Full text data of NIT1
NIT1
[Confidence: low (only semi-automatic identification from reviews)]
Nitrilase homolog 1; 3.5.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nitrilase homolog 1; 3.5.-.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q86X76
ID NIT1_HUMAN Reviewed; 327 AA.
AC Q86X76; B1AQP3; D3DVF4; O76091;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Nitrilase homolog 1;
DE EC=3.5.-.-;
GN Name=NIT1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), AND
RP TISSUE SPECIFICITY.
RX PubMed=9671749; DOI=10.1073/pnas.95.15.8744;
RA Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y.,
RA Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K.,
RA Buchberg A.M., Mazo A., Brenner C., Croce C.M.;
RT "Nitrilase and Fhit homologs are encoded as fusion proteins in
RT Drosophila melanogaster and Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-239 (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
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).
CC -!- FUNCTION: Plays a role in cell growth and apoptosis: loss of
CC expression promotes cell growth and resistance to DNA damage
CC stress. Has tumor suppressor properties that enhances the
CC apoptotic responsiveness in cancer cells; this effect is additive
CC to the tumor suppressor activity of FHIT. It is also a negative
CC regulator of primary T-cells. Has apparently no omega-amidase
CC activity such as NIT2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2;
CC IsoId=Q86X76-1; Sequence=Displayed;
CC Note=Major isoform;
CC Name=1; Synonyms=3;
CC IsoId=Q86X76-2; Sequence=VSP_011546;
CC Name=4;
CC IsoId=Q86X76-3; Sequence=VSP_011544, VSP_011547;
CC Name=5;
CC IsoId=Q86X76-4; Sequence=VSP_011545;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver,
CC skeletal muscle, kidney and pancreas.
CC -!- MISCELLANEOUS: According to Rosetta Stone theory, the existence of
CC a fusion protein in one genome predicts that the separate
CC polypeptides expressed in other organisms function in the same
CC cellular or biochemical pathway. In Drosophila melanogaster and
CC Caenorhabditis elegans, NitFhit is a fusion protein composed of a
CC C-terminal Fhit domain and a domain related to plant and bacterial
CC nitrilase.
CC -!- SIMILARITY: Belongs to the nitrilase superfamily. NIT1/NIT2
CC family.
CC -!- SIMILARITY: Contains 1 CN hydrolase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46149.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal exon is derived from the last exon of the DEDD gene;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF069984; AAC39901.1; -; Genomic_DNA.
DR EMBL; AF069987; AAC39907.1; -; mRNA.
DR EMBL; CR541814; CAG46613.1; -; mRNA.
DR EMBL; CR541846; CAG46644.1; -; mRNA.
DR EMBL; AL591806; CAI15379.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52656.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52654.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52657.1; -; Genomic_DNA.
DR EMBL; BC046149; AAH46149.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001172021.1; NM_001185092.1.
DR RefSeq; NP_001172022.1; NM_001185093.1.
DR RefSeq; NP_001172023.1; NM_001185094.1.
DR RefSeq; NP_005591.1; NM_005600.2.
DR RefSeq; XP_005245273.1; XM_005245216.1.
DR UniGene; Hs.146406; -.
DR ProteinModelPortal; Q86X76; -.
DR SMR; Q86X76; 48-319.
DR IntAct; Q86X76; 2.
DR MINT; MINT-1194030; -.
DR STRING; 9606.ENSP00000356988; -.
DR PhosphoSite; Q86X76; -.
DR DMDM; 51704324; -.
DR PaxDb; Q86X76; -.
DR PRIDE; Q86X76; -.
DR DNASU; 4817; -.
DR Ensembl; ENST00000368007; ENSP00000356986; ENSG00000158793.
DR Ensembl; ENST00000368009; ENSP00000356988; ENSG00000158793.
DR Ensembl; ENST00000392190; ENSP00000376028; ENSG00000158793.
DR GeneID; 4817; -.
DR KEGG; hsa:4817; -.
DR UCSC; uc001fxv.2; human.
DR CTD; 4817; -.
DR GeneCards; GC01P161087; -.
DR HGNC; HGNC:7828; NIT1.
DR HPA; HPA006657; -.
DR MIM; 604618; gene.
DR neXtProt; NX_Q86X76; -.
DR PharmGKB; PA31636; -.
DR eggNOG; COG0388; -.
DR HOGENOM; HOG000222700; -.
DR HOVERGEN; HBG052628; -.
DR InParanoid; Q86X76; -.
DR KO; K01506; -.
DR OMA; STPDKEQ; -.
DR OrthoDB; EOG7XDBGD; -.
DR PhylomeDB; Q86X76; -.
DR BRENDA; 3.5.5.1; 2681.
DR GenomeRNAi; 4817; -.
DR NextBio; 18562; -.
DR PRO; PR:Q86X76; -.
DR ArrayExpress; Q86X76; -.
DR Bgee; Q86X76; -.
DR CleanEx; HS_NIT1; -.
DR Genevestigator; Q86X76; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000257; F:nitrilase activity; TAS:ProtInc.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Mitochondrion; Reference proteome.
FT CHAIN 1 327 Nitrilase homolog 1.
FT /FTId=PRO_0000213251.
FT DOMAIN 47 320 CN hydrolase.
FT ACT_SITE 86 86 Proton acceptor (Potential).
FT ACT_SITE 161 161 By similarity.
FT ACT_SITE 203 203 Nucleophile (By similarity).
FT VAR_SEQ 1 36 Missing (in isoform 1).
FT /FTId=VSP_011546.
FT VAR_SEQ 1 33 MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQPR -> MTFG
FT LRKRLSEERGFSLM (in isoform 5).
FT /FTId=VSP_011545.
FT VAR_SEQ 1 31 MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQ -> MVLAIS
FT SCWASSPGLLTDSCPFCVLDSGYLNSQYFVLSPGRTYSLSR
FT R (in isoform 4).
FT /FTId=VSP_011544.
FT VAR_SEQ 327 327 S -> SDLTSVSLDLPLPPPPCHYELVLM (in isoform
FT 4).
FT /FTId=VSP_011547.
SQ SEQUENCE 327 AA; 35896 MW; 90F7FB9D4BA627B1 CRC64;
MLGFITRPPH RFLSLLCPGL RIPQLSVLCA QPRPRAMAIS SSSCELPLVA VCQVTSTPDK
QQNFKTCAEL VREAARLGAC LAFLPEAFDF IARDPAETLH LSEPLGGKLL EEYTQLAREC
GLWLSLGGFH ERGQDWEQTQ KIYNCHVLLN SKGAVVATYR KTHLCDVEIP GQGPMCESNS
TMPGPSLESP VSTPAGKIGL AVCYDMRFPE LSLALAQAGA EILTYPSAFG SITGPAHWEV
LLRARAIETQ CYVVAAAQCG RHHEKRASYG HSMVVDPWGT VVARCSEGPG LCLARIDLNY
LRQLRRHLPV FQHRRPDLYG NLGHPLS
//
ID NIT1_HUMAN Reviewed; 327 AA.
AC Q86X76; B1AQP3; D3DVF4; O76091;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 31-AUG-2004, sequence version 2.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Nitrilase homolog 1;
DE EC=3.5.-.-;
GN Name=NIT1;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), AND
RP TISSUE SPECIFICITY.
RX PubMed=9671749; DOI=10.1073/pnas.95.15.8744;
RA Pekarsky Y., Campiglio M., Siprashvili Z., Druck T., Sedkov Y.,
RA Tillib S., Draganescu A., Wermuth P., Rothman J.H., Huebner K.,
RA Buchberg A.M., Mazo A., Brenner C., Croce C.M.;
RT "Nitrilase and Fhit homologs are encoded as fusion proteins in
RT Drosophila melanogaster and Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-239 (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
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).
CC -!- FUNCTION: Plays a role in cell growth and apoptosis: loss of
CC expression promotes cell growth and resistance to DNA damage
CC stress. Has tumor suppressor properties that enhances the
CC apoptotic responsiveness in cancer cells; this effect is additive
CC to the tumor suppressor activity of FHIT. It is also a negative
CC regulator of primary T-cells. Has apparently no omega-amidase
CC activity such as NIT2 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2;
CC IsoId=Q86X76-1; Sequence=Displayed;
CC Note=Major isoform;
CC Name=1; Synonyms=3;
CC IsoId=Q86X76-2; Sequence=VSP_011546;
CC Name=4;
CC IsoId=Q86X76-3; Sequence=VSP_011544, VSP_011547;
CC Name=5;
CC IsoId=Q86X76-4; Sequence=VSP_011545;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver,
CC skeletal muscle, kidney and pancreas.
CC -!- MISCELLANEOUS: According to Rosetta Stone theory, the existence of
CC a fusion protein in one genome predicts that the separate
CC polypeptides expressed in other organisms function in the same
CC cellular or biochemical pathway. In Drosophila melanogaster and
CC Caenorhabditis elegans, NitFhit is a fusion protein composed of a
CC C-terminal Fhit domain and a domain related to plant and bacterial
CC nitrilase.
CC -!- SIMILARITY: Belongs to the nitrilase superfamily. NIT1/NIT2
CC family.
CC -!- SIMILARITY: Contains 1 CN hydrolase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46149.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal exon is derived from the last exon of the DEDD gene;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF069984; AAC39901.1; -; Genomic_DNA.
DR EMBL; AF069987; AAC39907.1; -; mRNA.
DR EMBL; CR541814; CAG46613.1; -; mRNA.
DR EMBL; CR541846; CAG46644.1; -; mRNA.
DR EMBL; AL591806; CAI15379.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52656.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52654.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52657.1; -; Genomic_DNA.
DR EMBL; BC046149; AAH46149.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001172021.1; NM_001185092.1.
DR RefSeq; NP_001172022.1; NM_001185093.1.
DR RefSeq; NP_001172023.1; NM_001185094.1.
DR RefSeq; NP_005591.1; NM_005600.2.
DR RefSeq; XP_005245273.1; XM_005245216.1.
DR UniGene; Hs.146406; -.
DR ProteinModelPortal; Q86X76; -.
DR SMR; Q86X76; 48-319.
DR IntAct; Q86X76; 2.
DR MINT; MINT-1194030; -.
DR STRING; 9606.ENSP00000356988; -.
DR PhosphoSite; Q86X76; -.
DR DMDM; 51704324; -.
DR PaxDb; Q86X76; -.
DR PRIDE; Q86X76; -.
DR DNASU; 4817; -.
DR Ensembl; ENST00000368007; ENSP00000356986; ENSG00000158793.
DR Ensembl; ENST00000368009; ENSP00000356988; ENSG00000158793.
DR Ensembl; ENST00000392190; ENSP00000376028; ENSG00000158793.
DR GeneID; 4817; -.
DR KEGG; hsa:4817; -.
DR UCSC; uc001fxv.2; human.
DR CTD; 4817; -.
DR GeneCards; GC01P161087; -.
DR HGNC; HGNC:7828; NIT1.
DR HPA; HPA006657; -.
DR MIM; 604618; gene.
DR neXtProt; NX_Q86X76; -.
DR PharmGKB; PA31636; -.
DR eggNOG; COG0388; -.
DR HOGENOM; HOG000222700; -.
DR HOVERGEN; HBG052628; -.
DR InParanoid; Q86X76; -.
DR KO; K01506; -.
DR OMA; STPDKEQ; -.
DR OrthoDB; EOG7XDBGD; -.
DR PhylomeDB; Q86X76; -.
DR BRENDA; 3.5.5.1; 2681.
DR GenomeRNAi; 4817; -.
DR NextBio; 18562; -.
DR PRO; PR:Q86X76; -.
DR ArrayExpress; Q86X76; -.
DR Bgee; Q86X76; -.
DR CleanEx; HS_NIT1; -.
DR Genevestigator; Q86X76; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000257; F:nitrilase activity; TAS:ProtInc.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR001110; UPF0012_CS.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS01227; UPF0012; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Mitochondrion; Reference proteome.
FT CHAIN 1 327 Nitrilase homolog 1.
FT /FTId=PRO_0000213251.
FT DOMAIN 47 320 CN hydrolase.
FT ACT_SITE 86 86 Proton acceptor (Potential).
FT ACT_SITE 161 161 By similarity.
FT ACT_SITE 203 203 Nucleophile (By similarity).
FT VAR_SEQ 1 36 Missing (in isoform 1).
FT /FTId=VSP_011546.
FT VAR_SEQ 1 33 MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQPR -> MTFG
FT LRKRLSEERGFSLM (in isoform 5).
FT /FTId=VSP_011545.
FT VAR_SEQ 1 31 MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQ -> MVLAIS
FT SCWASSPGLLTDSCPFCVLDSGYLNSQYFVLSPGRTYSLSR
FT R (in isoform 4).
FT /FTId=VSP_011544.
FT VAR_SEQ 327 327 S -> SDLTSVSLDLPLPPPPCHYELVLM (in isoform
FT 4).
FT /FTId=VSP_011547.
SQ SEQUENCE 327 AA; 35896 MW; 90F7FB9D4BA627B1 CRC64;
MLGFITRPPH RFLSLLCPGL RIPQLSVLCA QPRPRAMAIS SSSCELPLVA VCQVTSTPDK
QQNFKTCAEL VREAARLGAC LAFLPEAFDF IARDPAETLH LSEPLGGKLL EEYTQLAREC
GLWLSLGGFH ERGQDWEQTQ KIYNCHVLLN SKGAVVATYR KTHLCDVEIP GQGPMCESNS
TMPGPSLESP VSTPAGKIGL AVCYDMRFPE LSLALAQAGA EILTYPSAFG SITGPAHWEV
LLRARAIETQ CYVVAAAQCG RHHEKRASYG HSMVVDPWGT VVARCSEGPG LCLARIDLNY
LRQLRRHLPV FQHRRPDLYG NLGHPLS
//
MIM
604618
*RECORD*
*FIELD* NO
604618
*FIELD* TI
*604618 NITRILASE 1; NIT1
*FIELD* TX
Bacterial and plant nitrilases are enzymes that cleave nitriles and
read moreorganic amides to the corresponding carboxylic acids plus ammonia. By
searching an EST database with the sequence of the nitrilase domain of
the Drosophila NitFhit protein, Pekarsky et al. (1998) identified human
ESTs encoding nitrilase-1 (NIT1). They found that the NIT1 gene is
expressed as alternatively spliced transcripts. The major NIT1
transcript encodes a deduced 327-amino acid protein that shares 90%
amino acid sequence identity with mouse Nit1, 58% identity with the
nitrilase domain of C. elegans NitFhit, and 53% identity with the
nitrilase domain of Drosophila NitFhit. The NIT1 gene spans
approximately 3.2 kb and contains 7 exons. Northern blot analysis
detected NIT1 transcripts of approximately 1.4 and 2.4 kb in all adult
tissues examined, namely heart, brain, lung, liver, pancreas, kidney,
skeletal muscle, and placenta. An approximately 1.2-kb NIT1 transcript
was found in skeletal muscle and heart.
By radiation hybrid mapping, Pekarsky et al. (1998) mapped the human
NIT1 gene to 1q21-q22. They mapped the mouse Nit1 gene to distal
chromosome 1, between the D1Mit35 and D1Mit209 markers. This region of
mouse chromosome 1 shares homology of synteny with human 1q.
*FIELD* RF
1. Pekarsky, Y.; Campiglio, M.; Siprashvili, Z.; Druck, T.; Sedkov,
Y.; Tillib, S.; Draganescu, A.; Wermuth, P.; Rothman, J. H.; Huebner,
K.; Buchberg, A. M.; Mazo, A.; Brenner, C.; Croce, C. M.: Nitrilase
and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster
and Caenorhabditis elegans. Proc. Nat. Acad. Sci. 95: 8744-8749,
1998.
*FIELD* CD
Patti M. Sherman: 2/25/2000
*FIELD* ED
mgross: 02/28/2000
psherman: 2/28/2000
*RECORD*
*FIELD* NO
604618
*FIELD* TI
*604618 NITRILASE 1; NIT1
*FIELD* TX
Bacterial and plant nitrilases are enzymes that cleave nitriles and
read moreorganic amides to the corresponding carboxylic acids plus ammonia. By
searching an EST database with the sequence of the nitrilase domain of
the Drosophila NitFhit protein, Pekarsky et al. (1998) identified human
ESTs encoding nitrilase-1 (NIT1). They found that the NIT1 gene is
expressed as alternatively spliced transcripts. The major NIT1
transcript encodes a deduced 327-amino acid protein that shares 90%
amino acid sequence identity with mouse Nit1, 58% identity with the
nitrilase domain of C. elegans NitFhit, and 53% identity with the
nitrilase domain of Drosophila NitFhit. The NIT1 gene spans
approximately 3.2 kb and contains 7 exons. Northern blot analysis
detected NIT1 transcripts of approximately 1.4 and 2.4 kb in all adult
tissues examined, namely heart, brain, lung, liver, pancreas, kidney,
skeletal muscle, and placenta. An approximately 1.2-kb NIT1 transcript
was found in skeletal muscle and heart.
By radiation hybrid mapping, Pekarsky et al. (1998) mapped the human
NIT1 gene to 1q21-q22. They mapped the mouse Nit1 gene to distal
chromosome 1, between the D1Mit35 and D1Mit209 markers. This region of
mouse chromosome 1 shares homology of synteny with human 1q.
*FIELD* RF
1. Pekarsky, Y.; Campiglio, M.; Siprashvili, Z.; Druck, T.; Sedkov,
Y.; Tillib, S.; Draganescu, A.; Wermuth, P.; Rothman, J. H.; Huebner,
K.; Buchberg, A. M.; Mazo, A.; Brenner, C.; Croce, C. M.: Nitrilase
and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster
and Caenorhabditis elegans. Proc. Nat. Acad. Sci. 95: 8744-8749,
1998.
*FIELD* CD
Patti M. Sherman: 2/25/2000
*FIELD* ED
mgross: 02/28/2000
psherman: 2/28/2000