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Reviewed, UniProtKB/Swiss-Prot Q96S55 (WRIP1_HUMAN)

Last modified July 22, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATPase WRNIP1
Alternative name(s):
    Werner helicase-interacting protein 1
Gene names
Name: WRNIP1
Synonyms: WHIP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

Homooligomer; most likely an octamer. Interacts with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of WRN.

Subcellular location

NucleusBy similarity. Note= Colocalizes with WRN in granular structures in the nucleus By similarity.

Tissue specificity

Ubiquitously expressed.

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords

   Biological processDNA damage
DNA replication
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processDNA synthesis during DNA repair Ref.8

Inferred from direct assay. Source: UniProtKB

regulation of DNA replication initiation Ref.8

Inferred from direct assay. Source: UniProtKB

   Cellular componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionATP binding Ref.8

Inferred by curator. Source: UniProtKB

ATPase activity Ref.8

Inferred from mutant phenotype. Source: UniProtKB

protein binding Ref.8

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96S55-1)

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: Q96S55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     338-362: Missing.
Notes: No experimental confirmation available.
Isoform 3 (identifier: Q96S55-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-220: Missing.
Notes: No experimental confirmation available.
Isoform 4 (identifier: Q96S55-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-384: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 665665ATPase WRNIP1

Regions

Nucleotide binding268 – 2758ATP Potential

Amino acid modifications

Modified residue651Phosphoserine
Modified residue751Phosphoserine
Modified residue921Phosphoserine By similarity
Modified residue1531Phosphoserine
Modified residue5341Phosphotyrosine
Modified residue5621Phosphotyrosine

Natural variations

Alternative sequence1 – 384384Missing in isoform 4.
Alternative sequence1 – 220220Missing in isoform 3.
Alternative sequence338 – 36225Missing in isoform 2.

Experimental info

Sequence conflict142 – 1432RP → KL Ref.5
Sequence conflict1441A → V in BAB60709. Ref.1
Sequence conflict170 – 1734Missing in BAD92960. Ref.2
Sequence conflict2651I → N in BAB60709. Ref.1
Sequence conflict3771L → F Ref.6
Sequence conflict4991H → Y in BAD97313. Ref.2
Sequence conflict5451E → G in BAB15383. Ref.6
Sequence conflict5681I → M in BAB60709. Ref.1
Sequence conflict5761L → F in BAB60709. Ref.1

Sequences

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

Last modified August 16, 2005. Version 2.
Checksum: DE43D8E59C4B29E8

FASTA66572,133
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 83117E6CEFDE7688
Show »

64069,459
Isoform 3 [UniParc].

Checksum: BDED370A47C0D894
Show »

44549,570
Isoform 4 [UniParc].

Checksum: 1099DF56AA75F54A
Show »

28131,339

References

« Hide 'large scale' references
[1]"A novel protein interacts with the Werner's syndrome gene product physically and functionally."
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.
J. Biol. Chem. 276:20364-20369(2001) [PubMed: 11301316] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Kidney.
[3]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Muscle.
[5]"Characterization of RuvB homologs in human and mouse."
Adamson A.W., Shannon M.E., Lamerdin J.E., Thelen M.P.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-665 (ISOFORM 1).
[6]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-665.
Tissue: Kidney epithelium.
[7]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta."
Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.
Genes Cells 10:13-22(2005) [PubMed: 15670210] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH POLD1; POLD2 AND POLD4.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, MASS SPECTROMETRY.
[10]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB056152 mRNA. Translation: BAB60709.1.
AB209723 mRNA. Translation: BAD92960.1.
AK223593 mRNA. Translation: BAD97313.1.
AL139092 Genomic DNA. Translation: CAH73663.1.
AL139092 Genomic DNA. Translation: CAH73664.1.
AL139092 Genomic DNA. Translation: CAH73665.1.
AL139092 Genomic DNA. Translation: CAH73666.1.
BC018923 mRNA. Translation: AAH18923.1.
AF218313 mRNA. Translation: AAF80563.1. Different initiation.
AK026179 mRNA. Translation: BAB15383.1. Different initiation.
RefSeqNP_064520.2.
NP_569079.1.
UniGeneHs.236828

3D structure databases

HSSPHSSP built from PDB template 1J7K based on UniProtKB Q56313.
ModBaseSearch...

PTM databases

PhosphoSiteQ96S55.

Genome annotation databases

EnsemblENSG00000124535. Homo sapiens. [Contig view]
GeneID56897.
KEGGhsa:56897.

Organism-specific databases

H-InvDBHIX0005529.
HGNCHGNC:20876. WRNIP1.
MIM608196. gene.
PharmGKBPA134982239.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ96S55.

Gene expression databases

ArrayExpressQ96S55.
CleanExHS_WRNIP1.
GermOnlineENSG00000124535. Homo sapiens.

Family and domain databases

InterProIPR003593. AAA+_ATPase_core.
IPR003959. AAA_ATPase_core.
IPR003960. AAA_ATPase_CS.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEPS00674. AAA. False negative.
[Graphical view]