Full text data of KPNA6
KPNA6
(IPOA7)
[Confidence: low (only semi-automatic identification from reviews)]
Importin subunit alpha-7 (Karyopherin subunit alpha-6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin subunit alpha-7 (Karyopherin subunit alpha-6)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O60684
ID IMA7_HUMAN Reviewed; 536 AA.
AC O60684; B2RDC7; D3DPP5; Q5VVU3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Importin subunit alpha-7;
DE AltName: Full=Karyopherin subunit alpha-6;
GN Name=KPNA6; Synonyms=IPOA7;
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], FUNCTION, INTERACTION WITH KPNB1, AND
RP TISSUE SPECIFICITY.
RX PubMed=10523667;
RA Koehler M., Speck C., Christiansen M., Bischoff F.R., Prehn S.,
RA Haller H., Goerlich D., Hartmann E.;
RT "Evidence for distinct substrate specificities of importin alpha
RT family members in nuclear protein import.";
RL Mol. Cell. Biol. 19:7782-7791(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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.,
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter
CC protein for nuclear receptor KPNB1. Binds specifically and
CC directly to substrates containing either a simple or bipartite NLS
CC motif. Docking of the importin/substrate complex to the nuclear
CC pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus.
CC -!- SUBUNIT: Interacts with ZIC3 (By similarity). Forms a complex with
CC importin subunit beta-1.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the importin alpha family.
CC -!- SIMILARITY: Contains 10 ARM repeats.
CC -!- SIMILARITY: Contains 1 IBB domain.
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DR EMBL; AF060543; AAC15233.1; -; mRNA.
DR EMBL; AK315490; BAG37874.1; -; mRNA.
DR EMBL; BT009843; AAP88845.1; -; mRNA.
DR EMBL; AL445248; CAH71948.1; -; Genomic_DNA.
DR EMBL; AL049795; CAH71948.1; JOINED; Genomic_DNA.
DR EMBL; AL049795; CAI22056.1; -; Genomic_DNA.
DR EMBL; AL445248; CAI22056.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07567.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07568.1; -; Genomic_DNA.
DR EMBL; BC020520; AAH20520.1; -; mRNA.
DR RefSeq; NP_036448.1; NM_012316.4.
DR UniGene; Hs.470588; -.
DR UniGene; Hs.711019; -.
DR ProteinModelPortal; O60684; -.
DR SMR; O60684; 32-506.
DR DIP; DIP-27609N; -.
DR IntAct; O60684; 14.
DR MINT; MINT-1144956; -.
DR STRING; 9606.ENSP00000362728; -.
DR PhosphoSite; O60684; -.
DR PaxDb; O60684; -.
DR PRIDE; O60684; -.
DR DNASU; 23633; -.
DR Ensembl; ENST00000373625; ENSP00000362728; ENSG00000025800.
DR GeneID; 23633; -.
DR KEGG; hsa:23633; -.
DR UCSC; uc001bug.3; human.
DR CTD; 23633; -.
DR GeneCards; GC01P032573; -.
DR HGNC; HGNC:6399; KPNA6.
DR HPA; HPA018863; -.
DR MIM; 610563; gene.
DR neXtProt; NX_O60684; -.
DR PharmGKB; PA30190; -.
DR eggNOG; COG5064; -.
DR HOVERGEN; HBG001846; -.
DR InParanoid; O60684; -.
DR PhylomeDB; O60684; -.
DR SignaLink; O60684; -.
DR ChiTaRS; KPNA6; human.
DR GeneWiki; KPNA6; -.
DR GenomeRNAi; 23633; -.
DR NextBio; 46411; -.
DR PRO; PR:O60684; -.
DR ArrayExpress; O60684; -.
DR Bgee; O60684; -.
DR CleanEx; HS_KPNA6; -.
DR Genevestigator; O60684; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR024931; Importing_su_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 536 Importin subunit alpha-7.
FT /FTId=PRO_0000120729.
FT DOMAIN 1 60 IBB.
FT REPEAT 76 115 ARM 1; truncated.
FT REPEAT 116 159 ARM 2.
FT REPEAT 160 204 ARM 3.
FT REPEAT 205 243 ARM 4.
FT REPEAT 244 288 ARM 5.
FT REPEAT 289 328 ARM 6.
FT REPEAT 329 370 ARM 7.
FT REPEAT 371 410 ARM 8.
FT REPEAT 411 453 ARM 9.
FT REPEAT 457 502 ARM 10; atypical.
FT REGION 147 239 NLS binding site (major) (By similarity).
FT REGION 316 404 NLS binding site (minor) (By similarity).
FT MOTIF 45 54 Nuclear localization signal (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 Phosphoserine.
SQ SEQUENCE 536 AA; 60030 MW; 9D0E27482B9BDED3 CRC64;
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
NTPRVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
EDVQEQAVWA LGNIAGDSSV CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSPKE SIRKEACWTI
SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQEGKRSG SGVNPYCGLI EEAYGLDKIE
FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
//
ID IMA7_HUMAN Reviewed; 536 AA.
AC O60684; B2RDC7; D3DPP5; Q5VVU3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Importin subunit alpha-7;
DE AltName: Full=Karyopherin subunit alpha-6;
GN Name=KPNA6; Synonyms=IPOA7;
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], FUNCTION, INTERACTION WITH KPNB1, AND
RP TISSUE SPECIFICITY.
RX PubMed=10523667;
RA Koehler M., Speck C., Christiansen M., Bischoff F.R., Prehn S.,
RA Haller H., Goerlich D., Hartmann E.;
RT "Evidence for distinct substrate specificities of importin alpha
RT family members in nuclear protein import.";
RL Mol. Cell. Biol. 19:7782-7791(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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.,
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter
CC protein for nuclear receptor KPNB1. Binds specifically and
CC directly to substrates containing either a simple or bipartite NLS
CC motif. Docking of the importin/substrate complex to the nuclear
CC pore complex (NPC) is mediated by KPNB1 through binding to
CC nucleoporin FxFG repeats and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC between the cytoplasm and nucleus.
CC -!- SUBUNIT: Interacts with ZIC3 (By similarity). Forms a complex with
CC importin subunit beta-1.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the importin alpha family.
CC -!- SIMILARITY: Contains 10 ARM repeats.
CC -!- SIMILARITY: Contains 1 IBB domain.
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DR EMBL; AF060543; AAC15233.1; -; mRNA.
DR EMBL; AK315490; BAG37874.1; -; mRNA.
DR EMBL; BT009843; AAP88845.1; -; mRNA.
DR EMBL; AL445248; CAH71948.1; -; Genomic_DNA.
DR EMBL; AL049795; CAH71948.1; JOINED; Genomic_DNA.
DR EMBL; AL049795; CAI22056.1; -; Genomic_DNA.
DR EMBL; AL445248; CAI22056.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07567.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07568.1; -; Genomic_DNA.
DR EMBL; BC020520; AAH20520.1; -; mRNA.
DR RefSeq; NP_036448.1; NM_012316.4.
DR UniGene; Hs.470588; -.
DR UniGene; Hs.711019; -.
DR ProteinModelPortal; O60684; -.
DR SMR; O60684; 32-506.
DR DIP; DIP-27609N; -.
DR IntAct; O60684; 14.
DR MINT; MINT-1144956; -.
DR STRING; 9606.ENSP00000362728; -.
DR PhosphoSite; O60684; -.
DR PaxDb; O60684; -.
DR PRIDE; O60684; -.
DR DNASU; 23633; -.
DR Ensembl; ENST00000373625; ENSP00000362728; ENSG00000025800.
DR GeneID; 23633; -.
DR KEGG; hsa:23633; -.
DR UCSC; uc001bug.3; human.
DR CTD; 23633; -.
DR GeneCards; GC01P032573; -.
DR HGNC; HGNC:6399; KPNA6.
DR HPA; HPA018863; -.
DR MIM; 610563; gene.
DR neXtProt; NX_O60684; -.
DR PharmGKB; PA30190; -.
DR eggNOG; COG5064; -.
DR HOVERGEN; HBG001846; -.
DR InParanoid; O60684; -.
DR PhylomeDB; O60684; -.
DR SignaLink; O60684; -.
DR ChiTaRS; KPNA6; human.
DR GeneWiki; KPNA6; -.
DR GenomeRNAi; 23633; -.
DR NextBio; 46411; -.
DR PRO; PR:O60684; -.
DR ArrayExpress; O60684; -.
DR Bgee; O60684; -.
DR CleanEx; HS_KPNA6; -.
DR Genevestigator; O60684; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0008565; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; TAS:ProtInc.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR024931; Importing_su_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1 536 Importin subunit alpha-7.
FT /FTId=PRO_0000120729.
FT DOMAIN 1 60 IBB.
FT REPEAT 76 115 ARM 1; truncated.
FT REPEAT 116 159 ARM 2.
FT REPEAT 160 204 ARM 3.
FT REPEAT 205 243 ARM 4.
FT REPEAT 244 288 ARM 5.
FT REPEAT 289 328 ARM 6.
FT REPEAT 329 370 ARM 7.
FT REPEAT 371 410 ARM 8.
FT REPEAT 411 453 ARM 9.
FT REPEAT 457 502 ARM 10; atypical.
FT REGION 147 239 NLS binding site (major) (By similarity).
FT REGION 316 404 NLS binding site (minor) (By similarity).
FT MOTIF 45 54 Nuclear localization signal (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 Phosphoserine.
SQ SEQUENCE 536 AA; 60030 MW; 9D0E27482B9BDED3 CRC64;
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
NTPRVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
EDVQEQAVWA LGNIAGDSSV CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSPKE SIRKEACWTI
SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQEGKRSG SGVNPYCGLI EEAYGLDKIE
FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
//
MIM
610563
*RECORD*
*FIELD* NO
610563
*FIELD* TI
*610563 KARYOPHERIN ALPHA-6; KPNA6
;;IMPORTIN ALPHA-7
*FIELD* TX
DESCRIPTION
Importin alpha proteins, such as KPNA6, play a pivotal role in the
read moreclassical nuclear protein import pathway. Importin alpha shuttles
between the nucleus and cytoplasm, binds nuclear localization
signal-bearing proteins, and functions as an adaptor to access the
importin beta (see KPNB1, 602738)-dependent import pathway (Kohler et
al., 1999).
CLONING
By searching a database for sequences similar to mouse importin
alpha-S2, followed by 5-prime RACE of a HeLa cell cDNA library, Kohler
et al. (1999) cloned KPNA6, which they called importin alpha-7. The
deduced 536-amino acid protein shares a high degree of identity with
KPNA5 (604545). Northern blot analysis detected an 8-kb transcript in
all tissues examined except thymus, with highest expression in skeletal
muscle. Western blot analysis detected the protein in all tissues
examined.
GENE FUNCTION
Using an in vitro import assay based on permeabilized HeLa cells to
study the import substrate specificity of all ubiquitously expressed
importins, including KPNA6, Kohler et al. (1999) found that all
importins tested were able to transport HNRNPK (600712) and PCAF
(602303), in addition to the standard test substrates, but only KPNA4
(601892) showed a strong preference for the import of GDP/GTP exchange
factor RCC1 (179710), which is exclusively located inside the nucleus.
When HNRNPK, PCAF, and RCC1 were offered with a competing substrate
nucleoplasmin (164040), they found that substrate binding was diminished
or abolished in some importins and retained in others.
By Western blot analysis and in vitro binding assays, Ma and Cao (2006)
found that nuclear translocation of STAT3 (102582) and STAT1 (600555) is
mediated by binding of human KPNA1 (600686) and KPNA6.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the KPNA6
gene to chromosome 1 (TMAP SHGC-74534).
*FIELD* RF
1. Kohler, M.; Speck, C.; Christiansen, M.; Bischoff, F. R.; Prehn,
S.; Haller, H.; Gorlich, D.; Hartmann, E.: Evidence for distinct
substrate specificities of importin alpha family members in nuclear
protein import. Molec. Cell. Biol. 19: 7782-7791, 1999.
2. Ma, J.; Cao, X.: Regulation of Stat3 nuclear import by importin
alpha-5 and importin alpha-7 via two different functional sequence
elements. Cell. Signal. 18: 1117-1126, 2006.
*FIELD* CD
Patricia A. Hartz: 11/14/2006
*FIELD* ED
wwang: 03/23/2007
wwang: 11/14/2006
*RECORD*
*FIELD* NO
610563
*FIELD* TI
*610563 KARYOPHERIN ALPHA-6; KPNA6
;;IMPORTIN ALPHA-7
*FIELD* TX
DESCRIPTION
Importin alpha proteins, such as KPNA6, play a pivotal role in the
read moreclassical nuclear protein import pathway. Importin alpha shuttles
between the nucleus and cytoplasm, binds nuclear localization
signal-bearing proteins, and functions as an adaptor to access the
importin beta (see KPNB1, 602738)-dependent import pathway (Kohler et
al., 1999).
CLONING
By searching a database for sequences similar to mouse importin
alpha-S2, followed by 5-prime RACE of a HeLa cell cDNA library, Kohler
et al. (1999) cloned KPNA6, which they called importin alpha-7. The
deduced 536-amino acid protein shares a high degree of identity with
KPNA5 (604545). Northern blot analysis detected an 8-kb transcript in
all tissues examined except thymus, with highest expression in skeletal
muscle. Western blot analysis detected the protein in all tissues
examined.
GENE FUNCTION
Using an in vitro import assay based on permeabilized HeLa cells to
study the import substrate specificity of all ubiquitously expressed
importins, including KPNA6, Kohler et al. (1999) found that all
importins tested were able to transport HNRNPK (600712) and PCAF
(602303), in addition to the standard test substrates, but only KPNA4
(601892) showed a strong preference for the import of GDP/GTP exchange
factor RCC1 (179710), which is exclusively located inside the nucleus.
When HNRNPK, PCAF, and RCC1 were offered with a competing substrate
nucleoplasmin (164040), they found that substrate binding was diminished
or abolished in some importins and retained in others.
By Western blot analysis and in vitro binding assays, Ma and Cao (2006)
found that nuclear translocation of STAT3 (102582) and STAT1 (600555) is
mediated by binding of human KPNA1 (600686) and KPNA6.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the KPNA6
gene to chromosome 1 (TMAP SHGC-74534).
*FIELD* RF
1. Kohler, M.; Speck, C.; Christiansen, M.; Bischoff, F. R.; Prehn,
S.; Haller, H.; Gorlich, D.; Hartmann, E.: Evidence for distinct
substrate specificities of importin alpha family members in nuclear
protein import. Molec. Cell. Biol. 19: 7782-7791, 1999.
2. Ma, J.; Cao, X.: Regulation of Stat3 nuclear import by importin
alpha-5 and importin alpha-7 via two different functional sequence
elements. Cell. Signal. 18: 1117-1126, 2006.
*FIELD* CD
Patricia A. Hartz: 11/14/2006
*FIELD* ED
wwang: 03/23/2007
wwang: 11/14/2006