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P49902

- 5NTC_HUMAN

UniProt

P49902 - 5NTC_HUMAN

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Protein

Cytosolic purine 5'-nucleotidase

Gene
NT5C2, NT5B, NT5CP, PNT5
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 magnesium 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
  5. protein binding Source: IntAct

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. drug metabolic process Source: Reactome
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. phosphorylation Source: GOC
  5. purine nucleobase metabolic process Source: Reactome
  6. purine nucleotide catabolic process Source: Reactome
  7. 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: 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) [MIM:613162]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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

PhosphoSiteiP49902.

Expressioni

Gene expression databases

ArrayExpressiP49902.
BgeeiP49902.
CleanExiHS_NT5C2.
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. 20 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 – 139
Helixi21 – 288
Helixi31 – 333
Beta strandi36 – 394
Helixi43 – 453
Beta strandi48 – 514
Turni55 – 573
Beta strandi58 – 603
Helixi64 – 7916
Helixi84 – 885
Beta strandi101 – 1033
Turni104 – 1074
Beta strandi108 – 1125
Beta strandi117 – 1237
Beta strandi126 – 1283
Helixi130 – 1367
Turni147 – 1493
Beta strandi150 – 1523
Helixi156 – 1583
Helixi159 – 17416
Beta strandi178 – 1814
Beta strandi184 – 1874
Beta strandi190 – 1934
Helixi194 – 21017
Helixi214 – 2207
Helixi222 – 2254
Helixi231 – 24212
Beta strandi243 – 2486
Helixi253 – 26311
Beta strandi266 – 2716
Helixi279 – 2824
Beta strandi284 – 2896
Helixi294 – 2963
Beta strandi302 – 3065
Turni307 – 3104
Beta strandi327 – 3293
Helixi332 – 3398
Helixi343 – 3453
Beta strandi346 – 3516
Helixi353 – 3575
Helixi358 – 3647
Beta strandi367 – 3715
Helixi375 – 38410
Helixi386 – 39813
Helixi421 – 43212
Beta strandi440 – 4434
Helixi449 – 4579
Beta strandi459 – 4635
Helixi465 – 4706
Helixi485 – 4873

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP49902.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni202 – 2109Substrate binding Reviewed prediction

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG75103.
HOGENOMiHOG000246075.
HOVERGENiHBG000025.
InParanoidiP49902.
KOiK01081.
OMAiHLENIKF.
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. Align

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

MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG    50
FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL 100
VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF 150
YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD 200
VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN 250
SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT 300
VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG 350
DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA 400
ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF 450
ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM 500
ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE 550
DDDEEEEEEE E 561
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. VSP_054235Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000404739; ENSP00000383960; ENSG00000076685.
ENST00000423468; ENSP00000392236; ENSG00000076685.
GeneIDi22978.
KEGGihsa:22978.
UCSCiuc001kwo.3. human. [P49902-1]

Polymorphism databases

DMDMi1703012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7544.1. [P49902-1 ]
PIRi JC2436.
RefSeqi NP_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 ]
UniGenei Hs.97439.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2J2C X-ray 2.20 A 1-536 [» ]
2JC9 X-ray 1.50 A 1-536 [» ]
2JCM X-ray 2.15 A 1-536 [» ]
2XCV X-ray 2.30 A 1-536 [» ]
2XCW X-ray 1.90 A 1-536 [» ]
2XCX X-ray 2.30 A 1-536 [» ]
2XJB X-ray 2.30 A 1-536 [» ]
2XJC X-ray 2.00 A 1-536 [» ]
2XJD X-ray 2.00 A 1-536 [» ]
2XJE X-ray 2.30 A 1-536 [» ]
2XJF X-ray 2.10 A 1-536 [» ]
4H4B X-ray 2.90 A 1-536 [» ]
ProteinModelPortali P49902.
SMRi P49902. Positions 3-488.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116627. 20 interactions.
IntActi P49902. 7 interactions.
MINTi MINT-1436872.
STRINGi 9606.ENSP00000339479.

Chemistry

DrugBanki DB00171. Adenosine triphosphate.
DB00811. Ribavirin.

PTM databases

PhosphoSitei P49902.

Polymorphism databases

DMDMi 1703012.

Proteomic databases

MaxQBi P49902.
PaxDbi P49902.
PeptideAtlasi P49902.
PRIDEi P49902.

Protocols and materials databases

DNASUi 22978.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343289 ; ENSP00000339479 ; ENSG00000076685 .
ENST00000404739 ; ENSP00000383960 ; ENSG00000076685 .
ENST00000423468 ; ENSP00000392236 ; ENSG00000076685 .
GeneIDi 22978.
KEGGi hsa:22978.
UCSCi uc001kwo.3. human. [P49902-1 ]

Organism-specific databases

CTDi 22978.
GeneCardsi GC10M104837.
HGNCi HGNC:8022. NT5C2.
HPAi HPA003751.
MIMi 600417. gene.
613162. phenotype.
neXtProti NX_P49902.
Orphaneti 320396. Autosomal recessive spastic paraplegia type 45.
PharmGKBi PA31801.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG75103.
HOGENOMi HOG000246075.
HOVERGENi HBG000025.
InParanoidi P49902.
KOi K01081.
OMAi HLENIKF.
OrthoDBi EOG7QK0BX.
PhylomeDBi P49902.
TreeFami TF315266.

Enzyme and pathway databases

BioCyci MetaCyc:HS01216-MONOMER.
BRENDAi 3.1.3.5. 2681.
Reactomei REACT_121388. Abacavir metabolism.
REACT_2086. Purine catabolism.
SABIO-RK P49902.

Miscellaneous databases

EvolutionaryTracei P49902.
GenomeRNAii 22978.
NextBioi 35479172.
PROi P49902.
SOURCEi Search...

Gene expression databases

ArrayExpressi P49902.
Bgeei P49902.
CleanExi HS_NT5C2.
Genevestigatori P49902.

Family and domain databases

Gene3Di 3.40.50.1000. 3 hits.
InterProi IPR023214. HAD-like_dom.
IPR008380. HAD-SF_hydro_IG_5-nucl.
IPR016695. Pur_nucleotidase.
[Graphical view ]
PANTHERi PTHR12103. PTHR12103. 1 hit.
Pfami PF05761. 5_nucleotid. 1 hit.
[Graphical view ]
PIRSFi PIRSF017434. Purine_5'-nucleotidase. 1 hit.
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR02244. HAD-IG-Ncltidse. 1 hit.
ProtoNeti Search...

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(1994) [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(2004) [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(2004) [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(2004) [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(2007) [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: September 3, 2014
This is version 137 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

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