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Protein

Cell cycle checkpoint control protein RAD9A

Gene

RAD9A

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

Functioni

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. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.2 Publications

Catalytic activityi

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

GO - Molecular functioni

  • 3'-5' exonuclease activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • exodeoxyribonuclease III activity Source: UniProtKB-EC
  • histone deacetylase binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • DNA damage checkpoint Source: UniProtKB
  • DNA repair Source: GO_Central
  • DNA replication checkpoint Source: ProtInc
  • intra-S DNA damage checkpoint Source: GO_Central
  • positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl

Keywordsi

Molecular functionExonuclease, Hydrolase, Nuclease
Biological processDNA damage

Enzyme and pathway databases

ReactomeiR-HSA-176187 Activation of ATR in response to replication stress
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
SignaLinkiQ99638
SIGNORiQ99638

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle checkpoint control protein RAD9A (EC:3.1.11.2)
Short name:
hRAD9
Alternative name(s):
DNA repair exonuclease rad9 homolog A
Gene namesi
Name:RAD9A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000172613.7
HGNCiHGNC:9827 RAD9A
MIMi603761 gene
neXtProtiNX_Q99638

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28Y → F: Abolishes phosphorylation by ABL1. 1 Publication1
Mutagenesisi272S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-277; A-328; A-341; A-375; A-380 and A-387. 1 Publication1
Mutagenesisi277S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-328; A-341; A-375; A-380 and A-387. 1 Publication1
Mutagenesisi328S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-341; A-375; A-380 and A-387. 1 Publication1
Mutagenesisi341S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-375; A-380 and A-387. 1 Publication1
Mutagenesisi375S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-380 and A-387. 1 Publication1
Mutagenesisi380S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-387. 1 Publication1
Mutagenesisi387S → A: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-380. 1 Publication1

Organism-specific databases

DisGeNETi5883
OpenTargetsiENSG00000172613
PharmGKBiPA294

Polymorphism and mutation databases

BioMutaiRAD9A
DMDMi74717382

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002250001 – 391Cell cycle checkpoint control protein RAD9AAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28Phosphotyrosine1 Publication1
Modified residuei272Phosphoserine1 Publication1
Modified residuei277PhosphoserineCombined sources1 Publication1
Modified residuei328PhosphoserineCombined sources1 Publication1
Modified residuei341Phosphoserine1 Publication1
Modified residuei375PhosphoserineCombined sources1 Publication1
Modified residuei380PhosphoserineCombined sources1 Publication1
Modified residuei387PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Constitutively phosphorylated on serine and threonine amino acids in absence of DNA damage. Hyperphosphorylated by PRKCD and ABL1 upon DNA damage. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99638
MaxQBiQ99638
PaxDbiQ99638
PeptideAtlasiQ99638
PRIDEiQ99638
ProteomicsDBi78371

PTM databases

iPTMnetiQ99638
PhosphoSitePlusiQ99638

Expressioni

Gene expression databases

BgeeiENSG00000172613
CleanExiHS_RAD9A
ExpressionAtlasiQ99638 baseline and differential
GenevisibleiQ99638 HS

Organism-specific databases

HPAiHPA006725
HPA048155

Interactioni

Subunit structurei

Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD9A interacts with BCL2L1, FEN1, PRKCD, RAD9B, HUS1, RAD1, ABL1, RPA1, ATAD5 and RPA2. Interacts with DNAJC7 and RHNO1.14 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • SH3 domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111820, 33 interactors
ComplexPortaliCPX-1829 Checkpoint clamp complex
CORUMiQ99638
DIPiDIP-24255N
DIP-40930N
IntActiQ99638, 7 interactors
MINTiQ99638
STRINGi9606.ENSP00000311360

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi8 – 21Combined sources14
Beta strandi25 – 32Combined sources8
Beta strandi35 – 41Combined sources7
Beta strandi47 – 53Combined sources7
Helixi55 – 57Combined sources3
Beta strandi58 – 62Combined sources5
Beta strandi66 – 68Combined sources3
Beta strandi73 – 76Combined sources4
Helixi77 – 84Combined sources8
Helixi87 – 93Combined sources7
Beta strandi94 – 100Combined sources7
Beta strandi106 – 114Combined sources9
Helixi115 – 117Combined sources3
Beta strandi119 – 125Combined sources7
Helixi138 – 140Combined sources3
Beta strandi142 – 148Combined sources7
Helixi149 – 156Combined sources8
Beta strandi165 – 170Combined sources6
Helixi172 – 174Combined sources3
Beta strandi176 – 181Combined sources6
Beta strandi187 – 189Combined sources3
Beta strandi194 – 199Combined sources6
Helixi201 – 203Combined sources3
Beta strandi205 – 208Combined sources4
Beta strandi214 – 218Combined sources5
Helixi219 – 231Combined sources13
Beta strandi235 – 240Combined sources6
Beta strandi241 – 245Combined sources5
Beta strandi247 – 252Combined sources6
Beta strandi254 – 262Combined sources9
Beta strandi267 – 269Combined sources3

3D structure databases

ProteinModelPortaliQ99638
SMRiQ99638
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99638

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 91Possesses 3'-5' exonuclease activityAdd BLAST41
Regioni266 – 391Sufficient for interaction with ABL11 PublicationAdd BLAST126

Sequence similaritiesi

Belongs to the rad9 family.Curated

Phylogenomic databases

eggNOGiKOG2810 Eukaryota
ENOG410XYYN LUCA
GeneTreeiENSGT00390000005767
HOGENOMiHOG000059650
HOVERGENiHBG058989
InParanoidiQ99638
KOiK10994
OMAiLHCLNGV
OrthoDBiEOG091G0B2E
PhylomeDBiQ99638
TreeFamiTF101212

Family and domain databases

InterProiView protein in InterPro
IPR026584 Rad9
IPR007268 Rad9/Ddc1
PANTHERiPTHR15237 PTHR15237, 1 hit
PfamiView protein in Pfam
PF04139 Rad9, 1 hit
PIRSFiPIRSF009303 Cell_cycle_RAD9, 1 hit

Sequencei

Sequence statusi: Complete.

Q99638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCLVTGGNV KVLGKAVHSL SRIGDELYLE PLEDGLSLRT VNSSRSAYAC
60 70 80 90 100
FLFAPLFFQQ YQAATPGQDL LRCKILMKSF LSVFRSLAML EKTVEKCCIS
110 120 130 140 150
LNGRSSRLVV QLHCKFGVRK THNLSFQDCE SLQAVFDPAS CPHMLRAPAR
160 170 180 190 200
VLGEAVLPFS PALAEVTLGI GRGRRVILRS YHEEEADSTA KAMVTEMCLG
210 220 230 240 250
EEDFQQLQAQ EGVAITFCLK EFRGLLSFAE SANLNLSIHF DAPGRPAIFT
260 270 280 290 300
IKDSLLDGHF VLATLSDTDS HSQDLGSPER HQPVPQLQAH STPHPDDFAN
310 320 330 340 350
DDIDSYMIAM ETTIGNEGSR VLPSISLSPG PQPPKSPGPH SEEEDEAEPS
360 370 380 390
TVPGTPPPKK FRSLFFGSIL APVRSPQGPS PVLAEDSEGE G
Length:391
Mass (Da):42,547
Last modified:May 1, 1997 - v1
Checksum:i4D4D6D4C6E1057D3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12V → A in CAG38746 (Ref. 2) Curated1
Sequence conflicti130E → A in AAH14848 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0254103C → F1 PublicationCorresponds to variant dbSNP:rs11575913Ensembl.1
Natural variantiVAR_05172471L → Q. Corresponds to variant dbSNP:rs2422490Ensembl.1
Natural variantiVAR_025411100S → A1 PublicationCorresponds to variant dbSNP:rs2066492Ensembl.1
Natural variantiVAR_025412239H → R1 PublicationCorresponds to variant dbSNP:rs17880039Ensembl.1
Natural variantiVAR_025413307M → T1 PublicationCorresponds to variant dbSNP:rs17882466Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53174 mRNA Translation: AAB39928.1
CR536508 mRNA Translation: CAG38746.1
AY766122 Genomic DNA Translation: AAU89725.1
AK315348 mRNA Translation: BAG37745.1
CH471076 Genomic DNA Translation: EAW74605.1
BC014848 mRNA Translation: AAH14848.1
CCDSiCCDS8159.1
RefSeqiNP_001230153.1, NM_001243224.1
NP_004575.1, NM_004584.2
UniGeneiHs.655354

Genome annotation databases

EnsembliENST00000307980; ENSP00000311360; ENSG00000172613
GeneIDi5883
KEGGihsa:5883
UCSCiuc001okr.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRAD9A_HUMAN
AccessioniPrimary (citable) accession number: Q99638
Secondary accession number(s): B2RCZ8, Q6FI29, Q96C41
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1997
Last modified: June 20, 2018
This is version 135 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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