ID WRIP1_HUMAN Reviewed; 665 AA. AC Q96S55; B2RDB0; Q53EP6; Q59ET8; Q5W0E2; Q5W0E4; Q8WV26; Q9H681; Q9NRJ6; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 27-MAR-2024, entry version 180. DE RecName: Full=ATPase WRNIP1; DE EC=3.6.1.- {ECO:0000269|PubMed:15670210}; DE AltName: Full=Werner helicase-interacting protein 1; GN Name=WRNIP1 {ECO:0000312|HGNC:HGNC:20876}; GN Synonyms=WHIP {ECO:0000312|EMBL:BAB60709.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB60709.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Cervix carcinoma; RX PubMed=11301316; DOI=10.1074/jbc.c100035200; RA Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F., RA Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.; RT "A novel protein interacts with the Werner's syndrome gene product RT physically and functionally."; RL J. Biol. Chem. 276:20364-20369(2001). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB15383.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 303-665 (ISOFORM 1). RC TISSUE=Kidney epithelium {ECO:0000312|EMBL:BAB15383.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD97313.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:BAD92960.1}, and Kidney RC {ECO:0000312|EMBL:BAD97313.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000305, ECO:0000312|EMBL:AL139092} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] {ECO:0000305, ECO:0000312|EMBL:BAD97313.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH18923.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Muscle {ECO:0000312|EMBL:AAH18923.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] {ECO:0000305, ECO:0000312|EMBL:BAD97313.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-665 (ISOFORM 1). RA Adamson A.W., Shannon M.E., Lamerdin J.E., Thelen M.P.; RT "Characterization of RuvB homologs in human and mouse."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, SUBUNIT, INTERACTION WITH POLD1; POLD2 AND POLD4, AND MUTAGENESIS RP OF THR-294. RX PubMed=15670210; DOI=10.1111/j.1365-2443.2004.00812.x; RA Tsurimoto T., Shinozaki A., Yano M., Seki M., Enomoto T.; RT "Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel RT modulator for DNA polymerase delta."; RL Genes Cells 10:13-22(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534 AND TYR-562, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP INTERACTION WITH POLYUBIQUITIN, SUMOYLATION, UBIQUITINATION AT LYS-81; RP LYS-141; LYS-225; LYS-301; LYS-310; LYS-316; LYS-322; LYS-335; LYS-482; RP LYS-627; LYS-633 AND LYS-636, AND DOMAIN UBZ-TYPE ZINC-FINGER. RX PubMed=17550899; DOI=10.1074/jbc.m701042200; RA Bish R.A., Myers M.P.; RT "Werner helicase-interacting protein 1 binds polyubiquitin via its zinc RT finger domain."; RL J. Biol. Chem. 282:23184-23193(2007). RN [12] RP SUBCELLULAR LOCATION, INTERACTION WITH POLYUBIQUITIN, AND SUBUNIT. RX PubMed=18842586; DOI=10.1074/jbc.m803219200; RA Crosetto N., Bienko M., Hibbert R.G., Perica T., Ambrogio C., Kensche T., RA Hofmann K., Sixma T.K., Dikic I.; RT "Human Wrnip1 is localized in replication factories in a ubiquitin-binding RT zinc finger-dependent manner."; RL J. Biol. Chem. 283:35173-35185(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-85; SER-91; SER-92 RP AND THR-116, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-91 AND SER-92, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-633, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-153, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-75; SER-139 AND RP SER-153, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP FUNCTION, INTERACTION WITH TRIM14 AND PPP6C, AND SUBCELLULAR LOCATION. RX PubMed=29053956; DOI=10.1016/j.molcel.2017.09.035; RA Tan P., He L., Cui J., Qian C., Cao X., Lin M., Zhu Q., Li Y., Xing C., RA Yu X., Wang H.Y., Wang R.F.; RT "Assembly of the WHIP-TRIM14-PPP6C mitochondrial complex promotes RIG-I- RT mediated antiviral signaling."; RL Mol. Cell 68:293-307(2017). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 17-40 IN COMPLEX WITH ZINC, AND RP MUTAGENESIS OF VAL-18; PRO-21; VAL-22; ILE-32; ASN-33; LEU-36; ASP-37; RP LEU-40; LEU-41; LEU-42 AND PRO-44. RX PubMed=27062441; DOI=10.1111/febs.13734; RA Suzuki N., Rohaim A., Kato R., Dikic I., Wakatsuki S., Kawasaki M.; RT "A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger RT domain of WRNIP1."; RL FEBS J. 283:2004-2017(2016). CC -!- FUNCTION: Functions as a modulator of initiation or reinitiation events CC during DNA polymerase delta-mediated DNA synthesis. In the presence of CC ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is CC decreased. Also plays a role in the innate immune defense against CC viruses. Stabilizes the RIGI dsRNA interaction and promotes RIGI 'Lys- CC 63'-linked polyubiquitination. In turn, RIGI transmits the signal CC through mitochondrial MAVS. {ECO:0000269|PubMed:15670210, CC ECO:0000269|PubMed:29053956}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:15670210}; CC -!- SUBUNIT: Forms homooligomers (PubMed:18842586), possibly octamers. CC Directly interacts with POLD1, POLD2 and POLD4 (PubMed:15670210). CC Interacts with the N-terminal domain of WRN (By similarity). Interacts CC (via UBZ4-type zinc finger) with monoubiquitin and polyubiquitin CC (PubMed:17550899, PubMed:18842586). Interacts with TRIM14 and PPP6C; CC these interactions positively regulate the RIGI signaling pathway CC (PubMed:29053956). {ECO:0000250|UniProtKB:Q91XU0, CC ECO:0000269|PubMed:15670210, ECO:0000269|PubMed:17550899, CC ECO:0000269|PubMed:18842586, ECO:0000269|PubMed:29053956}. CC -!- INTERACTION: CC Q96S55; P28340: POLD1; NbExp=2; IntAct=EBI-2513471, EBI-716569; CC Q96S55; P49005: POLD2; NbExp=2; IntAct=EBI-2513471, EBI-372354; CC Q96S55; Q9HCU8: POLD4; NbExp=2; IntAct=EBI-2513471, EBI-864968; CC Q96S55; O95786: RIGI; NbExp=2; IntAct=EBI-2513471, EBI-995350; CC Q96S55; Q9H0E2: TOLLIP; NbExp=2; IntAct=EBI-2513471, EBI-74615; CC Q96S55; Q96S55: WRNIP1; NbExp=2; IntAct=EBI-2513471, EBI-2513471; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18842586}. Cytoplasm CC {ECO:0000269|PubMed:29053956}. Note=Colocalizes with WRN in granular CC structures in the nucleus. {ECO:0000269|PubMed:18842586, CC ECO:0000269|PubMed:29053956}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1 {ECO:0000269|PubMed:11301316}; CC IsoId=Q96S55-1; Sequence=Displayed; CC Name=2 {ECO:0000303|PubMed:14574404}; CC IsoId=Q96S55-2; Sequence=VSP_051783; CC Name=3 {ECO:0000303|PubMed:14574404}; CC IsoId=Q96S55-3; Sequence=VSP_051781; CC Name=4 {ECO:0000303|PubMed:14574404}; CC IsoId=Q96S55-4; Sequence=VSP_051782; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11301316}. CC -!- DOMAIN: The UBZ4-type zinc finger binds ubiquitin. CC {ECO:0000269|PubMed:27062441}. CC -!- PTM: Sumoylated with SUMO1 and SUMO2/3. {ECO:0000269|PubMed:17550899}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF80563.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15383.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB056152; BAB60709.1; -; mRNA. DR EMBL; AK026179; BAB15383.1; ALT_INIT; mRNA. DR EMBL; AK315471; BAG37857.1; -; mRNA. DR EMBL; AB209723; BAD92960.1; -; mRNA. DR EMBL; AK223593; BAD97313.1; -; mRNA. DR EMBL; AL139092; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55087.1; -; Genomic_DNA. DR EMBL; BC018923; AAH18923.1; -; mRNA. DR EMBL; AF218313; AAF80563.1; ALT_INIT; mRNA. DR CCDS; CCDS4475.1; -. [Q96S55-1] DR CCDS; CCDS4476.1; -. [Q96S55-2] DR RefSeq; NP_064520.2; NM_020135.2. [Q96S55-1] DR RefSeq; NP_569079.1; NM_130395.2. [Q96S55-2] DR PDB; 3VHS; X-ray; 1.90 A; A/B=17-40. DR PDB; 3VHT; X-ray; 2.40 A; B=9-46. DR PDBsum; 3VHS; -. DR PDBsum; 3VHT; -. DR AlphaFoldDB; Q96S55; -. DR SMR; Q96S55; -. DR BioGRID; 121227; 115. DR IntAct; Q96S55; 40. DR MINT; Q96S55; -. DR STRING; 9606.ENSP00000370150; -. DR GlyGen; Q96S55; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96S55; -. DR PhosphoSitePlus; Q96S55; -. DR BioMuta; WRNIP1; -. DR DMDM; 73622085; -. DR EPD; Q96S55; -. DR jPOST; Q96S55; -. DR MassIVE; Q96S55; -. DR MaxQB; Q96S55; -. DR PaxDb; 9606-ENSP00000370150; -. DR PeptideAtlas; Q96S55; -. DR ProteomicsDB; 78070; -. [Q96S55-1] DR ProteomicsDB; 78071; -. [Q96S55-2] DR ProteomicsDB; 78072; -. [Q96S55-3] DR ProteomicsDB; 78073; -. [Q96S55-4] DR Pumba; Q96S55; -. DR Antibodypedia; 9254; 250 antibodies from 33 providers. DR DNASU; 56897; -. DR Ensembl; ENST00000380764.1; ENSP00000370141.1; ENSG00000124535.16. [Q96S55-4] DR Ensembl; ENST00000380769.8; ENSP00000370146.3; ENSG00000124535.16. [Q96S55-3] DR Ensembl; ENST00000380771.8; ENSP00000370148.4; ENSG00000124535.16. [Q96S55-2] DR Ensembl; ENST00000380773.9; ENSP00000370150.4; ENSG00000124535.16. [Q96S55-1] DR Ensembl; ENST00000618555.4; ENSP00000477551.1; ENSG00000124535.16. [Q96S55-1] DR GeneID; 56897; -. DR KEGG; hsa:56897; -. DR MANE-Select; ENST00000380773.9; ENSP00000370150.4; NM_020135.3; NP_064520.2. DR UCSC; uc003mtz.4; human. [Q96S55-1] DR AGR; HGNC:20876; -. DR CTD; 56897; -. DR DisGeNET; 56897; -. DR GeneCards; WRNIP1; -. DR HGNC; HGNC:20876; WRNIP1. DR HPA; ENSG00000124535; Low tissue specificity. DR MIM; 608196; gene. DR neXtProt; NX_Q96S55; -. DR OpenTargets; ENSG00000124535; -. DR PharmGKB; PA134982239; -. DR VEuPathDB; HostDB:ENSG00000124535; -. DR eggNOG; KOG2028; Eukaryota. DR GeneTree; ENSGT00390000008538; -. DR HOGENOM; CLU_017985_0_2_1; -. DR InParanoid; Q96S55; -. DR OMA; RIILSQC; -. DR OrthoDB; 206891at2759; -. DR PhylomeDB; Q96S55; -. DR TreeFam; TF324547; -. DR PathwayCommons; Q96S55; -. DR SignaLink; Q96S55; -. DR BioGRID-ORCS; 56897; 10 hits in 1169 CRISPR screens. DR ChiTaRS; WRNIP1; human. DR GeneWiki; WRNIP1; -. DR GenomeRNAi; 56897; -. DR Pharos; Q96S55; Tbio. DR PRO; PR:Q96S55; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96S55; Protein. DR Bgee; ENSG00000124535; Expressed in tendon of biceps brachii and 183 other cell types or tissues. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:UniProtKB. DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:UniProtKB. DR CDD; cd00009; AAA; 1. DR CDD; cd18139; HLD_clamp_RarA; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.272.10; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032423; AAA_assoc_2. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR021886; MgsA_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006642; Rad18_UBZ4. DR InterPro; IPR040539; Znf-WRNIP1_ubi. DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1. DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF16193; AAA_assoc_2; 1. DR Pfam; PF12002; MgsA_C; 1. DR Pfam; PF18279; zf-WRNIP1_ubi; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00734; ZnF_Rad18; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1. DR PROSITE; PS51908; ZF_UBZ4; 1. DR Genevisible; Q96S55; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW DNA damage; DNA repair; DNA replication; Hydrolase; Immunity; KW Innate immunity; Isopeptide bond; Metal-binding; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..665 FT /note="ATPase WRNIP1" FT /id="PRO_0000084785" FT ZN_FING 17..44 FT /note="UBZ4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256" FT REGION 48..190 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..188 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256, FT ECO:0000269|PubMed:27062441, ECO:0007744|PDB:3VHS, FT ECO:0007744|PDB:3VHT" FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256, FT ECO:0000269|PubMed:27062441, ECO:0007744|PDB:3VHS, FT ECO:0007744|PDB:3VHT" FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27062441, FT ECO:0007744|PDB:3VHS" FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256, FT ECO:0000269|PubMed:27062441, ECO:0007744|PDB:3VHS, FT ECO:0007744|PDB:3VHT" FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256, FT ECO:0000269|PubMed:27062441, ECO:0007744|PDB:3VHT" FT BINDING 270..276 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 85 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 116 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 534 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 562 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 633 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 81 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 225 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 301 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 310 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 316 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 322 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 335 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 482 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 482 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 627 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 633 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:17550899" FT CROSSLNK 636 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17550899" FT VAR_SEQ 1..384 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_051782" FT VAR_SEQ 1..220 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_051781" FT VAR_SEQ 338..362 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14574404, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_051783" FT MUTAGEN 18 FT /note="V->A: Reduced affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 21 FT /note="P->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 22 FT /note="V->A: Reduced affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 32 FT /note="I->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 33 FT /note="N->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 36 FT /note="L->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 37 FT /note="D->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 40 FT /note="L->A: Loss of affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 41 FT /note="L->A: Normal affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 42 FT /note="L->A: Normal affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 44 FT /note="P->A: Normal affinity for ubiquitin." FT /evidence="ECO:0000269|PubMed:27062441" FT MUTAGEN 294 FT /note="T->A: Loss of ATPase activity." FT /evidence="ECO:0000269|PubMed:15670210" FT CONFLICT 144 FT /note="A -> V (in Ref. 1; BAB60709)" FT /evidence="ECO:0000305" FT CONFLICT 170..173 FT /note="Missing (in Ref. 3; BAD92960)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="I -> N (in Ref. 1; BAB60709)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="L -> F (in Ref. 2; BAB15383)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="H -> Y (in Ref. 3; BAD97313)" FT /evidence="ECO:0000305" FT CONFLICT 545 FT /note="E -> G (in Ref. 2; BAB15383)" FT /evidence="ECO:0000305" FT CONFLICT 568 FT /note="I -> M (in Ref. 1; BAB60709)" FT /evidence="ECO:0000305" FT CONFLICT 576 FT /note="L -> F (in Ref. 1; BAB60709)" FT /evidence="ECO:0000305" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:3VHS" FT TURN 21..23 FT /evidence="ECO:0007829|PDB:3VHS" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:3VHS" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:3VHS" FT HELIX 32..39 FT /evidence="ECO:0007829|PDB:3VHS" SQ SEQUENCE 665 AA; 72133 MW; DE43D8E59C4B29E8 CRC64; MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP AAGSHRAGER AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD DGGETESRES YDAPPTPSGA RLIPDFPVAR SSSPGRKGSG KRPAAAAAAG SASPRSWDEA EAQEEEEAVG DGDGDGDADA DGEDDPGHWD ADAAEAATAF GASGGGRPHP RALAAEEIRQ MLQGKPLADT MRPDTLQDYF GQSKAVGQDT LLRSLLETNE IPSLILWGPP GCGKTTLAHI IASNSKKHSI RFVTLSATNA KTNDVRDVIK QAQNEKSFFK RKTILFIDEI HRFNKSQQDT FLPHVECGTI TLIGATTENP SFQVNAALLS RCRVIVLEKL PVEAMVTILM RAINSLGIHV LDSSRPTDPL SHSSNSSSEP AMFIEDKAVD TLAYLSDGDA RAGLNGLQLA VLARLSSRKM FCKKSGQSYS PSRVLITEND VKEGLQRSHI LYDRAGEEHY NCISALHKSM RGSDQNASLY WLARMLEGGE DPLYVARRLV RFASEDIGLA DPSALTQAVA AYQGCHFIGM PECEVLLAQC VVYFARAPKS IEVYSAYNNV KACLRNHQGP LPPVPLHLRN APTRLMKDLG YGKGYKYNPM YSEPVDQEYL PEELRGVDFF KQRRC //