AMPL_HUMAN
ID AMPL_HUMAN Reviewed; 519 AA.
AC P28838; B3KMQ3; Q6IAM6; Q6P0L6; Q9UQE3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000305};
DE EC=3.4.11.1 {ECO:0000250|UniProtKB:P00727};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000250|UniProtKB:P00727};
DE EC=3.4.13.23 {ECO:0000250|UniProtKB:P00727};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000312|HGNC:HGNC:18449};
DE Short=LAP-3;
DE AltName: Full=Leucyl aminopeptidase {ECO:0000250|UniProtKB:P00727};
DE AltName: Full=Peptidase S {ECO:0000312|HGNC:HGNC:18449};
DE AltName: Full=Proline aminopeptidase {ECO:0000250|UniProtKB:P28839};
DE EC=3.4.11.5 {ECO:0000250|UniProtKB:P28839};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000303|PubMed:1908238};
GN Name=LAP3 {ECO:0000312|HGNC:HGNC:18449};
GN Synonyms=LAPEP, PEPS {ECO:0000312|HGNC:HGNC:18449};
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).
RA Mao M., Liu T., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y.,
RA Wang Z., Chen S., Chen Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lung;
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 [5]
RP PROTEIN SEQUENCE OF 33-54.
RC TISSUE=Liver;
RX PubMed=1908238; DOI=10.1016/0006-291x(91)91057-j;
RA Matsushima M., Takahashi T., Ichinose M., Miki K., Kurokawa K.,
RA Takahashi K.;
RT "Structural and immunological evidence for the identity of prolyl
RT aminopeptidase with leucyl aminopeptidase.";
RL Biochem. Biophys. Res. Commun. 178:1459-1464(1991).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of
CC unsubstituted N-terminal hydrophobic amino acids from various peptides.
CC The presence of Zn(2+) ions is essential for the peptidase activity,
CC and the association with other cofactors can modulate the substrate
CC spectificity of the enzyme. For instance, in the presence of Mn(2+), it
CC displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-
CC conjugates. Involved in the metabolism of glutathione and in the
CC degradation of glutathione S-conjugates, which may play a role in the
CC control of the cell redox status. {ECO:0000250|UniProtKB:P00727}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000305|PubMed:1908238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000250|UniProtKB:P00727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000250|UniProtKB:P28839};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC Note=Binds two metal ions per subunit. Two metal binding sites with
CC different affinities are located in the enzyme active site and can be
CC occupied in vitro by different metals: site 1 is occupied by Zn(2+),
CC Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be
CC occupied by only Zn(2+) or Co(2+). One Zn(2+) ion is tightly bound to
CC site 2 and essential for enzyme activity in vivo, while site 1 can be
CC occupied by different metals to give different enzymatic activities.
CC Mn(2+) is required for Cys-Gly hydrolysis activity. A third metal
CC binding site may serve a structural role, possibly stabilizing part of
CC the interface between the N-terminal and the catalytic domain.
CC {ECO:0000250|UniProtKB:P00727};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P00727}.
CC -!- INTERACTION:
CC P28838; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-2339312, EBI-11524452;
CC P28838; Q13185: CBX3; NbExp=6; IntAct=EBI-2339312, EBI-78176;
CC P28838; P45973: CBX5; NbExp=3; IntAct=EBI-2339312, EBI-78219;
CC P28838; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-2339312, EBI-726739;
CC P28838; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2339312, EBI-10232538;
CC P28838; Q92569: PIK3R3; NbExp=3; IntAct=EBI-2339312, EBI-79893;
CC P28838; P22415: USF1; NbExp=3; IntAct=EBI-2339312, EBI-1054489;
CC P28838; P36508: ZNF76; NbExp=3; IntAct=EBI-2339312, EBI-7254550;
CC P28838; Q15942: ZYX; NbExp=3; IntAct=EBI-2339312, EBI-444225;
CC P28838; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2339312, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P28838-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28838-2; Sequence=VSP_022631;
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; AF061738; AAD17527.1; -; mRNA.
DR EMBL; CR457128; CAG33409.1; -; mRNA.
DR EMBL; AK022055; BAG51065.1; -; mRNA.
DR EMBL; AK298613; BAG60795.1; -; mRNA.
DR EMBL; BC065564; AAH65564.1; -; mRNA.
DR EMBL; BC006199; AAH06199.3; -; mRNA.
DR CCDS; CCDS3422.1; -. [P28838-1]
DR PIR; PT0431; PT0431.
DR RefSeq; NP_056991.2; NM_015907.2. [P28838-1]
DR AlphaFoldDB; P28838; -.
DR SMR; P28838; -.
DR BioGRID; 119248; 93.
DR IntAct; P28838; 27.
DR MINT; P28838; -.
DR STRING; 9606.ENSP00000226299; -.
DR BindingDB; P28838; -.
DR ChEMBL; CHEMBL3965; -.
DR DrugBank; DB07448; (2S)-3-[(R)-[(1S)-1-amino-3-phenylpropyl](hydroxy)phosphoryl]-2-benzylpropanoic acid.
DR DrugBank; DB02386; Leucine Phosphonic Acid.
DR DrugBank; DB08766; Zofenoprilat.
DR DrugCentral; P28838; -.
DR MEROPS; M17.001; -.
DR GlyGen; P28838; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28838; -.
DR MetOSite; P28838; -.
DR PhosphoSitePlus; P28838; -.
DR BioMuta; LAP3; -.
DR DMDM; 124028615; -.
DR REPRODUCTION-2DPAGE; IPI00789806; -.
DR REPRODUCTION-2DPAGE; P28838; -.
DR UCD-2DPAGE; P28838; -.
DR EPD; P28838; -.
DR jPOST; P28838; -.
DR MassIVE; P28838; -.
DR MaxQB; P28838; -.
DR PaxDb; P28838; -.
DR PeptideAtlas; P28838; -.
DR PRIDE; P28838; -.
DR ProteomicsDB; 54502; -. [P28838-1]
DR ProteomicsDB; 54503; -. [P28838-2]
DR Antibodypedia; 23080; 240 antibodies from 32 providers.
DR CPTC; P28838; 1 antibody.
DR DNASU; 51056; -.
DR Ensembl; ENST00000226299.9; ENSP00000226299.4; ENSG00000002549.13. [P28838-1]
DR Ensembl; ENST00000606142.5; ENSP00000476028.1; ENSG00000002549.13. [P28838-2]
DR Ensembl; ENST00000618908.4; ENSP00000481000.1; ENSG00000002549.13. [P28838-1]
DR GeneID; 51056; -.
DR KEGG; hsa:51056; -.
DR MANE-Select; ENST00000226299.9; ENSP00000226299.4; NM_015907.3; NP_056991.2.
DR UCSC; uc003gph.1; human. [P28838-1]
DR CTD; 51056; -.
DR DisGeNET; 51056; -.
DR GeneCards; LAP3; -.
DR HGNC; HGNC:18449; LAP3.
DR HPA; ENSG00000002549; Low tissue specificity.
DR MIM; 170250; gene.
DR neXtProt; NX_P28838; -.
DR OpenTargets; ENSG00000002549; -.
DR PharmGKB; PA38537; -.
DR VEuPathDB; HostDB:ENSG00000002549; -.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_1_2_1; -.
DR InParanoid; P28838; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 562530at2759; -.
DR PhylomeDB; P28838; -.
DR TreeFam; TF314954; -.
DR BRENDA; 3.4.11.1; 2681.
DR BRENDA; 3.4.11.2; 2681.
DR PathwayCommons; P28838; -.
DR SignaLink; P28838; -.
DR SIGNOR; P28838; -.
DR BioGRID-ORCS; 51056; 16 hits in 1089 CRISPR screens.
DR ChiTaRS; LAP3; human.
DR GenomeRNAi; 51056; -.
DR Pharos; P28838; Tchem.
DR PRO; PR:P28838; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P28838; protein.
DR Bgee; ENSG00000002549; Expressed in palpebral conjunctiva and 207 other tissues.
DR ExpressionAtlas; P28838; baseline and differential.
DR Genevisible; P28838; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0004177; F:aminopeptidase activity; NAS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:RHEA.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008235; F:metalloexopeptidase activity; NAS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Aminopeptidase; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Zinc.
FT CHAIN 1..519
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165825"
FT ACT_SITE 294
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT ACT_SITE 368
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FS4"
FT MOD_RES 45
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FS4"
FT MOD_RES 61
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 455
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 476
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPY7"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022631"
FT CONFLICT 20
FT /note="R -> V (in Ref. 1; AAD17527)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="F -> S (in Ref. 1; AAD17527)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="T -> A (in Ref. 2; CAG33409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 56166 MW; D960F8F5B9024585 CRC64;
MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD
KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN
IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS
GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI
EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE
ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL
DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA
