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Q99638 (RAD9A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceEvidence 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.30

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.30

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 processDNA damage
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from mutant phenotype Ref.30. 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 DNA damage stimulus

Inferred from direct assay PubMed 9872989. Source: UniProtKB

cellular response to ionizing radiation

Inferred from direct assay Ref.30. Source: UniProtKB

intra-S DNA damage checkpoint

Inferred from electronic annotation. Source: Ensembl

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.10. Source: GOC

positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcheckpoint clamp complex

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_function3'-5' exonuclease activity

Inferred from direct assay Ref.10. Source: UniProtKB

SH3 domain binding

Inferred from physical interaction Ref.14. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 15326225. Source: UniProtKB

exodeoxyribonuclease III activity

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.12Ref.14Ref.15Ref.22Ref.30. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Cell cycle checkpoint control protein RAD9A
PRO_0000225000

Regions

Region51 – 9141Possesses 3'-5' exonuclease activity
Region266 – 391126Sufficient for interaction with ABL1

Amino acid modifications

Modified residue281Phosphotyrosine Ref.14
Modified residue2721Phosphoserine Ref.7
Modified residue2771Phosphoserine Ref.7 Ref.24 Ref.26 Ref.27
Modified residue3281Phosphoserine Ref.7
Modified residue3411Phosphoserine Ref.7
Modified residue3751Phosphoserine Ref.7 Ref.23 Ref.26 Ref.27
Modified residue3801Phosphoserine Ref.7 Ref.23
Modified residue3871Phosphoserine Ref.7 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29

Natural variations

Natural variant31C → F. Ref.3
VAR_025410
Natural variant711L → Q.
Corresponds to variant rs2422490 [ dbSNP | Ensembl ].
VAR_051724
Natural variant1001S → A. Ref.3
Corresponds to variant rs2066492 [ dbSNP | Ensembl ].
VAR_025411
Natural variant2391H → R. Ref.3
Corresponds to variant rs17880039 [ dbSNP | Ensembl ].
VAR_025412
Natural variant3071M → T. Ref.3
Corresponds to variant rs17882466 [ dbSNP | Ensembl ].
VAR_025413

Experimental info

Mutagenesis281Y → F: Abolishes phosphorylation by ABL1. Ref.14
Mutagenesis2721S → 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
Mutagenesis2771S → 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
Mutagenesis3281S → 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
Mutagenesis3411S → 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
Mutagenesis3751S → 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
Mutagenesis3801S → 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
Mutagenesis3871S → 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 conflict121V → A in CAG38746. Ref.2
Sequence conflict1301E → A in AAH14848. Ref.6

Secondary structure

.......................................................... 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99638 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 4D4D6D4C6E1057D3

FASTA39142,547
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.

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.
CCDSCCDS8159.1.
RefSeqNP_001230153.1. NM_001243224.1.
NP_004575.1. NM_004584.2.
UniGeneHs.655354.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A1JX-ray2.50A1-266[»]
3G65X-ray2.90A1-270[»]
3GGRX-ray3.20A1-270[»]
ProteinModelPortalQ99638.
SMRQ99638. Positions 1-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111820. 27 interactions.
DIPDIP-24255N.
DIP-40930N.
IntActQ99638. 7 interactions.
MINTMINT-134869.
STRING9606.ENSP00000311360.

PTM databases

PhosphoSiteQ99638.

Polymorphism databases

DMDM74717382.

Proteomic databases

MaxQBQ99638.
PaxDbQ99638.
PeptideAtlasQ99638.
PRIDEQ99638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307980; ENSP00000311360; ENSG00000172613.
GeneID5883.
KEGGhsa:5883.
UCSCuc001okr.3. human.

Organism-specific databases

CTD5883.
GeneCardsGC11P067159.
HGNCHGNC:9827. RAD9A.
HPAHPA006725.
HPA048155.
MIM603761. gene.
neXtProtNX_Q99638.
PharmGKBPA294.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236850.
HOGENOMHOG000059650.
HOVERGENHBG058989.
InParanoidQ99638.
KOK10994.
OMAVILRSYQ.
OrthoDBEOG70PBXW.
PhylomeDBQ99638.
TreeFamTF101212.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkQ99638.

Gene expression databases

ArrayExpressQ99638.
BgeeQ99638.
CleanExHS_RAD9A.
GenevestigatorQ99638.

Family and domain databases

InterProIPR026584. Rad9.
IPR007268. Rad9/Ddc1.
[Graphical view]
PANTHERPTHR15237. PTHR15237. 1 hit.
PfamPF04139. Rad9. 1 hit.
[Graphical view]
PIRSFPIRSF009303. Cell_cycle_RAD9. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRAD9A. human.
EvolutionaryTraceQ99638.
GeneWikiRAD9A.
GenomeRNAi5883.
NextBio22862.
PROQ99638.
SOURCESearch...

Entry information

Entry nameRAD9A_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM