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Q8WXE1 (ATRIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATR-interacting protein
Alternative name(s):
ATM and Rad3-related-interacting protein
Gene names
Name:ATRIP
Synonyms:AGS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length791 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein. Ref.7

Subunit structure

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. Ref.1 Ref.7 Ref.10 Ref.13

Subcellular location

Nucleus. Note: Redistributes to discrete nuclear foci upon DNA damage. Ref.1 Ref.10

Tissue specificity

Ubiquitous. Ref.1

Domain

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage. Ref.8

Post-translational modification

Phosphorylated by ATR. Ref.1

Sequence similarities

Belongs to the ATRIP family.

Caution

The gene for this protein is either identical to or adjacent to that of TREX1. Some of the mRNAs that encode ATRIP also encode TREX1 in another reading frame.

Sequence caution

The sequence BAB14029.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14029.1 differs from that shown. Reason: Frameshift at position 650.

The sequence BAF84257.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDK9P507503EBI-747353,EBI-1383449

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WXE1-1)

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.
Isoform 2 (identifier: Q8WXE1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     661-687: Missing.
Isoform 3 (identifier: Q8WXE1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8WXE1-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 791790ATR-interacting protein
PRO_0000064740

Regions

Region118 – 15639Interaction with CINP
Coiled coil108 – 217110 Potential
Motif769 – 7768EEXXXDL motif

Amino acid modifications

Modified residue21N-acetylalanine Ref.17
Modified residue2241Phosphoserine Ref.11 Ref.12 Ref.15
Modified residue5181Phosphoserine Ref.12 Ref.14 Ref.15 Ref.16
Cross-link96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Natural variations

Alternative sequence1 – 127127Missing in isoform 4.
VSP_047011
Alternative sequence1 – 9393Missing in isoform 3.
VSP_010501
Alternative sequence661 – 68727Missing in isoform 2.
VSP_010504
Natural variant1251K → Q.
Corresponds to variant rs11925638 [ dbSNP | Ensembl ].
VAR_050683
Natural variant2401P → L.
Corresponds to variant rs35240314 [ dbSNP | Ensembl ].
VAR_050684

Experimental info

Mutagenesis769 – 7702EE → AA: Abolishes interaction with ATR and its recruitment to sites of DNA damage. Ref.8
Mutagenesis774 – 7752DD → AA: Abolishes interaction with ATR and its recruitment to sites of DNA damage. Ref.8
Sequence conflict2801P → L in AAH14153. Ref.5
Sequence conflict3431T → A in BAF84257. Ref.2
Sequence conflict4921V → I in BAF84257. Ref.2
Sequence conflict6471A → T in BAG62254. Ref.2
Sequence conflict6831N → D in BAF84257. Ref.2
Sequence conflict6871V → I in AAH30597. Ref.5
Sequence conflict7121Q → K in BAF84257. Ref.2
Sequence conflict7771C → G in BAF84257. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 58981602F7961756

FASTA79185,838
        10         20         30         40         50         60 
MAGTSAPGSK RRSEPPAPRP GPPPGTGHPP SKRARGFSAA AAPDPDDPFG AHGDFTADDL 

        70         80         90        100        110        120 
EELDTLASQA LSQCPAAARD VSSDHKVHRL LDGMSKNPSG KNRETVPIKD NFELEVLQAQ 

       130        140        150        160        170        180 
YKELKEKMKV MEEEVLIKNG EIKILRDSLH QTESVLEEQR RSHFLLEQEK TQALSDKEKE 

       190        200        210        220        230        240 
FSKKLQSLQS ELQFKDAEMN ELRTKLQTSE RANKLAAPSV SHVSPRKNPS VVIKPEACSP 

       250        260        270        280        290        300 
QFGKTSFPTK ESFSANMSLP HPCQTESGYK PLVGREDSKP HSLRGDSIKQ EEAQKSFVDS 

       310        320        330        340        350        360 
WRQRSNTQGS ILINLLLKQP LIPGSSLSLC HLLSSSSESP AGTPLQPPGF GSTLAGMSGL 

       370        380        390        400        410        420 
RTTGSYDGSF SLSALREAQN LAFTGLNLVA RNECSRDGDP AEGGRRAFPL CQLPGAVHFL 

       430        440        450        460        470        480 
PLVQFFIGLH CQALQDLAAA KRSGAPGDSP THSSCVSSGV ETNPEDSVCI LEGFSVTALS 

       490        500        510        520        530        540 
ILQHLVCHSG AVVSLLLSGV GADSAAGEGN RSLVHRLSDG DMTSALRGVA DDQGQHPLLK 

       550        560        570        580        590        600 
MLLHLLAFSS AATGHLQASV LTQCLKVLVK LAENTSCDFL PRFQCVFQVL PKCLSPETPL 

       610        620        630        640        650        660 
PSVLLAVELL SLLADHDQLA PQLCSHSEGC LLLLLYMYIT SRPDRVALET QWLQLEQEVV 

       670        680        690        700        710        720 
WLLAKLGVQS PLPPVTGSNC QCNVEVVRAL TVMLHRQWLT VRRAGGPPRT DQQRRTVRCL 

       730        740        750        760        770        780 
RDTVLLLHGL SQKDKLFMMH CVEVLHQFDQ VMPGVSMLIR GLPDVTDCEE AALDDLCAAE 

       790 
TDVEDPEVEC G 

« Hide

Isoform 2 [UniParc].

Checksum: 94E7E31A6BCAAC1D
Show »

FASTA76483,003
Isoform 3 [UniParc].

Checksum: 417F5811408F2799
Show »

FASTA69876,336
Isoform 4 [UniParc].

Checksum: 460E7E097BCA1C30
Show »

FASTA66472,362

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]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].
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"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-224 AND SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Functional genomic screens identify CINP as a genome maintenance protein."
Lovejoy C.A., Xu X., Bansbach C.E., Glick G.G., Zhao R., Ye F., Sirbu B.M., Titus L.C., Shyr Y., Cortez D.
Proc. Natl. Acad. Sci. U.S.A. 106:19304-19309(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001257951.1. NM_001271022.1.
NP_001257952.1. NM_001271023.1.
NP_115542.2. NM_032166.3.
NP_569055.1. NM_130384.2.
UniGeneHs.694840.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IGKX-ray1.75C/D237-243[»]
4NB3X-ray1.35C/D54-67[»]
ProteinModelPortalQ8WXE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid313463. 22 interactions.
DIPDIP-46495N.
IntActQ8WXE1. 8 interactions.
MINTMINT-5009350.

PTM databases

PhosphoSiteQ8WXE1.

Polymorphism databases

DMDM48428109.

Proteomic databases

PaxDbQ8WXE1.
PRIDEQ8WXE1.

Protocols and materials databases

DNASU84126.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320211; ENSP00000323099; ENSG00000164053. [Q8WXE1-1]
ENST00000346691; ENSP00000302338; ENSG00000164053. [Q8WXE1-2]
ENST00000357105; ENSP00000349620; ENSG00000164053. [Q8WXE1-5]
ENST00000412052; ENSP00000400930; ENSG00000164053. [Q8WXE1-3]
GeneID84126.
KEGGhsa:84126.
UCSCuc003ctf.2. human. [Q8WXE1-1]
uc003ctg.2. human. [Q8WXE1-2]

Organism-specific databases

CTD84126.
GeneCardsGC03P048488.
HGNCHGNC:33499. ATRIP.
HPACAB033109.
HPA030683.
MIM606605. gene.
neXtProtNX_Q8WXE1.
Orphanet808. Seckel syndrome.
PharmGKBPA162377290.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87267.
HOVERGENHBG050618.
InParanoidQ8WXE1.
KOK10905.
OMATGSNCQC.
OrthoDBEOG744T92.
PhylomeDBQ8WXE1.
TreeFamTF324417.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ8WXE1.
BgeeQ8WXE1.
CleanExHS_ATRIP.
GenevestigatorQ8WXE1.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi84126.
NextBio35475126.
PROQ8WXE1.
SOURCESearch...

Entry information

Entry nameATRIP_HUMAN
AccessionPrimary (citable) accession number: Q8WXE1
Secondary accession number(s): A8K6A3 expand/collapse secondary AC list , A8K714, B2RCE7, B4DU92, B5MEB7, Q69YK9, Q8NHQ2, Q8WUG7, Q96CL3, Q9HA30
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 102 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 3

Human chromosome 3: entries, gene names and cross-references to MIM