Full text data of HINT3
HINT3
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histidine triad nucleotide-binding protein 3; HINT-3; 3.-.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histidine triad nucleotide-binding protein 3; HINT-3; 3.-.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NQE9
ID HINT3_HUMAN Reviewed; 182 AA.
AC Q9NQE9; B3KQ91; Q8N0Y9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Histidine triad nucleotide-binding protein 3;
DE Short=HINT-3;
DE EC=3.-.-.-;
GN Name=HINT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-36.
RA Huang C.-H.;
RT "Human HINT-4 is a novel member of the histidine triad protein family
RT with differential polyadenylation.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng J.L., Liu B.L., Chou T.F., Drontle D., Wagner C.R.;
RT "HINT-3-2, a novel member of HIT family, and Hint3-1 with
RT phosphoramidase activity.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-36.
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GENE FAMILY.
RX PubMed=12119013; DOI=10.1021/bi025942q;
RA Brenner C.;
RT "Hint, Fhit, and GalT: function, structure, evolution, and mechanism
RT of three branches of the histidine triad superfamily of nucleotide
RT hydrolases and transferases.";
RL Biochemistry 41:9003-9014(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT
RP ALA-36, ACTIVE SITE, AND MUTAGENESIS OF HIS-145.
RX PubMed=17870088; DOI=10.1016/j.jmb.2007.08.023;
RA Chou T.-F., Cheng J., Tikh I.B., Wagner C.R.;
RT "Evidence that human histidine triad nucleotide binding protein 3
RT (Hint3) is a distinct branch of the histidine triad (HIT)
RT superfamily.";
RL J. Mol. Biol. 373:978-989(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Hydrolyzes phosphoramidate and acyl-adenylate
CC substrates.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for indolepropinoic acyl-adenylate;
CC KM=22 uM for adenine;
CC KM=29 uM for guanine;
CC KM=32 uM for hypoxanthine;
CC KM=121 uM for uracil;
CC KM=181 uM for cytosine;
CC Note=HINT3 prefers purine over pyrimidine-based substrates;
CC -!- SUBUNIT: Forms dimers to octamers and even larger oligomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized as
CC aggregates in the cytoplasm and the nucleus.
CC -!- SIMILARITY: Belongs to the HINT family.
CC -!- SIMILARITY: Contains 1 HIT domain.
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DR EMBL; AY035387; AAK71347.1; -; mRNA.
DR EMBL; AY035388; AAK71348.1; -; mRNA.
DR EMBL; AY486460; AAR89533.1; -; mRNA.
DR EMBL; AY486461; AAR89534.1; -; mRNA.
DR EMBL; AK057688; BAG51953.1; -; mRNA.
DR EMBL; AL035689; CAB92728.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48129.1; -; Genomic_DNA.
DR EMBL; BC015732; AAH15732.1; -; mRNA.
DR RefSeq; NP_612638.3; NM_138571.4.
DR UniGene; Hs.72325; -.
DR ProteinModelPortal; Q9NQE9; -.
DR SMR; Q9NQE9; 47-149.
DR PhosphoSite; Q9NQE9; -.
DR DMDM; 74752900; -.
DR PaxDb; Q9NQE9; -.
DR PeptideAtlas; Q8N0Y9; -.
DR PRIDE; Q9NQE9; -.
DR DNASU; 135114; -.
DR Ensembl; ENST00000229633; ENSP00000229633; ENSG00000111911.
DR GeneID; 135114; -.
DR KEGG; hsa:135114; -.
DR UCSC; uc003qal.4; human.
DR CTD; 135114; -.
DR GeneCards; GC06P126277; -.
DR HGNC; HGNC:18468; HINT3.
DR HPA; HPA027914; -.
DR MIM; 609998; gene.
DR neXtProt; NX_Q9NQE9; -.
DR PharmGKB; PA29288; -.
DR eggNOG; NOG254977; -.
DR HOGENOM; HOG000061067; -.
DR HOVERGEN; HBG057291; -.
DR InParanoid; Q9NQE9; -.
DR OMA; NNFTDFT; -.
DR OrthoDB; EOG77M8Q7; -.
DR PhylomeDB; Q9NQE9; -.
DR SABIO-RK; Q9NQE9; -.
DR ChiTaRS; HINT3; human.
DR GenomeRNAi; 135114; -.
DR NextBio; 83449; -.
DR PRO; PR:Q9NQE9; -.
DR Bgee; Q9NQE9; -.
DR CleanEx; HS_HINT3; -.
DR Genevestigator; Q9NQE9; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR PANTHER; PTHR12486; PTHR12486; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; FALSE_NEG.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Nucleus; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 182 Histidine triad nucleotide-binding
FT protein 3.
FT /FTId=PRO_0000324327.
FT DOMAIN 49 160 HIT.
FT NP_BIND 76 77 Purine nucleotide phosphoramidate (By
FT similarity).
FT NP_BIND 145 147 Purine nucleotide phosphoramidate (By
FT similarity).
FT MOTIF 143 147 Histidine triad motif.
FT ACT_SITE 145 145 Tele-AMP-histidine intermediate.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 36 36 G -> A (2.5-fold increase in affinity for
FT indolepropinoic acyl-adenylate and
FT cytosine; 2-fold decrease in hypoxanthine
FT affinity; nearly no change in affinity
FT for adenine, guanine and uracil;
FT dbSNP:rs2295005).
FT /FTId=VAR_039734.
FT MUTAGEN 145 145 H->A: Abolishes hydrolase activity.
SQ SEQUENCE 182 AA; 20361 MW; B5E7EA8A07068251 CRC64;
MAEEQVNRSA GLAPDCEASA TAETTVSSVG TCEAAGKSPE PKDYDSTCVF CRIAGRQDPG
TELLHCENED LICFKDIKPA ATHHYLVVPK KHIGNCRTLR KDQVELVENM VTVGKTILER
NNFTDFTNVR MGFHMPPFCS ISHLHLHVLA PVDQLGFLSK LVYRVNSYWF ITADHLIEKL
RT
//
ID HINT3_HUMAN Reviewed; 182 AA.
AC Q9NQE9; B3KQ91; Q8N0Y9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Histidine triad nucleotide-binding protein 3;
DE Short=HINT-3;
DE EC=3.-.-.-;
GN Name=HINT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-36.
RA Huang C.-H.;
RT "Human HINT-4 is a novel member of the histidine triad protein family
RT with differential polyadenylation.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng J.L., Liu B.L., Chou T.F., Drontle D., Wagner C.R.;
RT "HINT-3-2, a novel member of HIT family, and Hint3-1 with
RT phosphoramidase activity.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-36.
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GENE FAMILY.
RX PubMed=12119013; DOI=10.1021/bi025942q;
RA Brenner C.;
RT "Hint, Fhit, and GalT: function, structure, evolution, and mechanism
RT of three branches of the histidine triad superfamily of nucleotide
RT hydrolases and transferases.";
RL Biochemistry 41:9003-9014(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT
RP ALA-36, ACTIVE SITE, AND MUTAGENESIS OF HIS-145.
RX PubMed=17870088; DOI=10.1016/j.jmb.2007.08.023;
RA Chou T.-F., Cheng J., Tikh I.B., Wagner C.R.;
RT "Evidence that human histidine triad nucleotide binding protein 3
RT (Hint3) is a distinct branch of the histidine triad (HIT)
RT superfamily.";
RL J. Mol. Biol. 373:978-989(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Hydrolyzes phosphoramidate and acyl-adenylate
CC substrates.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for indolepropinoic acyl-adenylate;
CC KM=22 uM for adenine;
CC KM=29 uM for guanine;
CC KM=32 uM for hypoxanthine;
CC KM=121 uM for uracil;
CC KM=181 uM for cytosine;
CC Note=HINT3 prefers purine over pyrimidine-based substrates;
CC -!- SUBUNIT: Forms dimers to octamers and even larger oligomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized as
CC aggregates in the cytoplasm and the nucleus.
CC -!- SIMILARITY: Belongs to the HINT family.
CC -!- SIMILARITY: Contains 1 HIT domain.
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DR EMBL; AY035387; AAK71347.1; -; mRNA.
DR EMBL; AY035388; AAK71348.1; -; mRNA.
DR EMBL; AY486460; AAR89533.1; -; mRNA.
DR EMBL; AY486461; AAR89534.1; -; mRNA.
DR EMBL; AK057688; BAG51953.1; -; mRNA.
DR EMBL; AL035689; CAB92728.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48129.1; -; Genomic_DNA.
DR EMBL; BC015732; AAH15732.1; -; mRNA.
DR RefSeq; NP_612638.3; NM_138571.4.
DR UniGene; Hs.72325; -.
DR ProteinModelPortal; Q9NQE9; -.
DR SMR; Q9NQE9; 47-149.
DR PhosphoSite; Q9NQE9; -.
DR DMDM; 74752900; -.
DR PaxDb; Q9NQE9; -.
DR PeptideAtlas; Q8N0Y9; -.
DR PRIDE; Q9NQE9; -.
DR DNASU; 135114; -.
DR Ensembl; ENST00000229633; ENSP00000229633; ENSG00000111911.
DR GeneID; 135114; -.
DR KEGG; hsa:135114; -.
DR UCSC; uc003qal.4; human.
DR CTD; 135114; -.
DR GeneCards; GC06P126277; -.
DR HGNC; HGNC:18468; HINT3.
DR HPA; HPA027914; -.
DR MIM; 609998; gene.
DR neXtProt; NX_Q9NQE9; -.
DR PharmGKB; PA29288; -.
DR eggNOG; NOG254977; -.
DR HOGENOM; HOG000061067; -.
DR HOVERGEN; HBG057291; -.
DR InParanoid; Q9NQE9; -.
DR OMA; NNFTDFT; -.
DR OrthoDB; EOG77M8Q7; -.
DR PhylomeDB; Q9NQE9; -.
DR SABIO-RK; Q9NQE9; -.
DR ChiTaRS; HINT3; human.
DR GenomeRNAi; 135114; -.
DR NextBio; 83449; -.
DR PRO; PR:Q9NQE9; -.
DR Bgee; Q9NQE9; -.
DR CleanEx; HS_HINT3; -.
DR Genevestigator; Q9NQE9; -.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR001310; Histidine_triad_HIT.
DR InterPro; IPR011146; HIT-like.
DR PANTHER; PTHR12486; PTHR12486; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; FALSE_NEG.
DR PROSITE; PS51084; HIT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Nucleus; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 182 Histidine triad nucleotide-binding
FT protein 3.
FT /FTId=PRO_0000324327.
FT DOMAIN 49 160 HIT.
FT NP_BIND 76 77 Purine nucleotide phosphoramidate (By
FT similarity).
FT NP_BIND 145 147 Purine nucleotide phosphoramidate (By
FT similarity).
FT MOTIF 143 147 Histidine triad motif.
FT ACT_SITE 145 145 Tele-AMP-histidine intermediate.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 36 36 G -> A (2.5-fold increase in affinity for
FT indolepropinoic acyl-adenylate and
FT cytosine; 2-fold decrease in hypoxanthine
FT affinity; nearly no change in affinity
FT for adenine, guanine and uracil;
FT dbSNP:rs2295005).
FT /FTId=VAR_039734.
FT MUTAGEN 145 145 H->A: Abolishes hydrolase activity.
SQ SEQUENCE 182 AA; 20361 MW; B5E7EA8A07068251 CRC64;
MAEEQVNRSA GLAPDCEASA TAETTVSSVG TCEAAGKSPE PKDYDSTCVF CRIAGRQDPG
TELLHCENED LICFKDIKPA ATHHYLVVPK KHIGNCRTLR KDQVELVENM VTVGKTILER
NNFTDFTNVR MGFHMPPFCS ISHLHLHVLA PVDQLGFLSK LVYRVNSYWF ITADHLIEKL
RT
//
MIM
609998
*RECORD*
*FIELD* NO
609998
*FIELD* TI
*609998 HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 3; HINT3
*FIELD* TX
DESCRIPTION
read more
Histidine triad proteins, such as HINT3, are nucleotide hydrolases and
transferases that act on the alpha-phosphate of ribonucleotides
(Brenner, 2002).
CLONING
Brenner (2002) stated that HINT3 encodes a deduced 182-amino acid
protein that contains 31 additional N-terminal amino acids and 25
additional C-terminal amino acids compared with HINT1 (601314).
MAPPING
Brenner (2002) stated that the HINT3 gene maps to chromosome 6q22.33.
*FIELD* RF
1. Brenner, C.: Hint, Fhit, and GalT: function, structure, evolution,
and mechanism of three branches of the histidine triad superfamily
of nucleotide hydrolases and transferases. Biochemistry 41: 9003-9014,
2002.
*FIELD* CD
Patricia A. Hartz: 3/22/2006
*FIELD* ED
mgross: 03/22/2006
*RECORD*
*FIELD* NO
609998
*FIELD* TI
*609998 HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 3; HINT3
*FIELD* TX
DESCRIPTION
read more
Histidine triad proteins, such as HINT3, are nucleotide hydrolases and
transferases that act on the alpha-phosphate of ribonucleotides
(Brenner, 2002).
CLONING
Brenner (2002) stated that HINT3 encodes a deduced 182-amino acid
protein that contains 31 additional N-terminal amino acids and 25
additional C-terminal amino acids compared with HINT1 (601314).
MAPPING
Brenner (2002) stated that the HINT3 gene maps to chromosome 6q22.33.
*FIELD* RF
1. Brenner, C.: Hint, Fhit, and GalT: function, structure, evolution,
and mechanism of three branches of the histidine triad superfamily
of nucleotide hydrolases and transferases. Biochemistry 41: 9003-9014,
2002.
*FIELD* CD
Patricia A. Hartz: 3/22/2006
*FIELD* ED
mgross: 03/22/2006