Q9Y6Y0 (NS1BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	IVNS1ABP
Synonyms:	ARA3, FLARA3, KIAA0850, NS1, NS1BP
ORF Names:	HSPC068

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2
Subunit structure	Homodimer; through the BTB domain By similarity. Interacts with NS/Influenza virus NS1A protein and with AHR/Aryl hydrocarbon receptor. Ref.1 Ref.2
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Nucleus › nucleoplasm. 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. Ref.1
Domain	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. Ref.2
Sequence similarities	Contains 1 BACK (BTB/Kelch associated) domain. Contains 1 BTB (POZ) domain. Contains 6 Kelch repeats.
Sequence caution	The sequence AAF29040.1 differs from that shown. Reason: Frameshift at positions 100 and 102. The sequence BAA74873.2 differs from that shown. Reason: Erroneous initiation. The sequence CAA10029.1 differs from that shown. Reason: Frameshift at position 612. The sequence CAI17867.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Kelch repeat Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Traceable author statement Ref.1. Source: ProtInc response to virus Traceable author statement Ref.1. Source: ProtInc transcription from RNA polymerase III promoter Traceable author statement Ref.1. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Traceable author statement Ref.1. Source: ProtInc transcription factor complex Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 642	642	Influenza virus NS1A-binding protein		PRO_0000285077
Regions
	Domain	32 – 99	68	BTB
	Domain	134 – 233	100	BACK
	Repeat	369 – 415	47	Kelch 1
	Repeat	416 – 463	48	Kelch 2
	Repeat	465 – 512	48	Kelch 3
	Repeat	513 – 559	47	Kelch 4
	Repeat	560 – 606	47	Kelch 5
	Repeat	608 – 642	35	Kelch 6
	Region	164 – 368	205	Sufficient for AHR interaction and signaling
Amino acid modifications
	Modified residue	246	1	Phosphoserine Ref.15
	Modified residue	277	1	Phosphoserine Ref.12
	Modified residue	322	1	Phosphoserine Ref.12
	Modified residue	336	1	Phosphoserine Ref.13
	Modified residue	338	1	Phosphoserine Ref.13 Ref.14
Experimental info
	Mutagenesis	198	1	V → M: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. Ref.2
	Mutagenesis	288	1	E → K: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. Ref.2
	Sequence conflict	111	1	K → E in CAA10029. Ref.1
	Sequence conflict	148	1	R → H in CAA10029. Ref.1
	Sequence conflict	218	1	E → G in AAH67739. Ref.10
	Sequence conflict	579	1	Y → H in ABE03889. Ref.2
	Sequence conflict	579	1	Y → H in ABE03890. Ref.2
	Sequence conflict	591	1	N → H in CAA10029. Ref.1
	Sequence conflict	623	1	V → A in CAA10029. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6Y0 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: 456E30DC4E351CCD	FASTA	642	71,729
	10 20 30 40 50 60 MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL ACCSPYLFEI 70 80 90 100 110 120 FNSDSDPHGI SHVKFDDLNP EAVEVLLNYA YTAQLKADKE LVKDVYSAAK KLKMDRVKQV 130 140 150 160 170 180 CGDYLLSRMD VTSCISYRNF ASCMGDSRLL NKVDAYIQEH LLQISEEEEF LKLPRLKLEV 190 200 210 220 230 240 MLEDNVCLPS NGKLYTKVIN WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNLLDGQ 250 260 270 280 290 300 AEVFGSDDDH IQFVQKKPPR ENGHKQISSS STGCLSSPNA TVQSPKHEWK IVASEKTSNN 310 320 330 340 350 360 TYLCLAVLDG IFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQQDELIEKP MSPMQYARSG 370 380 390 400 410 420 LGTAEMNGKL IAAGGYNREE CLRTVECYNP HTDHWSFLAP MRTPRARFQM AVLMGQLYVV 430 440 450 460 470 480 GGSNGHSDDL SCGEMYDSNI DDWIPVPELR TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK 490 500 510 520 530 540 NCDVFDPVTK LWTSCAPLNI RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT 550 560 570 580 590 600 LIAPMNVARR GAGVAVLNGK LFVCGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG 610 620 630 640 IATVGNTIYA VGGFDGNEFL NTVEVYNLES NEWSPYTKIF QF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-338, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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 SER-246, MASS SPECTROMETRY. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00014319.
RefSeq	NP_006460.2. NM_006469.4.
UniGene	Hs.497183.
3D structure databases
HSSP	HSSP built from PDB template 1X2J based on UniProtKB Q9Z2X8.
ProteinModelPortal	Q9Y6Y0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6Y0. 9 interactions.
MINT	MINT-1371090.
PTM databases
PhosphoSite	Q9Y6Y0.
Polymorphism databases
DMDM	146325015.
Proteomic databases
PaxDb	Q9Y6Y0.
PRIDE	Q9Y6Y0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367497; ENSP00000356467; ENSG00000116679. ENST00000367498; ENSP00000356468; ENSG00000116679.
GeneID	10625.
KEGG	hsa:10625.
UCSC	uc001grl.3. human.
Organism-specific databases
CTD	10625.
GeneCards	GC01M185265.
HGNC	HGNC:16951. IVNS1ABP.
HPA	HPA003405.
MIM	609209. gene.
neXtProt	NX_Q9Y6Y0.
PharmGKB	PA134875300.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236155.
HOVERGEN	HBG082407.
InParanoid	Q9Y6Y0.
KO	K15046.
OMA	ARNEWKM.
OrthoDB	EOG4W6NVG.
Gene expression databases
ArrayExpress	Q9Y6Y0.
Bgee	Q9Y6Y0.
CleanEx	HS_IVNS1ABP.
Genevestigator	Q9Y6Y0.
Family and domain databases
Gene3D	2.130.10.80. 2 hits. 3.30.710.10. 1 hit.
InterPro	IPR011705. BACK. IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. IPR015916. Gal_Oxidase_b-propeller. IPR017096. Kelch-like_gigaxonin. IPR006652. Kelch_1. [Graphical view]
Pfam	PF07707. BACK. 1 hit. PF00651. BTB. 1 hit. PF01344. Kelch_1. 6 hits. [Graphical view]
PIRSF	PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMART	SM00875. BACK. 1 hit. SM00225. BTB. 1 hit. SM00612. Kelch. 6 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	IVNS1ABP. human.
GenomeRNAi	10625.
NextBio	40368.
SOURCE	Search...

Entry information

Entry name

NS1BP_HUMAN

Accession

Primary (citable) accession number: Q9Y6Y0
Secondary accession number(s): A8K8R6 , Q1G4T6, Q1G4T7, Q5TF75, Q6NW38, Q7LCG2, Q9NZX0, Q9Y480

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.