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Protein

Cytosolic purine 5'-nucleotidase

Gene

NT5C2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Enzyme regulationi

Allosterically activated by various compounds, including ATP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521Nucleophile
Metal bindingi52 – 521Magnesium
Active sitei54 – 541Proton donor
Metal bindingi54 – 541Magnesium; via carbonyl oxygen
Binding sitei127 – 1271Allosteric activator 1
Binding sitei154 – 1541Allosteric activator 2
Metal bindingi351 – 3511Magnesium
Binding sitei354 – 3541Allosteric activator 2
Binding sitei436 – 4361Allosteric activator 1; via carbonyl oxygen
Binding sitei453 – 4531Allosteric activator 2

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: Reactome
  2. metal ion binding Source: UniProtKB-KW
  3. nucleoside phosphotransferase activity Source: Reactome
  4. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. adenosine metabolic process Source: GO_Central
  2. dephosphorylation Source: GOC
  3. drug metabolic process Source: Reactome
  4. IMP metabolic process Source: GO_Central
  5. nucleobase-containing small molecule metabolic process Source: Reactome
  6. phosphorylation Source: GOC
  7. purine nucleobase metabolic process Source: Reactome
  8. purine nucleotide catabolic process Source: Reactome
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01216-MONOMER.
BRENDAi3.1.3.5. 2681.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_2086. Purine catabolism.
SABIO-RKP49902.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosolic purine 5'-nucleotidase (EC:3.1.3.5)
Alternative name(s):
Cytosolic 5'-nucleotidase II
Gene namesi
Name:NT5C2
Synonyms:NT5B, NT5CP, PNT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:8022. NT5C2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 45, autosomal recessive (SPG45)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Some SPG45 patients manifest mental retardation, contractures and learning disability.

See also OMIM:613162

Keywords - Diseasei

Hereditary spastic paraplegia, Neurodegeneration

Organism-specific databases

MIMi613162. phenotype.
Orphaneti320396. Autosomal recessive spastic paraplegia type 45.
PharmGKBiPA31801.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Cytosolic purine 5'-nucleotidasePRO_0000064389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei502 – 5021Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP49902.
PaxDbiP49902.
PeptideAtlasiP49902.
PRIDEiP49902.

PTM databases

DEPODiP49902.
PhosphoSiteiP49902.

Expressioni

Gene expression databases

BgeeiP49902.
CleanExiHS_NT5C2.
ExpressionAtlasiP49902. baseline and differential.
GenevestigatoriP49902.

Organism-specific databases

HPAiHPA003751.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FXR2P511163EBI-742084,EBI-740459
MOB3BQ86TA13EBI-742084,EBI-751703
NUDT18Q6ZVK83EBI-742084,EBI-740486

Protein-protein interaction databases

BioGridi116627. 25 interactions.
IntActiP49902. 7 interactions.
MINTiMINT-1436872.
STRINGi9606.ENSP00000339479.

Structurei

Secondary structure

1
561
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Helixi21 – 288Combined sources
Helixi31 – 333Combined sources
Beta strandi36 – 394Combined sources
Helixi43 – 453Combined sources
Beta strandi48 – 514Combined sources
Turni55 – 573Combined sources
Beta strandi58 – 603Combined sources
Helixi64 – 7916Combined sources
Helixi84 – 885Combined sources
Beta strandi101 – 1033Combined sources
Turni104 – 1074Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi117 – 1237Combined sources
Beta strandi126 – 1283Combined sources
Helixi130 – 1367Combined sources
Turni147 – 1493Combined sources
Beta strandi150 – 1523Combined sources
Helixi156 – 1583Combined sources
Helixi159 – 17416Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi190 – 1934Combined sources
Helixi194 – 21017Combined sources
Helixi214 – 2207Combined sources
Helixi222 – 2254Combined sources
Helixi231 – 24212Combined sources
Beta strandi243 – 2486Combined sources
Helixi253 – 26311Combined sources
Beta strandi266 – 2716Combined sources
Helixi279 – 2824Combined sources
Beta strandi284 – 2896Combined sources
Helixi294 – 2963Combined sources
Beta strandi302 – 3065Combined sources
Turni307 – 3104Combined sources
Beta strandi327 – 3293Combined sources
Helixi332 – 3398Combined sources
Helixi343 – 3453Combined sources
Beta strandi346 – 3516Combined sources
Helixi353 – 3575Combined sources
Helixi358 – 3647Combined sources
Beta strandi367 – 3715Combined sources
Helixi375 – 38410Combined sources
Helixi386 – 39813Combined sources
Helixi421 – 43212Combined sources
Beta strandi440 – 4434Combined sources
Helixi449 – 4579Combined sources
Beta strandi459 – 4635Combined sources
Helixi465 – 4706Combined sources
Helixi485 – 4873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J2CX-ray2.20A1-536[»]
2JC9X-ray1.50A1-536[»]
2JCMX-ray2.15A1-536[»]
2XCVX-ray2.30A1-536[»]
2XCWX-ray1.90A1-536[»]
2XCXX-ray2.30A1-536[»]
2XJBX-ray2.30A1-536[»]
2XJCX-ray2.00A1-536[»]
2XJDX-ray2.00A1-536[»]
2XJEX-ray2.30A1-536[»]
2XJFX-ray2.10A1-536[»]
4H4BX-ray2.90A1-536[»]
ProteinModelPortaliP49902.
SMRiP49902. Positions 3-488.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49902.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni202 – 2109Substrate bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi549 – 56113Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG75103.
GeneTreeiENSGT00550000074539.
HOGENOMiHOG000246075.
HOVERGENiHBG000025.
KOiK01081.
OMAiVEHIHVD.
OrthoDBiEOG7QK0BX.
PhylomeDBiP49902.
TreeFamiTF315266.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
InterProiIPR023214. HAD-like_dom.
IPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]
PANTHERiPTHR12103. PTHR12103. 1 hit.
PfamiPF05761. 5_nucleotid. 1 hit.
[Graphical view]
PIRSFiPIRSF017434. Purine_5'-nucleotidase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02244. HAD-IG-Ncltidse. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49902-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG
60 70 80 90 100
FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL
110 120 130 140 150
VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF
160 170 180 190 200
YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD
210 220 230 240 250
VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN
260 270 280 290 300
SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT
310 320 330 340 350
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG
360 370 380 390 400
DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA
410 420 430 440 450
ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF
460 470 480 490 500
ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM
510 520 530 540 550
ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE
560
DDDEEEEEEE E
Length:561
Mass (Da):64,970
Last modified:October 1, 1996 - v1
Checksum:i4C27D762575E0EA2
GO
Isoform 2 (identifier: P49902-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MSTSWSDRLQNAADMPANMDKHALKKYRREAYHR → MSKEG

Note: No experimental confirmation available.

Show »
Length:532
Mass (Da):61,441
Checksum:iE0DA487A03BC5F7E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31T → A.1 Publication
Corresponds to variant rs10883841 [ dbSNP | Ensembl ].
VAR_024244
Natural varianti136 – 1361Q → R.
Corresponds to variant rs12262171 [ dbSNP | Ensembl ].
VAR_030242

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434MSTSW…EAYHR → MSKEG in isoform 2. 1 PublicationVSP_054235Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38524 mRNA. Translation: BAA07529.1.
AK295593 mRNA. Translation: BAH12118.1.
AL139817, AL360001 Genomic DNA. Translation: CAI40080.1.
AL360001, AL139817 Genomic DNA. Translation: CAI13473.1.
CH471066 Genomic DNA. Translation: EAW49656.1.
CH471066 Genomic DNA. Translation: EAW49657.1.
BC001595 mRNA. Translation: AAH01595.1.
CCDSiCCDS7544.1. [P49902-1]
PIRiJC2436.
RefSeqiNP_001127845.1. NM_001134373.2. [P49902-1]
NP_036361.1. NM_012229.4. [P49902-1]
XP_005269693.1. XM_005269636.2. [P49902-1]
XP_005269696.1. XM_005269639.2. [P49902-2]
UniGeneiHs.97439.

Genome annotation databases

EnsembliENST00000343289; ENSP00000339479; ENSG00000076685. [P49902-1]
ENST00000404739; ENSP00000383960; ENSG00000076685. [P49902-1]
GeneIDi22978.
KEGGihsa:22978.
UCSCiuc001kwo.3. human. [P49902-1]
uc010qqp.2. human.

Polymorphism databases

DMDMi1703012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38524 mRNA. Translation: BAA07529.1.
AK295593 mRNA. Translation: BAH12118.1.
AL139817, AL360001 Genomic DNA. Translation: CAI40080.1.
AL360001, AL139817 Genomic DNA. Translation: CAI13473.1.
CH471066 Genomic DNA. Translation: EAW49656.1.
CH471066 Genomic DNA. Translation: EAW49657.1.
BC001595 mRNA. Translation: AAH01595.1.
CCDSiCCDS7544.1. [P49902-1]
PIRiJC2436.
RefSeqiNP_001127845.1. NM_001134373.2. [P49902-1]
NP_036361.1. NM_012229.4. [P49902-1]
XP_005269693.1. XM_005269636.2. [P49902-1]
XP_005269696.1. XM_005269639.2. [P49902-2]
UniGeneiHs.97439.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J2CX-ray2.20A1-536[»]
2JC9X-ray1.50A1-536[»]
2JCMX-ray2.15A1-536[»]
2XCVX-ray2.30A1-536[»]
2XCWX-ray1.90A1-536[»]
2XCXX-ray2.30A1-536[»]
2XJBX-ray2.30A1-536[»]
2XJCX-ray2.00A1-536[»]
2XJDX-ray2.00A1-536[»]
2XJEX-ray2.30A1-536[»]
2XJFX-ray2.10A1-536[»]
4H4BX-ray2.90A1-536[»]
ProteinModelPortaliP49902.
SMRiP49902. Positions 3-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116627. 25 interactions.
IntActiP49902. 7 interactions.
MINTiMINT-1436872.
STRINGi9606.ENSP00000339479.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.
DB00811. Ribavirin.

PTM databases

DEPODiP49902.
PhosphoSiteiP49902.

Polymorphism databases

DMDMi1703012.

Proteomic databases

MaxQBiP49902.
PaxDbiP49902.
PeptideAtlasiP49902.
PRIDEiP49902.

Protocols and materials databases

DNASUi22978.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343289; ENSP00000339479; ENSG00000076685. [P49902-1]
ENST00000404739; ENSP00000383960; ENSG00000076685. [P49902-1]
GeneIDi22978.
KEGGihsa:22978.
UCSCiuc001kwo.3. human. [P49902-1]
uc010qqp.2. human.

Organism-specific databases

CTDi22978.
GeneCardsiGC10M104837.
HGNCiHGNC:8022. NT5C2.
HPAiHPA003751.
MIMi600417. gene.
613162. phenotype.
neXtProtiNX_P49902.
Orphaneti320396. Autosomal recessive spastic paraplegia type 45.
PharmGKBiPA31801.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG75103.
GeneTreeiENSGT00550000074539.
HOGENOMiHOG000246075.
HOVERGENiHBG000025.
KOiK01081.
OMAiVEHIHVD.
OrthoDBiEOG7QK0BX.
PhylomeDBiP49902.
TreeFamiTF315266.

Enzyme and pathway databases

BioCyciMetaCyc:HS01216-MONOMER.
BRENDAi3.1.3.5. 2681.
ReactomeiREACT_121388. Abacavir metabolism.
REACT_2086. Purine catabolism.
SABIO-RKP49902.

Miscellaneous databases

ChiTaRSiNT5C2. human.
EvolutionaryTraceiP49902.
GenomeRNAii22978.
NextBioi35479172.
PROiP49902.
SOURCEiSearch...

Gene expression databases

BgeeiP49902.
CleanExiHS_NT5C2.
ExpressionAtlasiP49902. baseline and differential.
GenevestigatoriP49902.

Family and domain databases

Gene3Di3.40.50.1000. 3 hits.
InterProiIPR023214. HAD-like_dom.
IPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view]
PANTHERiPTHR12103. PTHR12103. 1 hit.
PfamiPF05761. 5_nucleotid. 1 hit.
[Graphical view]
PIRSFiPIRSF017434. Purine_5'-nucleotidase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of human cytosolic purine 5'-nucleotidase."
    Oka J., Matsumoto A., Hosokawa Y., Inoue S.
    Biochem. Biophys. Res. Commun. 205:917-922(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hippocampus.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-3.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: INVOLVEMENT IN SPG45.
  9. "Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition."
    Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S., Loppnau P., Bianchi V., Nordlund P.
    J. Biol. Chem. 282:17828-17836(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-536 IN COMPLEX WITH ALLOSTERIC EFFECTOR AND MAGNESIUM IONS, SUBUNIT.

Entry informationi

Entry namei5NTC_HUMAN
AccessioniPrimary (citable) accession number: P49902
Secondary accession number(s): B7Z382, D3DR91, Q5JUV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.