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Q86X76 (NIT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrilase homolog 1

EC=3.5.-.-
Gene names
Name:NIT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in cell growth and apoptosis: loss of expression promotes cell growth and resistance to DNA damage stress. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. Has apparently no omega-amidase activity such as NIT2 By similarity.

Subcellular location

Cytoplasm. Mitochondrion By similarity.

Tissue specificity

Detected in heart, brain, placenta, liver, skeletal muscle, kidney and pancreas. Ref.1

Miscellaneous

According to Rosetta Stone theory, the existence of a fusion protein in one genome predicts that the separate polypeptides expressed in other organisms function in the same cellular or biochemical pathway. In Drosophila melanogaster and Caenorhabditis elegans, NitFhit is a fusion protein composed of a C-terminal Fhit domain and a domain related to plant and bacterial nitrilase.

Sequence similarities

Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.

Contains 1 CN hydrolase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionnitrilase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q86X76-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.
Isoform 1 (identifier: Q86X76-2)

Also known as: 3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.
Isoform 4 (identifier: Q86X76-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQ → MVLAISSCWA...PGRTYSLSRR
     327-327: S → SDLTSVSLDLPLPPPPCHYELVLM
Isoform 5 (identifier: Q86X76-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MLGFITRPPHRFLSLLCPGLRIPQLSVLCAQPR → MTFGLRKRLSEERGFSLM
Isoform 6 (identifier: Q86X76-5)

The sequence of this isoform differs from the canonical sequence as follows:
     240-243: VLLR → PVSS
     244-327: Missing.
Note: Based on a naturally occurring readthrough transcript which produces a NIT1-DEDD fusion protein. The last 4 amino acids of this isoform (PVSS) are encoded by the last DEDD exon. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 327327Nitrilase homolog 1
PRO_0000213251

Regions

Domain47 – 320274CN hydrolase

Sites

Active site861Proton acceptor By similarity
Active site1611Proton donor By similarity
Active site2031Nucleophile By similarity

Natural variations

Alternative sequence1 – 3636Missing in isoform 1.
VSP_011546
Alternative sequence1 – 3333MLGFI…CAQPR → MTFGLRKRLSEERGFSLM in isoform 5.
VSP_011545
Alternative sequence1 – 3131MLGFI…VLCAQ → MVLAISSCWASSPGLLTDSC PFCVLDSGYLNSQYFVLSPG RTYSLSRR in isoform 4.
VSP_011544
Alternative sequence240 – 2434VLLR → PVSS in isoform 6.
VSP_053711
Alternative sequence244 – 32784Missing in isoform 6.
VSP_053712
Alternative sequence3271S → SDLTSVSLDLPLPPPPCHYE LVLM in isoform 4.
VSP_011547

Experimental info

Sequence conflict791A → P in AAH46149. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 90F7FB9D4BA627B1

FASTA32735,896
        10         20         30         40         50         60 
MLGFITRPPH RFLSLLCPGL RIPQLSVLCA QPRPRAMAIS SSSCELPLVA VCQVTSTPDK 

        70         80         90        100        110        120 
QQNFKTCAEL VREAARLGAC LAFLPEAFDF IARDPAETLH LSEPLGGKLL EEYTQLAREC 

       130        140        150        160        170        180 
GLWLSLGGFH ERGQDWEQTQ KIYNCHVLLN SKGAVVATYR KTHLCDVEIP GQGPMCESNS 

       190        200        210        220        230        240 
TMPGPSLESP VSTPAGKIGL AVCYDMRFPE LSLALAQAGA EILTYPSAFG SITGPAHWEV 

       250        260        270        280        290        300 
LLRARAIETQ CYVVAAAQCG RHHEKRASYG HSMVVDPWGT VVARCSEGPG LCLARIDLNY 

       310        320 
LRQLRRHLPV FQHRRPDLYG NLGHPLS 

« Hide

Isoform 1 (3) [UniParc].

Checksum: 314677E205F7ADDE
Show »

FASTA29131,859
Isoform 4 [UniParc].

Checksum: 178F0C4BBFE65D25
Show »

FASTA36740,200
Isoform 5 [UniParc].

Checksum: A0BFFE4B76D24EE0
Show »

FASTA31234,323
Isoform 6 [UniParc].

Checksum: 283B9E8D6A4EF67D
Show »

FASTA24326,326

References

« Hide 'large scale' references
[1]"Nitrilase and Fhit homologs are encoded as fusion proteins in Drosophila melanogaster and Caenorhabditis elegans."
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.
Proc. Natl. Acad. Sci. U.S.A. 95:8744-8749(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 4 AND 5), TISSUE SPECIFICITY.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Brain.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069984 Genomic DNA. Translation: AAC39901.1.
AF069987 mRNA. Translation: AAC39907.1.
CR541814 mRNA. Translation: CAG46613.1.
CR541846 mRNA. Translation: CAG46644.1.
AL591806 Genomic DNA. Translation: CAI15379.1.
CH471121 Genomic DNA. Translation: EAW52656.1.
CH471121 Genomic DNA. Translation: EAW52654.1.
CH471121 Genomic DNA. Translation: EAW52657.1.
BC046149 mRNA. Translation: AAH46149.1.
CCDSCCDS1218.1. [Q86X76-1]
CCDS53402.1. [Q86X76-4]
CCDS53403.1. [Q86X76-2]
RefSeqNP_001172021.1. NM_001185092.1. [Q86X76-5]
NP_001172022.1. NM_001185093.1. [Q86X76-4]
NP_001172023.1. NM_001185094.1. [Q86X76-2]
NP_005591.1. NM_005600.2. [Q86X76-1]
XP_005245273.1. XM_005245216.2. [Q86X76-2]
UniGeneHs.146406.

3D structure databases

ProteinModelPortalQ86X76.
SMRQ86X76. Positions 48-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110882. 4 interactions.
IntActQ86X76. 2 interactions.
MINTMINT-1194030.
STRING9606.ENSP00000356988.

PTM databases

PhosphoSiteQ86X76.

Polymorphism databases

DMDM51704324.

Proteomic databases

MaxQBQ86X76.
PaxDbQ86X76.
PRIDEQ86X76.

Protocols and materials databases

DNASU4817.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368007; ENSP00000356986; ENSG00000158793. [Q86X76-4]
ENST00000368008; ENSP00000356987; ENSG00000158793. [Q86X76-5]
ENST00000368009; ENSP00000356988; ENSG00000158793. [Q86X76-1]
ENST00000392190; ENSP00000376028; ENSG00000158793. [Q86X76-2]
GeneID4817.
KEGGhsa:4817.
UCSCuc001fxv.2. human. [Q86X76-1]
uc010pka.2. human. [Q86X76-4]

Organism-specific databases

CTD4817.
GeneCardsGC01P161087.
HGNCHGNC:7828. NIT1.
HPAHPA006657.
MIM604618. gene.
neXtProtNX_Q86X76.
PharmGKBPA31636.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0388.
HOGENOMHOG000222700.
HOVERGENHBG052628.
InParanoidQ86X76.
KOK01506.
OMASTPDKEQ.
OrthoDBEOG7XDBGD.
PhylomeDBQ86X76.
TreeFamTF313080.

Enzyme and pathway databases

BRENDA3.5.5.1. 2681.

Gene expression databases

ArrayExpressQ86X76.
BgeeQ86X76.
CleanExHS_NIT1.
GenevestigatorQ86X76.

Family and domain databases

Gene3D3.60.110.10. 1 hit.
InterProIPR003010. C-N_Hydrolase.
IPR001110. UPF0012_CS.
[Graphical view]
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMSSF56317. SSF56317. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
PS01227. UPF0012. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi4817.
NextBio18562.
PROQ86X76.
SOURCESearch...

Entry information

Entry nameNIT1_HUMAN
AccessionPrimary (citable) accession number: Q86X76
Secondary accession number(s): B1AQP3, D3DVF4, O76091
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM