NIFK

Protein sy'n cael ei godio yn y corff dynol gan y genyn NIFK yw NIFK a elwir hefyd yn Nucleolar protein interacting with the FHA domain of MKI67 (Saesneg). Segment o DNA yw'r genyn, sy'n amgodio ffwythiant arbennig. Mae'r genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 2, band 2q14.3.

NIFK
Strwythurau PDB Human UniProt search: PDBe RCSB Rhestr o ddynodwyr PDB 2AFF
Dynodwyr
Cyfenwau	NIFK, MKI67IP, Nopp34, nucleolar protein interacting with the FHA domain of MKI67
Dynodwyr allanol	OMIM: 611970 HomoloGene: 49862 GeneCards: NIFK
Patrwm RNA pattern Rhagor o gyfeiriadau
Ontoleg y genyn Gweithrediad moleciwlaidd • GO:0001948, GO:0016582 protein binding • RNA binding • nucleic acid binding Cydrannau o'r gell • cytoplasm • condensed nuclear chromosome • Cromosom • nucleolus • cnewyllyn cell • nucleoplasm Prosesau biolegol • negative regulation of phosphatase activity • rRNA transcription • rRNA metabolic process • GO:0034622 protein-containing complex assembly Sources:Amigo / QuickGO
Orthologau
Species	Bod dynol	Llygoden
Entrez	84365	n/a
Ensembl	ENSG00000155438	n/a
UniProt	Q9BYG3	n/a
RefSeq (mRNA)	NM_032390	n/a
RefSeq (protein)	NP_115766	n/a
Lleoliad (UCSC)	n/a	n/a
PubMed search		n/a
Wicidata
Gweld/Golygu Bod dynol

Cyfystyron

Yn aml mae gan enynnau lawer o gyfystyron. Mae hyn oherwydd eu bod yn aml yn cael eu darganfod gan nifer o bobl mewn cyd-destunau gwahanol heb wybod mai'r un genynnau oeddyn nhw. Hefyd mae gan wahanol gymunedau gwyddonol safonau gwahanol ar gyfer enwi genynnau. Dyma restr o gyfystyron ar gyfer y genyn NIFK.

• Nopp34
• MKI67IP

Llyfryddiaeth

• "Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions. ". J Mol Biol. 2004. PMID 14659764.
• "The nucleolar protein NIFK promotes cancer progression via CK1α/β-catenin in metastasis and Ki-67-dependent cell proliferation. ". Elife. 2016. PMID 26984280.
• "The RNA recognition motif of NIFK is required for rRNA maturation during cell cycle progression. ". RNA Biol. 2015. PMID 25826659.
• "Direct observations of shifts in the β-sheet register of a protein-peptide complex using explicit solvent simulations. ". Biophys J. 2011. PMID 21539773.
• "Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.". Nat Struct Mol Biol. 2005. PMID 16244663.