Reviewed, UniProtKB/Swiss-Prot Q96S55 (WRIP1_HUMAN)

Names and origin

Protein names

Recommended name:
    ATPase WRNIP1
Alternative name(s):
    Werner helicase-interacting protein 1

Gene names

Name:	WRNIP1
Synonyms:	WHIP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9
Subunit structure	Homooligomer; most likely an octamer. Interacts with POLD1, POLD2 and POLD4. Interacts with the N-terminal domain of WRN. Interacts (via Rad18-type zinc finger) with polyubiquitin. Ref.9
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 by SUMO1 and SUMO2/3.
Sequence similarities	Belongs to the AAA ATPase family. Contains 1 Rad18-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA replication
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA synthesis during DNA repair Ref.9 Inferred from direct assay. Source: UniProtKB regulation of DNA replication initiation Ref.9 Inferred from direct assay. Source: UniProtKB
Cellular component	nucleus Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Ref.9 Inferred from mutant phenotype. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: InterPro protein binding Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 665	665	ATPase WRNIP1		PRO_0000084785
Regions
	Zinc finger	17 – 40	24	Rad18-type
	Nucleotide binding	268 – 275	8	ATP Potential
Amino acid modifications
	Modified residue	65	1	Phosphoserine Ref.8
	Modified residue	75	1	Phosphoserine Ref.11 Ref.14
	Modified residue	85	1	Phosphothreonine Ref.14 Ref.18
	Modified residue	91	1	Phosphoserine Ref.14 Ref.18 Ref.16
	Modified residue	92	1	Phosphoserine Ref.14 Ref.18 Ref.16
	Modified residue	116	1	Phosphothreonine Ref.14 Ref.18
	Modified residue	151	1	Phosphoserine
	Modified residue	153	1	Phosphoserine Ref.13
	Modified residue	534	1	Phosphotyrosine Ref.18 Ref.10
	Modified residue	562	1	Phosphotyrosine Ref.10
	Modified residue	633	1	N6-acetyllysine Ref.19
	Cross-link	81		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	141		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	225		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	301		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	310		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	316		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	322		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	335		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	482		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	627		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	633		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	636		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Natural variations
	Alternative sequence	1 – 384	384	Missing in isoform 4. Ref.4		VSP_051782
	Alternative sequence	1 – 220	220	Missing in isoform 3. Ref.4		VSP_051781
	Alternative sequence	338 – 362	25	Missing in isoform 2. Ref.4		VSP_051783
Experimental info
	Sequence conflict	144	1	A → V in BAB60709. Ref.1
	Sequence conflict	170 – 173	4	Missing in BAD92960. Ref.3
	Sequence conflict	265	1	I → N in BAB60709. Ref.1
	Sequence conflict	377	1	L → F in BAB15383. Ref.2
	Sequence conflict	499	1	H → Y in BAD97313. Ref.3
	Sequence conflict	545	1	E → G in BAB15383. Ref.2
	Sequence conflict	568	1	I → M in BAB60709. Ref.1
	Sequence conflict	576	1	L → F in BAB60709. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: DE43D8E59C4B29E8	FASTA	665	72,133
	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
	Isoform 2. Checksum: 83117E6CEFDE7688	FASTA	640	69,459
	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 HRFNKSQQVN AALLSRCRVI VLEKLPVEAM 370 380 390 400 410 420 VTILMRAINS LGIHVLDSSR PTDPLSHSSN SSSEPAMFIE DKAVDTLAYL SDGDARAGLN 430 440 450 460 470 480 GLQLAVLARL SSRKMFCKKS GQSYSPSRVL ITENDVKEGL QRSHILYDRA GEEHYNCISA 490 500 510 520 530 540 LHKSMRGSDQ NASLYWLARM LEGGEDPLYV ARRLVRFASE DIGLADPSAL TQAVAAYQGC 550 560 570 580 590 600 HFIGMPECEV LLAQCVVYFA RAPKSIEVYS AYNNVKACLR NHQGPLPPVP LHLRNAPTRL 610 620 630 640 MKDLGYGKGY KYNPMYSEPV DQEYLPEELR GVDFFKQRRC
	Isoform 3. Checksum: BDED370A47C0D894	FASTA	445	49,570
	10 20 30 40 50 60 MLQGKPLADT MRPDTLQDYF GQSKAVGQDT LLRSLLETNE IPSLILWGPP GCGKTTLAHI 70 80 90 100 110 120 IASNSKKHSI RFVTLSATNA KTNDVRDVIK QAQNEKSFFK RKTILFIDEI HRFNKSQQDT 130 140 150 160 170 180 FLPHVECGTI TLIGATTENP SFQVNAALLS RCRVIVLEKL PVEAMVTILM RAINSLGIHV 190 200 210 220 230 240 LDSSRPTDPL SHSSNSSSEP AMFIEDKAVD TLAYLSDGDA RAGLNGLQLA VLARLSSRKM 250 260 270 280 290 300 FCKKSGQSYS PSRVLITEND VKEGLQRSHI LYDRAGEEHY NCISALHKSM RGSDQNASLY 310 320 330 340 350 360 WLARMLEGGE DPLYVARRLV RFASEDIGLA DPSALTQAVA AYQGCHFIGM PECEVLLAQC 370 380 390 400 410 420 VVYFARAPKS IEVYSAYNNV KACLRNHQGP LPPVPLHLRN APTRLMKDLG YGKGYKYNPM 430 440 YSEPVDQEYL PEELRGVDFF KQRRC
	Isoform 4. Checksum: 1099DF56AA75F54A	FASTA	281	31,339
	10 20 30 40 50 60 MVTILMRAIN SLGIHVLDSS RPTDPLSHSS NSSSEPAMFI EDKAVDTLAY LSDGDARAGL 70 80 90 100 110 120 NGLQLAVLAR LSSRKMFCKK SGQSYSPSRV LITENDVKEG LQRSHILYDR AGEEHYNCIS 130 140 150 160 170 180 ALHKSMRGSD QNASLYWLAR MLEGGEDPLY VARRLVRFAS EDIGLADPSA LTQAVAAYQG 190 200 210 220 230 240 CHFIGMPECE VLLAQCVVYF ARAPKSIEVY SAYNNVKACL RNHQGPLPPV PLHLRNAPTR 250 260 270 280 LMKDLGYGKG YKYNPMYSEP VDQEYLPEEL RGVDFFKQRR C

References

	« Hide 'large scale' referencesShow '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]	"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. , 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] (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. , 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].
[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. , 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: 15489334] [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]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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: 17550899] [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, RAD18-TYPE ZINC FINGER.
[13]	"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.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; THR-85; SER-91; SER-92 AND THR-116, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-92, MASS SPECTROMETRY.
[17]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-153, MASS SPECTROMETRY.
[18]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-91; SER-92; THR-116 AND TYR-534, MASS SPECTROMETRY. Tissue: T-cell.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-633, MASS SPECTROMETRY.
+	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.
IPI	IPI00102997. IPI00290314. IPI00642533. IPI00645459.
RefSeq	NP_064520.2. NP_569079.1.
UniGene	Hs.236828
3D structure databases
SMR	Q96S55. Positions 230-552, 496-662.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96S55.
PTM databases
PhosphoSite	Q96S55.
Proteomic databases
PRIDE	Q96S55.
Genome annotation databases
Ensembl	ENST00000380773; ENSP00000370150; ENSG00000124535; Homo sapiens. [Genome view]
GeneID	56897.
KEGG	hsa:56897.
UCSC	uc003mtz.1. human. uc003mua.1. human.
Organism-specific databases
CTD	56897.
GeneCards	GC06P002710.
H-InvDB	HIX0005529.
HGNC	HGNC:20876. WRNIP1.
MIM	608196. gene.
PharmGKB	PA134982239.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11381.
HOVERGEN	Q96S55.
InParanoid	Q96S55.
OMA	GEDDPGH.
PhylomeDB	Q96S55.
Gene expression databases
ArrayExpress	Q96S55.
Bgee	Q96S55.
CleanEx	HS_WRNIP1.
Genevestigator	Q96S55.
GermOnline	ENSG00000124535. Homo sapiens.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR006642. Znf_Rad18_put. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM00734. ZnF_Rad18. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	62333.
SOURCE	Search...

Entry information

Entry name

WRIP1_HUMAN

Accession

Primary (citable) accession number: Q96S55
Secondary accession number(s): B2RDB0 , 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:	February 9, 2010
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.