MFHA1_HUMAN
ID MFHA1_HUMAN Reviewed; 1052 AA.
AC Q9Y4C4; Q96CI0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Malignant fibrous histiocytoma-amplified sequence 1 {ECO:0000305};
DE AltName: Full=Malignant fibrous histiocytoma-amplified sequence with leucine-rich tandem repeats 1 {ECO:0000303|PubMed:9973190};
GN Name=MFHAS1 {ECO:0000312|HGNC:HGNC:16982};
GN Synonyms=MASL1 {ECO:0000303|PubMed:9973190};
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], TISSUE SPECIFICITY, AND VARIANT PRO-892.
RC TISSUE=Fetal brain;
RX PubMed=9973190;
RA Sakabe T., Shinomiya T., Mori T., Ariyama Y., Fukuda Y., Fujiwara T.,
RA Nakamura Y., Inazawa J.;
RT "Identification of a novel gene, MASL1, within an amplicon at 8p23.1
RT detected in malignant fibrous histiocytomas by comparative genomic
RT hybridization.";
RL Cancer Res. 59:511-515(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-1052, AND VARIANT PRO-892.
RC TISSUE=B-cell;
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 [4]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH 14Q21 ELEMENT.
RX PubMed=14691450; DOI=10.1038/sj.onc.1207352;
RA Tagawa H., Karnan S., Kasugai Y., Tuzuki S., Suzuki R., Hosokawa Y.,
RA Seto M.;
RT "MASL1, a candidate oncogene found in amplification at 8p23.1, is
RT translocated in immunoblastic B-cell lymphoma cell line OCI-LY8.";
RL Oncogene 23:2576-2581(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-601, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP INDUCTION.
RX PubMed=20616063; DOI=10.1073/pnas.1000093107;
RA Ng A.C., Eisenberg J.M., Heath R.J., Huett A., Robinson C.M., Nau G.J.,
RA Xavier R.J.;
RT "Human leucine-rich repeat proteins: a genome-wide bioinformatic
RT categorization and functional analysis in innate immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4631-4638(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION, INTERACTION WITH RAF1, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF 414-LEU--ARG-556 AND SER-450.
RX PubMed=23327923; DOI=10.1182/blood-2011-10-385252;
RA Kumkhaek C., Aerbajinai W., Liu W., Zhu J., Uchida N., Kurlander R.,
RA Hsieh M.M., Tisdale J.F., Rodgers G.P.;
RT "MASL1 induces erythroid differentiation in human erythropoietin-dependent
RT CD34+ cells through the Raf/MEK/ERK pathway.";
RL Blood 121:3216-3227(2013).
RN [9]
RP GTP-BINDING, INTERACTION WITH HSPD1, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF LYS-443.
RX PubMed=24286120; DOI=10.1111/febs.12593;
RA Dihanich S., Civiero L., Manzoni C., Mamais A., Bandopadhyay R.,
RA Greggio E., Lewis P.A.;
RT "GTP binding controls complex formation by the human ROCO protein MASL1.";
RL FEBS J. 281:261-274(2014).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=26599367; DOI=10.1371/journal.pone.0143662;
RA Zhong J., Shi Q.Q., Zhu M.M., Shen J., Wang H.H., Ma D., Miao C.H.;
RT "MFHAS1 is associated with sepsis and stimulates TLR2/NF-kappaB signaling
RT pathway following negative regulation.";
RL PLoS ONE 10:E0143662-E0143662(2015).
RN [11]
RP FUNCTION, INTERACTION WITH PJA2, UBIQUITINATION BY PJA2, AND REGION.
RX PubMed=28471450; DOI=10.1038/cddis.2017.102;
RA Zhong J., Wang H., Chen W., Sun Z., Chen J., Xu Y., Weng M., Shi Q., Ma D.,
RA Miao C.;
RT "Ubiquitylation of MFHAS1 by the ubiquitin ligase praja2 promotes M1
RT macrophage polarization by activating JNK and p38 pathways.";
RL Cell Death Dis. 8:E2763-E2763(2017).
RN [12]
RP FUNCTION, INTERACTION WITH PPP2CA AND PPP2R2A, AND REGION.
RX PubMed=28609714; DOI=10.1016/j.molimm.2017.06.017;
RA Shi Q., Xiong B., Zhong J., Wang H., Ma D., Miao C.;
RT "MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C subunit
RT cytoplasm translocation and inhibition of c-Jun dephosphorylation at
RT Thr239.";
RL Mol. Immunol. 88:79-88(2017).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=29168081; DOI=10.1007/s10753-017-0696-0;
RA Wang H.H., Sun P.F., Chen W.K., Zhong J., Shi Q.Q., Weng M.L., Ma D.,
RA Miao C.H.;
RT "High Glucose Stimulates Expression of MFHAS1 to Mitigate Inflammation via
RT Akt/HO-1 Pathway in Human Umbilical Vein Endothelial Cells.";
RL Inflammation 41:400-408(2018).
CC -!- FUNCTION: Probable GTP-binding protein (PubMed:24286120). Functions in
CC innate immunity and more specifically the inflammatory response as a
CC regulator of the Toll-like receptor TLR2 and TLR4 signaling pathways
CC (PubMed:26599367, PubMed:28471450, PubMed:28609714). Negatively
CC regulates the part of the TLR4 signaling pathway that leads to the
CC activation of the transcription factor AP-1. By retaining the
CC phosphatase complex PP2A into the cytoplasm, prevents the
CC dephosphorylation of the AP-1 subunit JUN which is required for proper
CC activation of the transcription factor (PubMed:28609714). Both inhibits
CC and activates the TLR2-dependent signaling pathway (PubMed:26599367).
CC Positively regulates the TLR2 signaling pathway to activate
CC specifically the downstream p38 and JNK MAP kinases and promote the
CC polarization of macrophages toward the pro-inflammatory M1 phenotype
CC (PubMed:28471450). It may also play a role in the regulation of
CC inflammation induced by high glucose through the PKB/AKT signaling
CC pathway (PubMed:29168081). Also involved in erythrocyte differentiation
CC through activation of the ERK1/ERK2 signaling pathway
CC (PubMed:23327923). {ECO:0000269|PubMed:23327923,
CC ECO:0000269|PubMed:24286120, ECO:0000269|PubMed:26599367,
CC ECO:0000269|PubMed:28471450, ECO:0000269|PubMed:28609714,
CC ECO:0000269|PubMed:29168081}.
CC -!- SUBUNIT: Interacts with RAF1 (PubMed:23327923). Interacts with HSPD1
CC (PubMed:24286120). Interacts with PPP2CA; retains PPP2CA into the
CC cytoplasm and excludes it from the nucleus (PubMed:28609714). Interacts
CC with PPP2R2A; the interaction is direct (PubMed:28609714). Interacts
CC with PJA2 (PubMed:28471450). {ECO:0000269|PubMed:23327923,
CC ECO:0000269|PubMed:24286120, ECO:0000269|PubMed:28471450,
CC ECO:0000269|PubMed:28609714}.
CC -!- INTERACTION:
CC Q9Y4C4; P10809: HSPD1; NbExp=3; IntAct=EBI-2864441, EBI-352528;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24286120}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Overexpressed in malignant
CC fibrous histiocytomas (PubMed:9973190). Expressed in red blood cells
CC (at protein level) (PubMed:23327923). {ECO:0000269|PubMed:23327923,
CC ECO:0000269|PubMed:9973190}.
CC -!- INDUCTION: Up-regulated during erythroid cells differentiation (at
CC protein level) (PubMed:23327923). Up-regulated upon Toll-like receptor
CC TLR2 stimulation (PubMed:26599367). Up-regulated in macrophages upon M.
CC tuberculosis infection (PubMed:20616063). Up-regulated upon sepsis
CC (PubMed:26599367). Up-regulated by glucose (PubMed:29168081).
CC {ECO:0000269|PubMed:20616063, ECO:0000269|PubMed:23327923,
CC ECO:0000269|PubMed:26599367, ECO:0000269|PubMed:29168081}.
CC -!- PTM: Ubiquitinated. Ubiquitination by PJA2 does not lead MFHAS1 to
CC proteasomal degradation but positively regulates its function in
CC polarization of macrophages. {ECO:0000269|PubMed:28471450}.
CC -!- DISEASE: Note=A chromosomal aberration involving MFHAS1 may be a cause
CC of B-cell lymphoma. Translocation t(8;14)(p23.1;q21) with a cryptic
CC exon named '14q21 element'. The resulting fusion protein named
CC 'chimeric MASL1' is tumorigenic in nude mice.
CC {ECO:0000269|PubMed:14691450}.
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DR EMBL; AB016816; BAA74737.1; -; mRNA.
DR EMBL; AC090567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014226; AAH14226.2; -; mRNA.
DR CCDS; CCDS34844.1; -.
DR RefSeq; NP_004216.2; NM_004225.2.
DR AlphaFoldDB; Q9Y4C4; -.
DR SMR; Q9Y4C4; -.
DR BioGRID; 114681; 128.
DR IntAct; Q9Y4C4; 94.
DR MINT; Q9Y4C4; -.
DR STRING; 9606.ENSP00000276282; -.
DR iPTMnet; Q9Y4C4; -.
DR PhosphoSitePlus; Q9Y4C4; -.
DR BioMuta; MFHAS1; -.
DR DMDM; 296437367; -.
DR EPD; Q9Y4C4; -.
DR jPOST; Q9Y4C4; -.
DR MassIVE; Q9Y4C4; -.
DR MaxQB; Q9Y4C4; -.
DR PaxDb; Q9Y4C4; -.
DR PeptideAtlas; Q9Y4C4; -.
DR PRIDE; Q9Y4C4; -.
DR ProteomicsDB; 86160; -.
DR Antibodypedia; 65867; 18 antibodies from 9 providers.
DR DNASU; 9258; -.
DR Ensembl; ENST00000276282.7; ENSP00000276282.6; ENSG00000147324.11.
DR GeneID; 9258; -.
DR KEGG; hsa:9258; -.
DR MANE-Select; ENST00000276282.7; ENSP00000276282.6; NM_004225.3; NP_004216.2.
DR UCSC; uc003wsj.2; human.
DR CTD; 9258; -.
DR DisGeNET; 9258; -.
DR GeneCards; MFHAS1; -.
DR HGNC; HGNC:16982; MFHAS1.
DR HPA; ENSG00000147324; Low tissue specificity.
DR MIM; 605352; gene.
DR neXtProt; NX_Q9Y4C4; -.
DR OpenTargets; ENSG00000147324; -.
DR PharmGKB; PA30773; -.
DR VEuPathDB; HostDB:ENSG00000147324; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158928; -.
DR HOGENOM; CLU_320767_0_0_1; -.
DR InParanoid; Q9Y4C4; -.
DR OMA; IVCPKNG; -.
DR OrthoDB; 1013039at2759; -.
DR PhylomeDB; Q9Y4C4; -.
DR TreeFam; TF351429; -.
DR PathwayCommons; Q9Y4C4; -.
DR SignaLink; Q9Y4C4; -.
DR BioGRID-ORCS; 9258; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; MFHAS1; human.
DR GenomeRNAi; 9258; -.
DR Pharos; Q9Y4C4; Tbio.
DR PRO; PR:Q9Y4C4; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y4C4; protein.
DR Bgee; ENSG00000147324; Expressed in saphenous vein and 185 other tissues.
DR Genevisible; Q9Y4C4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020859; ROC_dom.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 13.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51450; LRR; 12.
DR PROSITE; PS51424; ROC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosomal rearrangement; Cytoplasm; GTP-binding; Immunity;
KW Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Signal transduction inhibitor; Tumor suppressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1052
FT /note="Malignant fibrous histiocytoma-amplified sequence 1"
FT /id="PRO_0000308609"
FT REPEAT 64..85
FT /note="LRR 1"
FT REPEAT 88..109
FT /note="LRR 2"
FT REPEAT 112..133
FT /note="LRR 3"
FT REPEAT 136..157
FT /note="LRR 4"
FT REPEAT 159..180
FT /note="LRR 5"
FT REPEAT 182..203
FT /note="LRR 6"
FT REPEAT 205..226
FT /note="LRR 7"
FT REPEAT 228..249
FT /note="LRR 8"
FT REPEAT 251..272
FT /note="LRR 9"
FT REPEAT 274..296
FT /note="LRR 10"
FT REPEAT 297..318
FT /note="LRR 11"
FT REPEAT 320..341
FT /note="LRR 12"
FT REPEAT 343..364
FT /note="LRR 13"
FT DOMAIN 403..649
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT REGION 64..649
FT /note="Required for interaction with PPP2R2A"
FT /evidence="ECO:0000269|PubMed:28609714"
FT REGION 64..364
FT /note="Required for interaction with PJA2"
FT /evidence="ECO:0000269|PubMed:28471450"
FT SITE 1000..1001
FT /note="Breakpoint for translocation to form chimeric MASL1"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 601
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 163
FT /note="L -> V (in dbSNP:rs34984230)"
FT /id="VAR_036846"
FT VARIANT 892
FT /note="L -> P (in dbSNP:rs429433)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9973190"
FT /id="VAR_036847"
FT MUTAGEN 414..556
FT /note="Missing: Dominant negative effect on the ERK1/ERK2
FT signaling pathway and EPO-induced erythroid
FT differentiation."
FT /evidence="ECO:0000269|PubMed:23327923"
FT MUTAGEN 443
FT /note="K->A: Loss of GTP-binding."
FT /evidence="ECO:0000269|PubMed:24286120"
FT MUTAGEN 450
FT /note="S->A: Dominant negative effect on the ERK1/ERK2
FT signaling pathway and EPO-induced erythroid
FT differentiation."
FT /evidence="ECO:0000269|PubMed:23327923"
FT CONFLICT 529
FT /note="H -> N (in Ref. 1; BAA74737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1052 AA; 116950 MW; D68AB60DEC5F6653 CRC64;
MAGMDSGNLK TARLWRDAAL RARKLRSNLR QLTLTAAGAC PGAGADALES PASPQLVLPA
NLGDIEALNL GNNGLEEVPE GLGSALGSLR VLVLRRNRFA RLPPAVAELG HHLTELDVSH
NRLTALGAEV VSALRELRKL NLSHNQLPAL PAQLGALAHL EELDVSFNRL AHLPDSLSCL
SRLRTLDVDH NQLTAFPRQL LQLVALEELD VSSNRLRGLP EDISALRALK ILWLSGAELG
TLPAGFCELA SLESLMLDNN GLQALPAQFS CLQRLKMLNL SSNLFEEFPA ALLPLAGLEE
LYLSRNQLTS VPSLISGLGR LLTLWLDNNR IRYLPDSIVE LTGLEELVLQ GNQIAVLPDH
FGQLSRVGLW KIKDNPLIQP PYEVCMKGIP YIAAYQKELA HSQPAVQPRL KLLLMGHKAA
GKTLLRHCLT EERVEGCPGG GDKEKCYPPS PPPVSKGIEV TSWTADASRG LRFIVYDLAG
DESYEVIQPF FLSPGALYVL VVNLATYEPR HFPTTVGSFL HRVGARVPHA VVCIVGTHAD
LCGERELEEK CLDIHRQIAL QEKHDAEGLS RLAKVVDEAL ARDFELRSAS PHAAYYGVSD
KNLRRRKAHF QYLLNHRLQI LSPVLPVSCR DPRHLRRLRD KLLSVAEHRE IFPNLHRVLP
RSWQVLEELH FQPPQAQRLW LSWWDSARLG LQAGLTEDRL QSALSYLHES GKLLYFEDSP
ALKEHVFHNL TRLIDILNVF FQRDPSLLLH KLLLGTSGEG KAEGESSPPM ARSTPSQELL
RATQLHQYVE GFLLHGLLPA HVIRLLLKPH VQAQQDLQLL LELLEKMGLC YCLNKPKGKP
LNGSTAWYKF PCYVQNEVPH AEAWINGTNL AGQSFVAEQL QIEYSFPFTF PLGLFARYSV
QINSHVVHRS DGKFQIFAYR GKVPVVVSYR PARGVLQPDT LSIASHASLP NIWTAWQAIT
PLVEELNVLL QEWPGLHYTV HILCSKCLKR GSPNPHAFPG ELLSQPRPEG VAEIICPKNG
SERVNVALVY PPTPTVISPC SKKNVGEKHR NQ
