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Protein

Nuclear fragile X mental retardation-interacting protein 1

Gene

NUFIP1

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

Functioni

Binds RNA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri174 – 19623C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • identical protein binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein binding, bridging Source: BHF-UCL
  • RNA binding Source: HGNC

GO - Biological processi

  • box C/D snoRNP assembly Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: HGNC
  • RNA processing Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear fragile X mental retardation-interacting protein 1
Alternative name(s):
Nuclear FMRP-interacting protein 1
Gene namesi
Name:NUFIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:8057. NUFIP1.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Distributed in the nucleus in a dot-like pattern.

GO - Cellular componenti

  • cytosolic ribosome Source: HGNC
  • nuclear matrix Source: HGNC
  • nucleolus Source: HGNC
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • perichromatin fibrils Source: HGNC
  • pre-snoRNP complex Source: BHF-UCL
  • presynaptic active zone Source: HGNC
  • protein complex Source: BHF-UCL
  • transcription elongation factor complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31843.

Polymorphism and mutation databases

BioMutaiNUFIP1.
DMDMi134047852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Nuclear fragile X mental retardation-interacting protein 1PRO_0000245518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei338 – 3381Phosphoserine4 Publications
Modified residuei340 – 3401Phosphoserine4 Publications
Modified residuei342 – 3421Phosphoserine4 Publications
Modified residuei403 – 4031Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UHK0.
PaxDbiQ9UHK0.
PRIDEiQ9UHK0.

Expressioni

Tissue specificityi

Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas.1 Publication

Gene expression databases

BgeeiQ9UHK0.
CleanExiHS_NUFIP1.
GenevisibleiQ9UHK0. HS.

Organism-specific databases

HPAiHPA029958.
HPA029959.
HPA029960.

Interactioni

Subunit structurei

Interacts with FMR1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NHP2L1P557692EBI-2563549,EBI-712228
ZNHIT6Q9NWK92EBI-2563549,EBI-2563515

Protein-protein interaction databases

BioGridi117807. 92 interactions.
DIPiDIP-41010N.
IntActiQ9UHK0. 8 interactions.
MINTiMINT-110099.
STRINGi9606.ENSP00000368459.

Structurei

3D structure databases

ProteinModelPortaliQ9UHK0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi243 – 26018Bipartite nuclear localization signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 10992Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri174 – 19623C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG73405.
GeneTreeiENSGT00390000003758.
HOGENOMiHOG000113888.
HOVERGENiHBG059841.
InParanoidiQ9UHK0.
OMAiKEPVFHY.
OrthoDBiEOG77T15S.
PhylomeDBiQ9UHK0.
TreeFamiTF329804.

Family and domain databases

InterProiIPR019496. NUFIP1_cons_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR022755. Znf_C2H2_jaz.
[Graphical view]
PfamiPF10453. NUFIP1. 1 hit.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UHK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPTSDFET PIGWHASPEL TPTLGPLSDT APPRDSWMFW AMLPPPPPPL
60 70 80 90 100
TSSLPAAGSK PSSESQPPME AQSLPGAPPP FDAQILPGAQ PPFDAQSPLD
110 120 130 140 150
SQPQPSGQPW NFHASTSWYW RQSSDRFPRH QKSFNPAVKN SYYPRKYDAK
160 170 180 190 200
FTDFSLPPSR KQKKKKRKEP VFHFFCDTCD RGFKNQEKYD KHMSEHTKCP
210 220 230 240 250
ELDCSFTAHE KIVQFHWRNM HAPGMKKIKL DTPEEIARWR EERRKNYPTL
260 270 280 290 300
ANIERKKKLK LEKEKRGAVL TTTQYGKMKG MSRHSQMAKI RSPGKNHKWK
310 320 330 340 350
NDNSRQRAVT GSGSHLCDLK LEGPPEANAD PLGVLINSDS ESDKEEKPQH
360 370 380 390 400
SVIPKEVTPA LCSLMSSYGS LSGSESEPEE TPIKTEADVL AENQVLDSSA
410 420 430 440 450
PKSPSQDVKA TVRNFSEAKS ENRKKSFEKT NPKRKKDYHN YQTLFEPRTH
460 470 480 490
HPYLLEMLLA PDIRHERNVI LQCVRYIIKK DFFGLDTNSA KSKDV
Length:495
Mass (Da):56,300
Last modified:March 20, 2007 - v2
Checksum:i318418FB08071001
GO

Sequence cautioni

The sequence AAH17745.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361S → R.1 Publication
Corresponds to variant rs1140993 [ dbSNP | Ensembl ].
VAR_026978

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9393.1.
RefSeqiNP_036477.2. NM_012345.2.
UniGeneiHs.525006.

Genome annotation databases

EnsembliENST00000379161; ENSP00000368459; ENSG00000083635.
GeneIDi26747.
KEGGihsa:26747.
UCSCiuc001uzp.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9393.1.
RefSeqiNP_036477.2. NM_012345.2.
UniGeneiHs.525006.

3D structure databases

ProteinModelPortaliQ9UHK0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117807. 92 interactions.
DIPiDIP-41010N.
IntActiQ9UHK0. 8 interactions.
MINTiMINT-110099.
STRINGi9606.ENSP00000368459.

Polymorphism and mutation databases

BioMutaiNUFIP1.
DMDMi134047852.

Proteomic databases

MaxQBiQ9UHK0.
PaxDbiQ9UHK0.
PRIDEiQ9UHK0.

Protocols and materials databases

DNASUi26747.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379161; ENSP00000368459; ENSG00000083635.
GeneIDi26747.
KEGGihsa:26747.
UCSCiuc001uzp.2. human.

Organism-specific databases

CTDi26747.
GeneCardsiGC13M045513.
H-InvDBHIX0011282.
HGNCiHGNC:8057. NUFIP1.
HPAiHPA029958.
HPA029959.
HPA029960.
MIMi604354. gene.
neXtProtiNX_Q9UHK0.
PharmGKBiPA31843.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73405.
GeneTreeiENSGT00390000003758.
HOGENOMiHOG000113888.
HOVERGENiHBG059841.
InParanoidiQ9UHK0.
OMAiKEPVFHY.
OrthoDBiEOG77T15S.
PhylomeDBiQ9UHK0.
TreeFamiTF329804.

Miscellaneous databases

GeneWikiiNUFIP1.
GenomeRNAii26747.
NextBioi49103.
PROiQ9UHK0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHK0.
CleanExiHS_NUFIP1.
GenevisibleiQ9UHK0. HS.

Family and domain databases

InterProiIPR019496. NUFIP1_cons_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR022755. Znf_C2H2_jaz.
[Graphical view]
PfamiPF10453. NUFIP1. 1 hit.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 AND SER-342, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNUFP1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHK0
Secondary accession number(s): Q8WVM5, Q96SG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 20, 2007
Last modified: July 22, 2015
This is version 117 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. 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.