NOA1_HUMAN
ID NOA1_HUMAN Reviewed; 698 AA.
AC Q8NC60; Q8N7L6; Q9BSQ9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nitric oxide-associated protein 1;
GN Name=NOA1; Synonyms=C4orf14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH MITOCHONDRIAL COMPLEX I; MRPL12; MRPS27 AND
RP DAP3, GTP-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=19103604; DOI=10.1074/jbc.m807797200;
RA Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H.,
RA Farquhar M.G.;
RT "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial
RT respiration and apoptosis.";
RL J. Biol. Chem. 284:5414-5424(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
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., Buerckstuemmer T.,
RA 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-579.
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in regulation of mitochondrial protein translation
CC and respiration. Plays a role in mitochondria-mediated cell death. May
CC act as a scaffolding protein or stabilizer of respiratory chain
CC supercomplexes. Binds GTP. {ECO:0000269|PubMed:19103604}.
CC -!- SUBUNIT: Homodimer or multimer (By similarity). Interacts with
CC mitochondrial complex I, DAP3, MRPL12 and MRPS27. {ECO:0000250,
CC ECO:0000269|PubMed:19103604}.
CC -!- INTERACTION:
CC Q8NC60; P51398: DAP3; NbExp=5; IntAct=EBI-717871, EBI-355912;
CC Q8NC60; Q16795: NDUFA9; NbExp=2; IntAct=EBI-717871, EBI-1045087;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:19103604}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19103604}; Matrix side
CC {ECO:0000269|PubMed:19103604}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOA1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05262.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK098215; BAC05262.1; ALT_INIT; mRNA.
DR EMBL; AK074953; BAC11311.1; -; mRNA.
DR EMBL; BC004894; AAH04894.1; -; mRNA.
DR CCDS; CCDS3510.1; -.
DR RefSeq; NP_115689.1; NM_032313.3.
DR AlphaFoldDB; Q8NC60; -.
DR SMR; Q8NC60; -.
DR BioGRID; 124000; 116.
DR IntAct; Q8NC60; 43.
DR MINT; Q8NC60; -.
DR STRING; 9606.ENSP00000264230; -.
DR iPTMnet; Q8NC60; -.
DR PhosphoSitePlus; Q8NC60; -.
DR BioMuta; NOA1; -.
DR DMDM; 93204549; -.
DR EPD; Q8NC60; -.
DR jPOST; Q8NC60; -.
DR MassIVE; Q8NC60; -.
DR MaxQB; Q8NC60; -.
DR PaxDb; Q8NC60; -.
DR PeptideAtlas; Q8NC60; -.
DR PRIDE; Q8NC60; -.
DR ProteomicsDB; 72856; -.
DR Antibodypedia; 44140; 127 antibodies from 24 providers.
DR DNASU; 84273; -.
DR Ensembl; ENST00000264230.5; ENSP00000264230.4; ENSG00000084092.7.
DR GeneID; 84273; -.
DR KEGG; hsa:84273; -.
DR MANE-Select; ENST00000264230.5; ENSP00000264230.4; NM_032313.4; NP_115689.1.
DR UCSC; uc003hck.4; human.
DR CTD; 84273; -.
DR DisGeNET; 84273; -.
DR GeneCards; NOA1; -.
DR HGNC; HGNC:28473; NOA1.
DR HPA; ENSG00000084092; Low tissue specificity.
DR MIM; 614919; gene.
DR neXtProt; NX_Q8NC60; -.
DR OpenTargets; ENSG00000084092; -.
DR PharmGKB; PA134878853; -.
DR VEuPathDB; HostDB:ENSG00000084092; -.
DR eggNOG; KOG1249; Eukaryota.
DR GeneTree; ENSGT00390000001695; -.
DR HOGENOM; CLU_014195_2_0_1; -.
DR InParanoid; Q8NC60; -.
DR OMA; LLNSDYC; -.
DR OrthoDB; 612803at2759; -.
DR PhylomeDB; Q8NC60; -.
DR TreeFam; TF314460; -.
DR PathwayCommons; Q8NC60; -.
DR SignaLink; Q8NC60; -.
DR BioGRID-ORCS; 84273; 89 hits in 1077 CRISPR screens.
DR ChiTaRS; NOA1; human.
DR GenomeRNAi; 84273; -.
DR Pharos; Q8NC60; Tbio.
DR PRO; PR:Q8NC60; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8NC60; protein.
DR Bgee; ENSG00000084092; Expressed in tibialis anterior and 172 other tissues.
DR Genevisible; Q8NC60; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0010941; P:regulation of cell death; IMP:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Apoptosis; GTP-binding; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..698
FT /note="Nitric oxide-associated protein 1"
FT /id="PRO_0000232510"
FT DOMAIN 202..503
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 42..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VARIANT 153
FT /note="A -> S (in dbSNP:rs3733306)"
FT /id="VAR_025941"
FT VARIANT 450
FT /note="K -> R (in dbSNP:rs11553077)"
FT /id="VAR_025942"
FT VARIANT 579
FT /note="Q -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035500"
FT CONFLICT 101..109
FT /note="EERQRQQRR -> Q (in Ref. 1; BAC05262)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="N -> S (in Ref. 1; BAC11311)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Y -> C (in Ref. 1; BAC05262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 78458 MW; EBEEBC588F578EE1 CRC64;
MLPARLPFRL LSLFLRGSAP TAARHGLREP LLERRCAAAS SFQHSSSLGR ELPYDPVDTE
GFGEGGDMQE RFLFPEYILD PEPQPTREKQ LQELQQQQEE EERQRQQRRE ERRQQNLRAR
SREHPVVGHP DPALPPSGVN CSGCGAELHC QDAGVPGYLP REKFLRTAEA DGGLARTVCQ
RCWLLSHHRR ALRLQVSREQ YLELVSAALR RPGPSLVLYM VDLLDLPDAL LPDLPALVGP
KQLIVLGNKV DLLPQDAPGY RQRLRERLWE DCARAGLLLA PGHQGPQRPV KDEPQDGENP
NPPNWSRTVV RDVRLISAKT GYGVEELISA LQRSWRYRGD VYLVGATNAG KSTLFNTLLE
SDYCTAKGSE AIDRATISPW PGTTLNLLKF PICNPTPYRM FKRHQRLKKD STQAEEDLSE
QEQNQLNVLK KHGYVVGRVG RTFLYSEEQK DNIPFEFDAD SLAFDMENDP VMGTHKSTKQ
VELTAQDVKD AHWFYDTPGI TKENCILNLL TEKEVNIVLP TQSIVPRTFV LKPGMVLFLG
AIGRIDFLQG NQSAWFTVVA SNILPVHITS LDRADALYQK HAGHTLLQIP MGGKERMAGF
PPLVAEDIML KEGLGASEAV ADIKFSSAGW VSVTPNFKDR LHLRGYTPEG TVLTVRPPLL
PYIVNIKGQR IKKSVAYKTK KPPSLMYNVR KKKGKINV
