Full text data of NUTF2
NUTF2
(NTF2)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear transport factor 2; NTF-2 (Placental protein 15; PP15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Nuclear transport factor 2; NTF-2 (Placental protein 15; PP15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61970
ID NTF2_HUMAN Reviewed; 127 AA.
AC P61970; B2R4G7; P13662; Q6IB67;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Nuclear transport factor 2;
DE Short=NTF-2;
DE AltName: Full=Placental protein 15;
DE Short=PP15;
GN Name=NUTF2; Synonyms=NTF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3380696; DOI=10.1093/nar/16.10.4721;
RA Grundmann U., Nerlich C., Rein T., Lottspeich F., Kuepper H.A.;
RT "Isolation of cDNA coding for the placental protein 15 (PP15).";
RL Nucleic Acids Res. 16:4721-4721(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RX PubMed=7744965; DOI=10.1083/jcb.129.4.925;
RA Paschal B.M., Gerace L.;
RT "Identification of NTF2, a cytosolic factor for nuclear import that
RT interacts with nuclear pore complex protein p62.";
RL J. Cell Biol. 129:925-937(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Facilitates protein transport into the nucleus.
CC Interacts with the nucleoporin p62 and with Ran. Acts at a
CC relatively late stage of nuclear protein import, subsequent to the
CC initial docking of nuclear import ligand at the nuclear envelope.
CC Could be part of a multicomponent system of cytosolic factors that
CC assemble at the pore complex during nuclear import.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X07315; CAA30278.1; -; mRNA.
DR EMBL; U43939; AAA85905.1; -; mRNA.
DR EMBL; CR456937; CAG33218.1; -; mRNA.
DR EMBL; AK311822; BAG34764.1; -; mRNA.
DR EMBL; CH471092; EAW83181.1; -; Genomic_DNA.
DR EMBL; BC002348; AAH02348.1; -; mRNA.
DR PIR; S00751; S00751.
DR RefSeq; NP_005787.1; NM_005796.1.
DR RefSeq; XP_005255828.1; XM_005255771.1.
DR UniGene; Hs.356630; -.
DR PDB; 1GY5; X-ray; 2.30 A; A/B=1-127.
DR PDBsum; 1GY5; -.
DR ProteinModelPortal; P61970; -.
DR SMR; P61970; 3-127.
DR DIP; DIP-6057N; -.
DR IntAct; P61970; 2.
DR MINT; MINT-5004387; -.
DR STRING; 9606.ENSP00000219169; -.
DR PhosphoSite; P61970; -.
DR DMDM; 48429030; -.
DR OGP; P61970; -.
DR PaxDb; P61970; -.
DR PeptideAtlas; P61970; -.
DR PRIDE; P61970; -.
DR DNASU; 10204; -.
DR Ensembl; ENST00000219169; ENSP00000219169; ENSG00000102898.
DR Ensembl; ENST00000568396; ENSP00000457022; ENSG00000102898.
DR Ensembl; ENST00000569436; ENSP00000457989; ENSG00000102898.
DR GeneID; 10204; -.
DR KEGG; hsa:10204; -.
DR UCSC; uc002eup.3; human.
DR CTD; 10204; -.
DR GeneCards; GC16P067880; -.
DR HGNC; HGNC:13722; NUTF2.
DR HPA; HPA040915; -.
DR HPA; HPA040956; -.
DR MIM; 605813; gene.
DR neXtProt; NX_P61970; -.
DR PharmGKB; PA38365; -.
DR eggNOG; NOG286483; -.
DR HOGENOM; HOG000197024; -.
DR HOVERGEN; HBG025070; -.
DR InParanoid; P61970; -.
DR OMA; FRLAIHN; -.
DR OrthoDB; EOG7TQV2N; -.
DR PhylomeDB; P61970; -.
DR ChiTaRS; NUTF2; human.
DR EvolutionaryTrace; P61970; -.
DR GeneWiki; NUTF2; -.
DR GenomeRNAi; 10204; -.
DR NextBio; 38624; -.
DR PRO; PR:P61970; -.
DR ArrayExpress; P61970; -.
DR Bgee; P61970; -.
DR CleanEx; HS_NUTF2; -.
DR Genevestigator; P61970; -.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0006611; P:protein export from nucleus; IDA:BHF-UCL.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR Pfam; PF02136; NTF2; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 127 Nuclear transport factor 2.
FT /FTId=PRO_0000194775.
FT DOMAIN 10 121 NTF2.
FT MOD_RES 4 4 N6-acetyllysine.
FT HELIX 6 24
FT HELIX 26 32
FT STRAND 33 41
FT STRAND 44 48
FT HELIX 49 57
FT STRAND 62 75
FT STRAND 81 94
FT STRAND 97 108
FT STRAND 111 124
SQ SEQUENCE 127 AA; 14478 MW; 817752F20E262FD3 CRC64;
MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP
FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR
LALHNFG
//
ID NTF2_HUMAN Reviewed; 127 AA.
AC P61970; B2R4G7; P13662; Q6IB67;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Nuclear transport factor 2;
DE Short=NTF-2;
DE AltName: Full=Placental protein 15;
DE Short=PP15;
GN Name=NUTF2; Synonyms=NTF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3380696; DOI=10.1093/nar/16.10.4721;
RA Grundmann U., Nerlich C., Rein T., Lottspeich F., Kuepper H.A.;
RT "Isolation of cDNA coding for the placental protein 15 (PP15).";
RL Nucleic Acids Res. 16:4721-4721(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RX PubMed=7744965; DOI=10.1083/jcb.129.4.925;
RA Paschal B.M., Gerace L.;
RT "Identification of NTF2, a cytosolic factor for nuclear import that
RT interacts with nuclear pore complex protein p62.";
RL J. Cell Biol. 129:925-937(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Facilitates protein transport into the nucleus.
CC Interacts with the nucleoporin p62 and with Ran. Acts at a
CC relatively late stage of nuclear protein import, subsequent to the
CC initial docking of nuclear import ligand at the nuclear envelope.
CC Could be part of a multicomponent system of cytosolic factors that
CC assemble at the pore complex during nuclear import.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X07315; CAA30278.1; -; mRNA.
DR EMBL; U43939; AAA85905.1; -; mRNA.
DR EMBL; CR456937; CAG33218.1; -; mRNA.
DR EMBL; AK311822; BAG34764.1; -; mRNA.
DR EMBL; CH471092; EAW83181.1; -; Genomic_DNA.
DR EMBL; BC002348; AAH02348.1; -; mRNA.
DR PIR; S00751; S00751.
DR RefSeq; NP_005787.1; NM_005796.1.
DR RefSeq; XP_005255828.1; XM_005255771.1.
DR UniGene; Hs.356630; -.
DR PDB; 1GY5; X-ray; 2.30 A; A/B=1-127.
DR PDBsum; 1GY5; -.
DR ProteinModelPortal; P61970; -.
DR SMR; P61970; 3-127.
DR DIP; DIP-6057N; -.
DR IntAct; P61970; 2.
DR MINT; MINT-5004387; -.
DR STRING; 9606.ENSP00000219169; -.
DR PhosphoSite; P61970; -.
DR DMDM; 48429030; -.
DR OGP; P61970; -.
DR PaxDb; P61970; -.
DR PeptideAtlas; P61970; -.
DR PRIDE; P61970; -.
DR DNASU; 10204; -.
DR Ensembl; ENST00000219169; ENSP00000219169; ENSG00000102898.
DR Ensembl; ENST00000568396; ENSP00000457022; ENSG00000102898.
DR Ensembl; ENST00000569436; ENSP00000457989; ENSG00000102898.
DR GeneID; 10204; -.
DR KEGG; hsa:10204; -.
DR UCSC; uc002eup.3; human.
DR CTD; 10204; -.
DR GeneCards; GC16P067880; -.
DR HGNC; HGNC:13722; NUTF2.
DR HPA; HPA040915; -.
DR HPA; HPA040956; -.
DR MIM; 605813; gene.
DR neXtProt; NX_P61970; -.
DR PharmGKB; PA38365; -.
DR eggNOG; NOG286483; -.
DR HOGENOM; HOG000197024; -.
DR HOVERGEN; HBG025070; -.
DR InParanoid; P61970; -.
DR OMA; FRLAIHN; -.
DR OrthoDB; EOG7TQV2N; -.
DR PhylomeDB; P61970; -.
DR ChiTaRS; NUTF2; human.
DR EvolutionaryTrace; P61970; -.
DR GeneWiki; NUTF2; -.
DR GenomeRNAi; 10204; -.
DR NextBio; 38624; -.
DR PRO; PR:P61970; -.
DR ArrayExpress; P61970; -.
DR Bgee; P61970; -.
DR CleanEx; HS_NUTF2; -.
DR Genevestigator; P61970; -.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0006611; P:protein export from nucleus; IDA:BHF-UCL.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR Pfam; PF02136; NTF2; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 127 Nuclear transport factor 2.
FT /FTId=PRO_0000194775.
FT DOMAIN 10 121 NTF2.
FT MOD_RES 4 4 N6-acetyllysine.
FT HELIX 6 24
FT HELIX 26 32
FT STRAND 33 41
FT STRAND 44 48
FT HELIX 49 57
FT STRAND 62 75
FT STRAND 81 94
FT STRAND 97 108
FT STRAND 111 124
SQ SEQUENCE 127 AA; 14478 MW; 817752F20E262FD3 CRC64;
MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP
FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR
LALHNFG
//
MIM
605813
*RECORD*
*FIELD* NO
605813
*FIELD* TI
*605813 NUCLEAR TRANSPORT FACTOR 2
;;NTF2;;
PLACENTAL PROTEIN 15; PP15
*FIELD* TX
read moreDESCRIPTION
Molecular trafficking between the cytoplasm and nucleus occurs through
proteinaceous structures called nuclear pore complexes, which span the
double membrane of the nuclear envelope and permit both passive
diffusion and active transport. Proteins destined for import typically
contain a nuclear localization signal (NLS), which is rich in basic
residues, and interact with an NLS receptor (e.g., KPNA2; 600685) before
docking to the nuclear envelope and interacting with a nucleoporin
(e.g., NUP62; 605815).
CLONING
By screening a placenta cDNA library for placental protein-15 (PP15), an
inhibitory molecule in the lymphocyte transformation test, Grundmann et
al. (1988) isolated a cDNA encoding PP15. The deduced 127-amino acid
protein contains a putative ribosome-binding site. Using biochemical
purification methods and micropeptide sequencing, followed by PCR,
Paschal and Gerace (1995) determined that NTF2 is encoded by the PP15
cDNA.
GENE FUNCTION
By functional analysis in NUP62-depleted cells, Paschal and Gerace
(1995) showed that NTF2 is required for nuclear protein import after the
association of the NLS ligand with the nuclear envelope. Reconstituting
permeabilized cells with NTF2 and RANBP1 (601180), as well as with a
'docking fraction' that probably contained an NLS receptor, showed that
these elements all perform distinct and necessary functions for nuclear
protein import. Paschal and Gerace (1995) concluded that NTF2 interacts
with NUP62 and acts after the docking step in the nuclear protein import
pathway.
Using an in vitro nuclear import system, Ribbeck et al. (1998) found
evidence that NTF2 is required for the nuclear import and reaccumulation
of RAN (601179), a molecule that is depleted from the nucleus as RAN-GTP
complexed with exported cargo. By mutation analysis and biochemical
studies, they determined that nuclear reaccumulation of RAN is mediated
by direct interaction between the 2 proteins and that RAN-GDP is the
species bound and transported by NTF2.
*FIELD* RF
1. Grundmann, U.; Nerlich, C.; Rein, T.; Lottspeich, F.; Kupper, H.
A.: Isolation of cDNA coding for the placental protein 15 (PP15). Nucleic
Acids Res. 16: 4721 only, 1988.
2. Paschal, B. M.; Gerace, L.: Identification of NTF2, a cytosolic
factor for nuclear import that interacts with nuclear pore complex
protein p62. J. Cell Biol. 129: 925-937, 1995.
3. Ribbeck, K.; Lipowsky, G.; Kent, H. M.; Stewart, M.; Gorlich, D.
: NTF2 mediates nuclear import of Ran. EMBO J. 17: 6587-6598, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 4/26/2002
*FIELD* CD
Paul J. Converse: 4/3/2001
*FIELD* ED
carol: 06/06/2003
carol: 4/29/2002
terry: 4/26/2002
mgross: 4/4/2001
mgross: 4/3/2001
*RECORD*
*FIELD* NO
605813
*FIELD* TI
*605813 NUCLEAR TRANSPORT FACTOR 2
;;NTF2;;
PLACENTAL PROTEIN 15; PP15
*FIELD* TX
read moreDESCRIPTION
Molecular trafficking between the cytoplasm and nucleus occurs through
proteinaceous structures called nuclear pore complexes, which span the
double membrane of the nuclear envelope and permit both passive
diffusion and active transport. Proteins destined for import typically
contain a nuclear localization signal (NLS), which is rich in basic
residues, and interact with an NLS receptor (e.g., KPNA2; 600685) before
docking to the nuclear envelope and interacting with a nucleoporin
(e.g., NUP62; 605815).
CLONING
By screening a placenta cDNA library for placental protein-15 (PP15), an
inhibitory molecule in the lymphocyte transformation test, Grundmann et
al. (1988) isolated a cDNA encoding PP15. The deduced 127-amino acid
protein contains a putative ribosome-binding site. Using biochemical
purification methods and micropeptide sequencing, followed by PCR,
Paschal and Gerace (1995) determined that NTF2 is encoded by the PP15
cDNA.
GENE FUNCTION
By functional analysis in NUP62-depleted cells, Paschal and Gerace
(1995) showed that NTF2 is required for nuclear protein import after the
association of the NLS ligand with the nuclear envelope. Reconstituting
permeabilized cells with NTF2 and RANBP1 (601180), as well as with a
'docking fraction' that probably contained an NLS receptor, showed that
these elements all perform distinct and necessary functions for nuclear
protein import. Paschal and Gerace (1995) concluded that NTF2 interacts
with NUP62 and acts after the docking step in the nuclear protein import
pathway.
Using an in vitro nuclear import system, Ribbeck et al. (1998) found
evidence that NTF2 is required for the nuclear import and reaccumulation
of RAN (601179), a molecule that is depleted from the nucleus as RAN-GTP
complexed with exported cargo. By mutation analysis and biochemical
studies, they determined that nuclear reaccumulation of RAN is mediated
by direct interaction between the 2 proteins and that RAN-GDP is the
species bound and transported by NTF2.
*FIELD* RF
1. Grundmann, U.; Nerlich, C.; Rein, T.; Lottspeich, F.; Kupper, H.
A.: Isolation of cDNA coding for the placental protein 15 (PP15). Nucleic
Acids Res. 16: 4721 only, 1988.
2. Paschal, B. M.; Gerace, L.: Identification of NTF2, a cytosolic
factor for nuclear import that interacts with nuclear pore complex
protein p62. J. Cell Biol. 129: 925-937, 1995.
3. Ribbeck, K.; Lipowsky, G.; Kent, H. M.; Stewart, M.; Gorlich, D.
: NTF2 mediates nuclear import of Ran. EMBO J. 17: 6587-6598, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 4/26/2002
*FIELD* CD
Paul J. Converse: 4/3/2001
*FIELD* ED
carol: 06/06/2003
carol: 4/29/2002
terry: 4/26/2002
mgross: 4/4/2001
mgross: 4/3/2001