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UniProtKB/Swiss-Prot entry Q96S55


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name WRIP1_HUMAN
Primary accession number Q96S55
Secondary accession numbers Q53EP6 Q59ET8 Q5W0E2 Q5W0E4 Q8WV26 Q9H681 Q9NRJ6
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on August 16, 2005 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 56)
Name and origin of the protein
Protein name ATPase WRNIP1
Synonym Werner helicase-interacting protein 1
Gene name
Name: WRNIP1
Synonyms: WHIP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
DOI=10.1074/jbc.C100035200; PubMed=11301316 [NCBI, ExPASy, EBI, Israel, Japan]
Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F., Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
"A novel protein interacts with the Werner's syndrome gene product physically and functionally.";
J. Biol. Chem. 276:20364-20369(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 142-665 (ISOFORM 1).
Adamson A.W., Shannon M.E., Lamerdin J.E., Thelen M.P.;
"Characterization of RuvB homologs in human and mouse.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-665.
TISSUE=Kidney epithelium;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[8]
FUNCTION, SUBUNIT, AND INTERACTION WITH POLD1; POLD2 AND POLD4.
DOI=10.1111/j.1365-2443.2004.00812.x; PubMed=15670210 [NCBI, ExPASy, EBI, Israel, Japan]
Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.;
"Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta.";
Genes Cells 10:13-22(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-85; SER-91; SER-92 AND THR-116, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: Functions as a modulator for initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. Has an intrinsic ATPase activity that functions as a sensor of DNA damage or of arrested replication forks and regulates the extent of DNA synthesis.
  • SUBUNIT: Homooligomer; most likely an octamer. Interacts with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of WRN.
  • SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Colocalizes with WRN in granular structures in the nucleus (By similarity).
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ96S55-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ96S55-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_051783.
    Name3
    Isoform IDQ96S55-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_051781.
    Name4
    Isoform IDQ96S55-4
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_051782.
  • TISSUE SPECIFICITY: Ubiquitously expressed.
  • SIMILARITY: Belongs to the AAA ATPase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB056152; BAB60709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209723; BAD92960.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223593; BAD97313.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139092; CAH73663.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139092; CAH73664.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139092; CAH73665.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139092; CAH73666.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018923; AAH18923.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF218313; AAF80563.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK026179; BAB15383.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_064520.2; -.
NP_569079.1; -.
UniGene Hs.236828
3D structure databases
HSSP Q56313; 1J7K. [HSSP ENTRY / PDB]
ModBase Q96S55.
PTM databases
PhosphoSite Q96S55; -.
Organism-specific databases
GeneCards GC06P002710; -.
H-InvDB HIX0005529; -.
HGNC HGNC:20876; WRNIP1.
GenAtlas WRNIP1.
MIM 608196; gene. [NCBI / EBI]
PharmGKB PA134982239; -.
GeneCards Q96S55.
Gene expression databases
ArrayExpress Q96S55; -.
CleanEx HS_WRNIP1; -.
GermOnline ENSG00000124535; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred by curator from UniProtKB).
GO:0016887; Molecular function: ATPase activity (inferred from mutant phenotype from UniProtKB).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0000731; Biological process: DNA synthesis during DNA repair (inferred from direct assay from UniProtKB).
GO:0030174; Biological process: regulation of DNA replication initiation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR003960; AAA_ATPase_CS.
IPR006642; Znf_Rad18_put.
Graphical view of domain structure.
Pfam PF00004; AAA; 1.
Pfam graphical view of domain structure.
SMART SM00382; AAA; 1.
SM00734; ZnF_Rad18; 1.
SMART graphical view of domain structure.
PROSITE PS00674; AAA; FALSE_NEG.
Proteomics databases
PRIDE Q96S55; -.
Genome annotation databases
Ensembl ENSG00000124535; Homo sapiens. [Contig view]
GeneID 56897; -.
KEGG hsa:56897; -.
Phylogenomic databases
HOVERGEN Q96S55; -.
Other
NextBio 62333; -.
SOURCE WRNIP1; Homo sapiens.
ProtoNet Q96S55.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; DNA damage; DNA replication; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   665  665     ATPase WRNIP1. PRO_0000084785
NP_BIND   268   275  8     ATP (Potential). 
MOD_RES   65    65        Phosphoserine. 
MOD_RES   75    75        Phosphoserine. 
MOD_RES   85    85        Phosphothreonine. 
MOD_RES   91    91        Phosphoserine. 
MOD_RES   92    92        Phosphoserine. 
MOD_RES   116   116        Phosphothreonine. 
MOD_RES   153   153        Phosphoserine. 
MOD_RES   534   534        Phosphotyrosine. 
MOD_RES   562   562        Phosphotyrosine. 
VAR_SEQ   1   384        Missing (in isoform 4). VSP_051782
VAR_SEQ   1   220        Missing (in isoform 3). VSP_051781
VAR_SEQ   338   362        Missing (in isoform 2). VSP_051783
CONFLICT   142   143        RP -> KL (in Ref. 5). 
CONFLICT   144   144        A -> V (in Ref. 1; BAB60709). 
CONFLICT   170   173        Missing (in Ref. 2; BAD92960). 
CONFLICT   265   265        I -> N (in Ref. 1; BAB60709). 
CONFLICT   377   377        L -> F (in Ref. 6). 
CONFLICT   499   499        H -> Y (in Ref. 2; BAD97313). 
CONFLICT   545   545        E -> G (in Ref. 6; BAB15383). 
CONFLICT   568   568        I -> M (in Ref. 1; BAB60709). 
CONFLICT   576   576        L -> F (in Ref. 1; BAB60709). 
Sequence information
Length: 665 AA [This is the length of the unprocessed precursor] Molecular weight: 72133 Da [This is the MW of the unprocessed precursor] CRC64: DE43D8E59C4B29E8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP AAGSHRAGER 

        70         80         90        100        110        120 
AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD DGGETESRES YDAPPTPSGA 

       130        140        150        160        170        180 
RLIPDFPVAR SSSPGRKGSG KRPAAAAAAG SASPRSWDEA EAQEEEEAVG DGDGDGDADA 

       190        200        210        220        230        240 
DGEDDPGHWD ADAAEAATAF GASGGGRPHP RALAAEEIRQ MLQGKPLADT MRPDTLQDYF 

       250        260        270        280        290        300 
GQSKAVGQDT LLRSLLETNE IPSLILWGPP GCGKTTLAHI IASNSKKHSI RFVTLSATNA 

       310        320        330        340        350        360 
KTNDVRDVIK QAQNEKSFFK RKTILFIDEI HRFNKSQQDT FLPHVECGTI TLIGATTENP 

       370        380        390        400        410        420 
SFQVNAALLS RCRVIVLEKL PVEAMVTILM RAINSLGIHV LDSSRPTDPL SHSSNSSSEP 

       430        440        450        460        470        480 
AMFIEDKAVD TLAYLSDGDA RAGLNGLQLA VLARLSSRKM FCKKSGQSYS PSRVLITEND 

       490        500        510        520        530        540 
VKEGLQRSHI LYDRAGEEHY NCISALHKSM RGSDQNASLY WLARMLEGGE DPLYVARRLV 

       550        560        570        580        590        600 
RFASEDIGLA DPSALTQAVA AYQGCHFIGM PECEVLLAQC VVYFARAPKS IEVYSAYNNV 

       610        620        630        640        650        660 
KACLRNHQGP LPPVPLHLRN APTRLMKDLG YGKGYKYNPM YSEPVDQEYL PEELRGVDFF 


KQRRC 

Q96S55 in FASTA format

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View entry in raw text format (no links)
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