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Q8WXE1

- ATRIP_HUMAN

UniProt

Q8WXE1 - ATRIP_HUMAN

Protein

ATR-interacting protein

Gene

ATRIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA damage checkpoint Source: UniProtKB
    2. DNA repair Source: UniProtKB-KW
    3. DNA replication Source: Reactome

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    ReactomeiREACT_6769. Activation of ATR in response to replication stress.
    REACT_897. G2/M DNA damage checkpoint.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATR-interacting protein
    Alternative name(s):
    ATM and Rad3-related-interacting protein
    Gene namesi
    Name:ATRIP
    Synonyms:AGS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:33499. ATRIP.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Redistributes to discrete nuclear foci upon DNA damage.

    GO - Cellular componenti

    1. microtubule cytoskeleton Source: HPA
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi769 – 7702EE → AA: Abolishes interaction with ATR and its recruitment to sites of DNA damage. 1 Publication
    Mutagenesisi774 – 7752DD → AA: Abolishes interaction with ATR and its recruitment to sites of DNA damage. 1 Publication

    Organism-specific databases

    Orphaneti808. Seckel syndrome.
    PharmGKBiPA162377290.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 791790ATR-interacting proteinPRO_0000064740Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Cross-linki96 – 96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei224 – 2241Phosphoserine4 Publications
    Modified residuei518 – 5181Phosphoserine5 Publications

    Post-translational modificationi

    Phosphorylated by ATR.6 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8WXE1.
    PaxDbiQ8WXE1.
    PRIDEiQ8WXE1.

    PTM databases

    PhosphoSiteiQ8WXE1.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ8WXE1.
    BgeeiQ8WXE1.
    CleanExiHS_ATRIP.
    GenevestigatoriQ8WXE1.

    Organism-specific databases

    HPAiCAB033109.
    HPA030683.

    Interactioni

    Subunit structurei

    Interacts with ATR By similarity. Heterodimer with ATR. The heterodimer binds the RPA complex and is then recruited to single-stranded DNA. Interacts with CEP164 (via N-terminus). Interacts with CINP.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK9P507503EBI-747353,EBI-1383449

    Protein-protein interaction databases

    BioGridi313463. 24 interactions.
    DIPiDIP-46495N.
    IntActiQ8WXE1. 8 interactions.
    MINTiMINT-5009350.

    Structurei

    Secondary structure

    1
    791
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi57 – 637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IGKX-ray1.75C/D237-243[»]
    4NB3X-ray1.35C/D54-67[»]
    ProteinModelPortaliQ8WXE1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni118 – 15639Interaction with CINPAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili108 – 217110Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi769 – 7768EEXXXDL motif

    Domaini

    The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.1 Publication

    Sequence similaritiesi

    Belongs to the ATRIP family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG87267.
    HOVERGENiHBG050618.
    InParanoidiQ8WXE1.
    KOiK10905.
    OMAiTGSNCQC.
    OrthoDBiEOG744T92.
    PhylomeDBiQ8WXE1.
    TreeFamiTF324417.

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WXE1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGTSAPGSK RRSEPPAPRP GPPPGTGHPP SKRARGFSAA AAPDPDDPFG    50
    AHGDFTADDL EELDTLASQA LSQCPAAARD VSSDHKVHRL LDGMSKNPSG 100
    KNRETVPIKD NFELEVLQAQ YKELKEKMKV MEEEVLIKNG EIKILRDSLH 150
    QTESVLEEQR RSHFLLEQEK TQALSDKEKE FSKKLQSLQS ELQFKDAEMN 200
    ELRTKLQTSE RANKLAAPSV SHVSPRKNPS VVIKPEACSP QFGKTSFPTK 250
    ESFSANMSLP HPCQTESGYK PLVGREDSKP HSLRGDSIKQ EEAQKSFVDS 300
    WRQRSNTQGS ILINLLLKQP LIPGSSLSLC HLLSSSSESP AGTPLQPPGF 350
    GSTLAGMSGL RTTGSYDGSF SLSALREAQN LAFTGLNLVA RNECSRDGDP 400
    AEGGRRAFPL CQLPGAVHFL PLVQFFIGLH CQALQDLAAA KRSGAPGDSP 450
    THSSCVSSGV ETNPEDSVCI LEGFSVTALS ILQHLVCHSG AVVSLLLSGV 500
    GADSAAGEGN RSLVHRLSDG DMTSALRGVA DDQGQHPLLK MLLHLLAFSS 550
    AATGHLQASV LTQCLKVLVK LAENTSCDFL PRFQCVFQVL PKCLSPETPL 600
    PSVLLAVELL SLLADHDQLA PQLCSHSEGC LLLLLYMYIT SRPDRVALET 650
    QWLQLEQEVV WLLAKLGVQS PLPPVTGSNC QCNVEVVRAL TVMLHRQWLT 700
    VRRAGGPPRT DQQRRTVRCL RDTVLLLHGL SQKDKLFMMH CVEVLHQFDQ 750
    VMPGVSMLIR GLPDVTDCEE AALDDLCAAE TDVEDPEVEC G 791
    Length:791
    Mass (Da):85,838
    Last modified:March 1, 2002 - v1
    Checksum:i58981602F7961756
    GO
    Isoform 2 (identifier: Q8WXE1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         661-687: Missing.

    Show »
    Length:764
    Mass (Da):83,003
    Checksum:i94E7E31A6BCAAC1D
    GO
    Isoform 3 (identifier: Q8WXE1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-93: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:698
    Mass (Da):76,336
    Checksum:i417F5811408F2799
    GO
    Isoform 4 (identifier: Q8WXE1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-127: Missing.

    Show »
    Length:664
    Mass (Da):72,362
    Checksum:i460E7E097BCA1C30
    GO

    Sequence cautioni

    The sequence BAB14029.1 differs from that shown. Reason: Frameshift at position 650.
    The sequence BAB14029.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAF84257.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti280 – 2801P → L in AAH14153. (PubMed:15489334)Curated
    Sequence conflicti343 – 3431T → A in BAF84257. (PubMed:14702039)Curated
    Sequence conflicti492 – 4921V → I in BAF84257. (PubMed:14702039)Curated
    Sequence conflicti647 – 6471A → T in BAG62254. (PubMed:14702039)Curated
    Sequence conflicti683 – 6831N → D in BAF84257. (PubMed:14702039)Curated
    Sequence conflicti687 – 6871V → I in AAH30597. (PubMed:15489334)Curated
    Sequence conflicti712 – 7121Q → K in BAF84257. (PubMed:14702039)Curated
    Sequence conflicti777 – 7771C → G in BAF84257. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251K → Q.
    Corresponds to variant rs11925638 [ dbSNP | Ensembl ].
    VAR_050683
    Natural varianti240 – 2401P → L.
    Corresponds to variant rs35240314 [ dbSNP | Ensembl ].
    VAR_050684

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 127127Missing in isoform 4. 1 PublicationVSP_047011Add
    BLAST
    Alternative sequencei1 – 9393Missing in isoform 3. 1 PublicationVSP_010501Add
    BLAST
    Alternative sequencei661 – 68727Missing in isoform 2. 2 PublicationsVSP_010504Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF451323 mRNA. Translation: AAL38042.1.
    AK022405 mRNA. Translation: BAB14029.1. Sequence problems.
    AK291568 mRNA. Translation: BAF84257.1. Different initiation.
    AK291829 mRNA. Translation: BAF84518.1.
    AK315075 mRNA. Translation: BAG37544.1.
    AK300548 mRNA. Translation: BAG62254.1.
    AC104448 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64876.1.
    CH471055 Genomic DNA. Translation: EAW64878.1.
    BC014153 mRNA. Translation: AAH14153.2.
    BC020563 mRNA. Translation: AAH20563.1.
    BC030597 mRNA. Translation: AAH30597.1.
    AL832917 mRNA. Translation: CAH10621.1.
    CCDSiCCDS2767.1. [Q8WXE1-2]
    CCDS2768.1. [Q8WXE1-1]
    CCDS59449.1. [Q8WXE1-3]
    CCDS59450.1. [Q8WXE1-5]
    RefSeqiNP_001257951.1. NM_001271022.1. [Q8WXE1-5]
    NP_001257952.1. NM_001271023.1. [Q8WXE1-3]
    NP_115542.2. NM_032166.3. [Q8WXE1-2]
    NP_569055.1. NM_130384.2. [Q8WXE1-1]
    UniGeneiHs.694840.

    Genome annotation databases

    EnsembliENST00000320211; ENSP00000323099; ENSG00000164053. [Q8WXE1-1]
    ENST00000346691; ENSP00000302338; ENSG00000164053. [Q8WXE1-2]
    ENST00000357105; ENSP00000349620; ENSG00000164053. [Q8WXE1-5]
    ENST00000412052; ENSP00000400930; ENSG00000164053. [Q8WXE1-3]
    GeneIDi84126.
    KEGGihsa:84126.
    UCSCiuc003ctf.2. human. [Q8WXE1-1]
    uc003ctg.2. human. [Q8WXE1-2]

    Polymorphism databases

    DMDMi48428109.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF451323 mRNA. Translation: AAL38042.1 .
    AK022405 mRNA. Translation: BAB14029.1 . Sequence problems.
    AK291568 mRNA. Translation: BAF84257.1 . Different initiation.
    AK291829 mRNA. Translation: BAF84518.1 .
    AK315075 mRNA. Translation: BAG37544.1 .
    AK300548 mRNA. Translation: BAG62254.1 .
    AC104448 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64876.1 .
    CH471055 Genomic DNA. Translation: EAW64878.1 .
    BC014153 mRNA. Translation: AAH14153.2 .
    BC020563 mRNA. Translation: AAH20563.1 .
    BC030597 mRNA. Translation: AAH30597.1 .
    AL832917 mRNA. Translation: CAH10621.1 .
    CCDSi CCDS2767.1. [Q8WXE1-2 ]
    CCDS2768.1. [Q8WXE1-1 ]
    CCDS59449.1. [Q8WXE1-3 ]
    CCDS59450.1. [Q8WXE1-5 ]
    RefSeqi NP_001257951.1. NM_001271022.1. [Q8WXE1-5 ]
    NP_001257952.1. NM_001271023.1. [Q8WXE1-3 ]
    NP_115542.2. NM_032166.3. [Q8WXE1-2 ]
    NP_569055.1. NM_130384.2. [Q8WXE1-1 ]
    UniGenei Hs.694840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IGK X-ray 1.75 C/D 237-243 [» ]
    4NB3 X-ray 1.35 C/D 54-67 [» ]
    ProteinModelPortali Q8WXE1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 313463. 24 interactions.
    DIPi DIP-46495N.
    IntActi Q8WXE1. 8 interactions.
    MINTi MINT-5009350.

    PTM databases

    PhosphoSitei Q8WXE1.

    Polymorphism databases

    DMDMi 48428109.

    Proteomic databases

    MaxQBi Q8WXE1.
    PaxDbi Q8WXE1.
    PRIDEi Q8WXE1.

    Protocols and materials databases

    DNASUi 84126.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320211 ; ENSP00000323099 ; ENSG00000164053 . [Q8WXE1-1 ]
    ENST00000346691 ; ENSP00000302338 ; ENSG00000164053 . [Q8WXE1-2 ]
    ENST00000357105 ; ENSP00000349620 ; ENSG00000164053 . [Q8WXE1-5 ]
    ENST00000412052 ; ENSP00000400930 ; ENSG00000164053 . [Q8WXE1-3 ]
    GeneIDi 84126.
    KEGGi hsa:84126.
    UCSCi uc003ctf.2. human. [Q8WXE1-1 ]
    uc003ctg.2. human. [Q8WXE1-2 ]

    Organism-specific databases

    CTDi 84126.
    GeneCardsi GC03P048488.
    GeneReviewsi ATRIP.
    HGNCi HGNC:33499. ATRIP.
    HPAi CAB033109.
    HPA030683.
    MIMi 606605. gene.
    neXtProti NX_Q8WXE1.
    Orphaneti 808. Seckel syndrome.
    PharmGKBi PA162377290.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87267.
    HOVERGENi HBG050618.
    InParanoidi Q8WXE1.
    KOi K10905.
    OMAi TGSNCQC.
    OrthoDBi EOG744T92.
    PhylomeDBi Q8WXE1.
    TreeFami TF324417.

    Enzyme and pathway databases

    Reactomei REACT_6769. Activation of ATR in response to replication stress.
    REACT_897. G2/M DNA damage checkpoint.

    Miscellaneous databases

    GenomeRNAii 84126.
    NextBioi 35475126.
    PROi Q8WXE1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WXE1.
    Bgeei Q8WXE1.
    CleanExi HS_ATRIP.
    Genevestigatori Q8WXE1.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "ATR and ATRIP: partners in checkpoint signaling."
      Cortez D., Guntuku S., Qin J., Elledge S.J.
      Science 294:1713-1716(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 147-160 AND 722-733, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING, PHOSPHORYLATION, INTERACTION WITH ATR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "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] (ISOFORMS 1; 2 AND 4).
      Tissue: Endothelial cell, Fetal brain, Placenta and Prostate.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 2 AND 3).
      Tissue: Colon, Lymph and Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-791 (ISOFORM 1).
      Tissue: Melanoma.
    7. "Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes."
      Zou L., Elledge S.J.
      Science 300:1542-1548(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE RPA COMPLEX.
    8. "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage."
      Falck J., Coates J., Jackson S.P.
      Nature 434:605-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF 769-GLU-GLU-770 AND 774-ASP-ASP-775.
    9. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
      Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
      J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96.
      Tissue: Lung adenocarcinoma.
    10. "Cep164 is a mediator protein required for the maintenance of genomic stability through modulation of MDC1, RPA, and CHK1."
      Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.
      Genes Dev. 22:587-600(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP164, SUBCELLULAR LOCATION.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: INTERACTION WITH CINP.
    14. "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-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-224 AND SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATRIP_HUMAN
    AccessioniPrimary (citable) accession number: Q8WXE1
    Secondary accession number(s): A8K6A3
    , A8K714, B2RCE7, B4DU92, B5MEB7, Q69YK9, Q8NHQ2, Q8WUG7, Q96CL3, Q9HA30
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [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 3
      Human chromosome 3: 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

    External Data

    Dasty 3