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Q7Z417 (NUFP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear fragile X mental retardation-interacting protein 2
Alternative name(s):
82 kDa FMRP-interacting protein
Short name=82-FIP
Cell proliferation-inducing gene 1 protein
FMRP-interacting protein 2
Gene names
Name:NUFIP2
Synonyms:KIAA1321
ORF Names:PIG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length695 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds RNA. Ref.1

Subunit structure

Interacts with FMRP. Ref.1

Subcellular location

Nucleus. Cytoplasm. Note: Distribution is cell cycle-modulated, being cytoplasmic in the G2/M phase and accumulating in nucleus during the G1 phase. Ref.1

Sequence caution

The sequence BAA92559.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 695695Nuclear fragile X mental retardation-interacting protein 2
PRO_0000245521

Regions

Compositional bias12 – 6049His-rich
Compositional bias373 – 41543Ser-rich

Amino acid modifications

Modified residue871Phosphothreonine Ref.9 Ref.17
Modified residue1121Phosphoserine Ref.13 Ref.17 Ref.19
Modified residue1131Phosphoserine Ref.13
Modified residue2121Phosphoserine Ref.8 Ref.13 Ref.16 Ref.17 Ref.19
Modified residue2141Phosphoserine Ref.13
Modified residue2181Phosphotyrosine Ref.13
Modified residue2191Phosphothreonine Ref.13
Modified residue2201Phosphothreonine Ref.8 Ref.13
Modified residue3761Phosphoserine Ref.16
Modified residue5711Phosphothreonine Ref.17
Modified residue5721Phosphoserine Ref.13 Ref.16 Ref.17 Ref.19
Modified residue6291Phosphoserine Ref.5 Ref.13 Ref.16 Ref.17 Ref.19
Modified residue6331Phosphothreonine Ref.17
Modified residue6371Phosphoserine Ref.13 Ref.16
Modified residue6521Phosphoserine Ref.6 Ref.7 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19
Modified residue6551Phosphoserine Ref.19
Modified residue6921Phosphoserine Ref.13 Ref.17 Ref.19

Sequences

Sequence LengthMass (Da)Tools
Q7Z417 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: BB5C94131F5B5426

FASTA69576,121
        10         20         30         40         50         60 
MEEKPGQPQP QHHHSHHHPH HHPQQQQQQP HHHHHYYFYN HSHNHHHHHH HQQPHQYLQH 

        70         80         90        100        110        120 
GAEGSPKAQP KPLKHEQKHT LQQHQETPKK KTGYGELNGN AGEREISLKN LSSDEATNPI 

       130        140        150        160        170        180 
SRVLNGNQQV VDTSLKQTVK ANTFGKAGIK TKNFIQKNSM DKKNGKSYEN KSGENQSVDK 

       190        200        210        220        230        240 
SDTIPIPNGV VTNNSGYITN GYMGKGADND GSGSESGYTT PKKRKARRNS AKGCENLNIV 

       250        260        270        280        290        300 
QDKIMQQETS VPTLKQGLET FKPDYSEQKG NRVDGSKPIW KYETGPGGTS RGKPAVGDML 

       310        320        330        340        350        360 
RKSSDSKPGV SSKKFDDRPK GKHASAVASK EDSWTLFKPP PVFPVDNSSA KIVPKISYAS 

       370        380        390        400        410        420 
KVKENLNKTI QNSSVSPTSS SSSSSSTGET QTQSSSRLSQ VPMSALKSVT SANFSNGPVL 

       430        440        450        460        470        480 
AGTDGNVYPP GGQPLLTTAA NTLTPISSGT DSVLQDMSLT SAAVEQIKTS LFIYPSNMQT 

       490        500        510        520        530        540 
MLLSTAQVDL PSQTDQQNLG DIFQNQWGLS FINEPSAGPE TVTGKSSEHK VMEVTFQGEY 

       550        560        570        580        590        600 
PATLVSQGAE IIPSGTEHPV FPKAYELEKR TSPQVLGSIL KSGTTSESGA LSLEPSHIGD 

       610        620        630        640        650        660 
LQKADTSSQG ALVFLSKDYE IESQNPLASP TNTLLGSAKE QRYQRGLERN DSWGSFDLRA 

       670        680        690 
AIVYHTKEME SIWNLQKQDP KRIITYNEAM DSPDQ 

« Hide

References

« Hide 'large scale' references
[1]"82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization."
Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.
Hum. Mol. Genet. 12:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-92 AND 593-609, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH FMRP.
[2]Kim J.W.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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].
Tissue: Uterus.
[5]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 92-104; 110-136; 233-269; 331-351; 369-397; 531-563; 571-639; 650-659; 668-677 AND 683-695, PHOSPHORYLATION AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[6]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"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-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-112; SER-113; SER-212; SER-214; TYR-218; THR-219; THR-220; SER-572; SER-629; SER-637; SER-652 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-376; SER-572; SER-629 AND SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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 THR-87; SER-112; SER-212; THR-571; SER-572; SER-629; THR-633; SER-652 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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-112; SER-212; SER-572; SER-629; SER-652; SER-655 AND SER-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ493465 mRNA. Translation: CAD38278.1.
AY232289 mRNA. Translation: AAP69984.1.
AB037742 mRNA. Translation: BAA92559.1. Different initiation.
BC108307 mRNA. Translation: AAI08308.1.
CCDSCCDS32600.1.
RefSeqNP_065823.1. NM_020772.2.
UniGeneHs.462598.

3D structure databases

ProteinModelPortalQ7Z417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121591. 22 interactions.
DIPDIP-29023N.
IntActQ7Z417. 4 interactions.
MINTMINT-4657915.
STRING9606.ENSP00000225388.

PTM databases

PhosphoSiteQ7Z417.

Polymorphism databases

DMDM74713454.

Proteomic databases

MaxQBQ7Z417.
PaxDbQ7Z417.
PeptideAtlasQ7Z417.
PRIDEQ7Z417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225388; ENSP00000225388; ENSG00000108256.
GeneID57532.
KEGGhsa:57532.
UCSCuc002hdy.4. human.

Organism-specific databases

CTD57532.
GeneCardsGC17M027582.
HGNCHGNC:17634. NUFIP2.
HPAHPA017344.
MIM609356. gene.
neXtProtNX_Q7Z417.
PharmGKBPA143485564.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85203.
HOGENOMHOG000220869.
HOVERGENHBG065794.
InParanoidQ7Z417.
OMAKEMESVW.
OrthoDBEOG71RXJ4.
PhylomeDBQ7Z417.
TreeFamTF332832.

Gene expression databases

ArrayExpressQ7Z417.
BgeeQ7Z417.
CleanExHS_NUFIP2.
GenevestigatorQ7Z417.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSNUFIP2. human.
GeneWikiNUFIP2.
GenomeRNAi57532.
NextBio63940.
PROQ7Z417.
SOURCESearch...

Entry information

Entry nameNUFP2_HUMAN
AccessionPrimary (citable) accession number: Q7Z417
Secondary accession number(s): Q9P2M5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM