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WW domain-containing adapter protein with coiled-coil

 WAC_HUMAN               Reviewed;         647 AA.
Q9BTA9; A8K2A9; C9JBT9; D3DRW5; D3DRW6; D3DRW7; Q53EN9; Q5JU75;
Q5JU77; Q5VXK0; Q5VXK2; Q8TCK1; Q96DP3; Q96FW6; Q96JI3;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 3.
23-MAY-2018, entry version 140.
RecName: Full=WW domain-containing adapter protein with coiled-coil;
Name=WAC; Synonyms=KIAA1844;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 157-647 (ISOFORM 4).
TISSUE=Kidney, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-647 (ISOFORMS 1/2).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"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.";
DNA Res. 8:85-95(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-471; SER-523 AND
SER-525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-302, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
FUNCTION.
PubMed=22354037; DOI=10.1038/emboj.2012.36;
McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
Johansen T., Tooze S.A.;
"Genome-wide siRNA screen reveals amino acid starvation-induced
autophagy requires SCOC and WAC.";
EMBO J. 31:1931-1946(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-131; SER-142;
SER-225; THR-293; SER-511; SER-523 AND SER-525, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293; SER-446; SER-523
AND SER-525, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
INVOLVEMENT IN DESSH.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
[20]
INVOLVEMENT IN DESSH.
PubMed=26264232; DOI=10.1136/jmedgenet-2015-103069;
DDD Study;
DeSanto C., D'Aco K., Araujo G.C., Shannon N., Vernon H., Rahrig A.,
Monaghan K.G., Niu Z., Vitazka P., Dodd J., Tang S., Manwaring L.,
Martir-Negron A., Schnur R.E., Juusola J., Schroeder A., Pan V.,
Helbig K.L., Friedman B., Shinawi M.;
"WAC loss-of-function mutations cause a recognisable syndrome
characterised by dysmorphic features, developmental delay and
hypotonia and recapitulate 10p11.23 microdeletion syndrome.";
J. Med. Genet. 52:754-761(2015).
[21]
FUNCTION, AND INTERACTION WITH MTOR; RPTOR; RUVBL1; RUVBL2; TTI1 AND
TTI2.
PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M.,
Yamamoto S., Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z.,
Zhang S., Bellen H.J.;
"WAC regulates mTOR activity by acting as an adaptor for the TTT and
Pontin/Reptin complexes.";
Dev. Cell 36:139-151(2016).
[22]
INVOLVEMENT IN INTELLECTUAL DISABILITY.
PubMed=26757981; DOI=10.1038/ejhg.2015.282;
Lugtenberg D., Reijnders M.R., Fenckova M., Bijlsma E.K., Bernier R.,
van Bon B.W., Smeets E., Vulto-van Silfhout A.T., Bosch D.,
Eichler E.E., Mefford H.C., Carvill G.L., Bongers E.M.,
Schuurs-Hoeijmakers J.H., Ruivenkamp C.A., Santen G.W.,
van den Maagdenberg A.M., Peeters-Scholte C.M., Kuenen S.,
Verstreken P., Pfundt R., Yntema H.G., de Vries P.F., Veltman J.A.,
Hoischen A., Gilissen C., de Vries B.B., Schenck A., Kleefstra T.,
Vissers L.E.;
"De novo loss-of-function mutations in WAC cause a recognizable
intellectual disability syndrome and learning deficits in
Drosophila.";
Eur. J. Hum. Genet. 24:1145-1153(2016).
[23]
VARIANT [LARGE SCALE ANALYSIS] LEU-475.
PubMed=16959974; DOI=10.1126/science.1133427;
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., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RNA POLYMERASE
II; RNF20; RNF40 AND UBE2A.
PubMed=21329877; DOI=10.1016/j.molcel.2011.01.024;
Zhang F., Yu X.;
"WAC, a functional partner of RNF20/40, regulates histone H2B
ubiquitination and gene transcription.";
Mol. Cell 41:384-397(2011).
[25]
VARIANT 47-ARG--VAL-647 DEL.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Acts as a linker between gene transcription and histone
H2B monoubiquitination at 'Lys-120' (H2BK120ub1)
(PubMed:21329877). 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 (PubMed:21329877). Regulates the
cell-cycle checkpoint activation in response to DNA damage
(PubMed:21329877). Positive regulator of amino acid starvation-
induced autophagy (PubMed:22354037). Also acts as a negative
regulator of basal autophagy (PubMed:26812014). Positively
regulates MTOR activity by promoting, in an energy-dependent
manner, the assembly of the TTT complex composed of TELO2, TTI1
and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into
the TTT-RUVBL complex. This leads to the dimerization of the
mTORC1 complex and its subsequent activation (PubMed:26812014).
May negatively regulate the ubiquitin proteasome pathway
(PubMed:21329877). {ECO:0000269|PubMed:21329877,
ECO:0000269|PubMed:22354037, ECO:0000269|PubMed:26812014}.
-!- SUBUNIT: Interacts (via coiled coil domain) with RNF20, RNF40 and
UBE2A (PubMed:21329877). Interacts (via WW domain) with RNA
polymerase II (PubMed:21329877). Interacts with MTOR and other
components of the MTOR pathway including RPTOR, RUVBL1, RUVBL2,
TTI1 and TTI2 (PubMed:26812014). {ECO:0000269|PubMed:21329877,
ECO:0000269|PubMed:26812014}.
-!- INTERACTION:
Q99996-2:AKAP9; NbExp=3; IntAct=EBI-749118, EBI-9641546;
Q8WWB3:DYDC1; NbExp=3; IntAct=EBI-749118, EBI-740680;
P42858:HTT; NbExp=5; IntAct=EBI-749118, EBI-466029;
Q6P597:KLC3; NbExp=3; IntAct=EBI-749118, EBI-1643885;
P19012:KRT15; NbExp=4; IntAct=EBI-749118, EBI-739566;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-749118, EBI-742948;
Q16236:NFE2L2; NbExp=3; IntAct=EBI-749118, EBI-2007911;
Q8TDW5:SYTL5; NbExp=3; IntAct=EBI-749118, EBI-2939487;
Q13077:TRAF1; NbExp=3; IntAct=EBI-749118, EBI-359224;
Q9Y228:TRAF3IP3; NbExp=3; IntAct=EBI-749118, EBI-765817;
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000250|UniProtKB:Q924H7}. Nucleus
{ECO:0000269|PubMed:21329877}. Note=In distinct nuclear speckles.
Colocalizes with pre-mRNA processing complexes.
{ECO:0000250|UniProtKB:Q924H7}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9BTA9-1; Sequence=Displayed;
Name=2;
IsoId=Q9BTA9-2; Sequence=VSP_021230;
Name=3;
IsoId=Q9BTA9-3; Sequence=VSP_021230, VSP_021233, VSP_021236;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=Q9BTA9-5; Sequence=VSP_021231;
-!- PTM: Phosphorylated on tyrosine residues.
{ECO:0000250|UniProtKB:Q924H7}.
-!- DISEASE: DeSanto-Shinawi syndrome (DESSH) [MIM:616708]: An
autosomal dominant syndrome characterized by developmental delay,
hypotonia, behavioral problems, eye abnormalities, constipation,
feeding difficulties, seizures and sleep problems. Patients
exhibit dysmorphic features, including broad/prominent forehead,
synophrys and/or bushy eyebrows, depressed nasal bridge and
bulbous nasal tip. Additional variable features are posteriorly
rotated ears, hirsutism, deep-set eyes, thin upper lip, inverted
nipples, hearing loss and branchial cleft anomalies.
{ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:26264232}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Defects in WAC are the cause of a form of
intellectual disability characterized by hypotonia, behavioral
problems and distinctive facial dysmorphisms including a square-
shaped face, deep set eyes, long palpebral fissures, and a broad
mouth and chin. {ECO:0000269|PubMed:26757981}.
-!- SEQUENCE CAUTION:
Sequence=AAH04258.2; Type=Frameshift; Positions=641; Evidence={ECO:0000305};
Sequence=AAH10356.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB47473.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=CAH70767.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI40921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI40923.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AK055852; BAB71029.1; -; mRNA.
EMBL; AK223600; BAD97320.1; -; mRNA.
EMBL; AK290174; BAF82863.1; -; mRNA.
EMBL; AL713727; CAD28517.1; -; mRNA.
EMBL; AL358234; CAH70766.1; -; Genomic_DNA.
EMBL; AL161936; CAH70766.1; JOINED; Genomic_DNA.
EMBL; AL358234; CAH70768.1; -; Genomic_DNA.
EMBL; AL161936; CAH70768.1; JOINED; Genomic_DNA.
EMBL; AL161936; CAI40922.1; -; Genomic_DNA.
EMBL; AL358234; CAI40922.1; JOINED; Genomic_DNA.
EMBL; AL161936; CAI40924.1; -; Genomic_DNA.
EMBL; AL358234; CAI40924.1; JOINED; Genomic_DNA.
EMBL; AL161936; CAI40921.1; ALT_SEQ; Genomic_DNA.
EMBL; AL358234; CAH70767.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161936; CAH70767.1; JOINED; Genomic_DNA.
EMBL; AL161936; CAI40923.1; ALT_SEQ; Genomic_DNA.
EMBL; AL358234; CAI40923.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW86032.1; -; Genomic_DNA.
EMBL; CH471072; EAW86035.1; -; Genomic_DNA.
EMBL; CH471072; EAW86037.1; -; Genomic_DNA.
EMBL; CH471072; EAW86039.1; -; Genomic_DNA.
EMBL; CH471072; EAW86040.1; -; Genomic_DNA.
EMBL; CH471072; EAW86042.1; -; Genomic_DNA.
EMBL; BC004258; AAH04258.2; ALT_FRAME; mRNA.
EMBL; BC010356; AAH10356.1; ALT_INIT; mRNA.
EMBL; AB058747; BAB47473.1; ALT_SEQ; mRNA.
CCDS; CCDS7159.1; -. [Q9BTA9-1]
CCDS; CCDS7160.1; -. [Q9BTA9-5]
CCDS; CCDS7161.1; -. [Q9BTA9-2]
RefSeq; NP_057712.2; NM_016628.4. [Q9BTA9-1]
RefSeq; NP_567822.1; NM_100264.2. [Q9BTA9-2]
RefSeq; NP_567823.1; NM_100486.3. [Q9BTA9-5]
RefSeq; XP_011517793.1; XM_011519491.2. [Q9BTA9-2]
UniGene; Hs.743224; -.
ProteinModelPortal; Q9BTA9; -.
SMR; Q9BTA9; -.
BioGrid; 119473; 36.
IntAct; Q9BTA9; 27.
STRING; 9606.ENSP00000346986; -.
iPTMnet; Q9BTA9; -.
PhosphoSitePlus; Q9BTA9; -.
BioMuta; WAC; -.
DMDM; 117949358; -.
EPD; Q9BTA9; -.
MaxQB; Q9BTA9; -.
PaxDb; Q9BTA9; -.
PeptideAtlas; Q9BTA9; -.
PRIDE; Q9BTA9; -.
DNASU; 51322; -.
Ensembl; ENST00000347934; ENSP00000311106; ENSG00000095787. [Q9BTA9-5]
Ensembl; ENST00000354911; ENSP00000346986; ENSG00000095787. [Q9BTA9-1]
Ensembl; ENST00000375664; ENSP00000364816; ENSG00000095787. [Q9BTA9-2]
Ensembl; ENST00000439676; ENSP00000415727; ENSG00000095787. [Q9BTA9-3]
GeneID; 51322; -.
KEGG; hsa:51322; -.
UCSC; uc001iud.3; human. [Q9BTA9-1]
CTD; 51322; -.
DisGeNET; 51322; -.
EuPathDB; HostDB:ENSG00000095787.21; -.
GeneCards; WAC; -.
HGNC; HGNC:17327; WAC.
HPA; HPA036528; -.
HPA; HPA042609; -.
MalaCards; WAC; -.
MIM; 615049; gene.
MIM; 616708; phenotype.
neXtProt; NX_Q9BTA9; -.
OpenTargets; ENSG00000095787; -.
PharmGKB; PA134978936; -.
eggNOG; ENOG410ISFU; Eukaryota.
eggNOG; ENOG4111EBW; LUCA.
GeneTree; ENSGT00440000037780; -.
HOVERGEN; HBG057585; -.
InParanoid; Q9BTA9; -.
OMA; PYQTLKY; -.
OrthoDB; EOG091G0JAB; -.
PhylomeDB; Q9BTA9; -.
TreeFam; TF328635; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SignaLink; Q9BTA9; -.
ChiTaRS; WAC; human.
GeneWiki; WAC_(gene); -.
GenomeRNAi; 51322; -.
PRO; PR:Q9BTA9; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000095787; -.
CleanEx; HS_WAC; -.
ExpressionAtlas; Q9BTA9; baseline and differential.
Genevisible; Q9BTA9; HS.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:BHF-UCL.
GO; GO:0005681; C:spliceosomal complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0044783; P:G1 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IMP:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IMP:UniProtKB.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00201; WW; 1.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00397; WW; 1.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 647 WW domain-containing adapter protein with
coiled-coil.
/FTId=PRO_0000254558.
DOMAIN 129 162 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
COILED 618 644 {ECO:0000255}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 293 293 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 302 302 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 471 471 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 523 523 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 45 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_021230.
VAR_SEQ 204 307 MEDKHSSDASSLLPQNILSQTSRHNDRDYRLPRAETHSSST
PVQHPIKPVVHPTATPSTVPSSPFTLQSDHQPKKSFDANGA
STLSKLPTPTSSVPAQKTERKE -> K (in isoform
4). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_021231.
VAR_SEQ 430 481 AQPSNQSPMSLTSDASSPRSYVSPRISTPQTNTVPIKPLIS
TPPVSSQPKVS -> DIPLHEGIQMERDTHRSKWEVKGSLC
QKADKQQECLVWNGSIMVQRLLQPSG (in isoform
3). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_021233.
VAR_SEQ 482 647 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_021236.
VARIANT 47 647 Missing (probable disease-associated
mutation found in a patient severe
intellectual disability).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_078694.
VARIANT 242 242 S -> R (in dbSNP:rs11595926).
/FTId=VAR_028838.
VARIANT 309 309 T -> A (in dbSNP:rs2232791).
/FTId=VAR_053448.
VARIANT 475 475 S -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036351.
VARIANT 531 531 T -> S (in dbSNP:rs7127).
/FTId=VAR_028839.
CONFLICT 426 426 L -> F (in Ref. 1; BAB71029).
{ECO:0000305}.
CONFLICT 581 581 K -> R (in Ref. 6; AAH10356).
{ECO:0000305}.
CONFLICT 599 599 S -> P (in Ref. 2; BAD97320).
{ECO:0000305}.
SEQUENCE 647 AA; 70724 MW; 15C32DAAA3A94129 CRC64;
MVMYARKQQR LSDGCHDRRG DSQPYQALKY SSKSHPSSGD HRHEKMRDAG DPSPPNKMLR
RSDSPENKYS DSTGHSKAKN VHTHRVRERD GGTSYSPQEN SHNHSALHSS NSHSSNPSNN
PSKTSDAPYD SADDWSEHIS SSGKKYYYNC RTEVSQWEKP KEWLEREQRQ KEANKMAVNS
FPKDRDYRRE VMQATATSGF ASGMEDKHSS DASSLLPQNI LSQTSRHNDR DYRLPRAETH
SSSTPVQHPI KPVVHPTATP STVPSSPFTL QSDHQPKKSF DANGASTLSK LPTPTSSVPA
QKTERKESTS GDKPVSHSCT TPSTSSASGL NPTSAPPTSA SAVPVSPVPQ SPIPPLLQDP
NLLRQLLPAL QATLQLNNSN VDISKINEVL TAAVTQASLQ SIIHKFLTAG PSAFNITSLI
SQAAQLSTQA QPSNQSPMSL TSDASSPRSY VSPRISTPQT NTVPIKPLIS TPPVSSQPKV
STPVVKQGPV SQSATQQPVT ADKQQGHEPV SPRSLQRSSS QRSPSPGPNH TSNSSNASNA
TVVPQNSSAR STCSLTPALA AHFSENLIKH VQGWPADHAE KQASRLREEA HNMGTIHMSE
ICTELKNLRS LVRVCEIQAT LREQRILFLR QQIKELEKLK NQNSFMV


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