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Q7Z5K2

- WAPL_HUMAN

UniProt

Q7Z5K2 - WAPL_HUMAN

Protein

Wings apart-like protein homolog

Gene

WAPAL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. Involved in both sister chromatid cohesion during interphase and sister-chromatid resolution during early stages of mitosis. Couples DNA replication to sister chromatid cohesion. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair.7 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    2. mitotic nuclear division Source: UniProtKB-KW
    3. negative regulation of chromatin binding Source: UniProtKB
    4. negative regulation of DNA replication Source: UniProtKB
    5. negative regulation of sister chromatid cohesion Source: UniProtKB
    6. protein localization to chromatin Source: UniProtKB
    7. regulation of cohesin localization to chromatin Source: UniProtKB
    8. response to toxic substance Source: Ensembl
    9. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wings apart-like protein homolog
    Alternative name(s):
    Friend of EBNA2 protein
    Gene namesi
    Name:WAPAL
    Synonyms:FOE, KIAA0261, WAPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23293. WAPAL.

    Subcellular locationi

    Nucleus. Chromosome. Cytoplasm
    Note: Associates with chromatin through the cohesin complex during interphase. Released in the cytoplasm from nuclear envelope breakdown until anaphase, it reaccumulates in nucleus at telophase.

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. chromosome Source: Reactome
    3. chromosome, centromeric region Source: Reactome
    4. cohesin complex Source: UniProtKB
    5. cytoplasm Source: UniProtKB
    6. cytosol Source: Reactome
    7. intracellular membrane-bounded organelle Source: HPA
    8. microtubule cytoskeleton Source: HPA
    9. nucleoplasm Source: Reactome
    10. nucleus Source: UniProtKB
    11. synaptonemal complex Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 753FGF → EGE: Loss of interaction with PDS5B; when associated with 429-E--E-431 and 453-E--E-455. 1 Publication
    Mutagenesisi429 – 4313FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 453-E--E-455. 1 Publication
    Mutagenesisi453 – 4553FGF → EGE: Loss of interaction with PDS5B; when associated with 73-E--E-75 and 429-E--E-431. 1 Publication
    Mutagenesisi639 – 6402VK → AE: Impaired sister chromatid cohesion and resolution. 1 Publication
    Mutagenesisi656 – 6572DD → KK: Impaired sister chromatid cohesion and resolution. 1 Publication
    Mutagenesisi770 – 7701E → K: No effect. 2 Publications
    Mutagenesisi777 – 7771E → K: No effect. 2 Publications
    Mutagenesisi787 – 7871E → K: No effect. 2 Publications
    Mutagenesisi790 – 7901T → A: No effect. 2 Publications
    Mutagenesisi1116 – 11161M → A: Impaired sister chromatid cohesion and resolution; when associated with A-1120. 2 Publications
    Mutagenesisi1120 – 11201I → A: Impaired sister chromatid cohesion and resolution; when associated with A-1116. 2 Publications

    Organism-specific databases

    PharmGKBiPA134872402.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11901190Wings apart-like protein homologPRO_0000245232Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine6 Publications
    Modified residuei168 – 1681N6-acetyllysine1 Publication
    Modified residuei221 – 2211Phosphoserine3 Publications
    Modified residuei223 – 2231Phosphoserine2 Publications
    Modified residuei226 – 2261Phosphoserine5 Publications
    Modified residuei380 – 3801Phosphoserine2 Publications
    Modified residuei459 – 4591Phosphoserine1 Publication
    Modified residuei461 – 4611Phosphoserine1 Publication
    Modified residuei904 – 9041Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z5K2.
    PaxDbiQ7Z5K2.
    PRIDEiQ7Z5K2.

    PTM databases

    PhosphoSiteiQ7Z5K2.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in uterine cervix tumor. Isoform 2 is widely expressed with a high level in skeletal muscle and heart.2 Publications

    Gene expression databases

    ArrayExpressiQ7Z5K2.
    BgeeiQ7Z5K2.
    CleanExiHS_WAPAL.
    GenevestigatoriQ7Z5K2.

    Organism-specific databases

    HPAiHPA037874.
    HPA037875.

    Interactioni

    Subunit structurei

    Interacts with the cohesin complex throughout the cell cycle; interacts with both chromatin-bound and soluble pools of the complex. Interacts with RAD21; the interaction is direct. Interacts with PDS5A; the interaction is direct, cohesin-dependent and competitive with CDCA5/SORORIN. Interacts (via FGF motifs) with PDS5B; the interaction is direct. Interacts with a SMC1 protein (SMC1A or SMC1B) and SMC3. Isoform 2 interacts with Epstein-Barr virus EBNA2.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDS5BQ9NTI59EBI-1022242,EBI-1175604
    RAD21O6021611EBI-1022242,EBI-80739

    Protein-protein interaction databases

    BioGridi116698. 26 interactions.
    DIPiDIP-31176N.
    IntActiQ7Z5K2. 14 interactions.
    MINTiMINT-4123122.
    STRINGi9606.ENSP00000298767.

    Structurei

    Secondary structure

    1
    1190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi631 – 64010
    Helixi652 – 66413
    Helixi671 – 68414
    Helixi688 – 6969
    Helixi700 – 7067
    Turni707 – 7093
    Helixi710 – 7123
    Helixi714 – 72714
    Turni733 – 7353
    Helixi738 – 74912
    Helixi765 – 78016
    Helixi786 – 7883
    Helixi791 – 80212
    Turni805 – 8073
    Helixi810 – 8178
    Helixi820 – 83617
    Helixi841 – 86222
    Helixi866 – 89732
    Beta strandi909 – 9113
    Helixi917 – 94125
    Helixi945 – 9528
    Helixi957 – 96610
    Helixi968 – 9714
    Helixi974 – 9763
    Helixi977 – 99216
    Helixi996 – 10038
    Helixi1032 – 105827
    Helixi1107 – 113529
    Helixi1137 – 114610
    Helixi1148 – 11503
    Helixi1153 – 116917
    Helixi1174 – 118815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4K6JX-ray2.62A/B631-1190[»]
    ProteinModelPortaliQ7Z5K2.
    SMRiQ7Z5K2. Positions 631-1190.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini626 – 1169544WAPLPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 659659Mediates interaction with the cohesin complexAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili260 – 28627Sequence AnalysisAdd
    BLAST
    Coiled coili749 – 78234Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi73 – 753FGF motif 1
    Motifi429 – 4313FGF motif 2
    Motifi453 – 4553FGF motif 3

    Sequence similaritiesi

    Belongs to the WAPL family.Curated
    Contains 1 WAPL domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG297597.
    HOGENOMiHOG000001563.
    HOVERGENiHBG088338.
    InParanoidiQ7Z5K2.
    OMAiWNSQFGK.
    OrthoDBiEOG7DZ8J3.
    PhylomeDBiQ7Z5K2.
    TreeFamiTF323477.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR012502. WAPL_metazoan_plants.
    IPR022771. WAPL_prot.
    [Graphical view]
    PfamiPF07814. WAPL. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    PROSITEiPS51271. WAPL. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Named isoforms=2.

    Isoform 1 (identifier: Q7Z5K2-1) [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

    MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN     50
    FKPDIQEIPK KPKVEEESTG DPFGFDSDDE SLPVSSKNLA QVKCSSYSES 100
    SEAAQLEEVT SVLEANSKIS HVVVEDTVVS DKCFPLEDTL LGKEKSTNRI 150
    VEDDASISSC NKLITSDKVE NFHEEHEKNS HHIHKNADDS TKKPNAETTV 200
    ASEIKETNDT WNSQFGKRPE SPSEISPIKG SVRTGLFEWD NDFEDIRSED 250
    CILSLDSDPL LEMKDDDFKN RLENLNEAIE EDIVQSVLRP TNCRTYCRAN 300
    KTKSSQGASN FDKLMDGTSQ ALAKANSESS KDGLNQAKKG GVSCGTSFRG 350
    TVGRTRDYTV LHPSCLSVCN VTIQDTMERS MDEFTASTPA DLGEAGRLRK 400
    KADIATSKTT TRFRPSNTKS KKDVKLEFFG FEDHETGGDE GGSGSSNYKI 450
    KYFGFDDLSE SEDDEDDDCQ VERKTSKKRT KTAPSPSLQP PPESNDNSQD 500
    SQSGTNNAEN LDFTEDLPGV PESVKKPINK QGDKSKENTR KIFSGPKRSP 550
    TKAVYNARHW NHPDSEELPG PPVVKPQSVT VRLSSKEPNQ KDDGVFKAPA 600
    PPSKVIKTVT IPTQPYQDIV TALKCRREDK ELYTVVQHVK HFNDVVEFGE 650
    NQEFTDDIEY LLSGLKSTQP LNTRCLSVIS LATKCAMPSF RMHLRAHGMV 700
    AMVFKTLDDS QHHQNLSLCT AALMYILSRD RLNMDLDRAS LDLMIRLLEL 750
    EQDASSAKLL NEKDMNKIKE KIRRLCETVH NKHLDLENIT TGHLAMETLL 800
    SLTSKRAGDW FKEELRLLGG LDHIVDKVKE CVDHLSRDED EEKLVASLWG 850
    AERCLRVLES VTVHNPENQS YLIAYKDSQL IVSSAKALQH CEELIQQYNR 900
    AEDSICLADS KPLPHQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK 950
    TGEQDGLIGT ALNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH 1000
    CLVNMETSCS FDSSICSGEG DDSLRIGGQV HAVQALVQLF LERERAAQLA 1050
    ESKTDELIKD APTTQHDKSG EWQETSGEIQ WVSTEKTDGT EEKHKKEEED 1100
    EELDLNKALQ HAGKHMEDCI VASYTALLLG CLCQESPINV TTVREYLPEG 1150
    DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC 1190
    Length:1,190
    Mass (Da):132,946
    Last modified:October 1, 2003 - v1
    Checksum:iA01026E520BFAB2F
    GO
    Isoform 2 (identifier: Q7Z5K2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVQGPVQTPALTIHRRKRRRRRRRRPVAKAPARLRGEYETGVKM
         510-515: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,227
    Mass (Da):137,314
    Checksum:i5431910072375C05
    GO
    Isoform 3 (identifier: Q7Z5K2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVQGPVQTPA...RGEYETGVKM

    Note: No experimental confirmation available.

    Show »
    Length:1,275
    Mass (Da):142,525
    Checksum:i5588D17DBB5C782F
    GO

    Sequence cautioni

    The sequence BAA13391.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAH73376.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI16708.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti124 – 1241V → I.
    Corresponds to variant rs10887621 [ dbSNP | Ensembl ].
    VAR_026967

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MVQGPVQTPALTIHRRKRRR RRRRRPVAKAPARLRGEYET GVKM in isoform 2. 1 PublicationVSP_019649
    Alternative sequencei1 – 11M → MVQGPVQTPALTIHRRKRRR SCPPNRASYLPKAESLASLG SHLPALLSRARVPRPPAGRR ERERRRRPVAKAPARLRGEY ETGVKM in isoform 3. 1 PublicationVSP_019650
    Alternative sequencei510 – 5156Missing in isoform 2. 1 PublicationVSP_019651

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB065003 mRNA. Translation: BAC78631.1.
    AF479418 mRNA. Translation: AAO14651.1.
    D87450 mRNA. Translation: BAA13391.1. Different initiation.
    AL844892, AL731569 Genomic DNA. Translation: CAH73376.1. Sequence problems.
    AL731569, AL844892 Genomic DNA. Translation: CAI16708.1. Sequence problems.
    CH471142 Genomic DNA. Translation: EAW80336.1.
    BC150269 mRNA. Translation: AAI50270.1.
    CCDSiCCDS7375.1. [Q7Z5K2-1]
    RefSeqiNP_055860.1. NM_015045.2. [Q7Z5K2-1]
    UniGeneiHs.203099.
    Hs.714876.

    Genome annotation databases

    EnsembliENST00000298767; ENSP00000298767; ENSG00000062650. [Q7Z5K2-1]
    GeneIDi23063.
    KEGGihsa:23063.
    UCSCiuc001kdn.3. human. [Q7Z5K2-2]
    uc001kdo.3. human. [Q7Z5K2-1]

    Polymorphism databases

    DMDMi74713658.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB065003 mRNA. Translation: BAC78631.1 .
    AF479418 mRNA. Translation: AAO14651.1 .
    D87450 mRNA. Translation: BAA13391.1 . Different initiation.
    AL844892 , AL731569 Genomic DNA. Translation: CAH73376.1 . Sequence problems.
    AL731569 , AL844892 Genomic DNA. Translation: CAI16708.1 . Sequence problems.
    CH471142 Genomic DNA. Translation: EAW80336.1 .
    BC150269 mRNA. Translation: AAI50270.1 .
    CCDSi CCDS7375.1. [Q7Z5K2-1 ]
    RefSeqi NP_055860.1. NM_015045.2. [Q7Z5K2-1 ]
    UniGenei Hs.203099.
    Hs.714876.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4K6J X-ray 2.62 A/B 631-1190 [» ]
    ProteinModelPortali Q7Z5K2.
    SMRi Q7Z5K2. Positions 631-1190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116698. 26 interactions.
    DIPi DIP-31176N.
    IntActi Q7Z5K2. 14 interactions.
    MINTi MINT-4123122.
    STRINGi 9606.ENSP00000298767.

    PTM databases

    PhosphoSitei Q7Z5K2.

    Polymorphism databases

    DMDMi 74713658.

    Proteomic databases

    MaxQBi Q7Z5K2.
    PaxDbi Q7Z5K2.
    PRIDEi Q7Z5K2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298767 ; ENSP00000298767 ; ENSG00000062650 . [Q7Z5K2-1 ]
    GeneIDi 23063.
    KEGGi hsa:23063.
    UCSCi uc001kdn.3. human. [Q7Z5K2-2 ]
    uc001kdo.3. human. [Q7Z5K2-1 ]

    Organism-specific databases

    CTDi 23063.
    GeneCardsi GC10M088185.
    HGNCi HGNC:23293. WAPAL.
    HPAi HPA037874.
    HPA037875.
    MIMi 610754. gene.
    neXtProti NX_Q7Z5K2.
    PharmGKBi PA134872402.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297597.
    HOGENOMi HOG000001563.
    HOVERGENi HBG088338.
    InParanoidi Q7Z5K2.
    OMAi WNSQFGK.
    OrthoDBi EOG7DZ8J3.
    PhylomeDBi Q7Z5K2.
    TreeFami TF323477.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.

    Miscellaneous databases

    ChiTaRSi WAPAL. human.
    GeneWikii WAPAL.
    GenomeRNAii 23063.
    NextBioi 44141.
    PROi Q7Z5K2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z5K2.
    Bgeei Q7Z5K2.
    CleanExi HS_WAPAL.
    Genevestigatori Q7Z5K2.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR012502. WAPL_metazoan_plants.
    IPR022771. WAPL_prot.
    [Graphical view ]
    Pfami PF07814. WAPL. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    PROSITEi PS51271. WAPL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of a novel human gene, human wings apart-like (hWAPL), is associated with cervical carcinogenesis and tumor progression."
      Oikawa K., Ohbayashi T., Kiyono T., Nishi H., Isaka K., Umezawa A., Kuroda M., Mukai K.
      Cancer Res. 64:3545-3549(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    2. "Identification and cloning of a novel chromatin-associated protein partner of Epstein-Barr nuclear protein 2."
      Kwiatkowski B.A., Ragoczy T., Ehly J., Schubach W.H.
      Exp. Cell Res. 300:223-233(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Bone marrow.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [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 1).
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Wapl controls the dynamic association of cohesin with chromatin."
      Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A., Mechtler K., Peters J.M.
      Cell 127:955-967(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH THE COHESIN COMPLEX AND PDS5A, SUBCELLULAR LOCATION.
    9. "Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase."
      Gandhi R., Gillespie P.J., Hirano T.
      Curr. Biol. 16:2406-2417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE COHESIN COMPLEX, SUBCELLULAR LOCATION.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-221; SER-223; SER-226; SER-380; SER-459; SER-461 AND SER-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Carrascal M., Abian J.
      Submitted (JAN-2008) to UniProtKB
      Cited for: PHOSPHORYLATION AT SER-223, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    13. "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].
    14. "Releasing cohesin from chromosome arms in early mitosis: opposing actions of Wapl-Pds5 and Sgo1."
      Shintomi K., Hirano T.
      Genes Dev. 23:2224-2236(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PDS5B AND RAD21, MUTAGENESIS OF 73-PHE--PHE-75; 429-PHE--PHE-431 AND 453-PHE--PHE-455, FGF MOTIFS.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Cohesin acetylation speeds the replication fork."
      Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.
      Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMC3.
    17. "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 SER-77 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-168, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: FUNCTION, INTERACTION WITH PDS5A.
    20. "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-77; SER-221 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-77; SER-221 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 631-1190, FUNCTION, INTERACTION WITH PDS5A; SMC1; SMC3; STAG2 AND CDCA5, SUBUNIT, MUTAGENESIS OF 639-VAL-LYS-640; 656-ASP-ASP-657; GLU-770; GLU-777; GLU-787; THR-790; MET-1116 AND ILE-1120.

    Entry informationi

    Entry nameiWAPL_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z5K2
    Secondary accession number(s): A7E2B5
    , Q5VSK5, Q8IX10, Q92549
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 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 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3