GLSL_HUMAN
ID GLSL_HUMAN Reviewed; 602 AA.
AC Q9UI32; B7Z8Q9; Q8IX91; Q9NYY2; Q9UI31;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Glutaminase liver isoform, mitochondrial;
DE Short=GLS;
DE EC=3.5.1.2 {ECO:0000250|UniProtKB:Q571F8};
DE AltName: Full=L-glutaminase;
DE AltName: Full=L-glutamine amidohydrolase;
DE Flags: Precursor;
GN Name=GLS2; Synonyms=GA;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Mammary cancer;
RX PubMed=10620514; DOI=10.1042/bj3450365;
RA Gomez-Fabre P.M., Aledo J.C., del Castillo-Olivares A., Alonso F.J.,
RA Nunez de Castro I., Campos J.A., Marquez J.;
RT "Molecular cloning, sequencing and expression studies of the human breast
RT cancer cell glutaminase.";
RL Biochem. J. 345:365-375(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain, and Mammary cancer;
RX PubMed=12444921; DOI=10.1042/bj20021445;
RA Perez-Gomez C., Mates J.M., Gomez-Fabre P.M., del Castillo-Olivares A.,
RA Alonso F.J., Marquez J.;
RT "Genomic organization and transcriptional analysis of the human l-
RT glutaminase gene.";
RL Biochem. J. 370:771-784(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-581.
RC TISSUE=Brain;
RA Chavez R.A., Wang C., Cong R., Hawkinson J.E., Forsayeth J.R.;
RT "Identification and expression of human renal and hepatic glutaminase
RT isoforms.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH SNTA1 AND TAX1BP3.
RX PubMed=11163757; DOI=10.1016/s0014-5793(00)02373-5;
RA Olalla L., Aledo J.C., Bannenberg G., Marquez J.;
RT "The C-terminus of human glutaminase L mediates association with PDZ
RT domain-containing proteins.";
RL FEBS Lett. 488:116-122(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20378837; DOI=10.1073/pnas.1001006107;
RA Hu W., Zhang C., Wu R., Sun Y., Levine A., Feng Z.;
RT "Glutaminase 2, a novel p53 target gene regulating energy metabolism and
RT antioxidant function.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7455-7460(2010).
RN [9]
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 [10] {ECO:0007744|PDB:4BQM}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 154-479.
RA Ferreira I.M., Vollmar M., Krojer T., Strain-Damerell C., Froese S.,
RA Coutandin D., Williams E., Burgess-Brown N., von Delft F., Arrowsmith C.H.,
RA Bountra C., Edwards A., Dias S.M.G., Ambrosio A.L.B., Yue W.W.;
RT "Crystal Structure of Human Liver-Type Glutaminase, Catalytic Domain.";
RL Submitted (MAY-2013) to the PDB data bank.
RN [11] {ECO:0007744|PDB:5U0K}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 485-602, ANK REPEATS, AND
RP SUBUNIT.
RX PubMed=28526749; DOI=10.1074/jbc.m117.787291;
RA Pasquali C.C., Islam Z., Adamoski D., Ferreira I.M., Righeto R.D.,
RA Bettini J., Portugal R.V., Yue W.W., Gonzalez A., Dias S.M.G.,
RA Ambrosio A.L.B.;
RT "The origin and evolution of human glutaminases and their atypical C-
RT terminal ankyrin repeats.";
RL J. Biol. Chem. 292:11572-11585(2017).
CC -!- FUNCTION: Plays an important role in the regulation of glutamine
CC catabolism. Promotes mitochondrial respiration and increases ATP
CC generation in cells by catalyzing the synthesis of glutamate and alpha-
CC ketoglutarate. Increases cellular anti-oxidant function via NADH and
CC glutathione production. May play a role in preventing tumor
CC proliferation. {ECO:0000269|PubMed:20378837}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q571F8};
CC -!- SUBUNIT: Homotetramer, dimer of dimers (Probable). Does not assemble
CC into higher oligomers (By similarity). Interacts with the PDZ domain of
CC the syntrophin SNTA1. Interacts with the PDZ domain of TAX1BP3
CC (PubMed:11163757). {ECO:0000250|UniProtKB:Q571F8,
CC ECO:0000269|PubMed:11163757, ECO:0000305|PubMed:28526749}.
CC -!- INTERACTION:
CC Q9UI32; O00291: HIP1; NbExp=3; IntAct=EBI-3938654, EBI-473886;
CC Q9UI32; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-3938654, EBI-2815120;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20378837}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UI32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI32-2; Sequence=VSP_057009, VSP_057010;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Expressed in brain and
CC pancreas. Not observed in heart, placenta, lung, skeletal muscle and
CC kidney. Expression is significantly reduced in hepatocellular
CC carcinomas. {ECO:0000269|PubMed:10620514, ECO:0000269|PubMed:20378837}.
CC -!- INDUCTION: Up-regulated by P53 (at protein and mRNA level) under both
CC stressed and non-stressed conditions. {ECO:0000269|PubMed:20378837}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR EMBL; AF110330; AAF21933.1; -; mRNA.
DR EMBL; AF110331; AAF21934.1; -; mRNA.
DR EMBL; AF348119; AAO13298.2; -; Genomic_DNA.
DR EMBL; AF223944; AAF33826.1; -; mRNA.
DR EMBL; AK303772; BAH14045.1; -; mRNA.
DR EMBL; AC097104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96943.1; -; Genomic_DNA.
DR CCDS; CCDS8921.1; -. [Q9UI32-1]
DR RefSeq; NP_001267727.1; NM_001280798.1.
DR RefSeq; NP_037399.2; NM_013267.3. [Q9UI32-1]
DR PDB; 4BQM; X-ray; 2.18 A; A/B=154-479.
DR PDB; 5U0K; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=485-602.
DR PDBsum; 4BQM; -.
DR PDBsum; 5U0K; -.
DR AlphaFoldDB; Q9UI32; -.
DR SMR; Q9UI32; -.
DR BioGRID; 118044; 20.
DR IntAct; Q9UI32; 3.
DR STRING; 9606.ENSP00000310447; -.
DR BindingDB; Q9UI32; -.
DR ChEMBL; CHEMBL4105730; -.
DR DrugBank; DB11118; Ammonia.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00130; L-Glutamine.
DR iPTMnet; Q9UI32; -.
DR PhosphoSitePlus; Q9UI32; -.
DR BioMuta; GLS2; -.
DR DMDM; 145559477; -.
DR EPD; Q9UI32; -.
DR jPOST; Q9UI32; -.
DR MassIVE; Q9UI32; -.
DR MaxQB; Q9UI32; -.
DR PaxDb; Q9UI32; -.
DR PeptideAtlas; Q9UI32; -.
DR PRIDE; Q9UI32; -.
DR ProteomicsDB; 6970; -.
DR ProteomicsDB; 84460; -. [Q9UI32-1]
DR Antibodypedia; 28236; 310 antibodies from 30 providers.
DR DNASU; 27165; -.
DR Ensembl; ENST00000311966.9; ENSP00000310447.4; ENSG00000135423.13. [Q9UI32-1]
DR Ensembl; ENST00000486896.5; ENSP00000419661.1; ENSG00000135423.13. [Q9UI32-2]
DR GeneID; 27165; -.
DR KEGG; hsa:27165; -.
DR MANE-Select; ENST00000311966.9; ENSP00000310447.4; NM_013267.4; NP_037399.2.
DR UCSC; uc001slj.5; human. [Q9UI32-1]
DR CTD; 27165; -.
DR DisGeNET; 27165; -.
DR GeneCards; GLS2; -.
DR HGNC; HGNC:29570; GLS2.
DR HPA; ENSG00000135423; Tissue enriched (liver).
DR MIM; 606365; gene.
DR neXtProt; NX_Q9UI32; -.
DR OpenTargets; ENSG00000135423; -.
DR PharmGKB; PA134933506; -.
DR VEuPathDB; HostDB:ENSG00000135423; -.
DR eggNOG; KOG0506; Eukaryota.
DR GeneTree; ENSGT00390000010463; -.
DR HOGENOM; CLU_016439_1_0_1; -.
DR InParanoid; Q9UI32; -.
DR OMA; MAGNEFM; -.
DR OrthoDB; 349094at2759; -.
DR PhylomeDB; Q9UI32; -.
DR TreeFam; TF313359; -.
DR PathwayCommons; Q9UI32; -.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; Q9UI32; -.
DR SignaLink; Q9UI32; -.
DR SIGNOR; Q9UI32; -.
DR BioGRID-ORCS; 27165; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; GLS2; human.
DR GenomeRNAi; 27165; -.
DR Pharos; Q9UI32; Tchem.
DR PRO; PR:Q9UI32; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UI32; protein.
DR Bgee; ENSG00000135423; Expressed in right lobe of liver and 141 other tissues.
DR ExpressionAtlas; Q9UI32; baseline and differential.
DR Genevisible; Q9UI32; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR041541; Glutaminase_EF-hand.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF17959; EF-hand_14; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Hydrolase;
KW Mitochondrion; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..602
FT /note="Glutaminase liver isoform, mitochondrial"
FT /id="PRO_0000011625"
FT REPEAT 518..547
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 552..581
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT MOD_RES 253
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 284
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q571F8"
FT VAR_SEQ 136..209
FT /note="CVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLA
FT KSNPDLWGVSLCTVDGQRHSVG -> HSERSLSFLILRSSRAMWIASLRMSKSSLEAKW
FT QPTSLSWPSQTQTCGVSPCALWMVNGTLWATQRSPSACSPV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057009"
FT VAR_SEQ 210..602
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057010"
FT VARIANT 581
FT /note="L -> P (in dbSNP:rs2657879)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_031615"
FT CONFLICT 87
FT /note="I -> T (in Ref. 1; AAF21933)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="N -> S (in Ref. 1; AAF21933)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="N -> D (in Ref. 1; AAF21933)"
FT /evidence="ECO:0000305"
FT CONFLICT 328..329
FT /note="LK -> HE (in Ref. 1; AAF21933)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="A -> V (in Ref. 3; AAF33826)"
FT /evidence="ECO:0000305"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 308..317
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 357..368
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:4BQM"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:4BQM"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 445..458
FT /evidence="ECO:0007829|PDB:4BQM"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:5U0K"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:5U0K"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:5U0K"
FT HELIX 522..529
FT /evidence="ECO:0007829|PDB:5U0K"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:5U0K"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:5U0K"
FT HELIX 566..578
FT /evidence="ECO:0007829|PDB:5U0K"
SQ SEQUENCE 602 AA; 66323 MW; 6D0E1EFF01BC3843 CRC64;
MRSMKALQKA LSRAGSHCGR GGWGHPSRSP LLGGGVRHHL SEAAAQGRET PHSHQPQHQD
HDSSESGMLS RLGDLLFYTI AEGQERIPIH KFTTALKATG LQTSDPRLRD CMSEMHRVVQ
ESSSGGLLDR DLFRKCVSSN IVLLTQAFRK KFVIPDFEEF TGHVDRIFED VKELTGGKVA
AYIPQLAKSN PDLWGVSLCT VDGQRHSVGH TKIPFCLQSC VKPLTYAISI STLGTDYVHK
FVGKEPSGLR YNKLSLNEEG IPHNPMVNAG AIVVSSLIKM DCNKAEKFDF VLQYLNKMAG
NEYMGFSNAT FQSEKETGDR NYAIGYYLKE KKCFPKGVDM MAALDLYFQL CSVEVTCESG
SVMAATLANG GICPITGESV LSAEAVRNTL SLMHSCGMYD FSGQFAFHVG LPAKSAVSGA
ILLVVPNVMG MMCLSPPLDK LGNSHRGTSF CQKLVSLFNF HNYDNLRHCA RKLDPRREGA
EIRNKTVVNL LFAAYSGDVS ALRRFALSAM DMEQKDYDSR TALHVAAAEG HIEVVKFLIE
ACKVNPFAKD RWGNIPLDDA VQFNHLEVVK LLQDYQDSYT LSETQAEAAA EALSKENLES
MV
