RGS19_HUMAN
ID RGS19_HUMAN Reviewed; 217 AA.
AC P49795; A8K216; E1P5G9; Q53XN0; Q8TD60;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Regulator of G-protein signaling 19;
DE Short=RGS19;
DE AltName: Full=G-alpha-interacting protein;
DE Short=GAIP;
GN Name=RGS19; Synonyms=GAIP, GNAI3IP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8524874; DOI=10.1073/pnas.92.25.11916;
RA de Vries L., Mousli M., Wurmser A., Farquhar M.G.;
RT "GAIP, a protein that specifically interacts with the trimeric G protein G
RT alpha i3, is a member of a protein family with a highly conserved core
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, Placenta, and Testis;
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 [8]
RP PALMITOYLATION.
RX PubMed=8986788; DOI=10.1073/pnas.93.26.15203;
RA de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.;
RT "GAIP is membrane-anchored by palmitoylation and interacts with the
RT activated (GTP-bound) form of G alpha i subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP STRUCTURE BY NMR OF 79-206.
RX PubMed=10452897; DOI=10.1006/jmbi.1999.2989;
RA de Alba E., De Vries L., Farquhar M.G., Tjandra N.;
RT "Solution structure of human GAIP (Galpha interacting protein): a regulator
RT of G protein signaling.";
RL J. Mol. Biol. 291:927-939(1999).
RN [13]
RP INHIBITION.
RX PubMed=9748280; DOI=10.1074/jbc.273.40.26014;
RA Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.;
RT "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane
RT association, regulation by Galphaz phosphorylation, and relationship to a
RT Gz GTPase-activating protein subfamily.";
RL J. Biol. Chem. 273:26014-26025(1998).
RN [14]
RP PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX PubMed=10993892; DOI=10.1074/jbc.m006198200;
RA Ogier-Denis E., Pattingre S., El Benna J., Codogno P.;
RT "Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates
RT its GTPase accelerating activity and autophagy in human colon cancer
RT cells.";
RL J. Biol. Chem. 275:39090-39095(2000).
CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC activity of G protein alpha subunits thereby driving them into their
CC inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the
CC order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha
CC is inhibited by phosphorylation and palmitoylation of the G-protein.
CC -!- SUBUNIT: Interacts with GIPC PDZ domain.
CC -!- INTERACTION:
CC P49795; P05187: ALPP; NbExp=3; IntAct=EBI-874907, EBI-1211484;
CC P49795; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-874907, EBI-744545;
CC P49795; P49639: HOXA1; NbExp=3; IntAct=EBI-874907, EBI-740785;
CC P49795; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-874907, EBI-10250562;
CC P49795; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-874907, EBI-10246358;
CC P49795; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-874907, EBI-1210753;
CC P49795; P32242: OTX1; NbExp=3; IntAct=EBI-874907, EBI-740446;
CC P49795; Q12837: POU4F2; NbExp=3; IntAct=EBI-874907, EBI-17236143;
CC P49795; P25786: PSMA1; NbExp=3; IntAct=EBI-874907, EBI-359352;
CC P49795; Q6EMK4: VASN; NbExp=3; IntAct=EBI-874907, EBI-10249550;
CC P49795; P08753: Gnai3; Xeno; NbExp=4; IntAct=EBI-874907, EBI-874897;
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- TISSUE SPECIFICITY: Highest expression in lung. Placenta, liver and
CC heart also express high levels of GAIP.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC motif. {ECO:0000269|PubMed:8986788}.
CC -!- PTM: Phosphorylated, mainly on serine residues.
CC {ECO:0000269|PubMed:10993892}.
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DR EMBL; X91809; CAA62919.1; -; mRNA.
DR EMBL; AF493939; AAM12653.1; -; mRNA.
DR EMBL; AY585188; AAS94232.1; -; mRNA.
DR EMBL; BT009804; AAP88806.1; -; mRNA.
DR EMBL; AK290081; BAF82770.1; -; mRNA.
DR EMBL; AL590548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75166.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75167.1; -; Genomic_DNA.
DR EMBL; BC001318; AAH01318.1; -; mRNA.
DR EMBL; BC054337; AAH54337.1; -; mRNA.
DR EMBL; BC063010; AAH63010.1; -; mRNA.
DR CCDS; CCDS13555.1; -.
DR RefSeq; NP_001034556.1; NM_001039467.1.
DR RefSeq; NP_005864.1; NM_005873.2.
DR RefSeq; XP_011526787.1; XM_011528485.2.
DR RefSeq; XP_011526788.1; XM_011528486.2.
DR PDB; 1CMZ; NMR; -; A=79-206.
DR PDBsum; 1CMZ; -.
DR AlphaFoldDB; P49795; -.
DR SMR; P49795; -.
DR BioGRID; 115576; 27.
DR CORUM; P49795; -.
DR IntAct; P49795; 21.
DR MINT; P49795; -.
DR STRING; 9606.ENSP00000378483; -.
DR BindingDB; P49795; -.
DR ChEMBL; CHEMBL3707468; -.
DR GuidetoPHARMACOLOGY; 2802; -.
DR iPTMnet; P49795; -.
DR PhosphoSitePlus; P49795; -.
DR SwissPalm; P49795; -.
DR BioMuta; RGS19; -.
DR DMDM; 1730186; -.
DR EPD; P49795; -.
DR jPOST; P49795; -.
DR MassIVE; P49795; -.
DR MaxQB; P49795; -.
DR PaxDb; P49795; -.
DR PeptideAtlas; P49795; -.
DR PRIDE; P49795; -.
DR ProteomicsDB; 56122; -.
DR Antibodypedia; 29985; 471 antibodies from 28 providers.
DR DNASU; 10287; -.
DR Ensembl; ENST00000332298.9; ENSP00000333194.5; ENSG00000171700.14.
DR Ensembl; ENST00000395042.2; ENSP00000378483.1; ENSG00000171700.14.
DR GeneID; 10287; -.
DR KEGG; hsa:10287; -.
DR MANE-Select; ENST00000395042.2; ENSP00000378483.1; NM_005873.3; NP_005864.1.
DR UCSC; uc002yhy.4; human.
DR CTD; 10287; -.
DR DisGeNET; 10287; -.
DR GeneCards; RGS19; -.
DR HGNC; HGNC:13735; RGS19.
DR HPA; ENSG00000171700; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605071; gene.
DR neXtProt; NX_P49795; -.
DR OpenTargets; ENSG00000171700; -.
DR PharmGKB; PA34370; -.
DR VEuPathDB; HostDB:ENSG00000171700; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000160391; -.
DR HOGENOM; CLU_059863_0_2_1; -.
DR InParanoid; P49795; -.
DR OMA; MSQHETS; -.
DR OrthoDB; 1409647at2759; -.
DR PhylomeDB; P49795; -.
DR TreeFam; TF315837; -.
DR PathwayCommons; P49795; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR SignaLink; P49795; -.
DR SIGNOR; P49795; -.
DR BioGRID-ORCS; 10287; 9 hits in 1077 CRISPR screens.
DR EvolutionaryTrace; P49795; -.
DR GeneWiki; RGS19; -.
DR GenomeRNAi; 10287; -.
DR Pharos; P49795; Tchem.
DR PRO; PR:P49795; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P49795; protein.
DR Bgee; ENSG00000171700; Expressed in granulocyte and 193 other tissues.
DR Genevisible; P49795; HS.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 2.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Signal transduction inhibitor.
FT CHAIN 1..217
FT /note="Regulator of G-protein signaling 19"
FT /id="PRO_0000204229"
FT DOMAIN 90..206
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..217
FT /note="Interaction with GIPC"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70521"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 151
FT /note="Phosphoserine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000269|PubMed:10993892"
FT MUTAGEN 151
FT /note="S->A: Diminishes gap activity towards G(i)-alpha3
FT and autophagy in colon cancer cells."
FT /evidence="ECO:0000269|PubMed:10993892"
FT CONFLICT 204
FT /note="A -> V (in Ref. 2; AAM12653)"
FT /evidence="ECO:0000305"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:1CMZ"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1CMZ"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:1CMZ"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1CMZ"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1CMZ"
SQ SEQUENCE 217 AA; 24636 MW; 925A5687DC222CBD CRC64;
MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ
ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW
LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA
QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA
