Q8WY41 (NANO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nanos homolog 1
Short name=NOS-1

Alternative name(s):
EC_Rep1a

Gene names

Name:	NANOS1
Synonyms:	NOS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May act as a translational repressor which regulates translation of specific mRNAs by forming a complex with PUM2 that associates with the 3'-UTR of mRNA targets. Capable of interfering with the proadhesive and anti-invasive functions of E-cadherin. Up-regulates the production of MMP14 to promote tumor cell invasion. Ref.2 Ref.4
Subunit structure	Interacts with PUM2, SNAPIN and CTNNB1. Interacts (via N-terminal region) with CTNND1. Ref.1 Ref.2 Ref.5
Subcellular location	Cytoplasm › perinuclear region. Cytoplasm. Note: Co-localizes with SNAPIN and PUM2 in the perinuclear region of germ cells. Ref.1 Ref.2 Ref.5
Tissue specificity	Testis and ovary (at protein level). Predominantly expressed in testis. Specifically expressed during germline development. In adult tissues, it is mainly expressed in spermatogonia, the stem cells of the germline. Also expressed during meiosis in spermatocytes. Not present in late, post-meiotic stage germ cells. Expressed in fetal ovaries, while it is weakly or not expressed in mature postmeiotic oocytes, suggesting that it may be expressed in premeiotic female germ cells. Expressed at high levels only in the E-cadherin deficient cell lines. Highly expressed in lung carcinomas and mostly detected in invasive tumor cells and its expression correlates with tumor aggressiveness. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6
Developmental stage	Fetal ovary and fetal testis (at protein level). Ref.6
Induction	Down-regulated by E-cadherin. Ref.2
Domain	The Nanos-type zinc finger is composed of two C2HC motifs, each motif binding one molecule of zinc. It is essential for the translation repression activity of the protein By similarity. The N-terminal region and C-terminal zinc-finger RNA-binding domain are both necessary for interaction with SNAPIN.
Sequence similarities	Belongs to the nanos family. Contains 1 nanos-type zinc finger.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	epithelial cell migration Inferred from direct assay Ref.2. Source: UniProtKB
Cellular component	perinuclear region of cytoplasm Inferred from direct assay Ref.2Ref.5. Source: UniProtKB
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.2Ref.5. Source: UniProtKB translation repressor activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	Nanos homolog 1		PRO_0000207685
Regions
	Zinc finger	213 – 267	55	Nanos-type
	Region	40 – 56	17	Essential for its translational repressor activity By similarity
	Motif	214 – 241	28	C2HC 1
	Motif	249 – 265	17	C2HC 2
	Compositional bias	136 – 204	69	Ala-rich

Sequences

	Sequence		Length	Mass (Da)
	Q8WY41 [UniParc]. Last modified February 2, 2004. Version 2. Checksum: 1E41AAE68992CDD7	FASTA	292	30,230
	10 20 30 40 50 60 MEAFPWAPRS PRRGRAPPPM ALVPSARYVS APGPAHPQPF SSWNDYLGLA TLITKAVDGE 70 80 90 100 110 120 PRFGCARGGN GGGGSPPSSS SSSCCSPHTG AGPGALGPAL GPPDYDEDDD DDSDEPGSRG 130 140 150 160 170 180 RYLGSALELR ALELCAGPAE AGLLEERFAE LSPFAGRAAA VLLGCAPAAA AAATTTSEAT 190 200 210 220 230 240 PREERAPAWA AEPRLHAASG AAAARLLKPE LQVCVFCRNN KEAMALYTTH ILKGPDGRVL 250 260 270 280 290 CPVLRRYTCP LCGASGDNAH TIKYCPLSKV PPPPARPPPR SARDGPPGKK LR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of a Pumilio-Nanos complex from Drosophila germ plasm to human germ cells." Jaruzelska J., Kotecki M., Kusz K., Spik A., Firpo M., Reijo Pera R.A. Dev. Genes Evol. 213:120-126(2003) [PubMed: 12690449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PUM2. Tissue: Testis.
[2]	"E-cadherin regulates human Nanos1, which interacts with p120ctn and induces tumor cell migration and invasion." Strumane K., Bonnomet A., Stove C., Vandenbroucke R., Nawrocki-Raby B., Bruyneel E., Mareel M., Birembaut P., Berx G., van Roy F. Cancer Res. 66:10007-10015(2006) [PubMed: 17047063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH CTNND1 AND CTNNB1, TISSUE SPECIFICITY.
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression." Bonnomet A., Polette M., Strumane K., Gilles C., Dalstein V., Kileztky C., Berx G., van Roy F., Birembaut P., Nawrocki-Raby B. Oncogene 27:3692-3699(2008) [PubMed: 18223680] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]	"The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells." Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J. Mol. Hum. Reprod. 15:173-179(2009) [PubMed: 19168546] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PUM2 AND SNAPIN.
[6]	"NANOS3 function in human germ cell development." Julaton V.T., Reijo Pera R.A. Hum. Mol. Genet. 20:2238-2250(2011) [PubMed: 21421998] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF275269 mRNA. Translation: AAL36982.2. AF458985 mRNA. Translation: AAQ04765.1. AL157788 Genomic DNA. Translation: CAI14718.1.
IPI	IPI00397510.
RefSeq	NP_955631.1. NM_199461.2.
UniGene	Hs.591918.
3D structure databases
ProteinModelPortal	Q8WY41.
SMR	Q8WY41. Positions 212-266.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8WY41.
Polymorphism databases
DMDM	41688589.
Proteomic databases
PRIDE	Q8WY41.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000425699; ENSP00000393275; ENSG00000188613.
GeneID	340719.
KEGG	hsa:340719.
UCSC	uc009xzf.1. human.
Organism-specific databases
CTD	340719.
GeneCards	GC10P120779.
H-InvDB	HIX0035319.
HGNC	HGNC:23044. NANOS1.
HPA	CAB012219.
MIM	608226. gene.
neXtProt	NX_Q8WY41.
PharmGKB	PA134876543.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000005985.
HOGENOM	HBG125811.
HOVERGEN	HBG052574.
InParanoid	Q8WY41.
OMA	MEAFPWA.
PhylomeDB	Q8WY41.
Gene expression databases
ArrayExpress	Q8WY41.
Bgee	Q8WY41.
CleanEx	HS_NANOS1. HS_NOS1.
Genevestigator	Q8WY41.
GermOnline	ENSG00000188613. Homo sapiens.
Family and domain databases
InterPro	IPR008705. Nanos/Xcar2. IPR024161. Znf_nanos-typ. [Graphical view]
PANTHER	PTHR12887. Znf_Nanos. 1 hit.
Pfam	PF05741. zf-nanos. 1 hit. [Graphical view]
PROSITE	PS51522. ZF_NANOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	98006.
SOURCE	Search...

Entry information

Entry name

NANO1_HUMAN

Accession

Primary (citable) accession number: Q8WY41

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 2, 2004
Last sequence update:	February 2, 2004
Last modified:	January 25, 2012
This is version 75 of the entry and version 2 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.