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Protein
Submitted name:

5'-nucleotidase, cytosolic IB

Gene

Nt5c1b

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • 5'-nucleotidase activity Source: RGD
  • magnesium ion binding Source: InterPro
  • nucleotide binding Source: InterPro

GO - Biological processi

  • adenosine metabolic process Source: RGD
  • dephosphorylation Source: GOC
  • nucleotide metabolic process Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-74259. Purine catabolism.

Names & Taxonomyi

Protein namesi
Submitted name:
5'-nucleotidase, cytosolic IBImported
Gene namesi
Name:Nt5c1bImported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Organism-specific databases

RGDi1309705. Nt5c1b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

PTM databases

iPTMnetiQ6AXN7.

Expressioni

Gene expression databases

ExpressionAtlasiQ6AXN7. baseline.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005731.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IE01. Eukaryota.
ENOG410XPRD. LUCA.
HOGENOMiHOG000243802.
HOVERGENiHBG050426.
KOiK01081.
OMAiPKPKHAI.
OrthoDBiEOG79KPF1.
PhylomeDBiQ6AXN7.

Family and domain databases

InterProiIPR010394. 5-nucleotidase.
[Graphical view]
PfamiPF06189. 5-nucleotidase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6AXN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTSLKTKK KNEPGMRYSK ESLDAEKRKD SDKSGARLST QGSQEIPVPN
60 70 80 90 100
TDSRGYVVRN QWSRTSRSPS TRAPSVDENR SRNTVVKQAP NSSANSRTSS
110 120 130 140 150
ASASQHETST SPPPQVSEKS PVQQPSPQTR TITPLDSQPP TPPETEPDSR
160 170 180 190 200
RTSKMYTATD PWAHRDNREP RDLQLREYAH SCDSREGIPK TREYPRTPPT
210 220 230 240 250
EWKSYVQRRL QYGSSVDMDP DCLPDGQHHR QKQQIEEDEV DEAYWSSVSM
260 270 280 290 300
LYEKIPSCTR PRPPKPKHAI TIAVSSRALF NMVDDRKIYE EEGLEKYMEY
310 320 330 340 350
QLTNENVILT PGPAFRFVKA LQHVNSRLRD LYPDEQDLFD IVLMTNNHAQ
360 370 380 390 400
VGVRLINSVN HYGLLIDRFC LTGGKSPIGY LKAYLTNLYL SADSEKVQEA
410 420 430 440 450
IKEGIASATM FAGAKDMAYC DTQLRVAFDG DAVLFSDESE HIAKDHGLDK
460 470 480 490 500
FFQHETLFEN KPLAQGPLKG FLEDLGKLQK KFYAKDERLL CPIRTYLVTA
510 520 530 540 550
RSAASSGARV LKTLRRWGLE IDEALFLAGA PKGPILVKIR PHIFFDDQMF
560 570
HIEAAQKFGT ITAHVPYGIA QKRN
Length:574
Mass (Da):64,923
Last modified:September 13, 2004 - v1
Checksum:iEF04D0530DC281E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079437 mRNA. Translation: AAH79437.1.
RefSeqiNP_001011982.1. NM_001011982.1.
UniGeneiRn.137540.

Genome annotation databases

GeneIDi298881.
KEGGirno:298881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079437 mRNA. Translation: AAH79437.1.
RefSeqiNP_001011982.1. NM_001011982.1.
UniGeneiRn.137540.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005731.

PTM databases

iPTMnetiQ6AXN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi298881.
KEGGirno:298881.

Organism-specific databases

CTDi93034.
RGDi1309705. Nt5c1b.

Phylogenomic databases

eggNOGiENOG410IE01. Eukaryota.
ENOG410XPRD. LUCA.
HOGENOMiHOG000243802.
HOVERGENiHBG050426.
KOiK01081.
OMAiPKPKHAI.
OrthoDBiEOG79KPF1.
PhylomeDBiQ6AXN7.

Enzyme and pathway databases

ReactomeiR-RNO-74259. Purine catabolism.

Gene expression databases

ExpressionAtlasiQ6AXN7. baseline.

Family and domain databases

InterProiIPR010394. 5-nucleotidase.
[Graphical view]
PfamiPF06189. 5-nucleotidase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: TestisImported.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiQ6AXN7_RAT
AccessioniPrimary (citable) accession number: Q6AXN7
Secondary accession number(s): F1MAT2
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 one 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.