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Q8WXE1

- ATRIP_HUMAN

UniProt

Q8WXE1 - ATRIP_HUMAN

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Protein

ATR-interacting protein

Gene
ATRIP, AGS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

GO - Cellular componenti

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

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 – 2241Phosphoserine3 Publications
Modified residuei518 – 5181Phosphoserine4 Publications

Post-translational modificationi

Phosphorylated by ATR.1 Publication

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.4 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.

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 217110 Reviewed predictionAdd
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.

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.

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. VSP_047011Add
BLAST
Alternative sequencei1 – 9393Missing in isoform 3. VSP_010501Add
BLAST
Alternative sequencei661 – 68727Missing in isoform 2. VSP_010504Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801P → L in AAH14153. 1 Publication
Sequence conflicti343 – 3431T → A in BAF84257. 1 Publication
Sequence conflicti492 – 4921V → I in BAF84257. 1 Publication
Sequence conflicti647 – 6471A → T in BAG62254. 1 Publication
Sequence conflicti683 – 6831N → D in BAF84257. 1 Publication
Sequence conflicti687 – 6871V → I in AAH30597. 1 Publication
Sequence conflicti712 – 7121Q → K in BAF84257. 1 Publication
Sequence conflicti777 – 7771C → G in BAF84257. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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