A report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_1902231Biological processpositive regulation of intrinsic apoptotic signaling pathway in response to DNA damage
GO_0006281Biological processDNA repair
GO_0006974Biological processDNA damage response
GO_0008630Biological processintrinsic apoptotic signaling pathway in response to DNA damage
GO_0031573Biological processmitotic intra-S DNA damage checkpoint signaling
GO_0071479Biological processcellular response to ionizing radiation
GO_0000076Biological processDNA replication checkpoint signaling
GO_0000077Biological processDNA damage checkpoint signaling
GO_0005654Cellular componentnucleoplasm
GO_0030896Cellular componentcheckpoint clamp complex
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_0019899Molecular functionenzyme binding
GO_0019901Molecular functionprotein kinase binding
GO_0008408Molecular function3'-5' exonuclease activity
GO_0008311Molecular functiondouble-stranded DNA 3'-5' DNA exonuclease activity
GO_0017124Molecular functionSH3 domain binding
GO_0005515Molecular functionprotein binding
GO_0042826Molecular functionhistone deacetylase binding

IV. Literature review

[source]
Gene nameRAD9A
Protein nameCell cycle checkpoint control protein RAD9A (hRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A)
RAD9 checkpoint clamp component A
RAD9 homolog A (S. pombe)
Synonyms
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 . RAD9A possesses 3'->5' double stranded DNA exonuclease activity . .

AccessionsENST00000544620.5
ENST00000542139.1
F5H492
F5H8A2
ENST00000307980.7
Q99638
ENST00000538013.5
ENST00000621995.1
A0A0G2JMD0
C4TNW8
F5H4F1
C4TNW7