Full text data of C11orf73
C11orf73
[Confidence: low (only semi-automatic identification from reviews)]
Protein Hikeshi
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein Hikeshi
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q53FT3
ID HIKES_HUMAN Reviewed; 197 AA.
AC Q53FT3; Q8WVE8; Q9NVQ2; Q9NZZ1; Q9P022; Q9P0N1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=Protein Hikeshi;
GN Name=C11orf73; ORFNames=HSPC138, HSPC179, HSPC248;
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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].
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-47.
RC TISSUE=Brain, and 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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP INTERACTION WITH NUP62; NUP153 AND HSP70 PROTEINS, AND INDUCTION.
RX PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
RA Kose S., Furuta M., Imamoto N.;
RT "Hikeshi, a nuclear import carrier for hsp70s, protects cells from
RT heat shock-induced nuclear damage.";
RL Cell 149:578-589(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Acts as a specific nuclear import carrier for HSP70
CC proteins following heat-shock stress: acts by mediating the
CC nucleoporin-dependent translocation of ATP-bound HSP70 proteins
CC into the nucleus. HSP70 proteins import is required to protect
CC cells from heat shock damages. Does not translocate ADP-bound
CC HSP70 proteins into the nucleus.
CC -!- SUBUNIT: Interacts with ATP-bound HSP70 proteins. Interacts with
CC NUP62 and NUP153 (via F-X-F-G repeats).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC -!- INDUCTION: Following heat-shock treatment.
CC -!- MISCELLANEOUS: 'Hikeshi' is a traditional Japanese compound word
CC used for a firefighter, smokejumper, or troubleshooter
CC (PubMed:22541429).
CC -!- SIMILARITY: Belongs to the OPI10 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29102.1; Type=Frameshift; Positions=62, 68;
CC Sequence=AAF29142.1; Type=Frameshift; Positions=9, 57;
CC Sequence=AAF36168.1; Type=Frameshift; Positions=67;
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; AF151082; AAF36168.1; ALT_FRAME; mRNA.
DR EMBL; AF161487; AAF29102.1; ALT_FRAME; mRNA.
DR EMBL; AF161527; AAF29142.1; ALT_FRAME; mRNA.
DR EMBL; AK001447; BAA91698.1; -; mRNA.
DR EMBL; AK223198; BAD96918.1; -; mRNA.
DR EMBL; BC001677; AAH01677.1; -; mRNA.
DR EMBL; BC006476; AAH06476.1; -; mRNA.
DR EMBL; BC015991; AAH15991.1; -; mRNA.
DR EMBL; BC018080; AAH18080.1; -; mRNA.
DR EMBL; BC021621; AAH21621.1; -; mRNA.
DR RefSeq; NP_057485.2; NM_016401.3.
DR UniGene; Hs.283322; -.
DR ProteinModelPortal; Q53FT3; -.
DR IntAct; Q53FT3; 5.
DR MINT; MINT-3047121; -.
DR STRING; 9606.ENSP00000278483; -.
DR DMDM; 110278911; -.
DR PaxDb; Q53FT3; -.
DR PRIDE; Q53FT3; -.
DR DNASU; 51501; -.
DR Ensembl; ENST00000278483; ENSP00000278483; ENSG00000149196.
DR GeneID; 51501; -.
DR KEGG; hsa:51501; -.
DR UCSC; uc001pbu.3; human.
DR CTD; 51501; -.
DR GeneCards; GC11P086013; -.
DR HGNC; HGNC:26938; C11orf73.
DR HPA; HPA035063; -.
DR MIM; 614908; gene.
DR neXtProt; NX_Q53FT3; -.
DR PharmGKB; PA144596492; -.
DR eggNOG; NOG328354; -.
DR HOGENOM; HOG000175561; -.
DR HOVERGEN; HBG081226; -.
DR InParanoid; Q53FT3; -.
DR OMA; NPNFWKS; -.
DR PhylomeDB; Q53FT3; -.
DR GeneWiki; C11orf73; -.
DR GenomeRNAi; 51501; -.
DR NextBio; 55179; -.
DR ArrayExpress; Q53FT3; -.
DR Bgee; Q53FT3; -.
DR CleanEx; HS_C11orf73; -.
DR Genevestigator; Q53FT3; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR InterPro; IPR008493; DUF775.
DR PANTHER; PTHR12925; PTHR12925; 1.
DR Pfam; PF05603; DUF775; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Nucleus; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 197 Protein Hikeshi.
FT /FTId=PRO_0000245262.
FT VARIANT 47 47 P -> A (in dbSNP:rs11539213).
FT /FTId=VAR_026968.
FT CONFLICT 82 82 F -> L (in Ref. 1; AAF29102 and 3;
FT BAD96918).
SQ SEQUENCE 197 AA; 21628 MW; 4FA524439B630511 CRC64;
MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ESINHVVVFM LGTIPFPEGM GGSVYFSYPD
SNGMPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM NIVRTPSVAQ IGISVELLDS
MAQQTPVGNA AVSSVDSFTQ FTQKMLDNFY NFASSFAVSQ AQMTPSPSEM FIPANVVLKW
YENFQRRLAQ NPLFWKT
//
ID HIKES_HUMAN Reviewed; 197 AA.
AC Q53FT3; Q8WVE8; Q9NVQ2; Q9NZZ1; Q9P022; Q9P0N1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 70.
DE RecName: Full=Protein Hikeshi;
GN Name=C11orf73; ORFNames=HSPC138, HSPC179, HSPC248;
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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].
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-47.
RC TISSUE=Brain, and 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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP INTERACTION WITH NUP62; NUP153 AND HSP70 PROTEINS, AND INDUCTION.
RX PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
RA Kose S., Furuta M., Imamoto N.;
RT "Hikeshi, a nuclear import carrier for hsp70s, protects cells from
RT heat shock-induced nuclear damage.";
RL Cell 149:578-589(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Acts as a specific nuclear import carrier for HSP70
CC proteins following heat-shock stress: acts by mediating the
CC nucleoporin-dependent translocation of ATP-bound HSP70 proteins
CC into the nucleus. HSP70 proteins import is required to protect
CC cells from heat shock damages. Does not translocate ADP-bound
CC HSP70 proteins into the nucleus.
CC -!- SUBUNIT: Interacts with ATP-bound HSP70 proteins. Interacts with
CC NUP62 and NUP153 (via F-X-F-G repeats).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC -!- INDUCTION: Following heat-shock treatment.
CC -!- MISCELLANEOUS: 'Hikeshi' is a traditional Japanese compound word
CC used for a firefighter, smokejumper, or troubleshooter
CC (PubMed:22541429).
CC -!- SIMILARITY: Belongs to the OPI10 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29102.1; Type=Frameshift; Positions=62, 68;
CC Sequence=AAF29142.1; Type=Frameshift; Positions=9, 57;
CC Sequence=AAF36168.1; Type=Frameshift; Positions=67;
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; AF151082; AAF36168.1; ALT_FRAME; mRNA.
DR EMBL; AF161487; AAF29102.1; ALT_FRAME; mRNA.
DR EMBL; AF161527; AAF29142.1; ALT_FRAME; mRNA.
DR EMBL; AK001447; BAA91698.1; -; mRNA.
DR EMBL; AK223198; BAD96918.1; -; mRNA.
DR EMBL; BC001677; AAH01677.1; -; mRNA.
DR EMBL; BC006476; AAH06476.1; -; mRNA.
DR EMBL; BC015991; AAH15991.1; -; mRNA.
DR EMBL; BC018080; AAH18080.1; -; mRNA.
DR EMBL; BC021621; AAH21621.1; -; mRNA.
DR RefSeq; NP_057485.2; NM_016401.3.
DR UniGene; Hs.283322; -.
DR ProteinModelPortal; Q53FT3; -.
DR IntAct; Q53FT3; 5.
DR MINT; MINT-3047121; -.
DR STRING; 9606.ENSP00000278483; -.
DR DMDM; 110278911; -.
DR PaxDb; Q53FT3; -.
DR PRIDE; Q53FT3; -.
DR DNASU; 51501; -.
DR Ensembl; ENST00000278483; ENSP00000278483; ENSG00000149196.
DR GeneID; 51501; -.
DR KEGG; hsa:51501; -.
DR UCSC; uc001pbu.3; human.
DR CTD; 51501; -.
DR GeneCards; GC11P086013; -.
DR HGNC; HGNC:26938; C11orf73.
DR HPA; HPA035063; -.
DR MIM; 614908; gene.
DR neXtProt; NX_Q53FT3; -.
DR PharmGKB; PA144596492; -.
DR eggNOG; NOG328354; -.
DR HOGENOM; HOG000175561; -.
DR HOVERGEN; HBG081226; -.
DR InParanoid; Q53FT3; -.
DR OMA; NPNFWKS; -.
DR PhylomeDB; Q53FT3; -.
DR GeneWiki; C11orf73; -.
DR GenomeRNAi; 51501; -.
DR NextBio; 55179; -.
DR ArrayExpress; Q53FT3; -.
DR Bgee; Q53FT3; -.
DR CleanEx; HS_C11orf73; -.
DR Genevestigator; Q53FT3; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR InterPro; IPR008493; DUF775.
DR PANTHER; PTHR12925; PTHR12925; 1.
DR Pfam; PF05603; DUF775; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Nucleus; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 197 Protein Hikeshi.
FT /FTId=PRO_0000245262.
FT VARIANT 47 47 P -> A (in dbSNP:rs11539213).
FT /FTId=VAR_026968.
FT CONFLICT 82 82 F -> L (in Ref. 1; AAF29102 and 3;
FT BAD96918).
SQ SEQUENCE 197 AA; 21628 MW; 4FA524439B630511 CRC64;
MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ESINHVVVFM LGTIPFPEGM GGSVYFSYPD
SNGMPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM NIVRTPSVAQ IGISVELLDS
MAQQTPVGNA AVSSVDSFTQ FTQKMLDNFY NFASSFAVSQ AQMTPSPSEM FIPANVVLKW
YENFQRRLAQ NPLFWKT
//
MIM
614908
*RECORD*
*FIELD* NO
614908
*FIELD* TI
*614908 CHROMOSOME 11 OPEN READING FRAME 73; C11ORF73
;;HIKESHI
*FIELD* TX
DESCRIPTION
read more
Hikeshi functions as a nuclear import carrier for heat-shock proteins
(Kose et al., 2012).
CLONING
Using liquid chromatography tandem mass spectrometry to identify a
protein involved in nuclear import of HSC70 (HSPA8; 600816) in
heat-shocked HeLa cells, followed by PCR of a HeLa cell cDNA library,
Kose et al. (2012) cloned C11ORF73. They renamed the deduced 197-amino
acid C11ORF73 protein Hikeshi after the Japanese Edo era compound word
for firefighter, smokejumper, or troubleshooter. Database analysis
revealed conservation of Hikeshi from yeast to humans.
GENE FUNCTION
Kose et al. (2012) found that heat stress induced expression of Hikeshi
and heat-shock proteins of the Hsp70 family (see 140550) in HeLa cells.
Depletion of Hikeshi had no effect on the ability of cells to mount a
response to heat stress, but it delayed cellular recovery after removal
of heat stress and reduced cell viability. Protein pull-down assays
showed that Hikeshi efficiently interacted with ATP-bound HSP70s, but
not ADP-bound HSP70s. Hikeshi mediated HSP70 import in an importin (see
602738)-independent manner. HSP110 (HSPH1; 610703), which functions as a
nucleotide exchange factor for HSP70, was required for interaction of
Hikeshi with HSP70. HSP40 (DNAJB1; 604572) inhibited interaction of
Hikeshi with HSP70 and countered Hikeshi-dependent HSP70 nuclear import.
Hikeshi also interacted human NUP62 (605815) and rat Nup153 (603948),
which are components of the nuclear pore. Kose et al. (2012)
hypothesized that Hikeshi functions during the HSP70 ATPase cycle and
recognizes ATP-bound HSP70 in the cytoplasm and releases ADP-bound HSP70
in the nucleus in conjunction with HSP110.
MAPPING
Hartz (2012) mapped the C11ORF73 gene to chromosome 11q14.2 based on an
alignment of the C11ORF73 sequence (GenBank GENBANK AF161487) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/19/2012.
2. Kose, S.; Furuta, M.; Imamoto, N.: Hikeshi, a nuclear import carrier
for Hsp70s, protects cells from heat shock-induced nuclear damage. Cell 149:
578-589, 2012.
*FIELD* CD
Patricia A. Hartz: 11/2/2012
*FIELD* ED
mgross: 11/02/2012
*RECORD*
*FIELD* NO
614908
*FIELD* TI
*614908 CHROMOSOME 11 OPEN READING FRAME 73; C11ORF73
;;HIKESHI
*FIELD* TX
DESCRIPTION
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Hikeshi functions as a nuclear import carrier for heat-shock proteins
(Kose et al., 2012).
CLONING
Using liquid chromatography tandem mass spectrometry to identify a
protein involved in nuclear import of HSC70 (HSPA8; 600816) in
heat-shocked HeLa cells, followed by PCR of a HeLa cell cDNA library,
Kose et al. (2012) cloned C11ORF73. They renamed the deduced 197-amino
acid C11ORF73 protein Hikeshi after the Japanese Edo era compound word
for firefighter, smokejumper, or troubleshooter. Database analysis
revealed conservation of Hikeshi from yeast to humans.
GENE FUNCTION
Kose et al. (2012) found that heat stress induced expression of Hikeshi
and heat-shock proteins of the Hsp70 family (see 140550) in HeLa cells.
Depletion of Hikeshi had no effect on the ability of cells to mount a
response to heat stress, but it delayed cellular recovery after removal
of heat stress and reduced cell viability. Protein pull-down assays
showed that Hikeshi efficiently interacted with ATP-bound HSP70s, but
not ADP-bound HSP70s. Hikeshi mediated HSP70 import in an importin (see
602738)-independent manner. HSP110 (HSPH1; 610703), which functions as a
nucleotide exchange factor for HSP70, was required for interaction of
Hikeshi with HSP70. HSP40 (DNAJB1; 604572) inhibited interaction of
Hikeshi with HSP70 and countered Hikeshi-dependent HSP70 nuclear import.
Hikeshi also interacted human NUP62 (605815) and rat Nup153 (603948),
which are components of the nuclear pore. Kose et al. (2012)
hypothesized that Hikeshi functions during the HSP70 ATPase cycle and
recognizes ATP-bound HSP70 in the cytoplasm and releases ADP-bound HSP70
in the nucleus in conjunction with HSP110.
MAPPING
Hartz (2012) mapped the C11ORF73 gene to chromosome 11q14.2 based on an
alignment of the C11ORF73 sequence (GenBank GENBANK AF161487) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/19/2012.
2. Kose, S.; Furuta, M.; Imamoto, N.: Hikeshi, a nuclear import carrier
for Hsp70s, protects cells from heat shock-induced nuclear damage. Cell 149:
578-589, 2012.
*FIELD* CD
Patricia A. Hartz: 11/2/2012
*FIELD* ED
mgross: 11/02/2012