Full text data of TNPO2
TNPO2
[Confidence: low (only semi-automatic identification from reviews)]
Transportin-2 (Karyopherin beta-2b)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transportin-2 (Karyopherin beta-2b)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O14787
ID TNPO2_HUMAN Reviewed; 897 AA.
AC O14787; O14655; Q6IN77;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Transportin-2;
DE AltName: Full=Karyopherin beta-2b;
GN Name=TNPO2;
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] (ISOFORM 1).
RX PubMed=9298975; DOI=10.1083/jcb.138.6.1181;
RA Siomi M.C., Eder P.S., Kataoka N., Wan L., Liu Q., Dreyfuss G.;
RT "Transportin-mediated nuclear import of heterogeneous nuclear RNP
RT proteins.";
RL J. Cell Biol. 138:1181-1192(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Bonifaci N., Radu A., Blobel G.;
RT "Human karyopherin beta2b: an homolog of human karyopherin beta2.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-862, 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 [7]
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).
RN [8]
RP VARIANT CYS-370.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Probably functions in nuclear protein import as nuclear
CC transport receptor. Serves as receptor for nuclear localization
CC signals (NLS) in cargo substrates. Is thought to mediate docking
CC of the importin/substrate complex to the nuclear pore complex
CC (NPC) through binding to nucleoporin and the complex is
CC subsequently translocated through the pore by an energy requiring,
CC Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14787-1; Sequence=Displayed;
CC Name=2; Synonyms=beta2b;
CC IsoId=O14787-2; Sequence=VSP_009657;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 13 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal 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; AF019039; AAB83973.1; -; mRNA.
DR EMBL; AF007748; AAB71349.1; -; mRNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84300.1; -; Genomic_DNA.
DR EMBL; BC072420; AAH72420.1; -; mRNA.
DR RefSeq; NP_001129667.1; NM_001136195.1.
DR RefSeq; NP_001129668.1; NM_001136196.1.
DR RefSeq; NP_038461.2; NM_013433.4.
DR RefSeq; XP_005259936.1; XM_005259879.1.
DR RefSeq; XP_005259937.1; XM_005259880.1.
DR RefSeq; XP_005259938.1; XM_005259881.1.
DR RefSeq; XP_005259939.1; XM_005259882.1.
DR UniGene; Hs.416049; -.
DR UniGene; Hs.714402; -.
DR ProteinModelPortal; O14787; -.
DR SMR; O14787; 3-896.
DR IntAct; O14787; 5.
DR MINT; MINT-2998321; -.
DR STRING; 9606.ENSP00000397379; -.
DR PhosphoSite; O14787; -.
DR PaxDb; O14787; -.
DR PRIDE; O14787; -.
DR Ensembl; ENST00000356861; ENSP00000349321; ENSG00000105576.
DR Ensembl; ENST00000425528; ENSP00000407182; ENSG00000105576.
DR Ensembl; ENST00000441499; ENSP00000389648; ENSG00000105576.
DR Ensembl; ENST00000450764; ENSP00000397379; ENSG00000105576.
DR Ensembl; ENST00000588216; ENSP00000465625; ENSG00000105576.
DR Ensembl; ENST00000592287; ENSP00000468434; ENSG00000105576.
DR GeneID; 30000; -.
DR KEGG; hsa:30000; -.
DR UCSC; uc002muo.3; human.
DR CTD; 30000; -.
DR GeneCards; GC19M012810; -.
DR HGNC; HGNC:19998; TNPO2.
DR HPA; CAB046446; -.
DR MIM; 603002; gene.
DR neXtProt; NX_O14787; -.
DR PharmGKB; PA134921349; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000203940; -.
DR HOVERGEN; HBG058963; -.
DR InParanoid; O14787; -.
DR OMA; VRRHVCQ; -.
DR OrthoDB; EOG7XM2X0; -.
DR PhylomeDB; O14787; -.
DR ChiTaRS; TNPO2; human.
DR GeneWiki; TNPO2; -.
DR GenomeRNAi; 30000; -.
DR NextBio; 52812; -.
DR PRO; PR:O14787; -.
DR ArrayExpress; O14787; -.
DR Bgee; O14787; -.
DR CleanEx; HS_TNPO2; -.
DR Genevestigator; O14787; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Polymorphism; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1 897 Transportin-2.
FT /FTId=PRO_0000120767.
FT DOMAIN 31 99 Importin N-terminal.
FT REPEAT 121 159 HEAT 1.
FT REPEAT 167 205 HEAT 2.
FT REPEAT 208 246 HEAT 3.
FT REPEAT 249 287 HEAT 4.
FT REPEAT 292 330 HEAT 5.
FT REPEAT 389 427 HEAT 6.
FT REPEAT 430 468 HEAT 7.
FT REPEAT 472 510 HEAT 8.
FT REPEAT 513 551 HEAT 9.
FT REPEAT 556 596 HEAT 10.
FT REPEAT 659 697 HEAT 11.
FT REPEAT 700 738 HEAT 12.
FT REPEAT 741 780 HEAT 13.
FT MOD_RES 862 862 N6-acetyllysine.
FT VAR_SEQ 769 778 Missing (in isoform 2).
FT /FTId=VSP_009657.
FT VARIANT 370 370 W -> C (found in a patient with severely
FT delayed development, autism, myopia,
FT strabismus and some dysmorphisms).
FT /FTId=VAR_069373.
FT CONFLICT 28 28 Q -> H (in Ref. 2; AAB71349).
FT CONFLICT 32 32 Q -> R (in Ref. 2; AAB71349).
FT CONFLICT 194 194 A -> G (in Ref. 2; AAB71349).
FT CONFLICT 398 401 LLKG -> YQS (in Ref. 1; AAB83973).
FT CONFLICT 492 492 R -> K (in Ref. 2; AAB71349).
FT CONFLICT 499 499 S -> I (in Ref. 2; AAB71349).
FT CONFLICT 507 507 E -> K (in Ref. 2; AAB71349).
FT CONFLICT 608 608 R -> C (in Ref. 2; AAB71349).
FT CONFLICT 645 645 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 646 646 S -> T (in Ref. 1; AAB83973).
FT CONFLICT 656 656 V -> L (in Ref. 1; AAB83973).
FT CONFLICT 687 687 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 691 691 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 696 697 FI -> SS (in Ref. 2; AAB71349).
FT CONFLICT 717 717 E -> K (in Ref. 1; AAB83973).
FT CONFLICT 812 812 R -> Q (in Ref. 1; AAB83973).
FT CONFLICT 841 841 F -> L (in Ref. 2; AAB71349).
SQ SEQUENCE 897 AA; 101388 MW; 26FE455583D7D35F CRC64;
MDWQPDEQGL QQVLQLLKDS QSPNTATQRI VQDKLKQLNQ FPDFNNYLIF VLTRLKSEDE
PTRSLSGLIL KNNVKAHYQS FPPPVADFIK QECLNNIGDA SSLIRATIGI LITTIASKGE
LQMWPELLPQ LCNLLNSEDY NTCEGAFGAL QKICEDSSEL LDSDALNRPL NIMIPKFLQF
FKHCSPKIRS HAIACVNQFI MDRAQALMDN IDTFIEHLFA LAVDDDPEVR KNVCRALVML
LEVRIDRLIP HMHSIIQYML QRTQDHDENV ALEACEFWLT LAEQPICKEV LASHLVQLIP
ILVNGMKYSE IDIILLKGDV EEDEAVPDSE QDIKPRFHKS RTVTLPHEAE RPDGSEDAED
DDDDDALSDW NLRKCSAAAL DVLANVFREE LLPHLLPLLK GLLFHPEWVV KESGILVLGA
IAEGCMQGMV PYLPELIPHL IQCLSDKKAL VRSIACWTLS RYAHWVVSQP PDMHLKPLMT
ELLKRILDGN KRVQEAACSA FATLEEEACT ELVPYLSYIL DTLVFAFGKY QHKNLLILYD
AIGTLADSVG HHLNQPEYIQ KLMPPLIQKW NELKDEDKDL FPLLECLSSV ATALQSGFLP
YCEPVYQRCV TLVQKTLAQA MMYTQHPEQY EAPDKDFMIV ALDLLSGLAE GLGGHVEQLV
ARSNIMTLLF QCMQDSMPEV RQSSFALLGD LTKACFIHVK PCIAEFMPIL GTNLNPEFIS
VCNNATWAIG EICMQMGAEM QPYVQMVLNN LVEIINRPNT PKTLLENTGR LTSPSAIPAI
TIGRLGYVCP QEVAPMLQQF IRPWCTSLRN IRDNEEKDSA FRGICMMIGV NPGGVVQDFI
FFCDAVASWV SPKDDLRDMF YKILHGFKDQ VGEDNWQQFS EQFPPLLKER LAAFYGV
//
ID TNPO2_HUMAN Reviewed; 897 AA.
AC O14787; O14655; Q6IN77;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 3.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Transportin-2;
DE AltName: Full=Karyopherin beta-2b;
GN Name=TNPO2;
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] (ISOFORM 1).
RX PubMed=9298975; DOI=10.1083/jcb.138.6.1181;
RA Siomi M.C., Eder P.S., Kataoka N., Wan L., Liu Q., Dreyfuss G.;
RT "Transportin-mediated nuclear import of heterogeneous nuclear RNP
RT proteins.";
RL J. Cell Biol. 138:1181-1192(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Bonifaci N., Radu A., Blobel G.;
RT "Human karyopherin beta2b: an homolog of human karyopherin beta2.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-862, 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 [7]
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).
RN [8]
RP VARIANT CYS-370.
RX PubMed=23033978; DOI=10.1056/NEJMoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
RA Brunner H.G., Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Probably functions in nuclear protein import as nuclear
CC transport receptor. Serves as receptor for nuclear localization
CC signals (NLS) in cargo substrates. Is thought to mediate docking
CC of the importin/substrate complex to the nuclear pore complex
CC (NPC) through binding to nucleoporin and the complex is
CC subsequently translocated through the pore by an energy requiring,
CC Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14787-1; Sequence=Displayed;
CC Name=2; Synonyms=beta2b;
CC IsoId=O14787-2; Sequence=VSP_009657;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 13 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal 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; AF019039; AAB83973.1; -; mRNA.
DR EMBL; AF007748; AAB71349.1; -; mRNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84300.1; -; Genomic_DNA.
DR EMBL; BC072420; AAH72420.1; -; mRNA.
DR RefSeq; NP_001129667.1; NM_001136195.1.
DR RefSeq; NP_001129668.1; NM_001136196.1.
DR RefSeq; NP_038461.2; NM_013433.4.
DR RefSeq; XP_005259936.1; XM_005259879.1.
DR RefSeq; XP_005259937.1; XM_005259880.1.
DR RefSeq; XP_005259938.1; XM_005259881.1.
DR RefSeq; XP_005259939.1; XM_005259882.1.
DR UniGene; Hs.416049; -.
DR UniGene; Hs.714402; -.
DR ProteinModelPortal; O14787; -.
DR SMR; O14787; 3-896.
DR IntAct; O14787; 5.
DR MINT; MINT-2998321; -.
DR STRING; 9606.ENSP00000397379; -.
DR PhosphoSite; O14787; -.
DR PaxDb; O14787; -.
DR PRIDE; O14787; -.
DR Ensembl; ENST00000356861; ENSP00000349321; ENSG00000105576.
DR Ensembl; ENST00000425528; ENSP00000407182; ENSG00000105576.
DR Ensembl; ENST00000441499; ENSP00000389648; ENSG00000105576.
DR Ensembl; ENST00000450764; ENSP00000397379; ENSG00000105576.
DR Ensembl; ENST00000588216; ENSP00000465625; ENSG00000105576.
DR Ensembl; ENST00000592287; ENSP00000468434; ENSG00000105576.
DR GeneID; 30000; -.
DR KEGG; hsa:30000; -.
DR UCSC; uc002muo.3; human.
DR CTD; 30000; -.
DR GeneCards; GC19M012810; -.
DR HGNC; HGNC:19998; TNPO2.
DR HPA; CAB046446; -.
DR MIM; 603002; gene.
DR neXtProt; NX_O14787; -.
DR PharmGKB; PA134921349; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000203940; -.
DR HOVERGEN; HBG058963; -.
DR InParanoid; O14787; -.
DR OMA; VRRHVCQ; -.
DR OrthoDB; EOG7XM2X0; -.
DR PhylomeDB; O14787; -.
DR ChiTaRS; TNPO2; human.
DR GeneWiki; TNPO2; -.
DR GenomeRNAi; 30000; -.
DR NextBio; 52812; -.
DR PRO; PR:O14787; -.
DR ArrayExpress; O14787; -.
DR Bgee; O14787; -.
DR CleanEx; HS_TNPO2; -.
DR Genevestigator; O14787; -.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0008139; F:nuclear localization sequence binding; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; FALSE_NEG.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Nucleus; Polymorphism; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1 897 Transportin-2.
FT /FTId=PRO_0000120767.
FT DOMAIN 31 99 Importin N-terminal.
FT REPEAT 121 159 HEAT 1.
FT REPEAT 167 205 HEAT 2.
FT REPEAT 208 246 HEAT 3.
FT REPEAT 249 287 HEAT 4.
FT REPEAT 292 330 HEAT 5.
FT REPEAT 389 427 HEAT 6.
FT REPEAT 430 468 HEAT 7.
FT REPEAT 472 510 HEAT 8.
FT REPEAT 513 551 HEAT 9.
FT REPEAT 556 596 HEAT 10.
FT REPEAT 659 697 HEAT 11.
FT REPEAT 700 738 HEAT 12.
FT REPEAT 741 780 HEAT 13.
FT MOD_RES 862 862 N6-acetyllysine.
FT VAR_SEQ 769 778 Missing (in isoform 2).
FT /FTId=VSP_009657.
FT VARIANT 370 370 W -> C (found in a patient with severely
FT delayed development, autism, myopia,
FT strabismus and some dysmorphisms).
FT /FTId=VAR_069373.
FT CONFLICT 28 28 Q -> H (in Ref. 2; AAB71349).
FT CONFLICT 32 32 Q -> R (in Ref. 2; AAB71349).
FT CONFLICT 194 194 A -> G (in Ref. 2; AAB71349).
FT CONFLICT 398 401 LLKG -> YQS (in Ref. 1; AAB83973).
FT CONFLICT 492 492 R -> K (in Ref. 2; AAB71349).
FT CONFLICT 499 499 S -> I (in Ref. 2; AAB71349).
FT CONFLICT 507 507 E -> K (in Ref. 2; AAB71349).
FT CONFLICT 608 608 R -> C (in Ref. 2; AAB71349).
FT CONFLICT 645 645 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 646 646 S -> T (in Ref. 1; AAB83973).
FT CONFLICT 656 656 V -> L (in Ref. 1; AAB83973).
FT CONFLICT 687 687 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 691 691 L -> F (in Ref. 2; AAB71349).
FT CONFLICT 696 697 FI -> SS (in Ref. 2; AAB71349).
FT CONFLICT 717 717 E -> K (in Ref. 1; AAB83973).
FT CONFLICT 812 812 R -> Q (in Ref. 1; AAB83973).
FT CONFLICT 841 841 F -> L (in Ref. 2; AAB71349).
SQ SEQUENCE 897 AA; 101388 MW; 26FE455583D7D35F CRC64;
MDWQPDEQGL QQVLQLLKDS QSPNTATQRI VQDKLKQLNQ FPDFNNYLIF VLTRLKSEDE
PTRSLSGLIL KNNVKAHYQS FPPPVADFIK QECLNNIGDA SSLIRATIGI LITTIASKGE
LQMWPELLPQ LCNLLNSEDY NTCEGAFGAL QKICEDSSEL LDSDALNRPL NIMIPKFLQF
FKHCSPKIRS HAIACVNQFI MDRAQALMDN IDTFIEHLFA LAVDDDPEVR KNVCRALVML
LEVRIDRLIP HMHSIIQYML QRTQDHDENV ALEACEFWLT LAEQPICKEV LASHLVQLIP
ILVNGMKYSE IDIILLKGDV EEDEAVPDSE QDIKPRFHKS RTVTLPHEAE RPDGSEDAED
DDDDDALSDW NLRKCSAAAL DVLANVFREE LLPHLLPLLK GLLFHPEWVV KESGILVLGA
IAEGCMQGMV PYLPELIPHL IQCLSDKKAL VRSIACWTLS RYAHWVVSQP PDMHLKPLMT
ELLKRILDGN KRVQEAACSA FATLEEEACT ELVPYLSYIL DTLVFAFGKY QHKNLLILYD
AIGTLADSVG HHLNQPEYIQ KLMPPLIQKW NELKDEDKDL FPLLECLSSV ATALQSGFLP
YCEPVYQRCV TLVQKTLAQA MMYTQHPEQY EAPDKDFMIV ALDLLSGLAE GLGGHVEQLV
ARSNIMTLLF QCMQDSMPEV RQSSFALLGD LTKACFIHVK PCIAEFMPIL GTNLNPEFIS
VCNNATWAIG EICMQMGAEM QPYVQMVLNN LVEIINRPNT PKTLLENTGR LTSPSAIPAI
TIGRLGYVCP QEVAPMLQQF IRPWCTSLRN IRDNEEKDSA FRGICMMIGV NPGGVVQDFI
FFCDAVASWV SPKDDLRDMF YKILHGFKDQ VGEDNWQQFS EQFPPLLKER LAAFYGV
//
MIM
603002
*RECORD*
*FIELD* NO
603002
*FIELD* TI
*603002 TRANSPORTIN 2; TNPO2
;;TRN2;;
KARYOPHERIN BETA-2B; KPNB2B
*FIELD* TX
CLONING
read more
Transportin-1 (KPNB2; 602901) interacts directly and specifically with
M9, the bidirectional transport signal of the nuclear shuttling protein
hnRNPA1 (164017) and mediates hnRNPA1 nuclear import. In the course of
isolating additional transportin-1 cDNAs, Siomi et al. (1997) isolated
cDNAs encoding a related protein that they designated 'transportin-2.'
The sequence of the predicted 894-amino acid protein shares 84% identity
with that of transportin-1. One notable difference is that transportin-2
contains a short extra sequence within the region corresponding to the
M9-interacting domain of transportin-1. Far Western blotting showed that
transportin-2 and transportin-1 have different substrate specificities.
Siomi et al. (1997) suggested that the insert in transportin-2 modifies
its interaction with import substrates.
GENE FUNCTION
Transport of macromolecules between the cell nucleus and cytoplasm
occurs through the nuclear pores and is mediated by soluble carriers
known as karyopherins, transportins, importins, or exportins. Shamsher
et al. (2002) found that transportin-2 forms complexes with the mRNA
export factor TAP (NXF1; 602647) that strictly depend on the presence of
RanGTP. The data supported the conclusion that transportin-2
participates directly in the export of a large proportion of cellular
mRNAs, and that TAP connects transportin-2 to mRNAs to be exported.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TRN2
gene to chromosome 19 (TMAP WI-30101).
*FIELD* RF
1. Shamsher, M. K.; Ploski, J.; Radu, A.: Karyopherin beta-2B participates
in mRNA export from the nucleus. Proc. Nat. Acad. Sci. 99: 14195-14199,
2002.
2. Siomi, M. C.; Eder, P. S.; Kataoka, N.; Wan, L.; Liu, Q.; Dreyfuss,
G.: Transportin-mediated nuclear import of heterogeneous nuclear
RNP proteins. J. Cell Biol. 138: 1181-1192, 1997.
*FIELD* CN
Victor A. McKusick - updated: 12/13/2002
Carol A. Bocchini - updated: 10/12/2001
*FIELD* CD
Rebekah S. Rasooly: 8/26/1998
*FIELD* ED
wwang: 06/11/2008
mgross: 4/7/2006
tkritzer: 12/17/2002
terry: 12/13/2002
carol: 10/12/2001
alopez: 8/27/1998
*RECORD*
*FIELD* NO
603002
*FIELD* TI
*603002 TRANSPORTIN 2; TNPO2
;;TRN2;;
KARYOPHERIN BETA-2B; KPNB2B
*FIELD* TX
CLONING
read more
Transportin-1 (KPNB2; 602901) interacts directly and specifically with
M9, the bidirectional transport signal of the nuclear shuttling protein
hnRNPA1 (164017) and mediates hnRNPA1 nuclear import. In the course of
isolating additional transportin-1 cDNAs, Siomi et al. (1997) isolated
cDNAs encoding a related protein that they designated 'transportin-2.'
The sequence of the predicted 894-amino acid protein shares 84% identity
with that of transportin-1. One notable difference is that transportin-2
contains a short extra sequence within the region corresponding to the
M9-interacting domain of transportin-1. Far Western blotting showed that
transportin-2 and transportin-1 have different substrate specificities.
Siomi et al. (1997) suggested that the insert in transportin-2 modifies
its interaction with import substrates.
GENE FUNCTION
Transport of macromolecules between the cell nucleus and cytoplasm
occurs through the nuclear pores and is mediated by soluble carriers
known as karyopherins, transportins, importins, or exportins. Shamsher
et al. (2002) found that transportin-2 forms complexes with the mRNA
export factor TAP (NXF1; 602647) that strictly depend on the presence of
RanGTP. The data supported the conclusion that transportin-2
participates directly in the export of a large proportion of cellular
mRNAs, and that TAP connects transportin-2 to mRNAs to be exported.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the TRN2
gene to chromosome 19 (TMAP WI-30101).
*FIELD* RF
1. Shamsher, M. K.; Ploski, J.; Radu, A.: Karyopherin beta-2B participates
in mRNA export from the nucleus. Proc. Nat. Acad. Sci. 99: 14195-14199,
2002.
2. Siomi, M. C.; Eder, P. S.; Kataoka, N.; Wan, L.; Liu, Q.; Dreyfuss,
G.: Transportin-mediated nuclear import of heterogeneous nuclear
RNP proteins. J. Cell Biol. 138: 1181-1192, 1997.
*FIELD* CN
Victor A. McKusick - updated: 12/13/2002
Carol A. Bocchini - updated: 10/12/2001
*FIELD* CD
Rebekah S. Rasooly: 8/26/1998
*FIELD* ED
wwang: 06/11/2008
mgross: 4/7/2006
tkritzer: 12/17/2002
terry: 12/13/2002
carol: 10/12/2001
alopez: 8/27/1998