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Q7Z417

- NUFP2_HUMAN

UniProt

Q7Z417 - NUFP2_HUMAN

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Protein

Nuclear fragile X mental retardation-interacting protein 2

Gene

NUFIP2

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

Functioni

Binds RNA.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: HGNC
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NUFIP2
Synonyms:KIAA1321
ORF Names:PIG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:17634. NUFIP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. membrane Source: UniProtKB
  3. nucleus Source: HGNC
  4. polysomal ribosome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485564.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 695695Nuclear fragile X mental retardation-interacting protein 2PRO_0000245521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei87 – 871Phosphothreonine2 Publications
Modified residuei112 – 1121Phosphoserine3 Publications
Modified residuei113 – 1131Phosphoserine1 Publication
Modified residuei212 – 2121Phosphoserine5 Publications
Modified residuei214 – 2141Phosphoserine1 Publication
Modified residuei218 – 2181Phosphotyrosine1 Publication
Modified residuei219 – 2191Phosphothreonine1 Publication
Modified residuei220 – 2201Phosphothreonine2 Publications
Modified residuei376 – 3761Phosphoserine1 Publication
Modified residuei571 – 5711Phosphothreonine1 Publication
Modified residuei572 – 5721Phosphoserine4 Publications
Modified residuei629 – 6291Phosphoserine5 Publications
Modified residuei633 – 6331Phosphothreonine1 Publication
Modified residuei637 – 6371Phosphoserine2 Publications
Modified residuei652 – 6521Phosphoserine7 Publications
Modified residuei655 – 6551Phosphoserine1 Publication
Modified residuei692 – 6921Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7Z417.
PaxDbiQ7Z417.
PeptideAtlasiQ7Z417.
PRIDEiQ7Z417.

PTM databases

PhosphoSiteiQ7Z417.

Expressioni

Gene expression databases

BgeeiQ7Z417.
CleanExiHS_NUFIP2.
ExpressionAtlasiQ7Z417. baseline and differential.
GenevestigatoriQ7Z417.

Organism-specific databases

HPAiHPA017344.

Interactioni

Subunit structurei

Interacts with FMRP.1 Publication

Protein-protein interaction databases

BioGridi121591. 18 interactions.
DIPiDIP-29023N.
IntActiQ7Z417. 4 interactions.
MINTiMINT-4657915.
STRINGi9606.ENSP00000225388.

Structurei

3D structure databases

ProteinModelPortaliQ7Z417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 6049His-richAdd
BLAST
Compositional biasi373 – 41543Ser-richAdd
BLAST

Phylogenomic databases

eggNOGiNOG85203.
GeneTreeiENSGT00440000038328.
HOGENOMiHOG000220869.
HOVERGENiHBG065794.
InParanoidiQ7Z417.
OMAiKEMESVW.
OrthoDBiEOG71RXJ4.
PhylomeDBiQ7Z417.
TreeFamiTF332832.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7Z417-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEEKPGQPQP QHHHSHHHPH HHPQQQQQQP HHHHHYYFYN HSHNHHHHHH
60 70 80 90 100
HQQPHQYLQH GAEGSPKAQP KPLKHEQKHT LQQHQETPKK KTGYGELNGN
110 120 130 140 150
AGEREISLKN LSSDEATNPI SRVLNGNQQV VDTSLKQTVK ANTFGKAGIK
160 170 180 190 200
TKNFIQKNSM DKKNGKSYEN KSGENQSVDK SDTIPIPNGV VTNNSGYITN
210 220 230 240 250
GYMGKGADND GSGSESGYTT PKKRKARRNS AKGCENLNIV QDKIMQQETS
260 270 280 290 300
VPTLKQGLET FKPDYSEQKG NRVDGSKPIW KYETGPGGTS RGKPAVGDML
310 320 330 340 350
RKSSDSKPGV SSKKFDDRPK GKHASAVASK EDSWTLFKPP PVFPVDNSSA
360 370 380 390 400
KIVPKISYAS KVKENLNKTI QNSSVSPTSS SSSSSSTGET QTQSSSRLSQ
410 420 430 440 450
VPMSALKSVT SANFSNGPVL AGTDGNVYPP GGQPLLTTAA NTLTPISSGT
460 470 480 490 500
DSVLQDMSLT SAAVEQIKTS LFIYPSNMQT MLLSTAQVDL PSQTDQQNLG
510 520 530 540 550
DIFQNQWGLS FINEPSAGPE TVTGKSSEHK VMEVTFQGEY PATLVSQGAE
560 570 580 590 600
IIPSGTEHPV FPKAYELEKR TSPQVLGSIL KSGTTSESGA LSLEPSHIGD
610 620 630 640 650
LQKADTSSQG ALVFLSKDYE IESQNPLASP TNTLLGSAKE QRYQRGLERN
660 670 680 690
DSWGSFDLRA AIVYHTKEME SIWNLQKQDP KRIITYNEAM DSPDQ
Length:695
Mass (Da):76,121
Last modified:October 1, 2003 - v1
Checksum:iBB5C94131F5B5426
GO
Isoform 2 (identifier: Q7Z417-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-667: Missing.

Show »
Length:120
Mass (Da):14,643
Checksum:i3C9F1A1AAACA7535
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 667575Missing in isoform 2. 2 PublicationsVSP_056177Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ493465 mRNA. Translation: CAD38278.1.
AY232289 mRNA. Translation: AAP69984.1.
AB037742 mRNA. Translation: BAA92559.1. Different initiation.
AK297732 mRNA. Translation: BAG60082.1.
AC005412 Genomic DNA. No translation available.
BC129989 mRNA. Translation: AAI29990.1.
BC108307 mRNA. Translation: AAI08308.1.
CCDSiCCDS32600.1. [Q7Z417-1]
RefSeqiNP_065823.1. NM_020772.2. [Q7Z417-1]
UniGeneiHs.462598.

Genome annotation databases

EnsembliENST00000225388; ENSP00000225388; ENSG00000108256. [Q7Z417-1]
ENST00000579665; ENSP00000463450; ENSG00000108256. [Q7Z417-2]
GeneIDi57532.
KEGGihsa:57532.
UCSCiuc002hdy.4. human. [Q7Z417-1]

Polymorphism databases

DMDMi74713454.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ493465 mRNA. Translation: CAD38278.1 .
AY232289 mRNA. Translation: AAP69984.1 .
AB037742 mRNA. Translation: BAA92559.1 . Different initiation.
AK297732 mRNA. Translation: BAG60082.1 .
AC005412 Genomic DNA. No translation available.
BC129989 mRNA. Translation: AAI29990.1 .
BC108307 mRNA. Translation: AAI08308.1 .
CCDSi CCDS32600.1. [Q7Z417-1 ]
RefSeqi NP_065823.1. NM_020772.2. [Q7Z417-1 ]
UniGenei Hs.462598.

3D structure databases

ProteinModelPortali Q7Z417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121591. 18 interactions.
DIPi DIP-29023N.
IntActi Q7Z417. 4 interactions.
MINTi MINT-4657915.
STRINGi 9606.ENSP00000225388.

PTM databases

PhosphoSitei Q7Z417.

Polymorphism databases

DMDMi 74713454.

Proteomic databases

MaxQBi Q7Z417.
PaxDbi Q7Z417.
PeptideAtlasi Q7Z417.
PRIDEi Q7Z417.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000225388 ; ENSP00000225388 ; ENSG00000108256 . [Q7Z417-1 ]
ENST00000579665 ; ENSP00000463450 ; ENSG00000108256 . [Q7Z417-2 ]
GeneIDi 57532.
KEGGi hsa:57532.
UCSCi uc002hdy.4. human. [Q7Z417-1 ]

Organism-specific databases

CTDi 57532.
GeneCardsi GC17M027582.
HGNCi HGNC:17634. NUFIP2.
HPAi HPA017344.
MIMi 609356. gene.
neXtProti NX_Q7Z417.
PharmGKBi PA143485564.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG85203.
GeneTreei ENSGT00440000038328.
HOGENOMi HOG000220869.
HOVERGENi HBG065794.
InParanoidi Q7Z417.
OMAi KEMESVW.
OrthoDBi EOG71RXJ4.
PhylomeDBi Q7Z417.
TreeFami TF332832.

Miscellaneous databases

ChiTaRSi NUFIP2. human.
GeneWikii NUFIP2.
GenomeRNAii 57532.
NextBioi 35460527.
PROi Q7Z417.
SOURCEi Search...

Gene expression databases

Bgeei Q7Z417.
CleanExi HS_NUFIP2.
ExpressionAtlasi Q7Z417. baseline and differential.
Genevestigatori Q7Z417.

Family and domain databases

ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2).
    Tissue: Uterus.
  7. 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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "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.
  14. "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.
  15. 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.
  16. "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].
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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].

Entry informationi

Entry nameiNUFP2_HUMAN
AccessioniPrimary (citable) accession number: Q7Z417
Secondary accession number(s): A1L3A6, Q9P2M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 95 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3