Q96S55 (WRIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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.

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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW DNA synthesis involved in DNA repair Inferred from direct assay Ref.8. Source: UniProtKB regulation of DNA-dependent DNA replication initiation Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay PubMed 17888034. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 17888034. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from mutant phenotype Ref.8. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-2513471,EBI-2513471
DDX58	O95786	2	EBI-2513471,EBI-995350
POLD1	P28340	2	EBI-2513471,EBI-716569
POLD2	P49005	2	EBI-2513471,EBI-372354
POLD4	Q9HCU8	2	EBI-2513471,EBI-864968
TOLLIP	Q9H0E2	2	EBI-2513471,EBI-74615

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

UBZ-type

Nucleotide binding

268 – 275

8

ATP Potential

Amino acid modifications

Modified residue

75

1

Phosphoserine Ref.13 Ref.17

Modified residue

85

1

Phosphothreonine Ref.13 Ref.15

Modified residue

91

1

Phosphoserine Ref.13 Ref.15

Modified residue

92

1

Phosphoserine Ref.13 Ref.15

Modified residue

116

1

Phosphothreonine Ref.13

Modified residue

153

1

Phosphoserine Ref.17 Ref.19

Modified residue

534

1

Phosphotyrosine Ref.9

Modified residue

562

1

Phosphotyrosine Ref.9

Modified residue

633

1

N6-acetyllysine; alternate Ref.16

Cross-link

81

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

141

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

225

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

301

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

310

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

316

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

322

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

335

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

482

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

627

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

Cross-link

633

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.11

Cross-link

636

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.11

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

665

Helix Strand Turn

Details...

Beta strand

17 – 19

3

Turn

21 – 23

3

Beta strand

26 – 28

3

Helix

29 – 31

3

Helix

32 – 39

8

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 [UniParc]. 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 [UniParc]. 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 [UniParc]. 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] [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. , 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. , 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. , 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, 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] [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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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, 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. NM_020135.2.
NP_569079.1. NM_130395.2.

UniGene

Hs.236828.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3VHS	X-ray	1.90	A/B	17-40	[»]
3VHT	X-ray	2.40	B	9-46	[»]

ProteinModelPortal

Q96S55.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96S55. 12 interactions.

STRING

9606.ENSP00000370150.

PTM databases

PhosphoSite

Q96S55.

Polymorphism databases

DMDM

73622085.

Proteomic databases

PaxDb

Q96S55.

PRIDE

Q96S55.

Protocols and materials databases

DNASU

56897.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380764; ENSP00000370141; ENSG00000124535.
ENST00000380769; ENSP00000370146; ENSG00000124535.
ENST00000380771; ENSP00000370148; ENSG00000124535.
ENST00000380773; ENSP00000370150; ENSG00000124535.

GeneID

56897.

KEGG

hsa:56897.

UCSC

uc003mtz.3. human.
uc003mua.3. human.

Organism-specific databases

CTD

56897.

GeneCards

GC06P002710.

H-InvDB

HIX0005529.

HGNC

HGNC:20876. WRNIP1.

HPA

HPA031752.

MIM

608196. gene.

neXtProt

NX_Q96S55.

PharmGKB

PA134982239.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2256.

HOVERGEN

HBG062192.

InParanoid

Q96S55.

KO

K07478.

OMA

PGHWDAD.

OrthoDB

EOG457568.

PhylomeDB

Q96S55.

Gene expression databases

Bgee

Q96S55.

CleanEx

HS_WRNIP1.

Genevestigator

Q96S55.

GermOnline

ENSG00000124535. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021886. MgsA_C.
IPR006642. Znf_Rad18_put.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF12002. MgsA_C. 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

GenomeRNAi

56897.

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:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.