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GATOR complex protein WDR59 (WD repeat-containing protein 59)

 WDR59_HUMAN             Reviewed;         974 AA.
Q6PJI9; B3KRC3; Q71RE7; Q96PW5; Q9BSW6; Q9HA43;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
12-SEP-2018, entry version 136.
RecName: Full=GATOR complex protein WDR59 {ECO:0000305};
AltName: Full=WD repeat-containing protein 59 {ECO:0000312|HGNC:HGNC:25706};
Name=WDR59 {ECO:0000312|HGNC:HGNC:25706};
Synonyms=KIAA1923 {ECO:0000312|EMBL:BAB67816.1};
ORFNames=FP977 {ECO:0000312|EMBL:AAQ15226.1};
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 3 AND 4).
TISSUE=Mammary gland;
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 3).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 170-974 (ISOFORM 1).
TISSUE=Lung, and Uterus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-974 (ISOFORM 1).
TISSUE=Brain;
PubMed=11572484; DOI=10.1093/dnares/8.4.179;
Nagase T., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XXI.
The complete sequences of 60 new cDNA clones from brain which code for
large proteins.";
DNA Res. 8:179-187(2001).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-822, 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).
[6]
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).
[7]
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).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; SER-822 AND
SER-830, 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).
[10]
INTERACTION WITH SESN1; SESN2 AND SESN3.
PubMed=25263562; DOI=10.1016/j.celrep.2014.09.014;
Chantranupong L., Wolfson R.L., Orozco J.M., Saxton R.A., Scaria S.M.,
Bar-Peled L., Spooner E., Isasa M., Gygi S.P., Sabatini D.M.;
"The Sestrins interact with GATOR2 to negatively regulate the amino-
acid-sensing pathway upstream of mTORC1.";
Cell Rep. 9:1-8(2014).
[11]
FUNCTION, AND INTERACTION WITH SESN2.
PubMed=25457612; DOI=10.1016/j.celrep.2014.10.019;
Parmigiani A., Nourbakhsh A., Ding B., Wang W., Kim Y.C.,
Akopiants K., Guan K.L., Karin M., Budanov A.V.;
"Sestrins inhibit mTORC1 kinase activation through the GATOR
complex.";
Cell Rep. 9:1281-1291(2014).
[12]
FUNCTION, IDENTIFICATION IN GATOR COMPLEX, AND SUBUNIT.
PubMed=23723238; DOI=10.1126/science.1232044;
Bar-Peled L., Chantranupong L., Cherniack A.D., Chen W.W.,
Ottina K.A., Grabiner B.C., Spear E.D., Carter S.L., Meyerson M.,
Sabatini D.M.;
"A Tumor suppressor complex with GAP activity for the Rag GTPases that
signal amino acid sufficiency to mTORC1.";
Science 340:1100-1106(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, 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).
[14]
INTERACTION WITH CASTOR2 AND CASTOR1.
PubMed=26972053; DOI=10.1016/j.cell.2016.02.035;
Chantranupong L., Scaria S.M., Saxton R.A., Gygi M.P., Shen K.,
Wyant G.A., Wang T., Harper J.W., Gygi S.P., Sabatini D.M.;
"The CASTOR proteins are arginine sensors for the mTORC1 pathway.";
Cell 165:153-164(2016).
[15]
FUNCTION.
PubMed=27487210; DOI=10.1038/nature19079;
Saxton R.A., Chantranupong L., Knockenhauer K.E., Schwartz T.U.,
Sabatini D.M.;
"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1.";
Nature 536:229-233(2016).
[16]
SUBCELLULAR LOCATION.
PubMed=28199306; DOI=10.1038/nature21423;
Wolfson R.L., Chantranupong L., Wyant G.A., Gu X., Orozco J.M.,
Shen K., Condon K.J., Petri S., Kedir J., Scaria S.M.,
Abu-Remaileh M., Frankel W.N., Sabatini D.M.;
"KICSTOR recruits GATOR1 to the lysosome and is necessary for
nutrients to regulate mTORC1.";
Nature 543:438-442(2017).
-!- FUNCTION: As a component of the GATOR subcomplex GATOR2, functions
within the amino acid-sensing branch of the TORC1 signaling
pathway. Indirectly activates mTORC1 and the TORC1 signaling
pathway through the inhibition of the GATOR1 subcomplex
(PubMed:23723238). It is negatively regulated by the upstream
amino acid sensors SESN2 and CASTOR1 (PubMed:25457612,
PubMed:27487210). {ECO:0000269|PubMed:23723238,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:27487210}.
-!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes (By
similarity). Within the GATOR complex, component of the GATOR2
subcomplex, made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR
complex strongly interacts with RRAGA/RRAGC and RRAGB/RRAGC
heterodimers. The GATOR2 complex interacts with CASTOR2 and
CASTOR1; the interaction is negatively regulated by arginine
(PubMed:26972053). The GATOR2 complex interacts with SESN1, SESN2
and SESN3; the interaction is negatively regulated by amino acids
(PubMed:25263562, PubMed:25457612). {ECO:0000250,
ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25263562,
ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:26972053}.
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000269|PubMed:28199306}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6PJI9-1; Sequence=Displayed;
Name=2;
IsoId=Q6PJI9-2; Sequence=VSP_023884;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6PJI9-3; Sequence=VSP_023882;
Name=4;
IsoId=Q6PJI9-4; Sequence=VSP_023881, VSP_023883;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat WDR59 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB67816.1; Type=Frameshift; Positions=157; Evidence={ECO:0000305};
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EMBL; AK022332; BAB14015.1; -; mRNA.
EMBL; AK091316; BAG52335.1; -; mRNA.
EMBL; AF370390; AAQ15226.1; -; mRNA.
EMBL; BC004519; AAH04519.1; -; mRNA.
EMBL; BC014887; AAH14887.2; -; mRNA.
EMBL; AB067510; BAB67816.1; ALT_FRAME; mRNA.
CCDS; CCDS32488.1; -. [Q6PJI9-1]
CCDS; CCDS82011.1; -. [Q6PJI9-2]
RefSeq; NP_001311100.1; NM_001324171.1. [Q6PJI9-2]
RefSeq; NP_085058.3; NM_030581.3. [Q6PJI9-1]
UniGene; Hs.280951; -.
ProteinModelPortal; Q6PJI9; -.
BioGrid; 122841; 39.
CORUM; Q6PJI9; -.
IntAct; Q6PJI9; 16.
STRING; 9606.ENSP00000262144; -.
iPTMnet; Q6PJI9; -.
PhosphoSitePlus; Q6PJI9; -.
BioMuta; WDR59; -.
DMDM; 134035358; -.
EPD; Q6PJI9; -.
MaxQB; Q6PJI9; -.
PaxDb; Q6PJI9; -.
PeptideAtlas; Q6PJI9; -.
PRIDE; Q6PJI9; -.
ProteomicsDB; 67210; -.
ProteomicsDB; 67211; -. [Q6PJI9-2]
ProteomicsDB; 67212; -. [Q6PJI9-3]
ProteomicsDB; 67213; -. [Q6PJI9-4]
Ensembl; ENST00000262144; ENSP00000262144; ENSG00000103091. [Q6PJI9-1]
Ensembl; ENST00000616369; ENSP00000482446; ENSG00000103091. [Q6PJI9-2]
GeneID; 79726; -.
KEGG; hsa:79726; -.
UCSC; uc002fdh.2; human. [Q6PJI9-1]
CTD; 79726; -.
DisGeNET; 79726; -.
EuPathDB; HostDB:ENSG00000103091.14; -.
GeneCards; WDR59; -.
H-InvDB; HIX0013239; -.
HGNC; HGNC:25706; WDR59.
HPA; HPA041084; -.
HPA; HPA048218; -.
MIM; 617418; gene.
neXtProt; NX_Q6PJI9; -.
OpenTargets; ENSG00000103091; -.
PharmGKB; PA142670593; -.
eggNOG; KOG0264; Eukaryota.
eggNOG; KOG0309; Eukaryota.
eggNOG; COG2319; LUCA.
GeneTree; ENSGT00910000144183; -.
HOGENOM; HOG000004834; -.
HOVERGEN; HBG092820; -.
InParanoid; Q6PJI9; -.
KO; K20409; -.
OMA; EFSLINV; -.
OrthoDB; EOG091G0S7I; -.
PhylomeDB; Q6PJI9; -.
TreeFam; TF314695; -.
SignaLink; Q6PJI9; -.
SIGNOR; Q6PJI9; -.
ChiTaRS; WDR59; human.
GenomeRNAi; 79726; -.
PRO; PR:Q6PJI9; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103091; Expressed in 226 organ(s), highest expression level in left lobe of thyroid gland.
CleanEx; HS_WDR59; -.
ExpressionAtlas; Q6PJI9; baseline and differential.
Genevisible; Q6PJI9; HS.
GO; GO:0061700; C:GATOR2 complex; IDA:SGD.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:SGD.
Gene3D; 2.130.10.10; -; 2.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR006575; RWD-domain.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR037591; WDR59.
PANTHER; PTHR22850:SF116; PTHR22850:SF116; 1.
Pfam; PF00400; WD40; 2.
SMART; SM00591; RWD; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS50908; RWD; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Lysosome; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; WD repeat.
CHAIN 1 974 GATOR complex protein WDR59.
/FTId=PRO_0000280721.
REPEAT 57 98 WD 1.
REPEAT 103 143 WD 2.
REPEAT 146 185 WD 3.
REPEAT 189 229 WD 4.
REPEAT 232 276 WD 5.
REPEAT 278 318 WD 6.
REPEAT 319 362 WD 7.
DOMAIN 393 494 RWD. {ECO:0000255|PROSITE-
ProRule:PRU00179}.
REPEAT 668 706 WD 8.
MOD_RES 564 564 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 830 830 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 556 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_023881.
VAR_SEQ 1 408 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15498874}.
/FTId=VSP_023882.
VAR_SEQ 557 571 MTMHRAVSPTEPTPR -> MTGLQPVWIIIIFNYR (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_023883.
VAR_SEQ 572 974 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023884.
VARIANT 201 201 P -> T (in dbSNP:rs11557260).
/FTId=VAR_053436.
CONFLICT 441 441 A -> S (in Ref. 4; BAB67816).
{ECO:0000305}.
SEQUENCE 974 AA; 109793 MW; 72F651A38EA51CBA CRC64;
MAARWSSENV VVEFRDSQAT AMSVDCLGQH AVLSGRRFLY IVNLDAPFEG HRKISRQSKW
DIGAVQWNPH DSFAHYFAAS SNQRVDLYKW KDGSGEVGTT LQGHTRVISD LDWAVFEPDL
LVTSSVDTYI YIWDIKDTRK PTVALSAVAG ASQVKWNKKN ANCLATSHDG DVRIWDKRKP
STAVEYLAAH LSKIHGLDWH PDSEHILATS SQDNSVKFWD YRQPRKYLNI LPCQVPVWKA
RYTPFSNGLV TVMVPQLRRE NSLLLWNVFD LNTPVHTFVG HDDVVLEFQW RKQKEGSKDY
QLVTWSRDQT LRMWRVDSQM QRLCANDILD GVDEFIESIS LLPEPEKTLH TEDTDHQHTA
SHGEEEALKE DPPRNLLEER KSDQLGLPQT LQQEFSLINV QIRNVNVEMD AADRSCTVSV
HCSNHRVKML VKFPAQYPNN AAPSFQFINP TTITSTMKAK LLKILKDTAL QKVKRGQSCL
EPCLRQLVSC LESFVNQEDS ASSNPFALPN SVTPPLPTFA RVTTAYGSYQ DANIPFPRTS
GARFCGAGYL VYFTRPMTMH RAVSPTEPTP RSLSALSAYH TGLIAPMKIR TEAPGNLRLY
SGSPTRSEKE QVSISSFYYK ERKSRRWKSK REGSDSGNRQ IKAAGKVIIQ DIACLLPVHK
SLGELYILNV NDIQETCQKN AASALLVGRK DLVQVWSLAT VATDLCLGPK SDPDLETPWA
RHPFGRQLLE SLLAHYCRLR DVQTLAMLCS VFEAQSRPQG LPNPFGPFPN RSSNLVVSHS
RYPSFTSSGS CSSMSDPGLN TGGWNIAGRE AEHLSSPWGE SSPEELRFGS LTYSDPRERE
RDQHDKNKRL LDPANTQQFD DFKKCYGEIL YRWGLREKRA EVLKFVSCPP DPHKGIEFGV
YCSHCRSEVR GTQCAICKGF TFQCAICHVA VRGSSNFCLT CGHGGHTSHM MEWFRTQEVC
PTGCGCHCLL ESTF


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EIAAB42295 fSAP35,Functional spliceosome-associated protein 35,Homo sapiens,Human,PSEC0006,THO complex subunit 6 homolog,THOC6,WD repeat-containing protein 58,WDR58


 

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