Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BTA9

- WAC_HUMAN

UniProt

Q9BTA9 - WAC_HUMAN

Protein

WW domain-containing adapter protein with coiled-coil

Gene

WAC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (31 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. May negatively regulate the ubiquitin proteasome pathway.2 Publications

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. G1 DNA damage checkpoint Source: UniProtKB
    3. histone H2B conserved C-terminal lysine ubiquitination Source: UniProtKB
    4. histone monoubiquitination Source: UniProtKB
    5. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
    6. positive regulation of macroautophagy Source: BHF-UCL
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiQ9BTA9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    WW domain-containing adapter protein with coiled-coil
    Gene namesi
    Name:WAC
    Synonyms:KIAA1844
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17327. WAC.

    Subcellular locationi

    Nucleus speckle By similarity. Nucleus 1 Publication
    Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes By similarity.By similarity

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: BHF-UCL
    3. spliceosomal complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134978936.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 647647WW domain-containing adapter protein with coiled-coilPRO_0000254558Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Phosphoserine2 Publications
    Modified residuei293 – 2931Phosphothreonine1 Publication
    Modified residuei302 – 3021N6-acetyllysine1 Publication
    Modified residuei471 – 4711Phosphothreonine1 Publication
    Modified residuei511 – 5111Phosphoserine1 Publication
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei525 – 5251Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine residues.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BTA9.
    PaxDbiQ9BTA9.
    PRIDEiQ9BTA9.

    PTM databases

    PhosphoSiteiQ9BTA9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BTA9.
    BgeeiQ9BTA9.
    CleanExiHS_WAC.
    GenevestigatoriQ9BTA9.

    Organism-specific databases

    HPAiHPA036528.
    HPA042609.

    Interactioni

    Subunit structurei

    Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428585EBI-749118,EBI-466029

    Protein-protein interaction databases

    BioGridi119473. 17 interactions.
    IntActiQ9BTA9. 12 interactions.
    MINTiMINT-2873194.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BTA9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 16234WWPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili618 – 64427Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 WW domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG299824.
    HOVERGENiHBG057585.
    InParanoidiQ9BTA9.
    OMAiHKILTAG.
    OrthoDBiEOG7T1RB9.
    PhylomeDBiQ9BTA9.
    TreeFamiTF328635.

    Family and domain databases

    InterProiIPR001202. WW_dom.
    [Graphical view]
    PfamiPF00397. WW. 1 hit.
    [Graphical view]
    SMARTiSM00456. WW. 1 hit.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 1 hit.
    PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BTA9-1) [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

    MVMYARKQQR LSDGCHDRRG DSQPYQALKY SSKSHPSSGD HRHEKMRDAG    50
    DPSPPNKMLR RSDSPENKYS DSTGHSKAKN VHTHRVRERD GGTSYSPQEN 100
    SHNHSALHSS NSHSSNPSNN PSKTSDAPYD SADDWSEHIS SSGKKYYYNC 150
    RTEVSQWEKP KEWLEREQRQ KEANKMAVNS FPKDRDYRRE VMQATATSGF 200
    ASGMEDKHSS DASSLLPQNI LSQTSRHNDR DYRLPRAETH SSSTPVQHPI 250
    KPVVHPTATP STVPSSPFTL QSDHQPKKSF DANGASTLSK LPTPTSSVPA 300
    QKTERKESTS GDKPVSHSCT TPSTSSASGL NPTSAPPTSA SAVPVSPVPQ 350
    SPIPPLLQDP NLLRQLLPAL QATLQLNNSN VDISKINEVL TAAVTQASLQ 400
    SIIHKFLTAG PSAFNITSLI SQAAQLSTQA QPSNQSPMSL TSDASSPRSY 450
    VSPRISTPQT NTVPIKPLIS TPPVSSQPKV STPVVKQGPV SQSATQQPVT 500
    ADKQQGHEPV SPRSLQRSSS QRSPSPGPNH TSNSSNASNA TVVPQNSSAR 550
    STCSLTPALA AHFSENLIKH VQGWPADHAE KQASRLREEA HNMGTIHMSE 600
    ICTELKNLRS LVRVCEIQAT LREQRILFLR QQIKELEKLK NQNSFMV 647
    Length:647
    Mass (Da):70,724
    Last modified:October 31, 2006 - v3
    Checksum:i15C32DAAA3A94129
    GO
    Isoform 2 (identifier: Q9BTA9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: Missing.

    Show »
    Length:602
    Mass (Da):65,482
    Checksum:i8CBBD18CA1EB3243
    GO
    Isoform 3 (identifier: Q9BTA9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: Missing.
         430-481: AQPSNQSPMS...PPVSSQPKVS → DIPLHEGIQM...MVQRLLQPSG
         482-647: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:436
    Mass (Da):47,717
    Checksum:i6C379F47ACC90136
    GO
    Isoform 4 (identifier: Q9BTA9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         204-307: MEDKHSSDAS...VPAQKTERKE → K

    Show »
    Length:544
    Mass (Da):59,505
    Checksum:i93716FBA60085245
    GO

    Sequence cautioni

    The sequence BAB47473.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAH04258.2 differs from that shown. Reason: Frameshift at position 641.
    The sequence AAH10356.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH70767.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI40921.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI40923.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti426 – 4261L → F in BAB71029. (PubMed:14702039)Curated
    Sequence conflicti581 – 5811K → R in AAH10356. (PubMed:15489334)Curated
    Sequence conflicti599 – 5991S → P in BAD97320. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti242 – 2421S → R.
    Corresponds to variant rs11595926 [ dbSNP | Ensembl ].
    VAR_028838
    Natural varianti309 – 3091T → A.
    Corresponds to variant rs2232791 [ dbSNP | Ensembl ].
    VAR_053448
    Natural varianti475 – 4751S → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036351
    Natural varianti531 – 5311T → S.
    Corresponds to variant rs7127 [ dbSNP | Ensembl ].
    VAR_028839

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4545Missing in isoform 2 and isoform 3. 2 PublicationsVSP_021230Add
    BLAST
    Alternative sequencei204 – 307104MEDKH…TERKE → K in isoform 4. 1 PublicationVSP_021231Add
    BLAST
    Alternative sequencei430 – 48152AQPSN…QPKVS → DIPLHEGIQMERDTHRSKWE VKGSLCQKADKQQECLVWNG SIMVQRLLQPSG in isoform 3. 1 PublicationVSP_021233Add
    BLAST
    Alternative sequencei482 – 647166Missing in isoform 3. 1 PublicationVSP_021236Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055852 mRNA. Translation: BAB71029.1.
    AK223600 mRNA. Translation: BAD97320.1.
    AK290174 mRNA. Translation: BAF82863.1.
    AL713727 mRNA. Translation: CAD28517.1.
    AL358234, AL161936 Genomic DNA. Translation: CAH70766.1.
    AL358234, AL161936 Genomic DNA. Translation: CAH70768.1.
    AL161936, AL358234 Genomic DNA. Translation: CAI40922.1.
    AL161936, AL358234 Genomic DNA. Translation: CAI40924.1.
    AL161936 Genomic DNA. Translation: CAI40921.1. Sequence problems.
    AL358234, AL161936 Genomic DNA. Translation: CAH70767.1. Sequence problems.
    AL161936, AL358234 Genomic DNA. Translation: CAI40923.1. Sequence problems.
    CH471072 Genomic DNA. Translation: EAW86032.1.
    CH471072 Genomic DNA. Translation: EAW86035.1.
    CH471072 Genomic DNA. Translation: EAW86037.1.
    CH471072 Genomic DNA. Translation: EAW86039.1.
    CH471072 Genomic DNA. Translation: EAW86040.1.
    CH471072 Genomic DNA. Translation: EAW86042.1.
    BC004258 mRNA. Translation: AAH04258.2. Frameshift.
    BC010356 mRNA. Translation: AAH10356.1. Different initiation.
    AB058747 mRNA. Translation: BAB47473.1. Sequence problems.
    CCDSiCCDS7159.1. [Q9BTA9-1]
    CCDS7160.1. [Q9BTA9-5]
    RefSeqiNP_057712.2. NM_016628.4. [Q9BTA9-1]
    NP_567823.1. NM_100486.3. [Q9BTA9-5]
    XP_005252514.1. XM_005252457.1. [Q9BTA9-2]
    UniGeneiHs.743224.

    Genome annotation databases

    EnsembliENST00000347934; ENSP00000311106; ENSG00000095787. [Q9BTA9-5]
    ENST00000354911; ENSP00000346986; ENSG00000095787. [Q9BTA9-1]
    ENST00000375664; ENSP00000364816; ENSG00000095787. [Q9BTA9-2]
    ENST00000428935; ENSP00000399706; ENSG00000095787. [Q9BTA9-3]
    ENST00000439676; ENSP00000415727; ENSG00000095787. [Q9BTA9-3]
    GeneIDi51322.
    KEGGihsa:51322.
    UCSCiuc001iud.3. human. [Q9BTA9-1]
    uc001iue.3. human. [Q9BTA9-5]

    Polymorphism databases

    DMDMi117949358.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055852 mRNA. Translation: BAB71029.1 .
    AK223600 mRNA. Translation: BAD97320.1 .
    AK290174 mRNA. Translation: BAF82863.1 .
    AL713727 mRNA. Translation: CAD28517.1 .
    AL358234 , AL161936 Genomic DNA. Translation: CAH70766.1 .
    AL358234 , AL161936 Genomic DNA. Translation: CAH70768.1 .
    AL161936 , AL358234 Genomic DNA. Translation: CAI40922.1 .
    AL161936 , AL358234 Genomic DNA. Translation: CAI40924.1 .
    AL161936 Genomic DNA. Translation: CAI40921.1 . Sequence problems.
    AL358234 , AL161936 Genomic DNA. Translation: CAH70767.1 . Sequence problems.
    AL161936 , AL358234 Genomic DNA. Translation: CAI40923.1 . Sequence problems.
    CH471072 Genomic DNA. Translation: EAW86032.1 .
    CH471072 Genomic DNA. Translation: EAW86035.1 .
    CH471072 Genomic DNA. Translation: EAW86037.1 .
    CH471072 Genomic DNA. Translation: EAW86039.1 .
    CH471072 Genomic DNA. Translation: EAW86040.1 .
    CH471072 Genomic DNA. Translation: EAW86042.1 .
    BC004258 mRNA. Translation: AAH04258.2 . Frameshift.
    BC010356 mRNA. Translation: AAH10356.1 . Different initiation.
    AB058747 mRNA. Translation: BAB47473.1 . Sequence problems.
    CCDSi CCDS7159.1. [Q9BTA9-1 ]
    CCDS7160.1. [Q9BTA9-5 ]
    RefSeqi NP_057712.2. NM_016628.4. [Q9BTA9-1 ]
    NP_567823.1. NM_100486.3. [Q9BTA9-5 ]
    XP_005252514.1. XM_005252457.1. [Q9BTA9-2 ]
    UniGenei Hs.743224.

    3D structure databases

    ProteinModelPortali Q9BTA9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119473. 17 interactions.
    IntActi Q9BTA9. 12 interactions.
    MINTi MINT-2873194.

    PTM databases

    PhosphoSitei Q9BTA9.

    Polymorphism databases

    DMDMi 117949358.

    Proteomic databases

    MaxQBi Q9BTA9.
    PaxDbi Q9BTA9.
    PRIDEi Q9BTA9.

    Protocols and materials databases

    DNASUi 51322.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347934 ; ENSP00000311106 ; ENSG00000095787 . [Q9BTA9-5 ]
    ENST00000354911 ; ENSP00000346986 ; ENSG00000095787 . [Q9BTA9-1 ]
    ENST00000375664 ; ENSP00000364816 ; ENSG00000095787 . [Q9BTA9-2 ]
    ENST00000428935 ; ENSP00000399706 ; ENSG00000095787 . [Q9BTA9-3 ]
    ENST00000439676 ; ENSP00000415727 ; ENSG00000095787 . [Q9BTA9-3 ]
    GeneIDi 51322.
    KEGGi hsa:51322.
    UCSCi uc001iud.3. human. [Q9BTA9-1 ]
    uc001iue.3. human. [Q9BTA9-5 ]

    Organism-specific databases

    CTDi 51322.
    GeneCardsi GC10P028861.
    HGNCi HGNC:17327. WAC.
    HPAi HPA036528.
    HPA042609.
    MIMi 615049. gene.
    neXtProti NX_Q9BTA9.
    PharmGKBi PA134978936.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299824.
    HOVERGENi HBG057585.
    InParanoidi Q9BTA9.
    OMAi HKILTAG.
    OrthoDBi EOG7T1RB9.
    PhylomeDBi Q9BTA9.
    TreeFami TF328635.

    Enzyme and pathway databases

    SignaLinki Q9BTA9.

    Miscellaneous databases

    ChiTaRSi WAC. human.
    GeneWikii WAC_(gene).
    GenomeRNAii 51322.
    NextBioi 54714.
    PROi Q9BTA9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BTA9.
    Bgeei Q9BTA9.
    CleanExi HS_WAC.
    Genevestigatori Q9BTA9.

    Family and domain databases

    InterProi IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00397. WW. 1 hit.
    [Graphical view ]
    SMARTi SM00456. WW. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 1 hit.
    PROSITEi PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Thalamus.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    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], ALTERNATIVE SPLICING.
    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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-647 (ISOFORM 4).
      Tissue: Kidney and Urinary bladder.
    7. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-647 (ISOFORMS 1/2).
      Tissue: Brain.
    8. "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-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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-471; SER-523 AND SER-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC."
      McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M., Johansen T., Tooze S.A.
      EMBO J. 31:1931-1946(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-475.
    18. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
      Zhang F., Yu X.
      Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF20; RNF40 AND UBE2A.

    Entry informationi

    Entry nameiWAC_HUMAN
    AccessioniPrimary (citable) accession number: Q9BTA9
    Secondary accession number(s): A8K2A9
    , C9JBT9, D3DRW5, D3DRW6, D3DRW7, Q53EN9, Q5JU75, Q5JU77, Q5VXK0, Q5VXK2, Q8TCK1, Q96DP3, Q96FW6, Q96JI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3