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Q96S55 (WRIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
ATPase WRNIP1

EC=3.6.1.3
Alternative name(s):
Werner helicase-interacting protein 1
Gene names
Name:WRNIP1
Synonyms:WHIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
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. Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.8

Subunit structure

Homooligomer; most likely an octamer. Interacts with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of WRN. Interacts (via UBZ-type zinc finger) with polyubiquitin. Ref.8

Subcellular location

Nucleus By similarity. Note: Colocalizes with WRN in granular structures in the nucleus By similarity.

Tissue specificity

Ubiquitously expressed. Ref.1

Post-translational modification

Sumoylated with SUMO1 and SUMO2/3. Ref.11

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 UBZ-type zinc finger.

Sequence caution

The sequence AAF80563.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB15383.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.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 Ref.4 (identifier: Q96S55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     338-362: Missing.
Note: No experimental confirmation available.
Isoform 3 Ref.4 (identifier: Q96S55-3)

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665ATPase WRNIP1
PRO_0000084785

Regions

Zinc finger17 – 4024UBZ-type
Nucleotide binding268 – 2758ATP Potential

Amino acid modifications

Modified residue751Phosphoserine Ref.13 Ref.18
Modified residue851Phosphothreonine Ref.13 Ref.16
Modified residue911Phosphoserine Ref.13 Ref.16
Modified residue921Phosphoserine Ref.13 Ref.16
Modified residue1161Phosphothreonine Ref.13
Modified residue1531Phosphoserine Ref.18 Ref.20
Modified residue5341Phosphotyrosine Ref.9
Modified residue5621Phosphotyrosine Ref.9
Modified residue6331N6-acetyllysine; alternate Ref.17
Cross-link81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link335Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link482Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11
Cross-link633Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.11
Cross-link636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Natural variations

Alternative sequence1 – 384384Missing in isoform 4. Ref.4
VSP_051782
Alternative sequence1 – 220220Missing in isoform 3. Ref.4
VSP_051781
Alternative sequence338 – 36225Missing in isoform 2. Ref.4
VSP_051783

Experimental info

Sequence conflict1441A → V in BAB60709. Ref.1
Sequence conflict170 – 1734Missing in BAD92960. Ref.3
Sequence conflict2651I → N in BAB60709. Ref.1
Sequence conflict3771L → F in BAB15383. Ref.2
Sequence conflict4991H → Y in BAD97313. Ref.3
Sequence conflict5451E → G in BAB15383. Ref.2
Sequence conflict5681I → M in BAB60709. Ref.1
Sequence conflict5761L → F in BAB60709. Ref.1

Secondary structure

......... 665
Helix Strand Turn

Details...

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 »

FASTA64069,459
Isoform 3 [UniParc].

Checksum: BDED370A47C0D894
Show »

FASTA44549,570
Isoform 4 [UniParc].

Checksum: 1099DF56AA75F54A
Show »

FASTA28131,339

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-665 (ISOFORM 1).
Tissue: Kidney epithelium.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Kidney.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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] (ISOFORM 2).
Tissue: Muscle.
[7]"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 144-665 (ISOFORM 1).
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain."
Bish R.A., Myers M.P.
J. Biol. Chem. 282:23184-23193(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, UBIQUITINATION AT LYS-81; LYS-141; LYS-225; LYS-301; LYS-310; LYS-316; LYS-322; LYS-335; LYS-482; LYS-627; LYS-633 AND LYS-636, DOMAIN UBZ-TYPE ZINC-FINGER.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-75; THR-85; SER-91; SER-92 AND THR-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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 THR-85; SER-91 AND SER-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-75 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB056152 mRNA. Translation: BAB60709.1.
AK026179 mRNA. Translation: BAB15383.1. Different initiation.
AK315471 mRNA. Translation: BAG37857.1.
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.
CH471087 Genomic DNA. Translation: EAW55087.1.
BC018923 mRNA. Translation: AAH18923.1.
AF218313 mRNA. Translation: AAF80563.1. Different initiation.
RefSeqNP_064520.2. NM_020135.2.
NP_569079.1. NM_130395.2.
UniGeneHs.236828.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VHSX-ray1.90A/B17-40[»]
3VHTX-ray2.40B9-46[»]
ProteinModelPortalQ96S55.
SMRQ96S55. Positions 12-46, 225-664.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121227. 24 interactions.
IntActQ96S55. 15 interactions.
MINTMINT-3058154.
STRING9606.ENSP00000370150.

PTM databases

PhosphoSiteQ96S55.

Polymorphism databases

DMDM73622085.

Proteomic databases

PaxDbQ96S55.
PRIDEQ96S55.

Protocols and materials databases

DNASU56897.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380764; ENSP00000370141; ENSG00000124535. [Q96S55-4]
ENST00000380769; ENSP00000370146; ENSG00000124535. [Q96S55-3]
ENST00000380771; ENSP00000370148; ENSG00000124535. [Q96S55-2]
ENST00000380773; ENSP00000370150; ENSG00000124535. [Q96S55-1]
GeneID56897.
KEGGhsa:56897.
UCSCuc003mtz.3. human. [Q96S55-1]
uc003mua.3. human. [Q96S55-2]

Organism-specific databases

CTD56897.
GeneCardsGC06P002766.
H-InvDBHIX0005529.
HGNCHGNC:20876. WRNIP1.
HPAHPA031752.
HPA031753.
MIM608196. gene.
neXtProtNX_Q96S55.
PharmGKBPA134982239.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2256.
HOVERGENHBG062192.
InParanoidQ96S55.
KOK07478.
OMAPGHWDAD.
OrthoDBEOG744T8W.
PhylomeDBQ96S55.
TreeFamTF324547.

Gene expression databases

BgeeQ96S55.
CleanExHS_WRNIP1.
GenevestigatorQ96S55.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR021886. MgsA_C.
IPR027417. P-loop_NTPase.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF12002. MgsA_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
SUPFAMSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GeneWikiWRNIP1.
GenomeRNAi56897.
NextBio62333.
PROQ96S55.
SOURCESearch...

Entry information

Entry nameWRIP1_HUMAN
AccessionPrimary (citable) accession number: Q96S55
Secondary accession number(s): B2RDB0 expand/collapse secondary AC list , Q53EP6, Q59ET8, Q5W0E2, Q5W0E4, Q8WV26, Q9H681, Q9NRJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: April 16, 2014
This is version 106 of the entry and version 2 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 chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM