HINT1_HUMAN
ID HINT1_HUMAN Reviewed; 126 AA.
AC P49773; Q9H5W8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Adenosine 5'-monophosphoramidase HINT1 {ECO:0000305|PubMed:15703176};
DE EC=3.9.1.- {ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17217311, ECO:0000269|PubMed:17337452, ECO:0000269|PubMed:23614568, ECO:0000269|PubMed:28691797};
DE AltName: Full=Desumoylating isopeptidase HINT1 {ECO:0000305|PubMed:31088288};
DE EC=3.4.22.- {ECO:0000269|PubMed:31088288};
DE AltName: Full=Histidine triad nucleotide-binding protein 1;
DE AltName: Full=Protein kinase C inhibitor 1;
DE AltName: Full=Protein kinase C-interacting protein 1;
DE Short=PKCI-1;
GN Name=HINT1; Synonyms=HINT, PKCI1, PRKCNH1;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8812426; DOI=10.1006/geno.1996.0435;
RA Brzoska P.M., Chen H., Levin N.A., Kuo W.L., Collins C., Fu K.K.,
RA Gray J.W., Christman M.F.;
RT "Cloning, mapping, and in vivo localization of a human member of the PKCI-1
RT protein family (PRKCNH1).";
RL Genomics 36:151-156(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7644499; DOI=10.1073/pnas.92.17.7824;
RA Brzoska P.M., Chen H., Zhu Y., Levin N.A., Disatnik M.H., Mochly-Rosen D.,
RA Murnane J.P., Christman M.F.;
RT "The product of the ataxia-telangiectasia group D complementing gene, ATDC,
RT interacts with a protein kinase C substrate and inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7824-7828(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, and Prostate;
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 NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND
RP SUBUNIT.
RX PubMed=8643579; DOI=10.1073/pnas.93.11.5357;
RA Lima C.D., Klein M.G., Weinstein I.B., Hendrickson W.A.;
RT "Three-dimensional structure of human protein kinase C interacting protein
RT 1, a member of the HIT family of proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5357-5362(1996).
RN [7]
RP PROTEIN SEQUENCE OF 2-24.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9770345; DOI=10.1006/excr.1998.4153;
RA Klein M.G., Yao Y., Slosberg E.D., Lima C.D., Doki Y., Weinstein I.B.;
RT "Characterization of PKCI and comparative studies with FHIT, related
RT members of the HIT protein family.";
RL Exp. Cell Res. 244:26-32(1998).
RN [9]
RP INTERACTION WITH CDK7, AND SUBCELLULAR LOCATION.
RX PubMed=10958787; DOI=10.1074/jbc.c000505200;
RA Korsisaari N., Makela T.P.;
RT "Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad
RT proteins.";
RL J. Biol. Chem. 275:34837-34840(2000).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=15703176; DOI=10.1074/jbc.m500434200;
RA Chou T.F., Bieganowski P., Shilinski K., Cheng J., Brenner C., Wagner C.R.;
RT "31P NMR and genetic analysis establish hinT as the only Escherchia coli
RT purine nucleoside phosphoramidase and as essential for growth under high
RT salt conditions.";
RL J. Biol. Chem. 280:15356-15361(2005).
RN [11]
RP INTERACTION WITH RUVBL1 AND RUVBL2, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16014379; DOI=10.1242/jcs.02437;
RA Weiske J., Huber O.;
RT "The histidine triad protein Hint1 interacts with Pontin and Reptin and
RT inhibits TCF-beta-catenin-mediated transcription.";
RL J. Cell Sci. 118:3117-3129(2005).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-105 AND SER-107,
RP CHARACTERIZATION OF VARIANT NMAN ASN-112, SUBUNIT, AND IDENTIFICATION IN A
RP COMPLEX WITH KAT5.
RX PubMed=16835243; DOI=10.1074/jbc.m513452200;
RA Weiske J., Huber O.;
RT "The histidine triad protein Hint1 triggers apoptosis independent of its
RT enzymatic activity.";
RL J. Biol. Chem. 281:27356-27366(2006).
RN [13]
RP CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF VAL-97, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17337452; DOI=10.1074/jbc.m606972200;
RA Chou T.F., Tikh I.B., Horta B.A., Ghosh B., De Alencastro R.B.,
RA Wagner C.R.;
RT "Engineered monomeric human histidine triad nucleotide-binding protein 1
RT hydrolyzes fluorogenic acyl-adenylate and lysyl-tRNA synthetase-generated
RT lysyl-adenylate.";
RL J. Biol. Chem. 282:15137-15147(2007).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17217311; DOI=10.1021/mp060070y;
RA Chou T.F., Baraniak J., Kaczmarek R., Zhou X., Cheng J., Ghosh B.,
RA Wagner C.R.;
RT "Phosphoramidate pronucleotides: a comparison of the phosphoramidase
RT substrate specificity of human and Escherichia coli histidine triad
RT nucleotide binding proteins.";
RL Mol. Pharm. 4:208-217(2007).
RN [15]
RP INTERACTION WITH CDC34 AND RBX1, IDENTIFICATION IN A UBIQUITIN LIGASE
RP COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19112177; DOI=10.1074/jbc.m804531200;
RA Cen B., Li H., Weinstein I.B.;
RT "Histidine triad nucleotide-binding protein 1 up-regulates cellular levels
RT of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src.";
RL J. Biol. Chem. 284:5265-5276(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-30, AND IDENTIFICATION
RP BY MASS 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 [17]
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 [18]
RP IDENTIFICATION IN A COMPLEX WITH MITF AND CTNNB1, AND FUNCTION.
RX PubMed=22647378; DOI=10.4161/cc.20765;
RA Genovese G., Ghosh P., Li H., Rettino A., Sioletic S., Cittadini A.,
RA Sgambato A.;
RT "The tumor suppressor HINT1 regulates MITF and beta-catenin transcriptional
RT activity in melanoma cells.";
RL Cell Cycle 11:2206-2215(2012).
RN [19]
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 [20]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF HIS-51; HIS-110 AND HIS-114.
RX PubMed=23614568; DOI=10.1021/bi301616c;
RA Zhou X., Chou T.F., Aubol B.E., Park C.J., Wolfenden R., Adams J.,
RA Wagner C.R.;
RT "Kinetic mechanism of human histidine triad nucleotide binding protein 1.";
RL Biochemistry 52:3588-3600(2013).
RN [21]
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 [22]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT NMAN ASN-112.
RX PubMed=28691797; DOI=10.1021/acs.biochem.7b00148;
RA Shah R., Maize K.M., Zhou X., Finzel B.C., Wagner C.R.;
RT "Caught before Released: Structural Mapping of the Reaction Trajectory for
RT the Sofosbuvir Activating Enzyme, Human Histidine Triad Nucleotide Binding
RT Protein 1 (hHint1).";
RL Biochemistry 56:3559-3570(2017).
RN [23]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ASP-43 AND ILE-44, AND CHARACTERIZATION OF VARIANTS NMAN
RP PRO-37; ARG-84; VAL-89; ASP-93 AND ASN-112.
RX PubMed=29787766; DOI=10.1016/j.jmb.2018.05.028;
RA Shah R.M., Maize K.M., West H.T., Strom A.M., Finzel B.C., Wagner C.R.;
RT "Structure and Functional Characterization of Human Histidine Triad
RT Nucleotide-Binding Protein 1 Mutations Associated with Inherited Axonal
RT Neuropathy with Neuromyotonia.";
RL J. Mol. Biol. 430:2709-2721(2018).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-33; GLU-34; CYS-38;
RP LYS-57; VAL-97 AND HIS-114, AND CHARACTERIZATION OF VARIANTS NMAN PRO-37;
RP ARG-51; ARG-84; VAL-89; ASP-93 AND ASN-112.
RX PubMed=31088288; DOI=10.1089/ars.2019.7724;
RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.;
RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and
RT Calmodulin-Regulated Cysteine SUMO Protease.";
RL Antioxid. Redox Signal. 31:503-520(2019).
RN [25]
RP FUNCTION.
RX PubMed=30772266; DOI=10.1016/j.bcp.2019.02.018;
RA Krakowiak A., Piotrzkowska D., Kocon-Rebowska B., Kaczmarek R.,
RA Maciaszek A.;
RT "The role of the Hint1 protein in the metabolism of phosphorothioate
RT oligonucleotides drugs and prodrugs, and the release of H2S under cellular
RT conditions.";
RL Biochem. Pharmacol. 163:250-259(2019).
RN [26]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31990367; DOI=10.1002/1873-3468.13745;
RA Strom A., Tong C.L., Wagner C.R.;
RT "Histidine triad nucleotide-binding proteins HINT1 and HINT2 share similar
RT substrate specificities and little affinity for the signaling dinucleotide
RT Ap4A.";
RL FEBS Lett. 594:1497-1505(2020).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH AMP; ADENOSINE
RP METHYLENE DIPHOSPHATE AND ADENOSINE-5'-DITUNGSTATE, AND SUBUNIT.
RX PubMed=9323207; DOI=10.1126/science.278.5336.286;
RA Lima C.D., Klein M.G., Hendrickson W.A.;
RT "Structure-based analysis of catalysis and substrate definition in the HIT
RT protein family.";
RL Science 278:286-290(1997).
RN [28] {ECO:0007744|PDB:3TW2}
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH AMP, AND SUBUNIT.
RX PubMed=22869114; DOI=10.1107/s1744309112029491;
RA Dolot R., Ozga M., Wlodarczyk A., Krakowiak A., Nawrot B.;
RT "A new crystal form of human histidine triad nucleotide-binding protein 1
RT (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 A resolution.";
RL Acta Crystallogr. F 68:883-888(2012).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS,
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-114 AND
RP TRP-123.
RX PubMed=22329685; DOI=10.1021/jp212457w;
RA Wang J., Fang P., Schimmel P., Guo M.;
RT "Side chain independent recognition of aminoacyl adenylates by the Hint1
RT transcription suppressor.";
RL J. Phys. Chem. B 116:6798-6805(2012).
RN [30]
RP VARIANTS NMAN PRO-37; ARG-51; ARG-84; VAL-89; ASP-93 AND ASN-112, AND
RP CHARACTERIZATION OF VARIANTS NMAN PRO-37; ARG-51; ARG-84 AND ASN-112.
RX PubMed=22961002; DOI=10.1038/ng.2406;
RA Zimon M., Baets J., Almeida-Souza L., De Vriendt E., Nikodinovic J.,
RA Parman Y., Battaloglu E., Matur Z., Guergueltcheva V., Tournev I.,
RA Auer-Grumbach M., De Rijk P., Petersen B.S., Muller T., Fransen E.,
RA Van Damme P., Loscher W.N., Barisic N., Mitrovic Z., Previtali S.C.,
RA Topaloglu H., Bernert G., Beleza-Meireles A., Todorovic S.,
RA Savic-Pavicevic D., Ishpekova B., Lechner S., Peeters K., Ooms T.,
RA Hahn A.F., Zuchner S., Timmerman V., Van Dijck P., Rasic V.M.,
RA Janecke A.R., De Jonghe P., Jordanova A.;
RT "Loss-of-function mutations in HINT1 cause axonal neuropathy with
RT neuromyotonia.";
RL Nat. Genet. 44:1080-1083(2012).
CC -!- FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity,
CC hydrolyzing purine nucleotide phosphoramidates with a single phosphate
CC group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP
CC and NH2 (PubMed:15703176, PubMed:16835243, PubMed:17337452,
CC PubMed:17217311, PubMed:23614568, PubMed:28691797, PubMed:29787766,
CC PubMed:31990367, PubMed:22329685). Hydrolyzes adenosine
CC 5'monophosphomorpholidate (AMP-morpholidate) and guanosine
CC 5'monophosphomorpholidate (GMP-morpholidate) (PubMed:15703176,
CC PubMed:16835243). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl
CC lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-
CC AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl
CC lysine methyl ester)) and AMP-N-alanine methyl ester (PubMed:15703176,
CC PubMed:22329685, PubMed:17337452). Hydrolyzes 3-indolepropionic acyl-
CC adenylate, tryptamine adenosine phosphoramidate monoester and other
CC fluorogenic purine nucleoside tryptamine phosphoramidates in vitro
CC (PubMed:17337452, PubMed:23614568, PubMed:29787766, PubMed:17217311,
CC PubMed:28691797, PubMed:31990367). Can also convert adenosine 5'-O-
CC phosphorothioate and guanosine 5'-O-phosphorothioate to the
CC corresponding nucleoside 5'-O-phosphates with concomitant release of
CC hydrogen sulfide (PubMed:30772266). In addition, functions as
CC scaffolding protein that modulates transcriptional activation by the
CC LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1
CC (PubMed:16014379, PubMed:22647378). Modulates p53/TP53 levels and
CC p53/TP53-mediated apoptosis (PubMed:16835243). Modulates proteasomal
CC degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3
CC ubiquitin-protein ligase complex (PubMed:19112177). Also exhibits SUMO-
CC specific isopeptidase activity, deconjugating SUMO1 from RGS17
CC (PubMed:31088288). Deconjugates SUMO1 from RANGAP1 (By similarity).
CC {ECO:0000250|UniProtKB:P80912, ECO:0000269|PubMed:15703176,
CC ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16835243,
CC ECO:0000269|PubMed:17217311, ECO:0000269|PubMed:17337452,
CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685,
CC ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:23614568,
CC ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766,
CC ECO:0000269|PubMed:30772266, ECO:0000269|PubMed:31088288,
CC ECO:0000269|PubMed:31990367}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphoramidate + H2O = AMP + NH4(+);
CC Xref=Rhea:RHEA:67916, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57890, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16835243,
CC ECO:0000269|PubMed:17217311, ECO:0000269|PubMed:17337452,
CC ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:23614568,
CC ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766,
CC ECO:0000269|PubMed:31990367};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 uM for 3-indolepropionic acyl-adenylate
CC {ECO:0000269|PubMed:17337452, ECO:0000269|PubMed:23614568};
CC KM=0.13 uM for tryptamine adenosine phosphoramidate
CC {ECO:0000269|PubMed:17337452, ECO:0000269|PubMed:23614568};
CC KM=0.10 uM for tryptamine adenosine phosphoramidate
CC {ECO:0000269|PubMed:29787766};
CC -!- SUBUNIT: Homodimer. Interacts with CDK7. Interacts with RUVBL1 and
CC RUVBL2 and is associated with the LEF1/TCF1-CTNNB1 complex and with a
CC KAT5 histone acetyltransferase complex. Identified in a complex with
CC MITF and CTNNB1. Interacts with CDC34 and RBX1, and is part of a SCF
CC (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex
CC (PubMed:19112177). Interacts with SUMO1, SUMO2 and RGS17 (By
CC similarity). Interacts with the Ten-1 ICD form of TENM1 (By
CC similarity). Interacts with CALM1; interaction increases in the
CC presence of calcium ions (By similarity).
CC {ECO:0000250|UniProtKB:P70349, ECO:0000269|PubMed:10958787,
CC ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16014379,
CC ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17337452,
CC ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685,
CC ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:22869114,
CC ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:8643579,
CC ECO:0000269|PubMed:9323207}.
CC -!- INTERACTION:
CC P49773; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-1054330, EBI-11523759;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10958787,
CC ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177,
CC ECO:0000269|PubMed:8812426}. Nucleus {ECO:0000269|PubMed:10958787,
CC ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177,
CC ECO:0000269|PubMed:9770345}. Note=Interaction with CDK7 leads to a more
CC nuclear localization. {ECO:0000269|PubMed:10958787}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Neuromyotonia and axonal neuropathy, autosomal recessive
CC (NMAN) [MIM:137200]: An autosomal recessive neurologic disorder
CC characterized by onset in the first or second decade of a peripheral
CC axonal neuropathy predominantly affecting motor more than sensory
CC nerves. The axonal neuropathy is reminiscent of Charcot-Marie-Tooth
CC disease type 2 and distal hereditary motor neuropathy. Individuals with
CC NMAN also have delayed muscle relaxation and action myotonia associated
CC with neuromyotonic discharges on needle EMG resulting from
CC hyperexcitability of the peripheral nerves.
CC {ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:22961002,
CC ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766,
CC ECO:0000269|PubMed:31088288}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the HINT family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a protein kinase C inhibitor and
CC to bind zinc in solution. Both seem to be incorrect. {ECO:0000305}.
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DR EMBL; U27143; AAA82926.1; -; mRNA.
DR EMBL; U51004; AAC71077.1; -; mRNA.
DR EMBL; AK026557; BAB15500.1; -; mRNA.
DR EMBL; CR457048; CAG33329.1; -; mRNA.
DR EMBL; BC001287; AAH01287.1; -; mRNA.
DR EMBL; BC007090; AAH07090.1; -; mRNA.
DR CCDS; CCDS4147.1; -.
DR PIR; S72501; S72501.
DR RefSeq; NP_005331.1; NM_005340.6.
DR PDB; 1AV5; X-ray; 2.00 A; A/B=2-126.
DR PDB; 1KPA; X-ray; 2.00 A; A/B=2-126.
DR PDB; 1KPB; X-ray; 2.00 A; A/B=2-126.
DR PDB; 1KPC; X-ray; 2.20 A; A/B/C/D=2-126.
DR PDB; 1KPE; X-ray; 1.80 A; A/B=2-126.
DR PDB; 1KPF; X-ray; 1.50 A; A=2-126.
DR PDB; 3TW2; X-ray; 1.38 A; A/B=1-126.
DR PDB; 4EQE; X-ray; 1.52 A; A/B=1-126.
DR PDB; 4EQG; X-ray; 1.52 A; A/B=1-126.
DR PDB; 4EQH; X-ray; 1.67 A; A/B=1-126.
DR PDB; 4ZKL; X-ray; 2.34 A; A/B/C/D=1-126.
DR PDB; 4ZKV; X-ray; 1.92 A; A/B/C/D=1-126.
DR PDB; 5ED3; X-ray; 1.31 A; A/B=1-126.
DR PDB; 5ED6; X-ray; 1.52 A; A/B=1-126.
DR PDB; 5EMT; X-ray; 1.50 A; A/B=1-126.
DR PDB; 5I2E; X-ray; 1.60 A; A/B=1-126.
DR PDB; 5I2F; X-ray; 1.25 A; A/B=1-126.
DR PDB; 5IPB; X-ray; 1.55 A; A/B=1-126.
DR PDB; 5IPC; X-ray; 1.30 A; A/B=1-126.
DR PDB; 5IPD; X-ray; 1.75 A; A/B=1-126.
DR PDB; 5IPE; X-ray; 1.45 A; A/B=1-126.
DR PDB; 5KLY; X-ray; 1.30 A; A/B=1-126.
DR PDB; 5KLZ; X-ray; 1.50 A; A/B=1-126.
DR PDB; 5KM0; X-ray; 1.53 A; A/B/C/D=1-126.
DR PDB; 5KM1; X-ray; 1.65 A; A/B=1-126.
DR PDB; 5KM2; X-ray; 1.25 A; A/B=1-126.
DR PDB; 5KM3; X-ray; 1.20 A; A/B=1-126.
DR PDB; 5KM4; X-ray; 1.40 A; A/B=1-126.
DR PDB; 5KM6; X-ray; 1.60 A; A=1-126.
DR PDB; 5KMA; X-ray; 1.55 A; A/B=1-126.
DR PDB; 5KMB; X-ray; 1.60 A; A/B=1-126.
DR PDB; 5KMC; X-ray; 1.35 A; A/B=1-126.
DR PDB; 5O8I; X-ray; 1.27 A; A/B=1-126.
DR PDB; 5WA8; X-ray; 1.30 A; A/B=1-126.
DR PDB; 5WA9; X-ray; 1.15 A; A/B=1-126.
DR PDB; 5WAA; X-ray; 1.10 A; A/B=1-126.
DR PDB; 6B42; X-ray; 1.13 A; A=1-126.
DR PDB; 6G9Z; X-ray; 1.43 A; A/B=1-126.
DR PDB; 6J53; X-ray; 1.52 A; A/B=1-126.
DR PDB; 6J58; X-ray; 1.52 A; A/B=1-126.
DR PDB; 6J5S; X-ray; 1.02 A; A/B=1-126.
DR PDB; 6J5Z; X-ray; 1.30 A; A/B/C/D=1-126.
DR PDB; 6J64; X-ray; 0.95 A; A/B=1-126.
DR PDB; 6J65; X-ray; 1.42 A; A/B/D/E=1-126.
DR PDB; 6N3V; X-ray; 1.45 A; A/B=1-126.
DR PDB; 6N3W; X-ray; 1.75 A; A/B=1-126.
DR PDB; 6N3X; X-ray; 1.10 A; A/B=1-126.
DR PDB; 6N3Y; X-ray; 1.80 A; A/B=1-126.
DR PDB; 6YQM; X-ray; 1.02 A; AAA/BBB=1-126.
DR PDB; 7Q2U; X-ray; 2.27 A; AAA/BBB/CCC/DDD=1-126.
DR PDBsum; 1AV5; -.
DR PDBsum; 1KPA; -.
DR PDBsum; 1KPB; -.
DR PDBsum; 1KPC; -.
DR PDBsum; 1KPE; -.
DR PDBsum; 1KPF; -.
DR PDBsum; 3TW2; -.
DR PDBsum; 4EQE; -.
DR PDBsum; 4EQG; -.
DR PDBsum; 4EQH; -.
DR PDBsum; 4ZKL; -.
DR PDBsum; 4ZKV; -.
DR PDBsum; 5ED3; -.
DR PDBsum; 5ED6; -.
DR PDBsum; 5EMT; -.
DR PDBsum; 5I2E; -.
DR PDBsum; 5I2F; -.
DR PDBsum; 5IPB; -.
DR PDBsum; 5IPC; -.
DR PDBsum; 5IPD; -.
DR PDBsum; 5IPE; -.
DR PDBsum; 5KLY; -.
DR PDBsum; 5KLZ; -.
DR PDBsum; 5KM0; -.
DR PDBsum; 5KM1; -.
DR PDBsum; 5KM2; -.
DR PDBsum; 5KM3; -.
DR PDBsum; 5KM4; -.
DR PDBsum; 5KM6; -.
DR PDBsum; 5KMA; -.
DR PDBsum; 5KMB; -.
DR PDBsum; 5KMC; -.
DR PDBsum; 5O8I; -.
DR PDBsum; 5WA8; -.
DR PDBsum; 5WA9; -.
DR PDBsum; 5WAA; -.
DR PDBsum; 6B42; -.
DR PDBsum; 6G9Z; -.
DR PDBsum; 6J53; -.
DR PDBsum; 6J58; -.
DR PDBsum; 6J5S; -.
DR PDBsum; 6J5Z; -.
DR PDBsum; 6J64; -.
DR PDBsum; 6J65; -.
DR PDBsum; 6N3V; -.
DR PDBsum; 6N3W; -.
DR PDBsum; 6N3X; -.
DR PDBsum; 6N3Y; -.
DR PDBsum; 6YQM; -.
DR PDBsum; 7Q2U; -.
DR AlphaFoldDB; P49773; -.
DR SMR; P49773; -.
DR BioGRID; 109341; 151.
DR CORUM; P49773; -.
DR IntAct; P49773; 34.
DR MINT; P49773; -.
DR STRING; 9606.ENSP00000304229; -.
DR BindingDB; P49773; -.
DR ChEMBL; CHEMBL5878; -.
DR DrugBank; DB02162; 5'-O-(N-Ethyl-Sulfamoyl)Adenosine.
DR DrugBank; DB03349; 8-Bromo-Adenosine-5'-Monophosphate.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB02183; Adenosine-5'-ditungstate.
DR DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR DrugBank; DB08934; Sofosbuvir.
DR GlyGen; P49773; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49773; -.
DR MetOSite; P49773; -.
DR PhosphoSitePlus; P49773; -.
DR SwissPalm; P49773; -.
DR BioMuta; HINT1; -.
DR DMDM; 1708543; -.
DR OGP; P49773; -.
DR UCD-2DPAGE; P49773; -.
DR EPD; P49773; -.
DR jPOST; P49773; -.
DR MassIVE; P49773; -.
DR MaxQB; P49773; -.
DR PaxDb; P49773; -.
DR PeptideAtlas; P49773; -.
DR PRIDE; P49773; -.
DR ProteomicsDB; 56116; -.
DR TopDownProteomics; P49773; -.
DR Antibodypedia; 25857; 299 antibodies from 37 providers.
DR DNASU; 3094; -.
DR Ensembl; ENST00000304043.10; ENSP00000304229.5; ENSG00000169567.13.
DR GeneID; 3094; -.
DR KEGG; hsa:3094; -.
DR MANE-Select; ENST00000304043.10; ENSP00000304229.5; NM_005340.7; NP_005331.1.
DR UCSC; uc003kve.5; human.
DR CTD; 3094; -.
DR DisGeNET; 3094; -.
DR GeneCards; HINT1; -.
DR GeneReviews; HINT1; -.
DR HGNC; HGNC:4912; HINT1.
DR HPA; ENSG00000169567; Low tissue specificity.
DR MalaCards; HINT1; -.
DR MIM; 137200; phenotype.
DR MIM; 601314; gene.
DR neXtProt; NX_P49773; -.
DR OpenTargets; ENSG00000169567; -.
DR Orphanet; 324442; Autosomal recessive axonal neuropathy with neuromyotonia.
DR PharmGKB; PA29286; -.
DR VEuPathDB; HostDB:ENSG00000169567; -.
DR eggNOG; KOG3275; Eukaryota.
DR GeneTree; ENSGT00940000154451; -.
DR HOGENOM; CLU_056776_8_1_1; -.
DR InParanoid; P49773; -.
DR OMA; YHLHAHL; -.
DR OrthoDB; 1190598at2759; -.
DR PhylomeDB; P49773; -.
DR TreeFam; TF314862; -.
DR PathwayCommons; P49773; -.
DR SABIO-RK; P49773; -.
DR SignaLink; P49773; -.
DR BioGRID-ORCS; 3094; 8 hits in 1046 CRISPR screens.
DR ChiTaRS; HINT1; human.
DR EvolutionaryTrace; P49773; -.
DR GeneWiki; HINT1; -.
DR GenomeRNAi; 3094; -.
DR Pharos; P49773; Tchem.
DR PRO; PR:P49773; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P49773; protein.
DR Bgee; ENSG00000169567; Expressed in endothelial cell and 211 other tissues.
DR ExpressionAtlas; P49773; baseline and differential.
DR Genevisible; P49773; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043530; F:adenosine 5'-monophosphoramidase activity; IDA:UniProtKB.
DR GO; GO:0016929; F:deSUMOylase activity; IMP:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0005080; F:protein kinase C binding; TAS:ProtInc.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0016926; P:protein desumoylation; IMP:UniProtKB.
DR GO; GO:0009154; P:purine ribonucleotide catabolic process; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR23089; PTHR23089; 1.
DR Pfam; PF01230; HIT; 1.
DR PRINTS; PR00332; HISTRIAD.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing;
KW Disease variant; Hydrolase; Neuropathy; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Transcription; Transcription regulation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..126
FT /note="Adenosine 5'-monophosphoramidase HINT1"
FT /id="PRO_0000109781"
FT DOMAIN 18..126
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT MOTIF 110..114
FT /note="Histidine triad motif"
FT ACT_SITE 112
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000269|PubMed:9323207"
FT BINDING 43..44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22869114,
FT ECO:0007744|PDB:3TW2"
FT BINDING 99
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22869114,
FT ECO:0007744|PDB:3TW2"
FT BINDING 105..107
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22869114,
FT ECO:0007744|PDB:3TW2"
FT BINDING 112..114
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:22869114,
FT ECO:0007744|PDB:3TW2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70349"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70349"
FT VARIANT 37
FT /note="R -> P (in NMAN; negligible protein expression due
FT to post-translational degradation; loss of
FT homodimerization; significant decrease in adenosine 5'-
FT monophosphoramidase activity; reduced SUMO-specific
FT isopeptidase activity; dbSNP:rs149782619)"
FT /evidence="ECO:0000269|PubMed:22961002,
FT ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288"
FT /id="VAR_069212"
FT VARIANT 51
FT /note="H -> R (in NMAN; no mutant protein is detected due
FT to post-translational degradation; no effect on SUMO-
FT specific isopeptidase activity; dbSNP:rs397514491)"
FT /evidence="ECO:0000269|PubMed:22961002,
FT ECO:0000269|PubMed:31088288"
FT /id="VAR_069213"
FT VARIANT 84
FT /note="C -> R (in NMAN; negligible protein expression due
FT to post-translational degradation; no effect on
FT homodimerization; no effect on adenosine 5'-
FT monophosphoramidase; no effect on affinity for tryptamine
FT adenosine phosphoramidate; loss of SUMO-specific
FT isopeptidase activity; dbSNP:rs397514489)"
FT /evidence="ECO:0000269|PubMed:22961002,
FT ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288"
FT /id="VAR_069214"
FT VARIANT 89
FT /note="G -> V (in NMAN; no effect on homodimerization; no
FT effect on adenosine 5'-monophosphoramidase activity; no
FT effect on affinity for tryptamine adenosine
FT phosphoramidate; loss of SUMO-specific isopeptidase
FT activity; dbSNP:rs397514490)"
FT /evidence="ECO:0000269|PubMed:22961002,
FT ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288"
FT /id="VAR_069215"
FT VARIANT 93
FT /note="G -> D (in NMAN; loss of homodimerization;
FT significant decrease in adenosine 5'-monophosphoramidase
FT activity; approximately 40-fold increased affinity for
FT tryptamine adenosine phosphoramidate; loss of SUMO-specific
FT isopeptidase activity; dbSNP:rs397514493)"
FT /evidence="ECO:0000269|PubMed:22961002,
FT ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288"
FT /id="VAR_069216"
FT VARIANT 112
FT /note="H -> N (in NMAN; the enzyme has no residual activity
FT although the mutant protein is expressed at normal levels;
FT no effect on homodimerization; loss of SUMO-specific
FT isopeptidase activity; dbSNP:rs373849532)"
FT /evidence="ECO:0000269|PubMed:16835243,
FT ECO:0000269|PubMed:22961002, ECO:0000269|PubMed:28691797,
FT ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288"
FT /id="VAR_069217"
FT MUTAGEN 33
FT /note="F->S: Loss of SUMO-specific isopeptidase activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 34
FT /note="E->K: Reduced SUMO-specific isopeptidase activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 38
FT /note="C->R: No effect on SUMO-specific isopeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 43
FT /note="D->N: Approximately 50-fold increased affinity for
FT tryptamine adenosine phosphoramidate."
FT /evidence="ECO:0000269|PubMed:29787766"
FT MUTAGEN 44
FT /note="I->F: Approximately 10-fold increased affinity for
FT tryptamine adenosine phosphoramidate."
FT /evidence="ECO:0000269|PubMed:29787766"
FT MUTAGEN 44
FT /note="I->W: Approximately 30-fold increased affinity for
FT tryptamine adenosine phosphoramidate."
FT /evidence="ECO:0000269|PubMed:29787766"
FT MUTAGEN 51
FT /note="H->A: No effect on affinity for 3-indolepropionic
FT acyl-adenylate but a 13.8-fold increased affinity for
FT tryptamine adenosine phosphoramidate monoester."
FT /evidence="ECO:0000269|PubMed:23614568"
FT MUTAGEN 57
FT /note="K->N: Loss of SUMO-specific isopeptidase activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 97
FT /note="V->D: Loss of dimerization. Strongly reduced
FT adenosine 5'-monophosphoramidase activity. A 110-fold
FT increased affinity for 3-indolepropionic acyl-adenylate and
FT a 100-fold increased affinity for tryptamine adenosine
FT phosphoramidate monoester."
FT /evidence="ECO:0000269|PubMed:17337452"
FT MUTAGEN 97
FT /note="V->E: Loss of dimerization. Strongly reduced
FT adenosine 5'-monophosphoramidase activity. A 128-fold
FT increased affinity for 3-indolepropionic acyl-adenylate and
FT a 1000-fold increased affinity for tryptamine adenosine
FT phosphoramidate monoester."
FT /evidence="ECO:0000269|PubMed:17337452"
FT MUTAGEN 97
FT /note="V->M: Loss of SUMO-specific isopeptidase activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 105
FT /note="G->A: Reduces adenosine 5'-monophosphoramidase
FT activity."
FT /evidence="ECO:0000269|PubMed:16835243"
FT MUTAGEN 107
FT /note="S->A: Reduces adenosine 5'-monophosphoramidase
FT activity."
FT /evidence="ECO:0000269|PubMed:16835243"
FT MUTAGEN 110
FT /note="H->A: No significant effect on affinity for 3-
FT indolepropionic acyl-adenylate and tryptamine adenosine
FT phosphoramidate monoester."
FT /evidence="ECO:0000269|PubMed:23614568"
FT MUTAGEN 114
FT /note="H->A: Nearly abolishes adenosine 5'-
FT monophosphoramidase activity. A 3-fold increased affinity
FT for 3-indolepropionic acyl-adenylate and a 2-fold increased
FT affinity for tryptamine adenosine phosphoramidate
FT monoester."
FT /evidence="ECO:0000269|PubMed:22329685,
FT ECO:0000269|PubMed:23614568"
FT MUTAGEN 114
FT /note="H->R: Loss of SUMO-specific isopeptidase activity."
FT /evidence="ECO:0000269|PubMed:31088288"
FT MUTAGEN 123
FT /note="W->A: Nearly abolishes adenosine 5'-
FT monophosphoramidase activity."
FT /evidence="ECO:0000269|PubMed:22329685"
FT CONFLICT 25
FT /note="K -> E (in Ref. 3; BAB15500)"
FT /evidence="ECO:0000305"
FT HELIX 18..23
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 47..58
FT /evidence="ECO:0007829|PDB:6J64"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:6J64"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6J64"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6J64"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6J64"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6J64"
SQ SEQUENCE 126 AA; 13802 MW; 6C2B0119370384AA CRC64;
MADEIAKAQV ARPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT HFLVIPKKHI
SQISVAEDDD ESLLGHLMIV GKKCAADLGL NKGYRMVVNE GSDGGQSVYH VHLHVLGGRQ
MHWPPG
