Full text data of IMPACT
IMPACT
[Confidence: low (only semi-automatic identification from reviews)]
Protein IMPACT (Imprinted and ancient gene protein homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein IMPACT (Imprinted and ancient gene protein homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9P2X3
ID IMPCT_HUMAN Reviewed; 320 AA.
AC Q9P2X3; A8MXG0; Q49AM0; Q9H2X4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Protein IMPACT;
DE AltName: Full=Imprinted and ancient gene protein homolog;
GN Name=IMPACT;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), LACK OF
RP IMPRINTING, TISSUE SPECIFICITY, AND VARIANT VAL-151.
RX PubMed=11116084; DOI=10.1101/gr.139200;
RA Okamura K., Hagiwara-Takeuchi Y., Li T., Vu T.H., Hirai M.,
RA Hattori M., Sakaki Y., Hoffman A.R., Ito T.;
RT "Comparative genome analysis of the mouse imprinted gene impact and
RT its nonimprinted human homolog IMPACT: toward the structural basis for
RT species-specific imprinting.";
RL Genome Res. 10:1878-1889(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11244491; DOI=10.1038/sj.mp.4000799;
RA Kosaki K., Suzuki T., Kosaki R., Yoshihashi H., Itoh M., Goto Y.,
RA Matsuo N.;
RT "Human homolog of the mouse imprinted gene Impact resides at the
RT pericentric region of chromosome 18 within the critical region for
RT bipolar affective disorder.";
RL Mol. Psychiatry 6:87-91(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-151.
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-151.
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-151.
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 [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).
CC -!- FUNCTION: Translational regulator that ensures constant high
CC levels of translation under amino acid starvation. Acts by
CC interacting with GCN1/GCN1L1, thereby preventing activation of
CC GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation
CC of protein synthesis (By similarity). May be required to regulate
CC translation in specific neuronal cells under amino acid starvation
CC conditions by preventing GCN2 activation and therefore ATF4
CC synthesis (By similarity). Through its action on GCN2, may also
CC facilitate neuritogenesis (By similarity).
CC -!- SUBUNIT: Interacts with GCN1/GCN1L1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=May be
CC associated with polysomes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2X3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2X3-2; Sequence=VSP_033136;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC brain.
CC -!- MISCELLANEOUS: In contrast to the mouse or rabbit ortholog, the
CC IMPACT locus is not imprinted in human.
CC -!- SIMILARITY: Belongs to the IMPACT family.
CC -!- SIMILARITY: Contains 1 RWD 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; AF232229; AAG23917.1; -; Genomic_DNA.
DR EMBL; AB026264; BAA95160.1; -; mRNA.
DR EMBL; AF208694; AAG35736.1; -; mRNA.
DR EMBL; AK292533; BAF85222.1; -; mRNA.
DR EMBL; AC007922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01186.1; -; Genomic_DNA.
DR EMBL; BC034016; AAH34016.1; -; mRNA.
DR EMBL; BC036074; AAH36074.1; -; mRNA.
DR RefSeq; NP_060909.1; NM_018439.3.
DR UniGene; Hs.515317; -.
DR ProteinModelPortal; Q9P2X3; -.
DR SMR; Q9P2X3; 182-274.
DR IntAct; Q9P2X3; 1.
DR STRING; 9606.ENSP00000284202; -.
DR DMDM; 296434540; -.
DR PaxDb; Q9P2X3; -.
DR PRIDE; Q9P2X3; -.
DR DNASU; 55364; -.
DR Ensembl; ENST00000284202; ENSP00000284202; ENSG00000154059.
DR GeneID; 55364; -.
DR KEGG; hsa:55364; -.
DR UCSC; uc002kvg.4; human.
DR CTD; 55364; -.
DR GeneCards; GC18P022006; -.
DR HGNC; HGNC:20387; IMPACT.
DR HPA; HPA041045; -.
DR HPA; HPA041968; -.
DR MIM; 615319; gene.
DR neXtProt; NX_Q9P2X3; -.
DR PharmGKB; PA143485502; -.
DR eggNOG; COG1739; -.
DR HOGENOM; HOG000160430; -.
DR HOVERGEN; HBG108005; -.
DR InParanoid; Q9P2X3; -.
DR OMA; WLKGQER; -.
DR OrthoDB; EOG7V766R; -.
DR PhylomeDB; Q9P2X3; -.
DR ChiTaRS; IMPACT; human.
DR GenomeRNAi; 55364; -.
DR NextBio; 59745; -.
DR PRO; PR:Q9P2X3; -.
DR ArrayExpress; Q9P2X3; -.
DR Bgee; Q9P2X3; -.
DR CleanEx; HS_IMPACT; -.
DR Genevestigator; Q9P2X3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:Ensembl.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.230.30; -; 1.
DR InterPro; IPR023582; Impact.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR020569; UPF0029_Impact_CS.
DR PANTHER; PTHR16301; PTHR16301; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF01205; UPF0029; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00910; UPF0029; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Translation regulation.
FT CHAIN 1 320 Protein IMPACT.
FT /FTId=PRO_0000330850.
FT DOMAIN 14 116 RWD.
FT VAR_SEQ 1 118 Missing (in isoform 2).
FT /FTId=VSP_033136.
FT VARIANT 125 125 D -> E (in dbSNP:rs582234).
FT /FTId=VAR_042723.
FT VARIANT 151 151 L -> V (in dbSNP:rs677688).
FT /FTId=VAR_042724.
SQ SEQUENCE 320 AA; 36476 MW; 75AAB91E00594212 CRC64;
MAEGDAGSDQ RQNEEIEAMA AIYGEEWCVI DDCAKIFCIR ISDDIDDPKW TLCLQVMLPN
EYPGTAPPIY QLNAPWLKGQ ERADLSNSLE EIYIQNIGES ILYLWVEKIR DVLIQKSQMT
EPGPDVKKKT EEEDVECEDD LILACQPESS LKALDFDISE TRTEVEVEEL PPIDHGIPIT
DRRSTFQAHL APVVCPKQVK MVLSKLYENK KIASATHNIY AYRIYCEDKQ TFLQDCEDDG
ETAAGGRLLH LMEILNVKNV MVVVSRWYGG ILLGPDRFKH INNCARNILV EKNYTNSPEE
SSKALGKNKK VRKDKKRNEH
//
ID IMPCT_HUMAN Reviewed; 320 AA.
AC Q9P2X3; A8MXG0; Q49AM0; Q9H2X4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Protein IMPACT;
DE AltName: Full=Imprinted and ancient gene protein homolog;
GN Name=IMPACT;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), LACK OF
RP IMPRINTING, TISSUE SPECIFICITY, AND VARIANT VAL-151.
RX PubMed=11116084; DOI=10.1101/gr.139200;
RA Okamura K., Hagiwara-Takeuchi Y., Li T., Vu T.H., Hirai M.,
RA Hattori M., Sakaki Y., Hoffman A.R., Ito T.;
RT "Comparative genome analysis of the mouse imprinted gene impact and
RT its nonimprinted human homolog IMPACT: toward the structural basis for
RT species-specific imprinting.";
RL Genome Res. 10:1878-1889(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11244491; DOI=10.1038/sj.mp.4000799;
RA Kosaki K., Suzuki T., Kosaki R., Yoshihashi H., Itoh M., Goto Y.,
RA Matsuo N.;
RT "Human homolog of the mouse imprinted gene Impact resides at the
RT pericentric region of chromosome 18 within the critical region for
RT bipolar affective disorder.";
RL Mol. Psychiatry 6:87-91(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-151.
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-151.
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
RA Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
RA Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
RA Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
RA Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
RA Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
RA O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-151.
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 [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).
CC -!- FUNCTION: Translational regulator that ensures constant high
CC levels of translation under amino acid starvation. Acts by
CC interacting with GCN1/GCN1L1, thereby preventing activation of
CC GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation
CC of protein synthesis (By similarity). May be required to regulate
CC translation in specific neuronal cells under amino acid starvation
CC conditions by preventing GCN2 activation and therefore ATF4
CC synthesis (By similarity). Through its action on GCN2, may also
CC facilitate neuritogenesis (By similarity).
CC -!- SUBUNIT: Interacts with GCN1/GCN1L1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=May be
CC associated with polysomes (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2X3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2X3-2; Sequence=VSP_033136;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
CC brain.
CC -!- MISCELLANEOUS: In contrast to the mouse or rabbit ortholog, the
CC IMPACT locus is not imprinted in human.
CC -!- SIMILARITY: Belongs to the IMPACT family.
CC -!- SIMILARITY: Contains 1 RWD 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; AF232229; AAG23917.1; -; Genomic_DNA.
DR EMBL; AB026264; BAA95160.1; -; mRNA.
DR EMBL; AF208694; AAG35736.1; -; mRNA.
DR EMBL; AK292533; BAF85222.1; -; mRNA.
DR EMBL; AC007922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01186.1; -; Genomic_DNA.
DR EMBL; BC034016; AAH34016.1; -; mRNA.
DR EMBL; BC036074; AAH36074.1; -; mRNA.
DR RefSeq; NP_060909.1; NM_018439.3.
DR UniGene; Hs.515317; -.
DR ProteinModelPortal; Q9P2X3; -.
DR SMR; Q9P2X3; 182-274.
DR IntAct; Q9P2X3; 1.
DR STRING; 9606.ENSP00000284202; -.
DR DMDM; 296434540; -.
DR PaxDb; Q9P2X3; -.
DR PRIDE; Q9P2X3; -.
DR DNASU; 55364; -.
DR Ensembl; ENST00000284202; ENSP00000284202; ENSG00000154059.
DR GeneID; 55364; -.
DR KEGG; hsa:55364; -.
DR UCSC; uc002kvg.4; human.
DR CTD; 55364; -.
DR GeneCards; GC18P022006; -.
DR HGNC; HGNC:20387; IMPACT.
DR HPA; HPA041045; -.
DR HPA; HPA041968; -.
DR MIM; 615319; gene.
DR neXtProt; NX_Q9P2X3; -.
DR PharmGKB; PA143485502; -.
DR eggNOG; COG1739; -.
DR HOGENOM; HOG000160430; -.
DR HOVERGEN; HBG108005; -.
DR InParanoid; Q9P2X3; -.
DR OMA; WLKGQER; -.
DR OrthoDB; EOG7V766R; -.
DR PhylomeDB; Q9P2X3; -.
DR ChiTaRS; IMPACT; human.
DR GenomeRNAi; 55364; -.
DR NextBio; 59745; -.
DR PRO; PR:Q9P2X3; -.
DR ArrayExpress; Q9P2X3; -.
DR Bgee; Q9P2X3; -.
DR CleanEx; HS_IMPACT; -.
DR Genevestigator; Q9P2X3; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:Ensembl.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.230.30; -; 1.
DR InterPro; IPR023582; Impact.
DR InterPro; IPR001498; Impact_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR020569; UPF0029_Impact_CS.
DR PANTHER; PTHR16301; PTHR16301; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF01205; UPF0029; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00910; UPF0029; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Translation regulation.
FT CHAIN 1 320 Protein IMPACT.
FT /FTId=PRO_0000330850.
FT DOMAIN 14 116 RWD.
FT VAR_SEQ 1 118 Missing (in isoform 2).
FT /FTId=VSP_033136.
FT VARIANT 125 125 D -> E (in dbSNP:rs582234).
FT /FTId=VAR_042723.
FT VARIANT 151 151 L -> V (in dbSNP:rs677688).
FT /FTId=VAR_042724.
SQ SEQUENCE 320 AA; 36476 MW; 75AAB91E00594212 CRC64;
MAEGDAGSDQ RQNEEIEAMA AIYGEEWCVI DDCAKIFCIR ISDDIDDPKW TLCLQVMLPN
EYPGTAPPIY QLNAPWLKGQ ERADLSNSLE EIYIQNIGES ILYLWVEKIR DVLIQKSQMT
EPGPDVKKKT EEEDVECEDD LILACQPESS LKALDFDISE TRTEVEVEEL PPIDHGIPIT
DRRSTFQAHL APVVCPKQVK MVLSKLYENK KIASATHNIY AYRIYCEDKQ TFLQDCEDDG
ETAAGGRLLH LMEILNVKNV MVVVSRWYGG ILLGPDRFKH INNCARNILV EKNYTNSPEE
SSKALGKNKK VRKDKKRNEH
//
MIM
615319
*RECORD*
*FIELD* NO
615319
*FIELD* TI
*615319 IMPACT RWD DOMAIN PROTEIN; IMPACT
;;IMPRINTED AND ANCIENT GENE, MOUSE, HOMOLOG OF
read more*FIELD* TX
DESCRIPTION
IMPACT is the nonimprinted human homolog of an imprinted mouse gene
(Okamura et al., 2000).
CLONING
By searching an EST database for sequences similar to mouse Impact,
followed by 5-prime and 3-prime RACE and RT-PCR of adult and fetal brain
RNA, Okamura et al. (2000) cloned human IMPACT. The deduced 320-amino
acid protein shares 82.2% identity with the mouse protein. The authors
also identified a close ortholog in Xenopus, with weaker conservation in
invertebrates, bacteria, and plants. Northern blot analysis detected
variable expression of a major IMPACT transcript of about 3.9 kb and a
minor transcript of about 2.1 kb in all 16 adult and 4 fetal human
tissues examined. The 2 transcripts appeared to differ in their 3-prime
UTRs. Unlike mouse Impact, the human gene was biallelically expressed.
Using Western blot analysis, Pereira et al. (2005) found that mouse
Impact was predominantly expressed in brain, with much weaker expression
in lung, kidney, and testis, and little to no expression in spleen,
heart, liver, and pancreas. Immunohistochemical analysis revealed
abundant Impact expression in hypothalamic neurons, with scattered
neuronal expression in other regions, including hippocampus and piriform
cortex.
GENE FUNCTION
Okamura et al. (2000) found that mouse Impact was imprinted and
expressed from the paternal allele only. They identified a CpG island
within intron 1 of the mouse gene that has a tandem repeat structure
characteristic of imprinted genes, and this CpG island was highly
methylated on the maternal allele. The human gene, which is
biallelically expressed, lacks the intronic CpG island.
Pereira et al. (2005) found that overexpression of Impact in mouse
embryonic fibroblasts inhibited Gcn2 (EIF2AK4; 609280)-dependent
phosphorylation of Eif2-alpha (EIF2S1; 603907) under leucine starvation
conditions. Overexpression of Impact also abolished expression of the
Eif2-alpha downstream targets Atf4 (604064) and Chop (DDIT3; 126337).
Roffe et al. (2013) found that expression of Impact increased in primary
mouse hippocampal neurons and N2a neuroblastoma cells upon
differentiation, concomitant with reduction in Gcn2 phosphorylation.
Upon differentiation, Impact associated with translating ribosomes,
enhanced translation initiation, and downregulated expression of Atf4.
Endogenous Impact promoted neurite outgrowth, whereas Gcn2 inhibited
neurite outgrowth.
GENE STRUCTURE
Okamura et al. (2000) determined that the IMPACT gene contains 11 exons
and spans about 30 kb. The last exon is over 2 kb long. The upstream
region contains an Alu element, and the promoter region and first exon
contain a CpG island. The human IMPACT gene lacks the differentially
methylated CpG island found in intron 1 of the mouse gene.
MAPPING
Using FISH, Okamura et al. (2000) mapped the IMPACT gene to chromosome
18q11.2-q12.1. They mapped the mouse Impact gene to a region of
chromosome 18A2-B1 that shares homology of synteny with human chromosome
18q11.2-q12.2.
*FIELD* RF
1. Okamura, K.; Hagiwara-Takeuchi, Y.; Li, T.; Vu, T. H.; Hirai, M.;
Hattori, M.; Sakaki, Y.; Hoffman, A. R.; Ito, T.: Comparative genome
analysis of the mouse imprinted gene Impact and its nonimprinted human
homolog IMPACT: toward the structural basis for species-specific imprinting. Genome
Res. 10: 1878-1889, 2000.
2. Pereira, C. M.; Sattlegger, E.; Jiang, H.-Y.; Longo, B. M.; Jaqueta,
C. B.; Hinnebusch, A. G.; Wek, R. C.; Mello, L. E. A. M.; Castilho,
B. A.: IMPACT, a protein preferentially expressed in the mouse brain,
binds GCN1 and inhibits GCN2 activation. J. Biol. Chem. 280: 28316-28323,
2005.
3. Roffe, M.; Hajj, G. N. M.; Azevedo, H. F.; Alves, V. S.; Castilho,
B. A.: IMPACT is a developmentally regulated protein in neurons that
opposes the eukaryotic initiation factor 2-alpha kinase GCN2 in the
modulation of neurite outgrowth. J. Biol. Chem. 288: 10860-10869,
2013.
*FIELD* CD
Patricia A. Hartz: 7/22/2013
*FIELD* ED
mgross: 07/22/2013
tpirozzi: 7/22/2013
*RECORD*
*FIELD* NO
615319
*FIELD* TI
*615319 IMPACT RWD DOMAIN PROTEIN; IMPACT
;;IMPRINTED AND ANCIENT GENE, MOUSE, HOMOLOG OF
read more*FIELD* TX
DESCRIPTION
IMPACT is the nonimprinted human homolog of an imprinted mouse gene
(Okamura et al., 2000).
CLONING
By searching an EST database for sequences similar to mouse Impact,
followed by 5-prime and 3-prime RACE and RT-PCR of adult and fetal brain
RNA, Okamura et al. (2000) cloned human IMPACT. The deduced 320-amino
acid protein shares 82.2% identity with the mouse protein. The authors
also identified a close ortholog in Xenopus, with weaker conservation in
invertebrates, bacteria, and plants. Northern blot analysis detected
variable expression of a major IMPACT transcript of about 3.9 kb and a
minor transcript of about 2.1 kb in all 16 adult and 4 fetal human
tissues examined. The 2 transcripts appeared to differ in their 3-prime
UTRs. Unlike mouse Impact, the human gene was biallelically expressed.
Using Western blot analysis, Pereira et al. (2005) found that mouse
Impact was predominantly expressed in brain, with much weaker expression
in lung, kidney, and testis, and little to no expression in spleen,
heart, liver, and pancreas. Immunohistochemical analysis revealed
abundant Impact expression in hypothalamic neurons, with scattered
neuronal expression in other regions, including hippocampus and piriform
cortex.
GENE FUNCTION
Okamura et al. (2000) found that mouse Impact was imprinted and
expressed from the paternal allele only. They identified a CpG island
within intron 1 of the mouse gene that has a tandem repeat structure
characteristic of imprinted genes, and this CpG island was highly
methylated on the maternal allele. The human gene, which is
biallelically expressed, lacks the intronic CpG island.
Pereira et al. (2005) found that overexpression of Impact in mouse
embryonic fibroblasts inhibited Gcn2 (EIF2AK4; 609280)-dependent
phosphorylation of Eif2-alpha (EIF2S1; 603907) under leucine starvation
conditions. Overexpression of Impact also abolished expression of the
Eif2-alpha downstream targets Atf4 (604064) and Chop (DDIT3; 126337).
Roffe et al. (2013) found that expression of Impact increased in primary
mouse hippocampal neurons and N2a neuroblastoma cells upon
differentiation, concomitant with reduction in Gcn2 phosphorylation.
Upon differentiation, Impact associated with translating ribosomes,
enhanced translation initiation, and downregulated expression of Atf4.
Endogenous Impact promoted neurite outgrowth, whereas Gcn2 inhibited
neurite outgrowth.
GENE STRUCTURE
Okamura et al. (2000) determined that the IMPACT gene contains 11 exons
and spans about 30 kb. The last exon is over 2 kb long. The upstream
region contains an Alu element, and the promoter region and first exon
contain a CpG island. The human IMPACT gene lacks the differentially
methylated CpG island found in intron 1 of the mouse gene.
MAPPING
Using FISH, Okamura et al. (2000) mapped the IMPACT gene to chromosome
18q11.2-q12.1. They mapped the mouse Impact gene to a region of
chromosome 18A2-B1 that shares homology of synteny with human chromosome
18q11.2-q12.2.
*FIELD* RF
1. Okamura, K.; Hagiwara-Takeuchi, Y.; Li, T.; Vu, T. H.; Hirai, M.;
Hattori, M.; Sakaki, Y.; Hoffman, A. R.; Ito, T.: Comparative genome
analysis of the mouse imprinted gene Impact and its nonimprinted human
homolog IMPACT: toward the structural basis for species-specific imprinting. Genome
Res. 10: 1878-1889, 2000.
2. Pereira, C. M.; Sattlegger, E.; Jiang, H.-Y.; Longo, B. M.; Jaqueta,
C. B.; Hinnebusch, A. G.; Wek, R. C.; Mello, L. E. A. M.; Castilho,
B. A.: IMPACT, a protein preferentially expressed in the mouse brain,
binds GCN1 and inhibits GCN2 activation. J. Biol. Chem. 280: 28316-28323,
2005.
3. Roffe, M.; Hajj, G. N. M.; Azevedo, H. F.; Alves, V. S.; Castilho,
B. A.: IMPACT is a developmentally regulated protein in neurons that
opposes the eukaryotic initiation factor 2-alpha kinase GCN2 in the
modulation of neurite outgrowth. J. Biol. Chem. 288: 10860-10869,
2013.
*FIELD* CD
Patricia A. Hartz: 7/22/2013
*FIELD* ED
mgross: 07/22/2013
tpirozzi: 7/22/2013