Full text data of NAA25
NAA25
(C12orf30, MDM20, NAP1)
[Confidence: low (only semi-automatic identification from reviews)]
N-alpha-acetyltransferase 25, NatB auxiliary subunit (Mitochondrial distribution and morphology protein 20; N-terminal acetyltransferase B complex subunit MDM20; NatB complex subunit MDM20; N-terminal acetyltransferase B complex subunit NAA25; p120)
N-alpha-acetyltransferase 25, NatB auxiliary subunit (Mitochondrial distribution and morphology protein 20; N-terminal acetyltransferase B complex subunit MDM20; NatB complex subunit MDM20; N-terminal acetyltransferase B complex subunit NAA25; p120)
UniProt
Q14CX7
ID NAA25_HUMAN Reviewed; 972 AA.
AC Q14CX7; A0JLU7; Q6MZH1; Q7Z4N6; Q9H911;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-AUG-2006, sequence version 1.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=N-alpha-acetyltransferase 25, NatB auxiliary subunit;
DE AltName: Full=Mitochondrial distribution and morphology protein 20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit MDM20;
DE Short=NatB complex subunit MDM20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit NAA25;
DE AltName: Full=p120;
GN Name=NAA25; Synonyms=C12orf30, MDM20, NAP1;
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).
RA Hotokezaka H., Wiedmann M.;
RT "P120 which associates with nascent polypeptide chain.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-972.
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 [5]
RP FUNCTION, INTERACTION WITH NAT5, AND SUBCELLULAR LOCATION.
RX PubMed=18570629; DOI=10.1042/BJ20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B
RT (hNatB): a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(2008).
RN [6]
RP NOMENCLATURE.
RX PubMed=19660095; DOI=10.1186/1753-6561-3-S6-S2;
RA Polevoda B., Arnesen T., Sherman F.;
RT "A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(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 [LARGE SCALE ANALYSIS] ARG-789.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Non-catalytic subunit of the NatB complex which
CC catalyzes acetylation of the N-terminal methionine residues of
CC peptides beginning with Met-Asp-Glu. May play a role in normal
CC cell-cycle progression.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC complex which is composed of NAA20 and NAA25.
CC -!- INTERACTION:
CC P24941:CDK2; NbExp=1; IntAct=EBI-1048503, EBI-375096;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14CX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CX7-2; Sequence=VSP_026629, VSP_026630;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the MDM20/NAA25 family.
CC -!- SIMILARITY: Contains 4 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14432.1; Type=Erroneous initiation;
CC Sequence=CAE46062.1; Type=Erroneous initiation;
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; AB054990; BAC80174.1; -; mRNA.
DR EMBL; BX641140; CAE46062.1; ALT_INIT; mRNA.
DR EMBL; BC034357; AAH34357.1; -; mRNA.
DR EMBL; BC113585; AAI13586.1; -; mRNA.
DR EMBL; BC113587; AAI13588.1; -; mRNA.
DR EMBL; AK023151; BAB14432.1; ALT_INIT; mRNA.
DR RefSeq; NP_079229.2; NM_024953.3.
DR UniGene; Hs.530941; -.
DR ProteinModelPortal; Q14CX7; -.
DR IntAct; Q14CX7; 2.
DR STRING; 9606.ENSP00000261745; -.
DR PhosphoSite; Q14CX7; -.
DR DMDM; 121948761; -.
DR PaxDb; Q14CX7; -.
DR PRIDE; Q14CX7; -.
DR Ensembl; ENST00000261745; ENSP00000261745; ENSG00000111300.
DR GeneID; 80018; -.
DR KEGG; hsa:80018; -.
DR UCSC; uc001ttm.3; human.
DR CTD; 80018; -.
DR GeneCards; GC12M112464; -.
DR H-InvDB; HIX0011004; -.
DR HGNC; HGNC:25783; NAA25.
DR HPA; HPA039322; -.
DR MIM; 612755; gene.
DR neXtProt; NX_Q14CX7; -.
DR PharmGKB; PA165513030; -.
DR eggNOG; NOG259643; -.
DR HOGENOM; HOG000060132; -.
DR InParanoid; Q14CX7; -.
DR OMA; QCTKFIN; -.
DR OrthoDB; EOG75F4CR; -.
DR PhylomeDB; Q14CX7; -.
DR ChiTaRS; NAA25; human.
DR GenomeRNAi; 80018; -.
DR NextBio; 70134; -.
DR PRO; PR:Q14CX7; -.
DR ArrayExpress; Q14CX7; -.
DR Bgee; Q14CX7; -.
DR CleanEx; HS_C12orf30; -.
DR Genevestigator; Q14CX7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF09797; NatB_MDM20; 1.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 972 N-alpha-acetyltransferase 25, NatB
FT auxiliary subunit.
FT /FTId=PRO_0000294337.
FT REPEAT 11 44 TPR 1.
FT REPEAT 45 78 TPR 2.
FT REPEAT 79 112 TPR 3.
FT REPEAT 114 146 TPR 4.
FT COMPBIAS 871 877 Poly-Lys.
FT VAR_SEQ 847 859 TISVILWVSSYCE -> VSFCSLPKRHCCS (in
FT isoform 2).
FT /FTId=VSP_026629.
FT VAR_SEQ 860 972 Missing (in isoform 2).
FT /FTId=VSP_026630.
FT VARIANT 426 426 L -> F (in dbSNP:rs16941860).
FT /FTId=VAR_054099.
FT VARIANT 789 789 S -> R (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035872.
FT VARIANT 876 876 K -> R (in dbSNP:rs12231744).
FT /FTId=VAR_033156.
FT VARIANT 915 915 L -> I (in dbSNP:rs12298022).
FT /FTId=VAR_054100.
FT CONFLICT 202 202 I -> T (in Ref. 4; BAB14432).
FT CONFLICT 466 466 Y -> S (in Ref. 4; BAB14432).
FT CONFLICT 672 672 S -> T (in Ref. 4; BAB14432).
FT CONFLICT 817 817 S -> G (in Ref. 2; CAE46062).
SQ SEQUENCE 972 AA; 112292 MW; 232B8FD14447DDD6 CRC64;
MATRGHVQDP NDRRLRPIYD YLDNGNNKMA IQQADKLLKK HKDLHCAKVL KAIGLQRTGK
QEEAFTLAQE VAALEPTDDN SLQALTILYR EMHRPELVTK LYEAAVKKVP NSEEYHSHLF
MAYARVGEYK KMQQAGMALY KIVPKNPYYF WSVMSLIMQS ISAQDENLSK TMFLPLAERM
VEKMVKEDKI EAEAEVELYY MILERLGKYQ EALDVIRGKL GEKLTSEIQS RENKCMAMYK
KLSRWPECNA LSRRLLLKNS DDWQFYLTYF DSVFRLIEEA WSPPAEGEHS LEGEVHYSAE
KAVKFIEDRI TEESKSSRHL RGPHLAKLEL IRRLRSQGCN DEYKLGDPEE LMFQYFKKFG
DKPCCFTDLK VFVDLLPATQ CTKFINQLLG VVPLSTPTED KLALPADIRA LQQHLCVVQL
TRLLGLYHTM DKNQKLSVVR ELMLRYQHGL EFGKTCLKTE LQFSDYYCLL AVHALIDVWR
ETGDETTVWQ ALTLLEEGLT HSPSNAQFKL LLVRIYCMLG AFEPVVDLYS SLDAKHIQHD
TIGYLLTRYA ESLGQYAAAS QSCNFALRFF HSNQKDTSEY IIQAYKYGAF EKIPEFIAFR
NRLNNSLHFA QVRTERMLLD LLLEANISTS LAESIKSMNL RPEEDDIPWE DLRDNRDLNV
FFSWDPKDRD VSEEHKKLSL EEETLWLRIR SLTLRLISGL PSLNHPVEPK NSEKTAENGV
SSRIDILRLL LQQLEATLET GKRFIEKDIQ YPFLGPVPTR MGGFFNSGCS QCQISSFYLV
NDIYELDTSG LEDTMEIQER IENSFKSLLD QLKDVFSKCK GDLLEVKDGN LKTHPTLLEN
LVFFVETISV ILWVSSYCES VLRPYKLNLQ KKKKKKKETS IIMPPVFTSF QDYVTGLQTL
ISNVVDHIKG LETHLIALKL EELILEDTSL SPEERKFSKT VQGKVQSSYL HSLLEMGELL
KKRLETTKKL KI
//
ID NAA25_HUMAN Reviewed; 972 AA.
AC Q14CX7; A0JLU7; Q6MZH1; Q7Z4N6; Q9H911;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-AUG-2006, sequence version 1.
DT 22-JAN-2014, entry version 73.
DE RecName: Full=N-alpha-acetyltransferase 25, NatB auxiliary subunit;
DE AltName: Full=Mitochondrial distribution and morphology protein 20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit MDM20;
DE Short=NatB complex subunit MDM20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit NAA25;
DE AltName: Full=p120;
GN Name=NAA25; Synonyms=C12orf30, MDM20, NAP1;
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).
RA Hotokezaka H., Wiedmann M.;
RT "P120 which associates with nascent polypeptide chain.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-972.
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 [5]
RP FUNCTION, INTERACTION WITH NAT5, AND SUBCELLULAR LOCATION.
RX PubMed=18570629; DOI=10.1042/BJ20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B
RT (hNatB): a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(2008).
RN [6]
RP NOMENCLATURE.
RX PubMed=19660095; DOI=10.1186/1753-6561-3-S6-S2;
RA Polevoda B., Arnesen T., Sherman F.;
RT "A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
RT nomenclature, subunits and substrates.";
RL BMC Proc. 3:S2-S2(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 [LARGE SCALE ANALYSIS] ARG-789.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Non-catalytic subunit of the NatB complex which
CC catalyzes acetylation of the N-terminal methionine residues of
CC peptides beginning with Met-Asp-Glu. May play a role in normal
CC cell-cycle progression.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC complex which is composed of NAA20 and NAA25.
CC -!- INTERACTION:
CC P24941:CDK2; NbExp=1; IntAct=EBI-1048503, EBI-375096;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14CX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CX7-2; Sequence=VSP_026629, VSP_026630;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the MDM20/NAA25 family.
CC -!- SIMILARITY: Contains 4 TPR repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14432.1; Type=Erroneous initiation;
CC Sequence=CAE46062.1; Type=Erroneous initiation;
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; AB054990; BAC80174.1; -; mRNA.
DR EMBL; BX641140; CAE46062.1; ALT_INIT; mRNA.
DR EMBL; BC034357; AAH34357.1; -; mRNA.
DR EMBL; BC113585; AAI13586.1; -; mRNA.
DR EMBL; BC113587; AAI13588.1; -; mRNA.
DR EMBL; AK023151; BAB14432.1; ALT_INIT; mRNA.
DR RefSeq; NP_079229.2; NM_024953.3.
DR UniGene; Hs.530941; -.
DR ProteinModelPortal; Q14CX7; -.
DR IntAct; Q14CX7; 2.
DR STRING; 9606.ENSP00000261745; -.
DR PhosphoSite; Q14CX7; -.
DR DMDM; 121948761; -.
DR PaxDb; Q14CX7; -.
DR PRIDE; Q14CX7; -.
DR Ensembl; ENST00000261745; ENSP00000261745; ENSG00000111300.
DR GeneID; 80018; -.
DR KEGG; hsa:80018; -.
DR UCSC; uc001ttm.3; human.
DR CTD; 80018; -.
DR GeneCards; GC12M112464; -.
DR H-InvDB; HIX0011004; -.
DR HGNC; HGNC:25783; NAA25.
DR HPA; HPA039322; -.
DR MIM; 612755; gene.
DR neXtProt; NX_Q14CX7; -.
DR PharmGKB; PA165513030; -.
DR eggNOG; NOG259643; -.
DR HOGENOM; HOG000060132; -.
DR InParanoid; Q14CX7; -.
DR OMA; QCTKFIN; -.
DR OrthoDB; EOG75F4CR; -.
DR PhylomeDB; Q14CX7; -.
DR ChiTaRS; NAA25; human.
DR GenomeRNAi; 80018; -.
DR NextBio; 70134; -.
DR PRO; PR:Q14CX7; -.
DR ArrayExpress; Q14CX7; -.
DR Bgee; Q14CX7; -.
DR CleanEx; HS_C12orf30; -.
DR Genevestigator; Q14CX7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR InterPro; IPR013026; TPR-contain_dom.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF09797; NatB_MDM20; 1.
DR PROSITE; PS50005; TPR; FALSE_NEG.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1 972 N-alpha-acetyltransferase 25, NatB
FT auxiliary subunit.
FT /FTId=PRO_0000294337.
FT REPEAT 11 44 TPR 1.
FT REPEAT 45 78 TPR 2.
FT REPEAT 79 112 TPR 3.
FT REPEAT 114 146 TPR 4.
FT COMPBIAS 871 877 Poly-Lys.
FT VAR_SEQ 847 859 TISVILWVSSYCE -> VSFCSLPKRHCCS (in
FT isoform 2).
FT /FTId=VSP_026629.
FT VAR_SEQ 860 972 Missing (in isoform 2).
FT /FTId=VSP_026630.
FT VARIANT 426 426 L -> F (in dbSNP:rs16941860).
FT /FTId=VAR_054099.
FT VARIANT 789 789 S -> R (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_035872.
FT VARIANT 876 876 K -> R (in dbSNP:rs12231744).
FT /FTId=VAR_033156.
FT VARIANT 915 915 L -> I (in dbSNP:rs12298022).
FT /FTId=VAR_054100.
FT CONFLICT 202 202 I -> T (in Ref. 4; BAB14432).
FT CONFLICT 466 466 Y -> S (in Ref. 4; BAB14432).
FT CONFLICT 672 672 S -> T (in Ref. 4; BAB14432).
FT CONFLICT 817 817 S -> G (in Ref. 2; CAE46062).
SQ SEQUENCE 972 AA; 112292 MW; 232B8FD14447DDD6 CRC64;
MATRGHVQDP NDRRLRPIYD YLDNGNNKMA IQQADKLLKK HKDLHCAKVL KAIGLQRTGK
QEEAFTLAQE VAALEPTDDN SLQALTILYR EMHRPELVTK LYEAAVKKVP NSEEYHSHLF
MAYARVGEYK KMQQAGMALY KIVPKNPYYF WSVMSLIMQS ISAQDENLSK TMFLPLAERM
VEKMVKEDKI EAEAEVELYY MILERLGKYQ EALDVIRGKL GEKLTSEIQS RENKCMAMYK
KLSRWPECNA LSRRLLLKNS DDWQFYLTYF DSVFRLIEEA WSPPAEGEHS LEGEVHYSAE
KAVKFIEDRI TEESKSSRHL RGPHLAKLEL IRRLRSQGCN DEYKLGDPEE LMFQYFKKFG
DKPCCFTDLK VFVDLLPATQ CTKFINQLLG VVPLSTPTED KLALPADIRA LQQHLCVVQL
TRLLGLYHTM DKNQKLSVVR ELMLRYQHGL EFGKTCLKTE LQFSDYYCLL AVHALIDVWR
ETGDETTVWQ ALTLLEEGLT HSPSNAQFKL LLVRIYCMLG AFEPVVDLYS SLDAKHIQHD
TIGYLLTRYA ESLGQYAAAS QSCNFALRFF HSNQKDTSEY IIQAYKYGAF EKIPEFIAFR
NRLNNSLHFA QVRTERMLLD LLLEANISTS LAESIKSMNL RPEEDDIPWE DLRDNRDLNV
FFSWDPKDRD VSEEHKKLSL EEETLWLRIR SLTLRLISGL PSLNHPVEPK NSEKTAENGV
SSRIDILRLL LQQLEATLET GKRFIEKDIQ YPFLGPVPTR MGGFFNSGCS QCQISSFYLV
NDIYELDTSG LEDTMEIQER IENSFKSLLD QLKDVFSKCK GDLLEVKDGN LKTHPTLLEN
LVFFVETISV ILWVSSYCES VLRPYKLNLQ KKKKKKKETS IIMPPVFTSF QDYVTGLQTL
ISNVVDHIKG LETHLIALKL EELILEDTSL SPEERKFSKT VQGKVQSSYL HSLLEMGELL
KKRLETTKKL KI
//
MIM
612755
*RECORD*
*FIELD* NO
612755
*FIELD* TI
*612755 MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY 20, YEAST, HOMOLOG OF
;;MDM20;;
CHROMOSOME 12 OPEN READING FRAME 30; C12ORF30
read more*FIELD* TX
DESCRIPTION
MDM20 is a component of N-acetyltransferase complex B (NatB). Human NatB
performs cotranslational N(alpha)-terminal acetylation of methionine
residues when they are followed by asparagine (Starheim et al., 2008).
CLONING
By searching a database for sequences similar to yeast Mdm20, Starheim
et al. (2008) identified human MDM20. The deduced 972-amino acid protein
has a calculated molecular mass of 112.3 kD. It has an N-terminal
tetratricopeptide repeat and a putative C-terminal nuclear localization
signal. MDM20 shares 20.4% and 92.9% amino acid identity with its yeast
and mouse homologs, respectively. Western blot analysis detected MDM20
in all human cell lines examined. Immunofluorescence analysis of HeLa
cells showed that MDM20 localized to the cytoplasm.
GENE FUNCTION
Using reciprocal immunoprecipitation analysis and Western blot analysis,
Starheim et al. (2008) showed that endogenous MDM20 and NAT3 (NAT5;
610833) interacted directly in HEK293 cells. The immunoprecipitated
complex showed NatB activity against the synthetic peptide MDEL, but not
against any other peptide examined. MDM20 and NAT3 also associated with
isolated HEK293 polysomes, as well as in the cytosolic fraction.
Knockdown of either protein via small interfering RNA disrupted cell
cycle progression. Knockdown of NAT3 led to reduced cell proliferation
and G0/G1 arrest, whereas knockdown of MDM20 decreased the number of
cells in the G0/G1 phase and resulted in some cell death. Starheim et
al. (2008) concluded that MDM20 is part of the NatB complex that
acetylates the N-terminal sequence met-asp-, and they suggested that
NatB may have an additional role in cell cycle progression.
MAPPING
Hartz (2009) mapped the MDM20 gene to chromosome 12q24.13 based on an
alignment of the MDM20 sequence (GenBank GENBANK AK023151) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/23/2009.
2. Starheim, K. K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug,
J. E.; Lillehaug, J. R.: Identification of the human N-alpha-acetyltransferase
complex B (hNatB): a complex important for cell-cycle progression. Biochem.
J. 415: 325-331, 2008.
*FIELD* CD
Patricia A. Hartz: 4/23/2009
*FIELD* ED
mgross: 04/23/2009
*RECORD*
*FIELD* NO
612755
*FIELD* TI
*612755 MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY 20, YEAST, HOMOLOG OF
;;MDM20;;
CHROMOSOME 12 OPEN READING FRAME 30; C12ORF30
read more*FIELD* TX
DESCRIPTION
MDM20 is a component of N-acetyltransferase complex B (NatB). Human NatB
performs cotranslational N(alpha)-terminal acetylation of methionine
residues when they are followed by asparagine (Starheim et al., 2008).
CLONING
By searching a database for sequences similar to yeast Mdm20, Starheim
et al. (2008) identified human MDM20. The deduced 972-amino acid protein
has a calculated molecular mass of 112.3 kD. It has an N-terminal
tetratricopeptide repeat and a putative C-terminal nuclear localization
signal. MDM20 shares 20.4% and 92.9% amino acid identity with its yeast
and mouse homologs, respectively. Western blot analysis detected MDM20
in all human cell lines examined. Immunofluorescence analysis of HeLa
cells showed that MDM20 localized to the cytoplasm.
GENE FUNCTION
Using reciprocal immunoprecipitation analysis and Western blot analysis,
Starheim et al. (2008) showed that endogenous MDM20 and NAT3 (NAT5;
610833) interacted directly in HEK293 cells. The immunoprecipitated
complex showed NatB activity against the synthetic peptide MDEL, but not
against any other peptide examined. MDM20 and NAT3 also associated with
isolated HEK293 polysomes, as well as in the cytosolic fraction.
Knockdown of either protein via small interfering RNA disrupted cell
cycle progression. Knockdown of NAT3 led to reduced cell proliferation
and G0/G1 arrest, whereas knockdown of MDM20 decreased the number of
cells in the G0/G1 phase and resulted in some cell death. Starheim et
al. (2008) concluded that MDM20 is part of the NatB complex that
acetylates the N-terminal sequence met-asp-, and they suggested that
NatB may have an additional role in cell cycle progression.
MAPPING
Hartz (2009) mapped the MDM20 gene to chromosome 12q24.13 based on an
alignment of the MDM20 sequence (GenBank GENBANK AK023151) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/23/2009.
2. Starheim, K. K.; Arnesen, T.; Gromyko, D.; Ryningen, A.; Varhaug,
J. E.; Lillehaug, J. R.: Identification of the human N-alpha-acetyltransferase
complex B (hNatB): a complex important for cell-cycle progression. Biochem.
J. 415: 325-331, 2008.
*FIELD* CD
Patricia A. Hartz: 4/23/2009
*FIELD* ED
mgross: 04/23/2009