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Q96S55

- WRIP1_HUMAN

UniProt

Q96S55 - WRIP1_HUMAN

Protein

ATPase WRNIP1

Gene

WRNIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri17 – 4024UBZ-typeAdd
    BLAST
    Nucleotide bindingi268 – 2758ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. DNA binding Source: InterPro
    4. identical protein binding Source: IntAct
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA replication Source: UniProtKB-KW
    3. DNA synthesis involved in DNA repair Source: UniProtKB
    4. regulation of DNA-dependent DNA replication initiation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA replication

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATPase WRNIP1 (EC:3.6.1.3)
    Alternative name(s):
    Werner helicase-interacting protein 1
    Gene namesi
    Name:WRNIP1Imported
    Synonyms:WHIPImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20876. WRNIP1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134982239.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 665665ATPase WRNIP1PRO_0000084785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751Phosphoserine2 Publications
    Cross-linki81 – 81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei85 – 851Phosphothreonine2 Publications
    Modified residuei91 – 911Phosphoserine2 Publications
    Modified residuei92 – 921Phosphoserine2 Publications
    Modified residuei116 – 1161Phosphothreonine1 Publication
    Cross-linki141 – 141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei153 – 1531Phosphoserine2 Publications
    Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki301 – 301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki310 – 310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki316 – 316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki322 – 322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki335 – 335Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki482 – 482Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei534 – 5341Phosphotyrosine1 Publication
    Modified residuei562 – 5621Phosphotyrosine1 Publication
    Cross-linki627 – 627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei633 – 6331N6-acetyllysine; alternate1 Publication
    Cross-linki633 – 633Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Cross-linki636 – 636Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Sumoylated with SUMO1 and SUMO2/3.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96S55.
    PaxDbiQ96S55.
    PRIDEiQ96S55.

    PTM databases

    PhosphoSiteiQ96S55.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ96S55.
    CleanExiHS_WRNIP1.
    GenevestigatoriQ96S55.

    Organism-specific databases

    HPAiHPA031752.
    HPA031753.

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2513471,EBI-2513471
    DDX58O957862EBI-2513471,EBI-995350
    POLD1P283402EBI-2513471,EBI-716569
    POLD2P490052EBI-2513471,EBI-372354
    POLD4Q9HCU82EBI-2513471,EBI-864968
    TOLLIPQ9H0E22EBI-2513471,EBI-74615

    Protein-protein interaction databases

    BioGridi121227. 25 interactions.
    IntActiQ96S55. 15 interactions.
    MINTiMINT-3058154.
    STRINGi9606.ENSP00000370150.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 193
    Turni21 – 233
    Beta strandi26 – 283
    Helixi29 – 313
    Helixi32 – 398

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VHSX-ray1.90A/B17-40[»]
    3VHTX-ray2.40B9-46[»]
    ProteinModelPortaliQ96S55.
    SMRiQ96S55. Positions 12-46, 225-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Sequence Analysis
    Contains 1 UBZ-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri17 – 4024UBZ-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2256.
    HOVERGENiHBG062192.
    InParanoidiQ96S55.
    KOiK07478.
    OMAiPGHWDAD.
    OrthoDBiEOG744T8W.
    PhylomeDBiQ96S55.
    TreeFamiTF324547.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. 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]
    PfamiPF00004. AAA. 1 hit.
    PF12002. MgsA_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00734. ZnF_Rad18. 1 hit.
    [Graphical view]
    SUPFAMiSSF48019. SSF48019. 1 hit.
    SSF52540. SSF52540. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q96S55-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP    50
    AAGSHRAGER AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD 100
    DGGETESRES YDAPPTPSGA RLIPDFPVAR SSSPGRKGSG KRPAAAAAAG 150
    SASPRSWDEA EAQEEEEAVG DGDGDGDADA DGEDDPGHWD ADAAEAATAF 200
    GASGGGRPHP RALAAEEIRQ MLQGKPLADT MRPDTLQDYF GQSKAVGQDT 250
    LLRSLLETNE IPSLILWGPP GCGKTTLAHI IASNSKKHSI RFVTLSATNA 300
    KTNDVRDVIK QAQNEKSFFK RKTILFIDEI HRFNKSQQDT FLPHVECGTI 350
    TLIGATTENP SFQVNAALLS RCRVIVLEKL PVEAMVTILM RAINSLGIHV 400
    LDSSRPTDPL SHSSNSSSEP AMFIEDKAVD TLAYLSDGDA RAGLNGLQLA 450
    VLARLSSRKM FCKKSGQSYS PSRVLITEND VKEGLQRSHI LYDRAGEEHY 500
    NCISALHKSM RGSDQNASLY WLARMLEGGE DPLYVARRLV RFASEDIGLA 550
    DPSALTQAVA AYQGCHFIGM PECEVLLAQC VVYFARAPKS IEVYSAYNNV 600
    KACLRNHQGP LPPVPLHLRN APTRLMKDLG YGKGYKYNPM YSEPVDQEYL 650
    PEELRGVDFF KQRRC 665
    Length:665
    Mass (Da):72,133
    Last modified:August 16, 2005 - v2
    Checksum:iDE43D8E59C4B29E8
    GO
    Isoform 21 Publication (identifier: Q96S55-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         338-362: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:640
    Mass (Da):69,459
    Checksum:i83117E6CEFDE7688
    GO
    Isoform 31 Publication (identifier: Q96S55-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-220: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:445
    Mass (Da):49,570
    Checksum:iBDED370A47C0D894
    GO
    Isoform 41 Publication (identifier: Q96S55-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-384: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:281
    Mass (Da):31,339
    Checksum:i1099DF56AA75F54A
    GO

    Sequence cautioni

    The sequence AAF80563.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB15383.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441A → V in BAB60709. (PubMed:11301316)Curated
    Sequence conflicti170 – 1734Missing in BAD92960. 1 PublicationCurated
    Sequence conflicti265 – 2651I → N in BAB60709. (PubMed:11301316)Curated
    Sequence conflicti377 – 3771L → F in BAB15383. (PubMed:14702039)Curated
    Sequence conflicti499 – 4991H → Y in BAD97313. 1 PublicationCurated
    Sequence conflicti545 – 5451E → G in BAB15383. (PubMed:14702039)Curated
    Sequence conflicti568 – 5681I → M in BAB60709. (PubMed:11301316)Curated
    Sequence conflicti576 – 5761L → F in BAB60709. (PubMed:11301316)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 384384Missing in isoform 4. 1 PublicationVSP_051782Add
    BLAST
    Alternative sequencei1 – 220220Missing in isoform 3. 1 PublicationVSP_051781Add
    BLAST
    Alternative sequencei338 – 36225Missing in isoform 2. 3 PublicationsVSP_051783Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4475.1. [Q96S55-1]
    CCDS4476.1. [Q96S55-2]
    RefSeqiNP_064520.2. NM_020135.2. [Q96S55-1]
    NP_569079.1. NM_130395.2. [Q96S55-2]
    UniGeneiHs.236828.

    Genome annotation databases

    EnsembliENST00000380764; ENSP00000370141; ENSG00000124535. [Q96S55-4]
    ENST00000380769; ENSP00000370146; ENSG00000124535. [Q96S55-3]
    ENST00000380771; ENSP00000370148; ENSG00000124535. [Q96S55-2]
    ENST00000380773; ENSP00000370150; ENSG00000124535. [Q96S55-1]
    GeneIDi56897.
    KEGGihsa:56897.
    UCSCiuc003mtz.3. human. [Q96S55-1]
    uc003mua.3. human. [Q96S55-2]

    Polymorphism databases

    DMDMi73622085.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS4475.1. [Q96S55-1 ]
    CCDS4476.1. [Q96S55-2 ]
    RefSeqi NP_064520.2. NM_020135.2. [Q96S55-1 ]
    NP_569079.1. NM_130395.2. [Q96S55-2 ]
    UniGenei Hs.236828.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VHS X-ray 1.90 A/B 17-40 [» ]
    3VHT X-ray 2.40 B 9-46 [» ]
    ProteinModelPortali Q96S55.
    SMRi Q96S55. Positions 12-46, 225-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121227. 25 interactions.
    IntActi Q96S55. 15 interactions.
    MINTi MINT-3058154.
    STRINGi 9606.ENSP00000370150.

    PTM databases

    PhosphoSitei Q96S55.

    Polymorphism databases

    DMDMi 73622085.

    Proteomic databases

    MaxQBi Q96S55.
    PaxDbi Q96S55.
    PRIDEi Q96S55.

    Protocols and materials databases

    DNASUi 56897.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380764 ; ENSP00000370141 ; ENSG00000124535 . [Q96S55-4 ]
    ENST00000380769 ; ENSP00000370146 ; ENSG00000124535 . [Q96S55-3 ]
    ENST00000380771 ; ENSP00000370148 ; ENSG00000124535 . [Q96S55-2 ]
    ENST00000380773 ; ENSP00000370150 ; ENSG00000124535 . [Q96S55-1 ]
    GeneIDi 56897.
    KEGGi hsa:56897.
    UCSCi uc003mtz.3. human. [Q96S55-1 ]
    uc003mua.3. human. [Q96S55-2 ]

    Organism-specific databases

    CTDi 56897.
    GeneCardsi GC06P002766.
    H-InvDB HIX0005529.
    HGNCi HGNC:20876. WRNIP1.
    HPAi HPA031752.
    HPA031753.
    MIMi 608196. gene.
    neXtProti NX_Q96S55.
    PharmGKBi PA134982239.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2256.
    HOVERGENi HBG062192.
    InParanoidi Q96S55.
    KOi K07478.
    OMAi PGHWDAD.
    OrthoDBi EOG744T8W.
    PhylomeDBi Q96S55.
    TreeFami TF324547.

    Miscellaneous databases

    GeneWikii WRNIP1.
    GenomeRNAii 56897.
    NextBioi 62333.
    PROi Q96S55.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96S55.
    CleanExi HS_WRNIP1.
    Genevestigatori Q96S55.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. 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 ]
    Pfami PF00004. AAA. 1 hit.
    PF12002. MgsA_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00734. ZnF_Rad18. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48019. SSF48019. 1 hit.
    SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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 epitheliumImported.
    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: BrainImported and KidneyImported.
    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. 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: MuscleImported.
    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. 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. 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. 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].

    Entry informationi

    Entry nameiWRIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q96S55
    Secondary accession number(s): B2RDB0
    , Q53EP6, Q59ET8, Q5W0E2, Q5W0E4, Q8WV26, Q9H681, Q9NRJ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3