Q99638 (RAD9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell cycle checkpoint control protein RAD9A
Short name=hRAD9
EC=3.1.11.2

Alternative name(s):
DNA repair exonuclease rad9 homolog A

Gene names

Name:

RAD9A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.29
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Subunit structure	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. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.29
Subcellular location	Nucleus Ref.16.
Post-translational modification	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. Ref.7 Ref.14 Ref.16
Sequence similarities	Belongs to the rad9 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Inferred from mutant phenotype Ref.29. Source: UniProtKB DNA repair Traceable author statement Ref.1. Source: ProtInc DNA replication Traceable author statement. Source: Reactome DNA replication checkpoint Traceable author statement Ref.1. Source: ProtInc cellular response to ionizing radiation Inferred from direct assay Ref.29. Source: UniProtKB positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara
Cellular_component	checkpoint clamp complex Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	3'-5' exonuclease activity Inferred from direct assay Ref.10. Source: UniProtKB exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HUS1	O60921	5	EBI-2606224,EBI-1056174
RAD1	O60671	2	EBI-2606224,EBI-721835

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 391

391

Cell cycle checkpoint control protein RAD9A

PRO_0000225000

Regions

Region

51 – 91

41

Possesses 3'-5' exonuclease activity

Region

266 – 391

126

Sufficient for interaction with ABL1

Amino acid modifications

Modified residue

28

1

Phosphotyrosine Ref.14

Modified residue

272

1

Phosphoserine Ref.7

Modified residue

277

1

Phosphoserine Ref.7 Ref.24 Ref.25 Ref.26

Modified residue

328

1

Phosphoserine Ref.7

Modified residue

341

1

Phosphoserine Ref.7

Modified residue

375

1

Phosphoserine Ref.7 Ref.23 Ref.25 Ref.26

Modified residue

380

1

Phosphoserine Ref.7 Ref.23

Modified residue

387

1

Phosphoserine Ref.7 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28

Natural variations

Natural variant

3

1

C → F. Ref.3

VAR_025410

Natural variant

71

1

L → Q.
Corresponds to variant rs2422490 [ dbSNP | Ensembl ].

VAR_051724

Natural variant

100

1

S → A. Ref.3
Corresponds to variant rs2066492 [ dbSNP | Ensembl ].

VAR_025411

Natural variant

239

1

H → R. Ref.3
Corresponds to variant rs17880039 [ dbSNP | Ensembl ].

VAR_025412

Natural variant

307

1

M → T. Ref.3
Corresponds to variant rs17882466 [ dbSNP | Ensembl ].

VAR_025413

Experimental info

Mutagenesis

28

1

Y → F: Abolishes phosphorylation by ABL1. Ref.14

Mutagenesis

272

1

S → 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. Ref.7

Mutagenesis

277

1

S → 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. Ref.7

Mutagenesis

328

1

S → 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. Ref.7

Mutagenesis

341

1

S → 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. Ref.7

Mutagenesis

375

1

S → 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. Ref.7

Mutagenesis

380

1

S → 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. Ref.7

Mutagenesis

387

1

S → 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. Ref.7

Sequence conflict

12

1

V → A in CAG38746. Ref.2

Sequence conflict

130

1

E → A in AAH14848. Ref.6

Secondary structure

1

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391

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

8 – 21

14

Beta strand

25 – 32

8

Beta strand

35 – 41

7

Beta strand

47 – 53

7

Helix

55 – 57

3

Beta strand

58 – 62

5

Beta strand

66 – 68

3

Beta strand

73 – 76

4

Helix

77 – 84

8

Helix

87 – 93

7

Beta strand

94 – 100

7

Beta strand

106 – 114

9

Helix

115 – 117

3

Beta strand

119 – 125

7

Helix

138 – 140

3

Beta strand

142 – 148

7

Helix

149 – 156

8

Beta strand

165 – 170

6

Helix

172 – 174

3

Beta strand

176 – 181

6

Beta strand

187 – 189

3

Beta strand

194 – 199

6

Helix

201 – 203

3

Beta strand

205 – 208

4

Beta strand

214 – 218

5

Helix

219 – 231

13

Beta strand

235 – 240

6

Beta strand

241 – 245

5

Beta strand

247 – 252

6

Beta strand

254 – 262

9

Beta strand

267 – 269

3

Sequences

	Sequence		Length	Mass (Da)
	Q99638 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 4D4D6D4C6E1057D3	FASTA	391	42,547
	10 20 30 40 50 60 MKCLVTGGNV KVLGKAVHSL SRIGDELYLE PLEDGLSLRT VNSSRSAYAC FLFAPLFFQQ 70 80 90 100 110 120 YQAATPGQDL LRCKILMKSF LSVFRSLAML EKTVEKCCIS LNGRSSRLVV QLHCKFGVRK 130 140 150 160 170 180 THNLSFQDCE SLQAVFDPAS CPHMLRAPAR VLGEAVLPFS PALAEVTLGI GRGRRVILRS 190 200 210 220 230 240 YHEEEADSTA KAMVTEMCLG EEDFQQLQAQ EGVAITFCLK EFRGLLSFAE SANLNLSIHF 250 260 270 280 290 300 DAPGRPAIFT IKDSLLDGHF VLATLSDTDS HSQDLGSPER HQPVPQLQAH STPHPDDFAN 310 320 330 340 350 360 DDIDSYMIAM ETTIGNEGSR VLPSISLSPG PQPPKSPGPH SEEEDEAEPS TVPGTPPPKK 370 380 390 FRSLFFGSIL APVRSPQGPS PVLAEDSEGE G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control gene." Lieberman H.B., Hopkins K.M., Nass M., Demetrick D., Davey S. Proc. Natl. Acad. Sci. U.S.A. 93:13890-13895(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIEHS SNPs program Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-3; ALA-100; ARG-239 AND THR-307.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[7]	"Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling." Roos-Mattjus P., Hopkins K.M., Oestreich A.J., Vroman B.T., Johnson K.L., Naylor S., Lieberman H.B., Karnitz L.M. J. Biol. Chem. 278:24428-24437(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 270-280; 326-329; 373-383 AND 385-390, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-272; SER-277; SER-328; SER-341; SER-375; SER-380 AND SER-387, MUTAGENESIS OF SER-272; SER-277; SER-328; SER-341; SER-375; SER-380 AND SER-387.
[8]	"The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1." St Onge R.P., Udell C.M., Casselman R., Davey S. Mol. Biol. Cell 10:1985-1995(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUS1 AND RAD1.
[9]	"Physical interaction among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression." Hang H., Lieberman H.B. Genomics 65:24-33(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUS1 AND RAD1.
[10]	"Human DNA damage checkpoint protein hRAD9 is a 3' to 5' exonuclease." Bessho T., Sancar A. J. Biol. Chem. 275:7451-7454(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EXONUCLEASE ACTIVITY.
[11]	"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins." Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D. J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH HDAC1.
[12]	"The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9." Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M. J. Biol. Chem. 275:29767-29771(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RAD17.
[13]	"The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9." Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C. Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNAJC7.
[14]	"c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage." Yoshida K., Komatsu K., Wang H.-G., Kufe D. Mol. Cell. Biol. 22:3292-3300(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABL1 AND BCL2L1, PHOSPHORYLATION, PHOSPHORYLATION AT TYR-28, MUTAGENESIS OF TYR-28.
[15]	"Expression of mammalian paralogues of HRAD9 and Mrad9 checkpoint control genes in normal and cancerous testicular tissue." Hopkins K.M., Wang X., Berlin A., Hang H., Thaker H.M., Lieberman H.B. Cancer Res. 63:5291-5298(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAD9B.
[16]	"Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9." Yoshida K., Wang H.-G., Miki Y., Kufe D. EMBO J. 22:1431-1441(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKCD, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[17]	"Loading of the human 9-1-1 checkpoint complex onto DNA by the checkpoint clamp loader hRad17-replication factor C complex in vitro." Bermudez V.P., Lindsey-Boltz L.A., Cesare A.J., Maniwa Y., Griffith J.D., Hurwitz J., Sancar A. Proc. Natl. Acad. Sci. U.S.A. 100:1633-1638(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION OF THE 9-1-1 COMPLEX WITH THE RAD17-RFC COMPLEX, ELECTRON MICROSCOPY OF THE 9-1-1 AND RAD17-RFC COMPLEXES BOUND TO DNA.
[18]	"The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair." Toueille M., El-Andaloussi N., Frouin I., Freire R., Funk D., Shevelev I., Friedrich-Heineken E., Villani G., Hottiger M.O., Huebscher U. Nucleic Acids Res. 32:3316-3324(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH POLB.
[19]	"The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1." Wang W., Brandt P., Rossi M.L., Lindsey-Boltz L., Podust V., Fanning E., Sancar A., Bambara R.A. Proc. Natl. Acad. Sci. U.S.A. 101:16762-16767(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1.
[20]	"The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery." Smirnova E., Toueille M., Markkanen E., Huebscher U. Biochem. J. 389:13-17(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH LIG1.
[21]	"The two DNA clamps Rad9/Rad1/Hus1 complex and proliferating cell nuclear antigen differentially regulate flap endonuclease 1 activity." Friedrich-Heineken E., Toueille M., Taennler B., Buerki C., Ferrari E., Hottiger M.O., Huebscher U. J. Mol. Biol. 353:980-989(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH FEN1, INTERACTION WITH FEN1.
[22]	"Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cells." Wu X., Shell S.M., Zou Y. Oncogene 24:4728-4735(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE 9-1-1 COMPLEX ASSOCIATED WITH RPA1 AND RPA2, INTERACTION WITH RPA1 AND RPA2.
[23]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-380 AND SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-375 AND SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, MASS SPECTROMETRY.
[29]	"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling." Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J. Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RHNO1, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005277.

RefSeq

NP_001230153.1. NM_001243224.1.
NP_004575.1. NM_004584.2.

UniGene

Hs.655354.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A1J	X-ray	2.50	A	1-266	[»]
3G65	X-ray	2.90	A	1-270	[»]
3GGR	X-ray	3.20	A	1-270	[»]

ProteinModelPortal

Q99638.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24255N.
DIP-40930N.

IntAct

Q99638. 2 interactions.

MINT

MINT-134869.

STRING

9606.ENSP00000311360.

PTM databases

PhosphoSite

Q99638.

Polymorphism databases

DMDM

74717382.

Proteomic databases

PaxDb

Q99638.

PeptideAtlas

Q99638.

PRIDE

Q99638.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307980; ENSP00000311360; ENSG00000172613.

GeneID

5883.

KEGG

hsa:5883.

UCSC

uc001okr.3. human.

Organism-specific databases

CTD

5883.

GeneCards

GC11P067159.

HGNC

HGNC:9827. RAD9A.

HPA

HPA006725.

MIM

603761. gene.

neXtProt

NX_Q99638.

PharmGKB

PA294.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG236850.

HOGENOM

HOG000059650.

HOVERGEN

HBG058989.

InParanoid

Q99638.

KO

K10994.

OMA

GVAITFC.

OrthoDB

EOG4QNMWT.

PhylomeDB

Q99638.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q99638.

Bgee

Q99638.

CleanEx

HS_RAD9A.

Genevestigator

Q99638.

GermOnline

ENSG00000172613. Homo sapiens.

Family and domain databases

InterPro

IPR026584. Rad9.
IPR007268. Rad9/Ddc1.
[Graphical view]

PANTHER

PTHR15237. PTHR15237. 1 hit.

Pfam

PF04139. Rad9. 1 hit.
[Graphical view]

PIRSF

PIRSF009303. Cell_cycle_RAD9. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RAD9A. human.

EvolutionaryTrace

Q99638.

GenomeRNAi

5883.

NextBio

22862.

SOURCE

Search...

Entry information

Entry name

RAD9A_HUMAN

Accession

Primary (citable) accession number: Q99638
Secondary accession number(s): B2RCZ8, Q6FI29, Q96C41

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.