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Protein

Influenza virus NS1A-binding protein

Gene

IVNS1ABP

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

Functioni

Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines (By similarity). May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription.By similarity1 Publication

GO - Biological processi

  • negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  • response to virus Source: ProtInc
  • RNA splicing Source: ProtInc
  • transcription from RNA polymerase III promoter Source: ProtInc
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Names & Taxonomyi

Protein namesi
Recommended name:
Influenza virus NS1A-binding protein
Short name:
NS1-BP
Short name:
NS1-binding protein
Alternative name(s):
Aryl hydrocarbon receptor-associated protein 3
Gene namesi
Name:IVNS1ABP
Synonyms:ARA3, FLARA3, KIAA0850, NS1, NS1BP
ORF Names:HSPC068
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16951. IVNS1ABP.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Nucleusnucleoplasm 1 Publication

  • Note: Associated with actin filaments (By similarity). Localization related to speckle domains which correspond to interchromatin granules and are enriched in factors involved in pre-mRNA splicing. Following influenza A virus infection, redistribution from speckles to a more diffuse distribution in the nucleoplasm.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: InterPro
  • cytoplasm Source: HPA
  • nucleoplasm Source: UniProtKB-SubCell
  • spliceosomal complex Source: ProtInc
  • transcription factor complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981V → M: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. 1 Publication
Mutagenesisi288 – 2881E → K: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. 1 Publication

Organism-specific databases

PharmGKBiPA134875300.

Polymorphism and mutation databases

BioMutaiIVNS1ABP.
DMDMi146325015.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 642642Influenza virus NS1A-binding proteinPRO_0000285077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei277 – 2771Phosphoserine1 Publication
Modified residuei322 – 3221Phosphoserine1 Publication
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei338 – 3381Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y6Y0.
PaxDbiQ9Y6Y0.
PRIDEiQ9Y6Y0.

PTM databases

PhosphoSiteiQ9Y6Y0.

Expressioni

Gene expression databases

BgeeiQ9Y6Y0.
CleanExiHS_IVNS1ABP.
ExpressionAtlasiQ9Y6Y0. baseline and differential.
GenevisibleiQ9Y6Y0. HS.

Organism-specific databases

HPAiHPA003405.

Interactioni

Subunit structurei

Homodimer; through the BTB domain (By similarity). Interacts with NS/Influenza virus NS1A protein and with AHR/Aryl hydrocarbon receptor.By similarity2 Publications

Protein-protein interaction databases

BioGridi115869. 58 interactions.
IntActiQ9Y6Y0. 10 interactions.
MINTiMINT-1371090.
STRINGi9606.ENSP00000356468.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6Y0.
SMRiQ9Y6Y0. Positions 19-202, 273-634.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9968BTBPROSITE-ProRule annotationAdd
BLAST
Domaini134 – 233100BACKAdd
BLAST
Repeati369 – 41547Kelch 1Add
BLAST
Repeati416 – 46348Kelch 2Add
BLAST
Repeati465 – 51248Kelch 3Add
BLAST
Repeati513 – 55947Kelch 4Add
BLAST
Repeati560 – 60647Kelch 5Add
BLAST
Repeati608 – 64235Kelch 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 368205Sufficient for AHR interaction and signalingAdd
BLAST

Domaini

When the BTB domain is lacking, AHR signaling induction promoted by IVNS1ABP is massively increased; Thus, the BTB domain inhibits AHR signaling induced by IVNS1ABP.1 Publication

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG236155.
GeneTreeiENSGT00760000119153.
HOVERGENiHBG082407.
InParanoidiQ9Y6Y0.
KOiK15046.
OMAiARNEWKM.
OrthoDBiEOG7327N7.
PhylomeDBiQ9Y6Y0.
TreeFamiTF329218.

Family and domain databases

Gene3Di2.130.10.80. 2 hits.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR015916. Gal_Oxidase_b-propeller.
IPR006652. Kelch_1.
IPR029849. NS1BP.
[Graphical view]
PANTHERiPTHR24411:SF7. PTHR24411:SF7. 1 hit.
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 6 hits.
[Graphical view]
PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y6Y0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL
60 70 80 90 100
ACCSPYLFEI FNSDSDPHGI SHVKFDDLNP EAVEVLLNYA YTAQLKADKE
110 120 130 140 150
LVKDVYSAAK KLKMDRVKQV CGDYLLSRMD VTSCISYRNF ASCMGDSRLL
160 170 180 190 200
NKVDAYIQEH LLQISEEEEF LKLPRLKLEV MLEDNVCLPS NGKLYTKVIN
210 220 230 240 250
WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNLLDGQ AEVFGSDDDH
260 270 280 290 300
IQFVQKKPPR ENGHKQISSS STGCLSSPNA TVQSPKHEWK IVASEKTSNN
310 320 330 340 350
TYLCLAVLDG IFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQQDELIEKP
360 370 380 390 400
MSPMQYARSG LGTAEMNGKL IAAGGYNREE CLRTVECYNP HTDHWSFLAP
410 420 430 440 450
MRTPRARFQM AVLMGQLYVV GGSNGHSDDL SCGEMYDSNI DDWIPVPELR
460 470 480 490 500
TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK NCDVFDPVTK LWTSCAPLNI
510 520 530 540 550
RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT LIAPMNVARR
560 570 580 590 600
GAGVAVLNGK LFVCGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG
610 620 630 640
IATVGNTIYA VGGFDGNEFL NTVEVYNLES NEWSPYTKIF QF
Length:642
Mass (Da):71,729
Last modified:May 1, 2007 - v3
Checksum:i456E30DC4E351CCD
GO

Sequence cautioni

The sequence AAF29040.1 differs from that shown. Reason: Frameshift at positions 100 and 102. Curated
The sequence BAA74873.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA10029.1 differs from that shown. Reason: Frameshift at position 612. Curated
The sequence CAI17867.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111K → E in CAA10029 (PubMed:9696811).Curated
Sequence conflicti148 – 1481R → H in CAA10029 (PubMed:9696811).Curated
Sequence conflicti218 – 2181E → G in AAH67739 (PubMed:15489334).Curated
Sequence conflicti579 – 5791Y → H in ABE03889 (PubMed:16582008).Curated
Sequence conflicti579 – 5791Y → H in ABE03890 (PubMed:16582008).Curated
Sequence conflicti591 – 5911N → H in CAA10029 (PubMed:9696811).Curated
Sequence conflicti623 – 6231V → A in CAA10029 (PubMed:9696811).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012449 mRNA. Translation: CAA10029.1. Frameshift.
DQ443528 mRNA. Translation: ABE03889.1.
DQ443529 mRNA. Translation: ABE03890.1.
AF205218 mRNA. Translation: AAG43485.1.
AB020657 mRNA. Translation: BAA74873.2. Different initiation.
AF161553 mRNA. Translation: AAF29040.1. Frameshift.
AL078644, AL356273 Genomic DNA. Translation: CAB72329.1.
AK292431 mRNA. Translation: BAF85120.1.
AL078644 Genomic DNA. Translation: CAI17867.1. Sequence problems.
AL356273, AL078644 Genomic DNA. Translation: CAI22094.1.
CH471067 Genomic DNA. Translation: EAW91194.1.
BC067739 mRNA. Translation: AAH67739.1.
CCDSiCCDS1368.1.
RefSeqiNP_006460.2. NM_006469.4.
UniGeneiHs.497183.

Genome annotation databases

EnsembliENST00000367498; ENSP00000356468; ENSG00000116679.
GeneIDi10625.
KEGGihsa:10625.
UCSCiuc001grl.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ012449 mRNA. Translation: CAA10029.1. Frameshift.
DQ443528 mRNA. Translation: ABE03889.1.
DQ443529 mRNA. Translation: ABE03890.1.
AF205218 mRNA. Translation: AAG43485.1.
AB020657 mRNA. Translation: BAA74873.2. Different initiation.
AF161553 mRNA. Translation: AAF29040.1. Frameshift.
AL078644, AL356273 Genomic DNA. Translation: CAB72329.1.
AK292431 mRNA. Translation: BAF85120.1.
AL078644 Genomic DNA. Translation: CAI17867.1. Sequence problems.
AL356273, AL078644 Genomic DNA. Translation: CAI22094.1.
CH471067 Genomic DNA. Translation: EAW91194.1.
BC067739 mRNA. Translation: AAH67739.1.
CCDSiCCDS1368.1.
RefSeqiNP_006460.2. NM_006469.4.
UniGeneiHs.497183.

3D structure databases

ProteinModelPortaliQ9Y6Y0.
SMRiQ9Y6Y0. Positions 19-202, 273-634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115869. 58 interactions.
IntActiQ9Y6Y0. 10 interactions.
MINTiMINT-1371090.
STRINGi9606.ENSP00000356468.

PTM databases

PhosphoSiteiQ9Y6Y0.

Polymorphism and mutation databases

BioMutaiIVNS1ABP.
DMDMi146325015.

Proteomic databases

MaxQBiQ9Y6Y0.
PaxDbiQ9Y6Y0.
PRIDEiQ9Y6Y0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367498; ENSP00000356468; ENSG00000116679.
GeneIDi10625.
KEGGihsa:10625.
UCSCiuc001grl.3. human.

Organism-specific databases

CTDi10625.
GeneCardsiGC01M185265.
HGNCiHGNC:16951. IVNS1ABP.
HPAiHPA003405.
MIMi609209. gene.
neXtProtiNX_Q9Y6Y0.
PharmGKBiPA134875300.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236155.
GeneTreeiENSGT00760000119153.
HOVERGENiHBG082407.
InParanoidiQ9Y6Y0.
KOiK15046.
OMAiARNEWKM.
OrthoDBiEOG7327N7.
PhylomeDBiQ9Y6Y0.
TreeFamiTF329218.

Miscellaneous databases

ChiTaRSiIVNS1ABP. human.
GeneWikiiIVNS1ABP.
GenomeRNAii10625.
NextBioi40368.
PROiQ9Y6Y0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6Y0.
CleanExiHS_IVNS1ABP.
ExpressionAtlasiQ9Y6Y0. baseline and differential.
GenevisibleiQ9Y6Y0. HS.

Family and domain databases

Gene3Di2.130.10.80. 2 hits.
InterProiIPR011705. BACK.
IPR017096. BTB-kelch_protein.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR015916. Gal_Oxidase_b-propeller.
IPR006652. Kelch_1.
IPR029849. NS1BP.
[Graphical view]
PANTHERiPTHR24411:SF7. PTHR24411:SF7. 1 hit.
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 6 hits.
[Graphical view]
PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NS1-Binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells."
    Wolff T., O'Neill R.E., Palese P.
    J. Virol. 72:7170-7180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NS, SUBCELLULAR LOCATION.
  2. "The aryl hydrocarbon receptor signaling pathway is modified through interactions with a Kelch protein."
    Dunham E.E., Stevens E.A., Glover E., Bradfield C.A.
    Mol. Pharmacol. 70:8-15(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, REGION, MUTAGENESIS OF VAL-198 AND GLU-288, INTERACTION WITH AHR.
  3. "A novel gene from endothelium cells stimulated by human plasma LDL --similar to NS1-binding protein."
    Chen B.S., Zhang K.M.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Blood.
  7. "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: Testis.
  8. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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: Testis.
  11. "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.
  12. "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-277 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-336 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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].
  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-246, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNS1BP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6Y0
Secondary accession number(s): A8K8R6
, Q1G4T6, Q1G4T7, Q5TF75, Q6NW38, Q7LCG2, Q9NZX0, Q9Y480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: July 22, 2015
This is version 114 of the entry and version 3 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.