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NANO2_HUMAN
ID   NANO2_HUMAN             Reviewed;         138 AA.
AC   P60321; Q17R30; Q4G0P8;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Nanos homolog 2;
DE            Short=NOS-2;
GN   Name=NANOS2; Synonyms=NOS2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT
RP   GLN-68.
RX   PubMed=19168545; DOI=10.1093/molehr/gap003;
RA   Kusz K.M., Tomczyk L., Sajek M., Spik A., Latos-Bielenska A.,
RA   Jedrzejczak P., Pawelczyk L., Jaruzelska J.;
RT   "The highly conserved NANOS2 protein: testis-specific expression and
RT   significance for the human male reproduction.";
RL   Mol. Hum. Reprod. 15:165-171(2009).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=21421998; DOI=10.1093/hmg/ddr114;
RA   Julaton V.T., Reijo Pera R.A.;
RT   "NANOS3 function in human germ cell development.";
RL   Hum. Mol. Genet. 20:2238-2250(2011).
CC   -!- FUNCTION: Plays a key role in the sexual differentiation of germ cells
CC       by promoting the male fate but suppressing the female fate. Represses
CC       the female fate pathways by suppressing meiosis, which in turn results
CC       in the promotion of the male fate. Maintains the suppression of meiosis
CC       by preventing STRA8 expression, which is required for premeiotic DNA
CC       replication, after CYP26B1 is decreased. Regulates the localization of
CC       the CCR4-NOT deadenylation complex to P-bodies and plays a role in
CC       recruiting the complex to trigger the degradation of mRNAs involved in
CC       meiosis. Required for the maintenance of the spermatogonial stem cell
CC       population. Not essential for the assembly of P-bodies but is required
CC       for the maintenance of their normal state (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CNOT1, CNOT3, CNOT6L, CNOT7 and CNOT9.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       P60321; O95273: CCNDBP1; NbExp=5; IntAct=EBI-10216569, EBI-748961;
CC       P60321; P43365: MAGEA12; NbExp=7; IntAct=EBI-10216569, EBI-749530;
CC       P60321; P60903: S100A10; NbExp=3; IntAct=EBI-10216569, EBI-717048;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19168545}.
CC       Cytoplasm, P-body {ECO:0000250}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:19168545}. Note=Localizes at P-bodies during
CC       gonocyte development (By similarity). More abundant in perinuclear
CC       region of the cytoplasm of the germ cells of the adult testis.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis and ovary. Expression found in several
CC       spermatogenic stages: in cells on the periphery of the tubules which
CC       could correspond to spermatogonia, in spermatocytes and in round
CC       spermatids (at protein level). {ECO:0000269|PubMed:19168545,
CC       ECO:0000269|PubMed:21421998}.
CC   -!- DEVELOPMENTAL STAGE: Fetal ovary and fetal testis. Present in all germ
CC       cells of seminiferous tubules of the 24-week fetus (at protein level).
CC       {ECO:0000269|PubMed:19168545, ECO:0000269|PubMed:21421998}.
CC   -!- DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each
CC       motif binding one molecule of zinc. It is essential for the translation
CC       repression activity of the protein. {ECO:0000255|PROSITE-
CC       ProRule:PRU00855}.
CC   -!- SIMILARITY: Belongs to the nanos family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00855}.
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DR   EMBL; BC042883; AAH42883.1; -; mRNA.
DR   EMBL; BC117484; AAI17485.1; -; mRNA.
DR   EMBL; BC117486; AAI17487.1; -; mRNA.
DR   CCDS; CCDS33056.1; -.
DR   RefSeq; NP_001025032.1; NM_001029861.2.
DR   AlphaFoldDB; P60321; -.
DR   SMR; P60321; -.
DR   BioGRID; 130871; 28.
DR   ELM; P60321; -.
DR   IntAct; P60321; 23.
DR   MINT; P60321; -.
DR   STRING; 9606.ENSP00000341021; -.
DR   BioMuta; NANOS2; -.
DR   DMDM; 41688561; -.
DR   MassIVE; P60321; -.
DR   PaxDb; P60321; -.
DR   PeptideAtlas; P60321; -.
DR   PRIDE; P60321; -.
DR   ProteomicsDB; 57191; -.
DR   Antibodypedia; 31412; 259 antibodies from 30 providers.
DR   DNASU; 339345; -.
DR   Ensembl; ENST00000341294.4; ENSP00000341021.2; ENSG00000188425.4.
DR   GeneID; 339345; -.
DR   KEGG; hsa:339345; -.
DR   MANE-Select; ENST00000341294.4; ENSP00000341021.2; NM_001029861.3; NP_001025032.1.
DR   UCSC; uc002pdu.4; human.
DR   CTD; 339345; -.
DR   DisGeNET; 339345; -.
DR   GeneCards; NANOS2; -.
DR   HGNC; HGNC:23292; NANOS2.
DR   HPA; ENSG00000188425; Tissue enriched (testis).
DR   MIM; 608228; gene.
DR   neXtProt; NX_P60321; -.
DR   OpenTargets; ENSG00000188425; -.
DR   PharmGKB; PA134909776; -.
DR   VEuPathDB; HostDB:ENSG00000188425; -.
DR   eggNOG; KOG4602; Eukaryota.
DR   GeneTree; ENSGT00950000183135; -.
DR   HOGENOM; CLU_094055_1_0_1; -.
DR   InParanoid; P60321; -.
DR   OMA; RHVYASH; -.
DR   OrthoDB; 1198436at2759; -.
DR   PhylomeDB; P60321; -.
DR   TreeFam; TF326882; -.
DR   PathwayCommons; P60321; -.
DR   SignaLink; P60321; -.
DR   SIGNOR; P60321; -.
DR   BioGRID-ORCS; 339345; 12 hits in 1067 CRISPR screens.
DR   GenomeRNAi; 339345; -.
DR   Pharos; P60321; Tbio.
DR   PRO; PR:P60321; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P60321; protein.
DR   Bgee; ENSG00000188425; Expressed in right testis and 24 other tissues.
DR   Genevisible; P60321; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030718; P:germ-line stem cell population maintenance; ISS:UniProtKB.
DR   GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL.
DR   GO; GO:0048477; P:oogenesis; IBA:GO_Central.
DR   GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:BHF-UCL.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   Gene3D; 4.10.60.30; -; 1.
DR   InterPro; IPR008705; Nanos/Xcar2.
DR   InterPro; IPR038129; Nanos_sf.
DR   InterPro; IPR024161; Znf_nanos-typ.
DR   PANTHER; PTHR12887; PTHR12887; 1.
DR   Pfam; PF05741; zf-nanos; 1.
DR   PROSITE; PS51522; ZF_NANOS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Metal-binding;
KW   Reference proteome; RNA-binding; Spermatogenesis; Translation regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..138
FT                   /note="Nanos homolog 2"
FT                   /id="PRO_0000207687"
FT   ZN_FING         62..116
FT                   /note="Nanos-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   REGION          31..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           63..90
FT                   /note="C2HC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   MOTIF           98..114
FT                   /note="C2HC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00855"
FT   VARIANT         68
FT                   /note="H -> Q (in dbSNP:rs148451980)"
FT                   /evidence="ECO:0000269|PubMed:19168545"
FT                   /id="VAR_065246"
SQ   SEQUENCE   138 AA;  15132 MW;  98469E0F1AA6BC11 CRC64;
     MQLPPFDMWK DYFNLSQVVW ALIASRGQRL ETQEIEEPSP GPPLGQDQGL GAPGANGGLG
     TLCNFCKHNG ESRHVYSSHQ LKTPDGVVVC PILRHYVCPV CGATGDQAHT LKYCPLNGGQ
     QSLYRRSGRN SAGRRVKR
 
 
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