WAC_MOUSE
ID WAC_MOUSE Reviewed; 646 AA.
AC Q924H7; Q3U0K1; Q66JM9; Q69Z92; Q8C2W2; Q8C8Q8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=WW domain-containing adapter protein with coiled-coil;
GN Name=Wac; Synonyms=Kiaa1844;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=11827461; DOI=10.1006/geno.2001.6684;
RA Xu G.M., Arnaout M.A.;
RT "WAC, a novel WW domain-containing adapter with a coiled-coil region, is
RT colocalized with splicing factor SC35.";
RL Genomics 79:87-94(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Ovary, Retina, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a linker between gene transcription and histone H2B
CC monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA
CC polymerase II transcriptional machinery via its WW domain and with
CC RNF20-RNF40 via its coiled coil region, thereby linking and regulating
CC H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint
CC activation in response to DNA damage. Positive regulator of amino acid
CC starvation-induced autophagy. Also acts as a negative regulator of
CC basal autophagy. Positively regulates MTOR activity by promoting, in an
CC energy-dependent manner, the assembly of the TTT complex composed of
CC TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and
CC RUVBL2 into the TTT-RUVBL complex. This leads to the dimerization of
CC the mTORC1 complex and its subsequent activation. May negatively
CC regulate the ubiquitin proteasome pathway.
CC {ECO:0000250|UniProtKB:Q9BTA9}.
CC -!- SUBUNIT: Interacts (via coiled coil domain) with RNF20, RNF40 and
CC UBE2A. Interacts (via WW domain) with RNA polymerase II. Interacts with
CC MTOR and other components of the MTOR pathway including RPTOR, RUVBL1,
CC RUVBL2, TTI1 and TTI2. {ECO:0000250|UniProtKB:Q9BTA9}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11827461}.
CC Nucleus {ECO:0000250|UniProtKB:Q9BTA9}. Note=In distinct nuclear
CC speckles. Colocalizes with pre-mRNA processing complexes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q924H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924H7-2; Sequence=VSP_021237;
CC Name=3;
CC IsoId=Q924H7-3; Sequence=VSP_021238;
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:11827461}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32552.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF320996; AAK73808.1; -; mRNA.
DR EMBL; AK173274; BAD32552.1; ALT_INIT; mRNA.
DR EMBL; AK044675; BAC32029.1; -; mRNA.
DR EMBL; AK087826; BAC40017.1; -; mRNA.
DR EMBL; AK156780; BAE33852.1; -; mRNA.
DR EMBL; BC080851; AAH80851.1; -; mRNA.
DR CCDS; CCDS29046.1; -. [Q924H7-1]
DR CCDS; CCDS50218.1; -. [Q924H7-3]
DR CCDS; CCDS70869.1; -. [Q924H7-2]
DR RefSeq; NP_001139770.1; NM_001146298.2. [Q924H7-3]
DR RefSeq; NP_001269022.1; NM_001282093.1. [Q924H7-2]
DR RefSeq; NP_694725.3; NM_153085.4. [Q924H7-1]
DR RefSeq; XP_006525868.1; XM_006525805.2.
DR RefSeq; XP_011245190.1; XM_011246888.2. [Q924H7-2]
DR AlphaFoldDB; Q924H7; -.
DR SMR; Q924H7; -.
DR BioGRID; 230359; 2.
DR STRING; 10090.ENSMUSP00000132117; -.
DR iPTMnet; Q924H7; -.
DR PhosphoSitePlus; Q924H7; -.
DR EPD; Q924H7; -.
DR jPOST; Q924H7; -.
DR MaxQB; Q924H7; -.
DR PaxDb; Q924H7; -.
DR PeptideAtlas; Q924H7; -.
DR PRIDE; Q924H7; -.
DR ProteomicsDB; 275196; -. [Q924H7-1]
DR ProteomicsDB; 275197; -. [Q924H7-2]
DR ProteomicsDB; 275198; -. [Q924H7-3]
DR Antibodypedia; 50013; 131 antibodies from 25 providers.
DR DNASU; 225131; -.
DR Ensembl; ENSMUST00000074919; ENSMUSP00000074454; ENSMUSG00000024283. [Q924H7-2]
DR Ensembl; ENSMUST00000092112; ENSMUSP00000089746; ENSMUSG00000024283. [Q924H7-3]
DR Ensembl; ENSMUST00000167020; ENSMUSP00000132117; ENSMUSG00000024283. [Q924H7-1]
DR GeneID; 225131; -.
DR KEGG; mmu:225131; -.
DR UCSC; uc008eab.3; mouse. [Q924H7-1]
DR UCSC; uc008eae.3; mouse. [Q924H7-3]
DR CTD; 51322; -.
DR MGI; MGI:2387357; Wac.
DR VEuPathDB; HostDB:ENSMUSG00000024283; -.
DR eggNOG; KOG0152; Eukaryota.
DR GeneTree; ENSGT00440000037780; -.
DR HOGENOM; CLU_024845_2_1_1; -.
DR InParanoid; Q924H7; -.
DR OMA; ICLSENC; -.
DR OrthoDB; 1111788at2759; -.
DR PhylomeDB; Q924H7; -.
DR TreeFam; TF328635; -.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 225131; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Wac; mouse.
DR PRO; PR:Q924H7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q924H7; protein.
DR Bgee; ENSMUSG00000024283; Expressed in undifferentiated genital tubercle and 254 other tissues.
DR ExpressionAtlas; Q924H7; baseline and differential.
DR Genevisible; Q924H7; MM.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; ISS:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; ISS:UniProtKB.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR CDD; cd00201; WW; 1.
DR InterPro; IPR038867; WAC.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR15911; PTHR15911; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..646
FT /note="WW domain-containing adapter protein with coiled-
FT coil"
FT /id="PRO_0000254559"
FT DOMAIN 129..162
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 617..643
FT /evidence="ECO:0000255"
FT COMPBIAS 35..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 302
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTA9"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021237"
FT VAR_SEQ 204..307
FT /note="MEDKHSSDASSLLPQNILSQTSRHNDKDYRLPRAETHSSSTPVQHPIKPVVH
FT PTATPSTVPSSPFTLQSDHQPKKSFDANGASTLSKLPTPTASLPAQKTERKE -> K
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_021238"
FT CONFLICT 265
FT /note="S -> F (in Ref. 3; BAC40017)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="S -> P (in Ref. 1; AAK73808)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="P -> S (in Ref. 4; AAH80851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 70680 MW; 62914680DB435756 CRC64;
MVMYARKQQR LSDGCHDRRG DSQPFQALKY SSKSHPSSGD HRHEKMRDAA DPSPPNKMLR
RSNSPENKYS DSTGHNKAKN VHTQRVRERD GGTSYSPQEN SHNHSALHSS NSHSSNPSNN
PSKTSDAPYD SADDWSEHIS SSGKKYYYNC RTEVSQWEKP KEWLEREQRQ KEANKLAVNS
FPKDRDYRRE VMQATATSGF TSGMEDKHSS DASSLLPQNI LSQTSRHNDK DYRLPRAETH
SSSTPVQHPI KPVVHPTATP STVPSSPFTL QSDHQPKKSF DANGASTLSK LPTPTASLPA
QKTERKESAP GDKSISHSCT TPSTSSASGL NPTSAPPTSA SAVPVSPVPQ STIPPLLQDP
NLFRQLLPAL QATLQLNNSN VDISKINEVL TAAVTQASLQ SIIHKFLTAG PSAFNITSLI
SQAAQLSTQA QPSNQSPMSL TSDASSPRSY VSPRISTPQT NTVPMKPLIS TPPVSSQPKV
STPVVKQGPV SHSATQQPVT ADKQQSHDPV SPRSLQRLSS QRSPSPGPNH TCSSNASTAT
VVPQNASARP ACSLTPTLAA HFNDNLIKHV QGWPADHAEK QASRLREEAH NMGSVHMSEI
CTELKNLRSL VRVCEIQATL REQRILFLRQ QIKELEKLKN QNSFMV
