SGSM1_HUMAN
ID SGSM1_HUMAN Reviewed; 1148 AA.
AC Q2NKQ1; A5LGW1; A8MUT4; B0QYW0; B0QYW1; B5MEG1; B9A6J4; Q5TFL3; Q8TF60;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Small G protein signaling modulator 1;
DE AltName: Full=RUN and TBC1 domain-containing protein 2;
GN Name=SGSM1; Synonyms=KIAA1941, RUTBC2;
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] (ISOFORM 3), INTERACTION WITH RAB3A; RAB4A;
RP RAB5A; RAB8A; RAB11A; RAP1A; RAP1B; RAP2A AND RAP2B, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT "Identification of three novel proteins (SGSM1, 2, 3) which modulate small
RT G protein (RAP and RAB)-mediated signaling pathway.";
RL Genomics 90:249-260(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-676 (ISOFORM 1).
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 [6]
RP FUNCTION, INTERACTION WITH RAB9A AND RAB9B, AND SUBCELLULAR LOCATION.
RX PubMed=22637480; DOI=10.1074/jbc.m112.362558;
RA Nottingham R.M., Pusapati G.V., Ganley I.G., Barr F.A., Lambright D.G.,
RA Pfeffer S.R.;
RT "RUTBC2 protein, a Rab9A effector and GTPase-activating protein for
RT Rab36.";
RL J. Biol. Chem. 287:22740-22748(2012).
CC -!- FUNCTION: Interacts with numerous Rab family members, functioning as
CC Rab effector for some, and as GTPase activator for others. Promotes GTP
CC hydrolysis by RAB34 and RAB36. Probably functions as GTPase effector
CC with RAB9A and RAB9B; does not stimulate GTP hydrolysis with RAB9A and
CC RAB9B. {ECO:0000269|PubMed:22637480}.
CC -!- SUBUNIT: Interacts with RAB9A (GTP-bound form) and RAB9B (GTP-bound
CC form); has much lower affinity for GDP-bound RAB9A and RAB9B
CC (PubMed:22637480). Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A,
CC RAP1A, RAP1B, RAP2A and RAP2B. No interaction with RAB27A
CC (PubMed:17509819). {ECO:0000269|PubMed:17509819,
CC ECO:0000269|PubMed:22637480}.
CC -!- INTERACTION:
CC Q2NKQ1-4; P05067-2: APP; NbExp=3; IntAct=EBI-10182463, EBI-17264467;
CC Q2NKQ1-4; Q86V38: ATN1; NbExp=3; IntAct=EBI-10182463, EBI-11954292;
CC Q2NKQ1-4; P54253: ATXN1; NbExp=6; IntAct=EBI-10182463, EBI-930964;
CC Q2NKQ1-4; Q12798: CETN1; NbExp=7; IntAct=EBI-10182463, EBI-2512818;
CC Q2NKQ1-4; P41208: CETN2; NbExp=6; IntAct=EBI-10182463, EBI-1789926;
CC Q2NKQ1-4; O15182: CETN3; NbExp=6; IntAct=EBI-10182463, EBI-712959;
CC Q2NKQ1-4; P02489: CRYAA; NbExp=3; IntAct=EBI-10182463, EBI-6875961;
CC Q2NKQ1-4; P50570-2: DNM2; NbExp=3; IntAct=EBI-10182463, EBI-10968534;
CC Q2NKQ1-4; P00488: F13A1; NbExp=3; IntAct=EBI-10182463, EBI-2565863;
CC Q2NKQ1-4; O14908-2: GIPC1; NbExp=3; IntAct=EBI-10182463, EBI-25913156;
CC Q2NKQ1-4; P42858: HTT; NbExp=12; IntAct=EBI-10182463, EBI-466029;
CC Q2NKQ1-4; O43920: NDUFS5; NbExp=3; IntAct=EBI-10182463, EBI-1246091;
CC Q2NKQ1-4; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10182463, EBI-748974;
CC Q2NKQ1-4; D3DTS7: PMP22; NbExp=3; IntAct=EBI-10182463, EBI-25882629;
CC Q2NKQ1-4; O60260-5: PRKN; NbExp=6; IntAct=EBI-10182463, EBI-21251460;
CC Q2NKQ1-4; P49768-2: PSEN1; NbExp=3; IntAct=EBI-10182463, EBI-11047108;
CC Q2NKQ1-4; P49810: PSEN2; NbExp=3; IntAct=EBI-10182463, EBI-2010251;
CC Q2NKQ1-4; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-10182463, EBI-6503765;
CC Q2NKQ1-4; Q16637: SMN2; NbExp=3; IntAct=EBI-10182463, EBI-395421;
CC Q2NKQ1-4; P37840: SNCA; NbExp=3; IntAct=EBI-10182463, EBI-985879;
CC Q2NKQ1-4; P00441: SOD1; NbExp=3; IntAct=EBI-10182463, EBI-990792;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q8BPQ7}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:22637480}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22637480}. Cytoplasm {ECO:0000269|PubMed:22637480}.
CC Note=Recruited to cytoplasmic vesicle membranes via its interaction
CC with Rab family members, such as RAB9A. {ECO:0000269|PubMed:22637480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2NKQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2NKQ1-3; Sequence=VSP_024665, VSP_024666, VSP_024667,
CC VSP_024668;
CC Name=3;
CC IsoId=Q2NKQ1-4; Sequence=VSP_024667;
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, heart and testis.
CC {ECO:0000269|PubMed:17509819}.
CC -!- SIMILARITY: Belongs to the RUTBC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85527.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB275761; BAF63511.1; -; mRNA.
DR EMBL; AB449879; BAH16622.1; -; mRNA.
DR EMBL; AB075821; BAB85527.1; ALT_INIT; mRNA.
DR EMBL; AL049759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036915; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS46674.1; -. [Q2NKQ1-1]
DR CCDS; CCDS46675.1; -. [Q2NKQ1-4]
DR RefSeq; NP_001035037.1; NM_001039948.3. [Q2NKQ1-1]
DR RefSeq; NP_001091967.1; NM_001098497.2. [Q2NKQ1-4]
DR RefSeq; NP_001091968.1; NM_001098498.2.
DR RefSeq; NP_597711.1; NM_133454.3.
DR AlphaFoldDB; Q2NKQ1; -.
DR SMR; Q2NKQ1; -.
DR BioGRID; 126182; 12.
DR IntAct; Q2NKQ1; 21.
DR STRING; 9606.ENSP00000383212; -.
DR CarbonylDB; Q2NKQ1; -.
DR iPTMnet; Q2NKQ1; -.
DR PhosphoSitePlus; Q2NKQ1; -.
DR BioMuta; SGSM1; -.
DR DMDM; 145566945; -.
DR jPOST; Q2NKQ1; -.
DR MassIVE; Q2NKQ1; -.
DR MaxQB; Q2NKQ1; -.
DR PaxDb; Q2NKQ1; -.
DR PeptideAtlas; Q2NKQ1; -.
DR PRIDE; Q2NKQ1; -.
DR ProteomicsDB; 61410; -. [Q2NKQ1-1]
DR ProteomicsDB; 61411; -. [Q2NKQ1-3]
DR ProteomicsDB; 61412; -. [Q2NKQ1-4]
DR Antibodypedia; 308; 92 antibodies from 28 providers.
DR DNASU; 129049; -.
DR Ensembl; ENST00000400358.9; ENSP00000383211.4; ENSG00000167037.19. [Q2NKQ1-4]
DR Ensembl; ENST00000400359.4; ENSP00000383212.4; ENSG00000167037.19. [Q2NKQ1-1]
DR GeneID; 129049; -.
DR KEGG; hsa:129049; -.
DR MANE-Select; ENST00000400358.9; ENSP00000383211.4; NM_001098497.3; NP_001091967.1. [Q2NKQ1-4]
DR UCSC; uc003abg.3; human. [Q2NKQ1-1]
DR CTD; 129049; -.
DR DisGeNET; 129049; -.
DR GeneCards; SGSM1; -.
DR HGNC; HGNC:29410; SGSM1.
DR HPA; ENSG00000167037; Tissue enhanced (brain, heart muscle).
DR MIM; 611417; gene.
DR neXtProt; NX_Q2NKQ1; -.
DR OpenTargets; ENSG00000167037; -.
DR PharmGKB; PA162403086; -.
DR VEuPathDB; HostDB:ENSG00000167037; -.
DR eggNOG; KOG1648; Eukaryota.
DR GeneTree; ENSGT00940000156871; -.
DR HOGENOM; CLU_006235_0_0_1; -.
DR InParanoid; Q2NKQ1; -.
DR OMA; KMMHRDS; -.
DR OrthoDB; 171826at2759; -.
DR PhylomeDB; Q2NKQ1; -.
DR TreeFam; TF318216; -.
DR PathwayCommons; Q2NKQ1; -.
DR SignaLink; Q2NKQ1; -.
DR BioGRID-ORCS; 129049; 7 hits in 1058 CRISPR screens.
DR ChiTaRS; SGSM1; human.
DR GeneWiki; SGSM1; -.
DR GenomeRNAi; 129049; -.
DR Pharos; Q2NKQ1; Tbio.
DR PRO; PR:Q2NKQ1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q2NKQ1; protein.
DR Bgee; ENSG00000167037; Expressed in cardiac muscle of right atrium and 138 other tissues.
DR ExpressionAtlas; Q2NKQ1; baseline and differential.
DR Genevisible; Q2NKQ1; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR CDD; cd15784; PH_RUTBC; 1.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR037745; SGSM1/2.
DR InterPro; IPR021935; SGSM1/2_RBD.
DR Pfam; PF12068; PH_RBD; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW GTPase activation; Membrane; Reference proteome.
FT CHAIN 1..1148
FT /note="Small G protein signaling modulator 1"
FT /id="PRO_0000284833"
FT DOMAIN 36..190
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 617..1081
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 256..297
FT /note="Important for interaction with RAB9A and RAB9B"
FT /evidence="ECO:0000250|UniProtKB:Q8BPQ7"
FT REGION 301..350
FT /note="Required for interaction with RAP family members"
FT REGION 377..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:19077034"
FT /id="VSP_024665"
FT VAR_SEQ 133
FT /note="T -> TALFEKVLDKIVHYLVENSSKYYEKEALLMDPVDGPILASLLVGPCA
FT LEYTKMKTADHFWTDPSADELVQRHRIHSSHVRQDSPTKRPALCIQKRHSSGSMDDRPS
FT LSARDYVESLHQNSRATLLYGKNNVLVQPRDDMEAVPGYLSLHQTADVMTLKS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:19077034"
FT /id="VSP_024666"
FT VAR_SEQ 432..486
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:17509819, ECO:0000303|PubMed:19077034"
FT /id="VSP_024667"
FT VAR_SEQ 645..705
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11853319,
FT ECO:0000303|PubMed:19077034"
FT /id="VSP_024668"
FT VARIANT 802
FT /note="T -> P (in dbSNP:rs6004350)"
FT /id="VAR_031834"
FT VARIANT 873
FT /note="R -> K (in dbSNP:rs2073201)"
FT /id="VAR_031835"
SQ SEQUENCE 1148 AA; 129718 MW; D619F453BA914376 CRC64;
MASAPAEAET RQRLLRTVKK EVKQIMEEAV TRKFVHEDSS HIISFCAAVE ACVLHGLRRR
AAGFLRSNKI AALFMKVGKN FPPAEDLSRK VQDLEQLIES ARNQIQGLQE NVRKLPKLPN
LSPLAIKHLW IRTALFEKVL DKIVHYLVEN SSKYYEKEAL LMDPVDGPIL ASLLVGPCAL
EYTKMKTADH FWTDPSADEL VQRHRIHSSH VRQDSPTKRP ALCIQKRHSS GSMDDRPSLS
ARDYVESLHQ NSRATLLYGK NNVLVQPRDD MEAVPGYLSL HQTADVMTLK WTPNQLMNGS
VGDLDYEKSV YWDYAMTIRL EEIVYLHCHQ QVDSGGTVVL VSQDGIQRPP FRFPKGGHLL
QFLSCLENGL LPHGQLDPPL WSQRGKGKVF PKLRKRSPQG SAESTSSDKD DDEATDYVFR
IIYPGMQSEF VAPDFLGSTS SVSVGPAWMM VPAGRSMLVV ARGSQWEPAR WDTTLPTPSP
KEQPPMPQDL MDVSVSNLPS LWQPSPRKSS CSSCSQSGSA DGSSTNGCNH ERAPLKLLCD
NMKYQILSRA FYGWLAYCRH LSTVRTHLSA LVNHMIVSPD LPCDAGQGLT ARIWEQYLHD
STSYEEQELL RLIYYGGIQP EIRKAVWPFL LGHYQFGMTE TERKEVDEQI HACYAQTMAE
WLGCEAIVRQ RERESHAAAL AKCSSGASLD SHLHRMLHRD STISNESSQS CSSGRQNIRL
HSDSSSSTQV FESVDEVEQV EAEGRLEEKQ PKIPNGNLVN GTCSPDSGHP SSHNFSSGLS
EHSEPSLSTE DSVLDAQRNT PTVLRPRDGS VDDRQSSEAT TSQDEAPREE LAVQDSLESD
LLANESMDEF MSITGSLDMA LPEKDDVVME GWRSSETEKH GQADSEDNLS EEPEMESLFP
ALASLAVTTS ANEVSPVSSS GVTYSPELLD LYTVNLHRIE KDVQRCDRNY WYFTPANLEK
LRNIMCSYIW QHIEIGYVQG MCDLLAPLLV ILDDEALAFS CFTELMKRMN QNFPHGGAMD
THFANMRSLI QILDSELFEL MHQNGDYTHF YFCYRWFLLD FKRELVYDDV FLVWETIWAA
KHVSSAHYVL FIALALVEVY RDIILENNMD FTDIIKFFNE MAERHNTKQV LKLARDLVYK
VQTLIENK
