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Q9UHY1

- NRBP_HUMAN

UniProt

Q9UHY1 - NRBP_HUMAN

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Protein

Nuclear receptor-binding protein

Gene

NRBP1

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

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 homodimerization activity Source: UniProtKB
  3. 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
Complete GO annotation...

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 projection Source: UniProtKB-KW
  2. endomembrane system Source: UniProtKB
  3. membrane Source: UniProtKB-KW
  4. nucleoplasm Source: Reactome
  5. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

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 – 21Phosphoserine2 Publications
Modified residuei433 – 4331Phosphothreonine3 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

BgeeiQ9UHY1.
CleanExiHS_NRBP1.
ExpressionAtlasiQ9UHY1. baseline and differential.
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. 20 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.
GeneTreeiENSGT00550000074385.
HOGENOMiHOG000267147.
HOVERGENiHBG057400.
InParanoidiQ9UHY1.
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

        10         20         30         40         50
MSEGESQTVL SSGSDPKVES SSSAPGLTSV SPPVTSTTSA ASPEEEEESE
60 70 80 90 100
DESEILEESP CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ
110 120 130 140 150
FSERKNYKLQ EEKVRAVFDN LIQLEHLNIV KFHKYWADIK ENKARVIFIT
160 170 180 190 200
EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW CTQILSALSY LHSCDPPIIH
210 220 230 240 250
GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL HFFAPEYGEV
260 270 280 290 300
TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDPLQ
310 320 330 340 350
REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE
360 370 380 390 400
NALEEITKNM DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG
410 420 430 440 450
IYPLTAFGLP RPQQPQQEEV TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN
460 470 480 490 500
IESVEEGVKH HLTLLLKLED KLNRHLSCDL MPNENIPELA AELVQLGFIS
510 520 530
EADQSRLTSL LEETLNKFNF ARNSTLNSAA VTVSS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 20 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.
GeneTreei ENSGT00550000074385.
HOGENOMi HOG000267147.
HOVERGENi HBG057400.
InParanoidi Q9UHY1.
KOi K08875.
PhylomeDBi Q9UHY1.
TreeFami TF315519.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki Q9UHY1.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9UHY1.
CleanExi HS_NRBP1.
ExpressionAtlasi Q9UHY1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 129 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