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Q9UHY1

- NRBP_HUMAN

UniProt

Q9UHY1 - NRBP_HUMAN

Protein

Nuclear receptor-binding protein

Gene

NRBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication.2 Publications1 Publication

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: UniProtKB
    4. protein kinase activity Source: InterPro

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: UniProtKB
    2. gene expression Source: Reactome
    3. transcription initiation from RNA polymerase II promoter Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiQ9UHY1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor-binding protein
    Gene namesi
    Name:NRBP1
    Synonyms:BCON3Imported, NRBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:7993. NRBP1.

    Subcellular locationi

    Cytoplasmcell cortex 1 Publication. Endomembrane system 1 Publication. Cell projectionlamellipodium 1 Publication
    Note: Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. endomembrane system Source: UniProtKB
    3. lamellipodium Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB-KW
    5. nucleoplasm Source: Reactome
    6. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31772.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 535534Nuclear receptor-binding proteinPRO_0000086449Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei2 – 21Phosphoserine3 Publications
    Modified residuei433 – 4331Phosphothreonine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHY1.
    PaxDbiQ9UHY1.
    PeptideAtlasiQ9UHY1.
    PRIDEiQ9UHY1.

    PTM databases

    PhosphoSiteiQ9UHY1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissues examined with high levels in the testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHY1.
    BgeeiQ9UHY1.
    CleanExiHS_NRBP1.
    GenevestigatoriQ9UHY1.

    Organism-specific databases

    HPAiCAB033078.
    HPA029527.

    Interactioni

    Subunit structurei

    Homodimer. Binds to MLF1, recruiting a serine kinase which phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P143404EBI-749731,EBI-465733From a different organism.
    RAC3P607633EBI-749731,EBI-767084
    Sall4Q8BX222EBI-749731,EBI-2312582From a different organism.

    Protein-protein interaction databases

    BioGridi118995. 18 interactions.
    IntActiQ9UHY1. 19 interactions.
    MINTiMINT-1406316.
    STRINGi9606.ENSP00000233557.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UHY1.
    SMRiQ9UHY1. Positions 81-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 327260Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The protein kinase domain is predicted to be catalytically inactive.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000267147.
    HOVERGENiHBG057400.
    KOiK08875.
    PhylomeDBiQ9UHY1.
    TreeFamiTF315519.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UHY1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEGESQTVL SSGSDPKVES SSSAPGLTSV SPPVTSTTSA ASPEEEEESE    50
    DESEILEESP CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ 100
    FSERKNYKLQ EEKVRAVFDN LIQLEHLNIV KFHKYWADIK ENKARVIFIT 150
    EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW CTQILSALSY LHSCDPPIIH 200
    GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL HFFAPEYGEV 250
    TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDPLQ 300
    REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE 350
    NALEEITKNM DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG 400
    IYPLTAFGLP RPQQPQQEEV TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN 450
    IESVEEGVKH HLTLLLKLED KLNRHLSCDL MPNENIPELA AELVQLGFIS 500
    EADQSRLTSL LEETLNKFNF ARNSTLNSAA VTVSS 535
    Length:535
    Mass (Da):59,845
    Last modified:May 1, 2000 - v1
    Checksum:i398078661547EDD0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631R → G in BAD96856. 1 PublicationCurated
    Sequence conflicti95 – 951V → M in BAB55185. (PubMed:14702039)Curated
    Sequence conflicti473 – 4731N → S in BAB55185. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti365 – 3651V → I.1 Publication
    Corresponds to variant rs56004639 [ dbSNP | Ensembl ].
    VAR_041359
    Natural varianti432 – 4321P → L in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_041360
    Natural varianti460 – 4601H → R.1 Publication
    Corresponds to variant rs34260196 [ dbSNP | Ensembl ].
    VAR_041361

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113249 mRNA. Translation: AAF21967.1.
    AK001946 mRNA. Translation: BAA91993.1.
    AK027538 mRNA. Translation: BAB55185.1.
    AK122664 mRNA. Translation: BAG53652.1.
    AL136682 mRNA. Translation: CAB66617.1.
    AK223136 mRNA. Translation: BAD96856.1.
    AC074117 Genomic DNA. Translation: AAY14847.1.
    CH471053 Genomic DNA. Translation: EAX00578.1.
    CH471053 Genomic DNA. Translation: EAX00579.1.
    CH471053 Genomic DNA. Translation: EAX00580.1.
    BC001221 mRNA. Translation: AAH01221.1.
    CCDSiCCDS1753.1.
    RefSeqiNP_037524.1. NM_013392.2.
    XP_005264331.1. XM_005264274.1.
    UniGeneiHs.515876.

    Genome annotation databases

    EnsembliENST00000233557; ENSP00000233557; ENSG00000115216.
    ENST00000379852; ENSP00000369181; ENSG00000115216.
    GeneIDi29959.
    KEGGihsa:29959.
    UCSCiuc002rko.3. human.

    Polymorphism databases

    DMDMi74761962.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113249 mRNA. Translation: AAF21967.1 .
    AK001946 mRNA. Translation: BAA91993.1 .
    AK027538 mRNA. Translation: BAB55185.1 .
    AK122664 mRNA. Translation: BAG53652.1 .
    AL136682 mRNA. Translation: CAB66617.1 .
    AK223136 mRNA. Translation: BAD96856.1 .
    AC074117 Genomic DNA. Translation: AAY14847.1 .
    CH471053 Genomic DNA. Translation: EAX00578.1 .
    CH471053 Genomic DNA. Translation: EAX00579.1 .
    CH471053 Genomic DNA. Translation: EAX00580.1 .
    BC001221 mRNA. Translation: AAH01221.1 .
    CCDSi CCDS1753.1.
    RefSeqi NP_037524.1. NM_013392.2.
    XP_005264331.1. XM_005264274.1.
    UniGenei Hs.515876.

    3D structure databases

    ProteinModelPortali Q9UHY1.
    SMRi Q9UHY1. Positions 81-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118995. 18 interactions.
    IntActi Q9UHY1. 19 interactions.
    MINTi MINT-1406316.
    STRINGi 9606.ENSP00000233557.

    PTM databases

    PhosphoSitei Q9UHY1.

    Polymorphism databases

    DMDMi 74761962.

    Proteomic databases

    MaxQBi Q9UHY1.
    PaxDbi Q9UHY1.
    PeptideAtlasi Q9UHY1.
    PRIDEi Q9UHY1.

    Protocols and materials databases

    DNASUi 29959.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233557 ; ENSP00000233557 ; ENSG00000115216 .
    ENST00000379852 ; ENSP00000369181 ; ENSG00000115216 .
    GeneIDi 29959.
    KEGGi hsa:29959.
    UCSCi uc002rko.3. human.

    Organism-specific databases

    CTDi 29959.
    GeneCardsi GC02P027651.
    HGNCi HGNC:7993. NRBP1.
    HPAi CAB033078.
    HPA029527.
    MIMi 606010. gene.
    neXtProti NX_Q9UHY1.
    PharmGKBi PA31772.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000267147.
    HOVERGENi HBG057400.
    KOi K08875.
    PhylomeDBi Q9UHY1.
    TreeFami TF315519.

    Enzyme and pathway databases

    Reactomei REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki Q9UHY1.

    Miscellaneous databases

    GeneWikii NRBP1.
    GenomeRNAii 29959.
    NextBioi 52679.
    PROi Q9UHY1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHY1.
    Bgeei Q9UHY1.
    CleanExi HS_NRBP1.
    Genevestigatori Q9UHY1.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the cDNA and localization of the gene encoding human NRBP, a ubiquitously expressed, multidomain putative adapter protein."
      Hooper J.D., Baker E., Ogbourne S.M., Sutherland G.R., Antalis T.M.
      Genomics 66:113-118(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "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].
      Tissue: NeuronImported, PlacentaImported and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: KidneyImported.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: LungImported.
    8. "Interaction of the small GTPase Rac3 with NRBP, a protein with a kinase-homology domain."
      De Langhe S., Haataja L., Senadheera D., Groffen J., Heisterkamp N.
      Int. J. Mol. Med. 9:451-459(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-426, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH RAC3.
    9. "The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure."
      Chua J.J.E., Ng M.M.L., Chow V.T.K.
      Virus Res. 102:151-163(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DENGUE VIRUS TYPE 2 NS3.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 THR-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "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 THR-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-365; LEU-432 AND ARG-460.

    Entry informationi

    Entry nameiNRBP_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHY1
    Secondary accession number(s): B3KV40
    , D6W558, Q53FZ5, Q96SU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 127 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

    Caution

    Author states that kinase activity observed in PubMed:11956649 may be due to sample contamination. This protein is predicted to be catalytically inactive.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3