Q9UHK0 (NUFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear fragile X mental retardation-interacting protein 1

Alternative name(s):
Nuclear FMRP-interacting protein 1

Gene names

Name:

NUFIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds RNA. Ref.1
Subunit structure	Interacts with FMR1. Ref.1
Subcellular location	Nucleus. Note: Distributed in the nucleus in a dot-like pattern. Ref.1
Tissue specificity	Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. Ref.1
Sequence similarities	Contains 1 C2H2-type zinc finger.
Sequence caution	The sequence AAH17745.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA processing Traceable author statement Ref.1. Source: ProtInc box C/D snoRNP assembly Inferred from mutant phenotype PubMed 17636026. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 15107825. Source: HGNC
Cellular_component	cytosolic ribosome Inferred from direct assay PubMed 12941608. Source: HGNC nuclear matrix Inferred from direct assay PubMed 12941608. Source: HGNC nucleolus Inferred from direct assay PubMed 12941608. Source: HGNC perichromatin fibrils Inferred from direct assay PubMed 12941608. Source: HGNC pre-snoRNP complex Inferred from direct assay PubMed 17636026. Source: BHF-UCL presynaptic active zone Inferred from direct assay PubMed 12941608. Source: HGNC transcription elongation factor complex Inferred from direct assay PubMed 15107825. Source: HGNC
Molecular_function	DNA binding Non-traceable author statement PubMed 15107825. Source: UniProtKB RNA binding Inferred from direct assay Ref.1. Source: HGNC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	Nuclear fragile X mental retardation-interacting protein 1		PRO_0000245518
Regions
	Zinc finger	174 – 196	23	C2H2-type
	Motif	243 – 260	18	Bipartite nuclear localization signal
	Compositional bias	18 – 109	92	Pro-rich
Amino acid modifications
	Modified residue	338	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7
	Modified residue	340	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7
	Modified residue	342	1	Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7
Natural variations
	Natural variant	36	1	S → R. Ref.1 Corresponds to variant rs1140993 [ dbSNP | Ensembl ].		VAR_026978

Sequences

	Sequence		Length	Mass (Da)
	Q9UHK0 [UniParc]. Last modified March 20, 2007. Version 2. Checksum: 318418FB08071001	FASTA	495	56,300
	10 20 30 40 50 60 MAEPTSDFET PIGWHASPEL TPTLGPLSDT APPRDSWMFW AMLPPPPPPL TSSLPAAGSK 70 80 90 100 110 120 PSSESQPPME AQSLPGAPPP FDAQILPGAQ PPFDAQSPLD SQPQPSGQPW NFHASTSWYW 130 140 150 160 170 180 RQSSDRFPRH QKSFNPAVKN SYYPRKYDAK FTDFSLPPSR KQKKKKRKEP VFHFFCDTCD 190 200 210 220 230 240 RGFKNQEKYD KHMSEHTKCP ELDCSFTAHE KIVQFHWRNM HAPGMKKIKL DTPEEIARWR 250 260 270 280 290 300 EERRKNYPTL ANIERKKKLK LEKEKRGAVL TTTQYGKMKG MSRHSQMAKI RSPGKNHKWK 310 320 330 340 350 360 NDNSRQRAVT GSGSHLCDLK LEGPPEANAD PLGVLINSDS ESDKEEKPQH SVIPKEVTPA 370 380 390 400 410 420 LCSLMSSYGS LSGSESEPEE TPIKTEADVL AENQVLDSSA PKSPSQDVKA TVRNFSEAKS 430 440 450 460 470 480 ENRKKSFEKT NPKRKKDYHN YQTLFEPRTH HPYLLEMLLA PDIRHERNVI LQCVRYIIKK 490 DFFGLDTNSA KSKDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel RNA-binding nuclear protein that interacts with the fragile X mental retardation (FMR1) protein." Bardoni B., Schenck A., Mandel J.-L. Hum. Mol. Genet. 8:2557-2566(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-36, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FMR1.
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] OF 163-495. Tissue: Duodenum.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF159548 mRNA. Translation: AAF15315.1. AL354816, AL359706 Genomic DNA. Translation: CAC40689.2. AL359706, AL354816 Genomic DNA. Translation: CAI12865.1. BC017745 mRNA. Translation: AAH17745.1. Different initiation.
IPI	IPI00017630.
RefSeq	NP_036477.2. NM_012345.2.
UniGene	Hs.525006.
3D structure databases
ProteinModelPortal	Q9UHK0.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41010N.
IntAct	Q9UHK0. 1 interaction.
MINT	MINT-110099.
STRING	9606.ENSP00000368459.
Polymorphism databases
DMDM	134047852.
Proteomic databases
PaxDb	Q9UHK0.
PRIDE	Q9UHK0.
Protocols and materials databases
DNASU	26747.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379161; ENSP00000368459; ENSG00000083635.
GeneID	26747.
KEGG	hsa:26747.
UCSC	uc001uzp.2. human.
Organism-specific databases
CTD	26747.
GeneCards	GC13M045513.
H-InvDB	HIX0011282.
HGNC	HGNC:8057. NUFIP1.
HPA	HPA029958. HPA029959. HPA029960.
MIM	604354. gene.
neXtProt	NX_Q9UHK0.
PharmGKB	PA31843.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG73405.
HOGENOM	HOG000113888.
HOVERGEN	HBG059841.
InParanoid	Q9UHK0.
OMA	MAKIRSP.
OrthoDB	EOG412M64.
PhylomeDB	Q9UHK0.
Gene expression databases
Bgee	Q9UHK0.
CleanEx	HS_NUFIP1.
Genevestigator	Q9UHK0.
GermOnline	ENSG00000083635. Homo sapiens.
Family and domain databases
InterPro	IPR019496. NUFIP1_cons_dom. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR022755. Znf_C2H2_jaz. [Graphical view]
Pfam	PF10453. NUFIP1. 1 hit. PF12171. zf-C2H2_jaz. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 2 hits. [Graphical view]
PROSITE	PS00028. ZINC_FINGER_C2H2_1. 1 hit. PS50157. ZINC_FINGER_C2H2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	26747.
NextBio	49103.
SOURCE	Search...

Entry information

Entry name

NUFP1_HUMAN

Accession

Primary (citable) accession number: Q9UHK0
Secondary accession number(s): Q8WVM5, Q96SG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	March 20, 2007
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.