NTF2_HUMAN
ID NTF2_HUMAN Reviewed; 127 AA.
AC P61970; B2R4G7; P13662; Q6IB67;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Nuclear transport factor 2 {ECO:0000303|PubMed:7744965};
DE Short=NTF-2;
DE AltName: Full=Placental protein 15 {ECO:0000303|PubMed:3380696};
DE Short=PP15 {ECO:0000303|PubMed:3380696};
GN Name=NUTF2 {ECO:0000312|HGNC:HGNC:13722};
GN Synonyms=NTF2 {ECO:0000303|PubMed:7744965};
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 [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, FUNCTION, INTERACTION
RP WITH NUP54; NUP58 AND NUP62, AND SUBCELLULAR LOCATION.
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, INTERACTION WITH GDP-BOUND RAN, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-42 AND HIS-124.
RX PubMed=10679025; DOI=10.1091/mbc.11.2.703;
RA Steggerda S.M., Black B.E., Paschal B.M.;
RT "Monoclonal antibodies to NTF2 inhibit nuclear protein import by preventing
RT nuclear translocation of the GTPase Ran.";
RL Mol. Biol. Cell 11:703-719(2000).
RN [8]
RP INTERACTION WITH CAPG.
RX PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x;
RA Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C.,
RA Vandekerckhove J., Gettemans J.;
RT "A new role for nuclear transport factor 2 and Ran: nuclear import of
RT CapG.";
RL Traffic 9:695-707(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [10]
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., Buerckstuemmer T.,
RA 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: Mediates the import of GDP-bound RAN from the cytoplasm into
CC the nucleus which is essential for the function of RAN in cargo
CC receptor-mediated nucleocytoplasmic transport. Thereby, plays
CC indirectly a more general role in cargo receptor-mediated
CC nucleocytoplasmic transport. Interacts with GDP-bound RAN in the
CC cytosol, recruits it to the nuclear pore complex via its interaction
CC with nucleoporins and promotes its nuclear import.
CC {ECO:0000269|PubMed:10679025, ECO:0000269|PubMed:7744965}.
CC -!- SUBUNIT: Homodimer (PubMed:7744965). Interacts with RAN (GDP-bound
CC form); the interaction is direct and regulates RAN nuclear import
CC (PubMed:10679025). Interacts with the nucleoporins NUP54, NUP58 and
CC NUP62 (via FG repeats); recruits NUTF2 to the nuclear pore complex a
CC step required for NUTF2-mediated GDP-bound RAN nuclear import
CC (PubMed:7744965). Interacts with CAPG; mediates its nuclear import
CC (PubMed:18266911). {ECO:0000269|PubMed:10679025,
CC ECO:0000269|PubMed:18266911, ECO:0000269|PubMed:7744965}.
CC -!- INTERACTION:
CC P61970; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-591778, EBI-10181188;
CC P61970; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-591778, EBI-10693038;
CC P61970; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-591778, EBI-12020154;
CC P61970; Q9BWC9: CCDC106; NbExp=3; IntAct=EBI-591778, EBI-711501;
CC P61970; Q8NCX0-3: CCDC150; NbExp=3; IntAct=EBI-591778, EBI-12235840;
CC P61970; Q9NX63: CHCHD3; NbExp=3; IntAct=EBI-591778, EBI-743375;
CC P61970; Q9BY43-2: CHMP4A; NbExp=3; IntAct=EBI-591778, EBI-12178895;
CC P61970; P12532: CKMT1B; NbExp=3; IntAct=EBI-591778, EBI-1050662;
CC P61970; Q16740: CLPP; NbExp=3; IntAct=EBI-591778, EBI-1056029;
CC P61970; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-591778, EBI-742802;
CC P61970; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-591778, EBI-740641;
CC P61970; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-591778, EBI-713401;
CC P61970; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-591778, EBI-9089060;
CC P61970; O43790: KRT86; NbExp=3; IntAct=EBI-591778, EBI-9996498;
CC P61970; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-591778, EBI-11958364;
CC P61970; Q14847-2: LASP1; NbExp=3; IntAct=EBI-591778, EBI-9088686;
CC P61970; Q5T751: LCE1C; NbExp=3; IntAct=EBI-591778, EBI-12224199;
CC P61970; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-591778, EBI-11955689;
CC P61970; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-591778, EBI-726510;
CC P61970; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-591778, EBI-2857471;
CC P61970; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-591778, EBI-5662487;
CC P61970; P15531: NME1; NbExp=3; IntAct=EBI-591778, EBI-741141;
CC P61970; O00746: NME4; NbExp=3; IntAct=EBI-591778, EBI-744871;
CC P61970; Q9NQ35: NRIP3; NbExp=3; IntAct=EBI-591778, EBI-10311735;
CC P61970; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-591778, EBI-741048;
CC P61970; P37198: NUP62; NbExp=7; IntAct=EBI-591778, EBI-347978;
CC P61970; P61970: NUTF2; NbExp=3; IntAct=EBI-591778, EBI-591778;
CC P61970; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-591778, EBI-10240813;
CC P61970; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-591778, EBI-10302990;
CC P61970; P12004: PCNA; NbExp=3; IntAct=EBI-591778, EBI-358311;
CC P61970; Q01813: PFKP; NbExp=3; IntAct=EBI-591778, EBI-359022;
CC P61970; Q9UIL8: PHF11; NbExp=3; IntAct=EBI-591778, EBI-2861403;
CC P61970; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-591778, EBI-710402;
CC P61970; P62826: RAN; NbExp=6; IntAct=EBI-591778, EBI-286642;
CC P61970; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-591778, EBI-747925;
CC P61970; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-591778, EBI-11995806;
CC P61970; Q9C004: SPRY4; NbExp=3; IntAct=EBI-591778, EBI-354861;
CC P61970; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-591778, EBI-12833746;
CC P61970; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-591778, EBI-17438286;
CC P61970; Q08117-2: TLE5; NbExp=3; IntAct=EBI-591778, EBI-11741437;
CC P61970; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-591778, EBI-2514383;
CC P61970; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-591778, EBI-12111538;
CC P61970; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-591778, EBI-2682299;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10679025,
CC ECO:0000269|PubMed:7744965}. Nucleus outer membrane
CC {ECO:0000250|UniProtKB:P61972}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P61972}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:P61972}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10679025}. Note=At steady state it is essentially
CC nucleoplasmic, enriched in nucleoplasmic foci.
CC {ECO:0000269|PubMed:10679025}.
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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 CCDS; CCDS10848.1; -.
DR PIR; S00751; S00751.
DR RefSeq; NP_001308967.1; NM_001322038.1.
DR RefSeq; NP_001308968.1; NM_001322039.1.
DR RefSeq; NP_001308969.1; NM_001322040.1.
DR RefSeq; NP_001308970.1; NM_001322041.1.
DR RefSeq; NP_005787.1; NM_005796.2.
DR PDB; 1GY5; X-ray; 2.30 A; A/B=1-127.
DR PDBsum; 1GY5; -.
DR AlphaFoldDB; P61970; -.
DR BMRB; P61970; -.
DR SMR; P61970; -.
DR BioGRID; 115499; 98.
DR DIP; DIP-6057N; -.
DR IntAct; P61970; 51.
DR STRING; 9606.ENSP00000219169; -.
DR iPTMnet; P61970; -.
DR MetOSite; P61970; -.
DR PhosphoSitePlus; P61970; -.
DR SwissPalm; P61970; -.
DR BioMuta; NUTF2; -.
DR DMDM; 48429030; -.
DR OGP; P61970; -.
DR EPD; P61970; -.
DR jPOST; P61970; -.
DR MassIVE; P61970; -.
DR MaxQB; P61970; -.
DR PaxDb; P61970; -.
DR PeptideAtlas; P61970; -.
DR PRIDE; P61970; -.
DR ProteomicsDB; 57351; -.
DR TopDownProteomics; P61970; -.
DR Antibodypedia; 15885; 212 antibodies from 29 providers.
DR DNASU; 10204; -.
DR Ensembl; ENST00000219169.9; ENSP00000219169.4; ENSG00000102898.12.
DR Ensembl; ENST00000568396.2; ENSP00000457022.1; ENSG00000102898.12.
DR Ensembl; ENST00000569436.6; ENSP00000457989.1; ENSG00000102898.12.
DR GeneID; 10204; -.
DR KEGG; hsa:10204; -.
DR MANE-Select; ENST00000219169.9; ENSP00000219169.4; NM_005796.3; NP_005787.1.
DR UCSC; uc002eup.4; human.
DR CTD; 10204; -.
DR DisGeNET; 10204; -.
DR GeneCards; NUTF2; -.
DR HGNC; HGNC:13722; NUTF2.
DR HPA; ENSG00000102898; Low tissue specificity.
DR MIM; 605813; gene.
DR neXtProt; NX_P61970; -.
DR OpenTargets; ENSG00000102898; -.
DR PharmGKB; PA38365; -.
DR VEuPathDB; HostDB:ENSG00000102898; -.
DR eggNOG; KOG2104; Eukaryota.
DR GeneTree; ENSGT00510000047030; -.
DR HOGENOM; CLU_131642_1_1_1; -.
DR InParanoid; P61970; -.
DR OMA; FTEFYYN; -.
DR OrthoDB; 1437819at2759; -.
DR PhylomeDB; P61970; -.
DR TreeFam; TF314422; -.
DR PathwayCommons; P61970; -.
DR SignaLink; P61970; -.
DR SIGNOR; P61970; -.
DR BioGRID-ORCS; 10204; 787 hits in 1081 CRISPR screens.
DR ChiTaRS; NUTF2; human.
DR EvolutionaryTrace; P61970; -.
DR GeneWiki; NUTF2; -.
DR GenomeRNAi; 10204; -.
DR Pharos; P61970; Tbio.
DR PRO; PR:P61970; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P61970; protein.
DR Bgee; ENSG00000102898; Expressed in hindlimb stylopod muscle and 160 other tissues.
DR ExpressionAtlas; P61970; baseline and differential.
DR Genevisible; P61970; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IDA:BHF-UCL.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0090204; P:protein localization to nuclear pore; ISS:UniProtKB.
DR CDD; cd00780; NTF2; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR045875; NTF2/Mtr2.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR PANTHER; PTHR12612; PTHR12612; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..127
FT /note="Nuclear transport factor 2"
FT /id="PRO_0000194775"
FT DOMAIN 10..121
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MUTAGEN 42
FT /note="E->K: No effect on localization to the nucleoplasm."
FT /evidence="ECO:0000269|PubMed:10679025"
FT MUTAGEN 124
FT /note="Missing: No effect on localization to the
FT nucleoplasm."
FT /evidence="ECO:0000269|PubMed:10679025"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:1GY5"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1GY5"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 62..75
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 97..108
FT /evidence="ECO:0007829|PDB:1GY5"
FT STRAND 111..124
FT /evidence="ECO:0007829|PDB:1GY5"
SQ SEQUENCE 127 AA; 14478 MW; 817752F20E262FD3 CRC64;
MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP
FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR
LALHNFG
