Q9BTA9 (WAC_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 93.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: WW domain-containing adapter protein with coiled-coil | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 647 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.15 Ref.17 |
| Subunit structure | Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II. Ref.17 |
| Subcellular location | Nucleus speckle By similarity. Nucleus. Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes By similarity. Ref.17 |
| Post-translational modification | Phosphorylated on tyrosine residues By similarity. |
| Sequence similarities | Contains 1 WW domain. |
| Sequence caution | 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 BAB47473.1 differs from that shown. Reason: Probable cloning artifact. 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. |
Ontologies
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9BTA9-1) 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 (identifier: Q9BTA9-2) The sequence of this isoform differs from the canonical sequence as follows: 1-45: Missing. | ||||||
| Isoform 3 (identifier: Q9BTA9-3) 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. | ||||||
| Isoform 4 (identifier: Q9BTA9-5) The sequence of this isoform differs from the canonical sequence as follows: 204-307: MEDKHSSDAS...VPAQKTERKE → K |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 647 | 647 | WW domain-containing adapter protein with coiled-coil | PRO_0000254558 | |||||
Regions | |||||||||
| Domain | 129 – 162 | 34 | WW | ||||||
| Coiled coil | 618 – 644 | 27 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 53 | 1 | Phosphoserine Ref.9 Ref.13 | ||||||
| Modified residue | 293 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 302 | 1 | N6-acetyllysine Ref.12 | ||||||
| Modified residue | 471 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 511 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 523 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 525 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 534 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 45 | 45 | Missing in isoform 2 and isoform 3. | VSP_021230 | |||||
| Alternative sequence | 204 – 307 | 104 | MEDKH…TERKE → K in isoform 4. | VSP_021231 | |||||
| Alternative sequence | 430 – 481 | 52 | AQPSN…QPKVS → DIPLHEGIQMERDTHRSKWE VKGSLCQKADKQQECLVWNG SIMVQRLLQPSG in isoform 3. | VSP_021233 | |||||
| Alternative sequence | 482 – 647 | 166 | Missing in isoform 3. | VSP_021236 | |||||
| Natural variant | 242 | 1 | S → R. Corresponds to variant rs11595926 [ dbSNP | Ensembl ]. | VAR_028838 | |||||
| Natural variant | 309 | 1 | T → A. Corresponds to variant rs2232791 [ dbSNP | Ensembl ]. | VAR_053448 | |||||
| Natural variant | 475 | 1 | S → L in a colorectal cancer sample; somatic mutation. Ref.16 | VAR_036351 | |||||
| Natural variant | 531 | 1 | T → S. Corresponds to variant rs7127 [ dbSNP | Ensembl ]. | VAR_028839 | |||||
Experimental info | |||||||||
| Sequence conflict | 426 | 1 | L → F in BAB71029. Ref.1 | ||||||
| Sequence conflict | 581 | 1 | K → R in AAH10356. Ref.6 | ||||||
| Sequence conflict | 599 | 1 | S → P in BAD97320. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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. Rogers J.Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. |
| [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. Venter J.C.Submitted (SEP-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 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "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 THR-293, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "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, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [12] | "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, MASS SPECTROMETRY. |
| [13] | "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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "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]. |
| [15] | "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. |
| [16] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-475. |
| [17] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00087375. IPI00152381. IPI00256605. IPI00478665. |
| RefSeq | NP_057712.2. NM_016628.4. NP_567823.1. NM_100486.3. |
| UniGene | Hs.435610. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1YWI based on UniProtKB O75400. |
| ProteinModelPortal | Q9BTA9. |
| SMR | Q9BTA9. Positions 134-160. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9BTA9. 9 interactions. |
| MINT | MINT-2873194. |
PTM databases | |
| PhosphoSite | Q9BTA9. |
Polymorphism databases | |
| DMDM | 117949358. |
Proteomic databases | |
| PaxDb | Q9BTA9. |
| PRIDE | Q9BTA9. |
Protocols and materials databases | |
| DNASU | 51322. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000347934; ENSP00000311106; ENSG00000095787. ENST00000354911; ENSP00000346986; ENSG00000095787. ENST00000375646; ENSP00000364797; ENSG00000095787. ENST00000375664; ENSP00000364816; ENSG00000095787. ENST00000428935; ENSP00000399706; ENSG00000095787. ENST00000439676; ENSP00000415727; ENSG00000095787. |
| GeneID | 51322. |
| KEGG | hsa:51322. |
| UCSC | uc001iud.3. human. uc001iue.3. human. |
Organism-specific databases | |
| CTD | 51322. |
| GeneCards | GC10P028861. |
| HGNC | HGNC:17327. WAC. |
| HPA | HPA036528. |
| MIM | 615049. gene. |
| neXtProt | NX_Q9BTA9. |
| PharmGKB | PA134978936. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG299824. |
| HOVERGEN | HBG057585. |
| InParanoid | Q9BTA9. |
| OMA | HKILTAG. |
Gene expression databases | |
| ArrayExpress | Q9BTA9. |
| Bgee | Q9BTA9. |
| CleanEx | HS_WAC. |
| Genevestigator | Q9BTA9. |
| GermOnline | ENSG00000095787. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR001202. WW_dom. [Graphical view] |
| Pfam | PF00397. WW. 1 hit. [Graphical view] |
| SMART | SM00456. WW. 1 hit. [Graphical view] |
| SUPFAM | SSF51045. WW_Rsp5_WWP. 1 hit. |
| PROSITE | PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | WAC. human. |
| GenomeRNAi | 51322. |
| NextBio | 54714. |
| SOURCE | Search... |
Entry information
| Entry name | WAC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BTA9 Secondary accession number(s): A8K2A9 Q96JI3 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 10 Human chromosome 10: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
