Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y6Y0 (NS1BP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Cytoplasmcytoskeleton. Nucleusnucleoplasm. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 642642Influenza virus NS1A-binding protein
PRO_0000285077

Regions

Domain32 – 9968BTB
Domain134 – 233100BACK
Repeat369 – 41547Kelch 1
Repeat416 – 46348Kelch 2
Repeat465 – 51248Kelch 3
Repeat513 – 55947Kelch 4
Repeat560 – 60647Kelch 5
Repeat608 – 64235Kelch 6
Region164 – 368205Sufficient for AHR interaction and signaling

Amino acid modifications

Modified residue2461Phosphoserine Ref.16
Modified residue2771Phosphoserine Ref.12
Modified residue3221Phosphoserine Ref.12
Modified residue3361Phosphoserine Ref.13
Modified residue3381Phosphoserine Ref.13 Ref.14

Experimental info

Mutagenesis1981V → M: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. Ref.2
Mutagenesis2881E → K: Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP. Ref.2
Sequence conflict1111K → E in CAA10029. Ref.1
Sequence conflict1481R → H in CAA10029. Ref.1
Sequence conflict2181E → G in AAH67739. Ref.10
Sequence conflict5791Y → H in ABE03889. Ref.2
Sequence conflict5791Y → H in ABE03890. Ref.2
Sequence conflict5911N → H in CAA10029. Ref.1
Sequence conflict6231V → A in CAA10029. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y6Y0 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 456E30DC4E351CCD

FASTA64271,729
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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, 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].
+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.
RefSeqNP_006460.2. NM_006469.4.
UniGeneHs.497183.

3D structure databases

ProteinModelPortalQ9Y6Y0.
SMRQ9Y6Y0. Positions 19-202, 273-634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115869. 19 interactions.
IntActQ9Y6Y0. 9 interactions.
MINTMINT-1371090.

PTM databases

PhosphoSiteQ9Y6Y0.

Polymorphism databases

DMDM146325015.

Proteomic databases

PaxDbQ9Y6Y0.
PRIDEQ9Y6Y0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367498; ENSP00000356468; ENSG00000116679.
GeneID10625.
KEGGhsa:10625.
UCSCuc001grl.3. human.

Organism-specific databases

CTD10625.
GeneCardsGC01M185265.
HGNCHGNC:16951. IVNS1ABP.
HPAHPA003405.
MIM609209. gene.
neXtProtNX_Q9Y6Y0.
PharmGKBPA134875300.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236155.
HOVERGENHBG082407.
InParanoidQ9Y6Y0.
KOK15046.
OMAKLWTSCA.
OrthoDBEOG7327N7.
PhylomeDBQ9Y6Y0.
TreeFamTF329218.

Gene expression databases

ArrayExpressQ9Y6Y0.
BgeeQ9Y6Y0.
CleanExHS_IVNS1ABP.
GenevestigatorQ9Y6Y0.

Family and domain databases

Gene3D2.130.10.80. 2 hits.
3.30.710.10. 1 hit.
InterProIPR011705. BACK.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR015916. Gal_Oxidase_b-propeller.
IPR017096. Kelch-like_gigaxonin-typ.
IPR006652. Kelch_1.
[Graphical view]
PfamPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 6 hits.
[Graphical view]
PIRSFPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIVNS1ABP. human.
GeneWikiIVNS1ABP.
GenomeRNAi10625.
NextBio40368.
PROQ9Y6Y0.
SOURCESearch...

Entry information

Entry nameNS1BP_HUMAN
AccessionPrimary (citable) accession number: Q9Y6Y0
Secondary accession number(s): A8K8R6 expand/collapse secondary AC list , 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: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM