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c-Myc-binding protein (Associate of Myc 1) (AMY-1)

 MYCBP_HUMAN             Reviewed;         103 AA.
Q99417; B2R4N0; Q5TA64; Q96HE2;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-JUN-2019, entry version 163.
RecName: Full=c-Myc-binding protein;
AltName: Full=Associate of Myc 1;
Short=AMY-1;
Name=MYCBP; Synonyms=AMY1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=9797456; DOI=10.1046/j.1365-2443.1998.00206.x;
Taira T., Maeda J., Ohishi T., Kitaura H., Yoshida S., Kato H.,
Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.;
"AMY-1, a novel C-MYC binding protein that stimulates transcription
activity of C-MYC.";
Genes Cells 3:549-565(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
INTERACTION WITH AKAP1.
PubMed=11483602; DOI=10.1074/jbc.M103885200;
Furusawa M., Ohnishi T., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
"AMY-1, a c-Myc-binding protein, is localized in the mitochondria of
sperm by association with S-AKAP84, an anchor protein of cAMP-
dependent protein kinase.";
J. Biol. Chem. 276:36647-36651(2001).
[9]
INTERACTION WITH MYCBPAP.
PubMed=12151104; DOI=10.1016/S0167-4781(02)00411-6;
Yukitake H., Furusawa M., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
"AMAP-1, a novel testis-specific AMY-1-binding protein, is
differentially expressed during the course of spermatogenesis.";
Biochim. Biophys. Acta 1577:126-132(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-94.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of c-myc-1 binding protein domain from Homo
sapiens.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: May control the transcriptional activity of MYC.
Stimulates the activation of E box-dependent transcription by MYC.
-!- SUBUNIT: Binds via its C-terminal region to the N-terminal region
of MYC. Associates with AKAP1/S-AKAP84. Interacts with MYCBPAP.
{ECO:0000269|PubMed:11483602, ECO:0000269|PubMed:12151104}.
-!- INTERACTION:
Q92667-2:AKAP1; NbExp=2; IntAct=EBI-716185, EBI-2120060;
Q9Y6D6:ARFGEF1; NbExp=3; IntAct=EBI-716185, EBI-1044254;
Q9Y6D5:ARFGEF2; NbExp=5; IntAct=EBI-716185, EBI-2837511;
Q7Z4T9-3:MAATS1; NbExp=5; IntAct=EBI-716185, EBI-17172567;
Q8TBZ2:MYCBPAP; NbExp=4; IntAct=EBI-716185, EBI-1391585;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion.
Note=Translocates into the nucleus in the S phase of the cell
cycle upon an increase of MYC expression. Found in the
mitochondria when associated with AKAP1.
-!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, pancreas,
skeletal muscle and kidney. Also present at low levels in lung.
-!- SIMILARITY: Belongs to the AMY1 family. {ECO:0000305}.
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EMBL; D50692; BAA09338.1; -; mRNA.
EMBL; BT007109; AAP35773.1; -; mRNA.
EMBL; AB007191; BAA22408.1; -; mRNA.
EMBL; AB451287; BAG70101.1; -; mRNA.
EMBL; AB451419; BAG70233.1; -; mRNA.
EMBL; AK311886; BAG34827.1; -; mRNA.
EMBL; AL139260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008686; AAH08686.1; -; mRNA.
CCDS; CCDS431.1; -.
RefSeq; NP_036465.2; NM_012333.4.
PDB; 2YY0; X-ray; 2.40 A; A/B/C/D=42-94.
PDBsum; 2YY0; -.
SMR; Q99417; -.
BioGrid; 117673; 46.
CORUM; Q99417; -.
IntAct; Q99417; 32.
MINT; Q99417; -.
STRING; 9606.ENSP00000380702; -.
iPTMnet; Q99417; -.
PhosphoSitePlus; Q99417; -.
BioMuta; MYCBP; -.
EPD; Q99417; -.
jPOST; Q99417; -.
MaxQB; Q99417; -.
PaxDb; Q99417; -.
PeptideAtlas; Q99417; -.
PRIDE; Q99417; -.
ProteomicsDB; 78257; -.
TopDownProteomics; Q99417; -.
DNASU; 26292; -.
Ensembl; ENST00000397572; ENSP00000380702; ENSG00000214114.
GeneID; 26292; -.
KEGG; hsa:26292; -.
UCSC; uc001ccs.4; human.
CTD; 26292; -.
DisGeNET; 26292; -.
GeneCards; MYCBP; -.
HGNC; HGNC:7554; MYCBP.
HPA; HPA041188; -.
MIM; 606535; gene.
neXtProt; NX_Q99417; -.
OpenTargets; ENSG00000214114; -.
PharmGKB; PA31354; -.
eggNOG; ENOG410J2G0; Eukaryota.
eggNOG; ENOG41126S1; LUCA.
GeneTree; ENSGT00390000017974; -.
HOGENOM; HOG000260967; -.
InParanoid; Q99417; -.
OrthoDB; 1497203at2759; -.
PhylomeDB; Q99417; -.
TreeFam; TF329224; -.
EvolutionaryTrace; Q99417; -.
GeneWiki; MYCBP; -.
GenomeRNAi; 26292; -.
PRO; PR:Q99417; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000214114; Expressed in 177 organ(s), highest expression level in testis.
ExpressionAtlas; Q99417; baseline and differential.
Genevisible; Q99417; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
InterPro; IPR026060; AMY1.
PANTHER; PTHR13168; PTHR13168; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Mitochondrion; Nucleus; Reference proteome; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 103 c-Myc-binding protein.
/FTId=PRO_0000220980.
CONFLICT 65 65 L -> V (in Ref. 1; BAA09338/BAA22408).
{ECO:0000305}.
HELIX 43 50 {ECO:0000244|PDB:2YY0}.
STRAND 51 54 {ECO:0000244|PDB:2YY0}.
HELIX 60 90 {ECO:0000244|PDB:2YY0}.
TURN 91 93 {ECO:0000244|PDB:2YY0}.
SEQUENCE 103 AA; 11967 MW; 72B9BD179A6808D0 CRC64;
MAHYKAADSK REQFRRYLEK SGVLDTLTKV LVALYEEPEK PNSALDFLKH HLGAATPENP
EIELLRLELA EMKEKYEAIV EENKKLKAKL AQYEPPQEEK RAE


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Related Genes :
[MYC2 BHLH6 EN38 JAI1 JIN1 RAP1 RD22BP1 ZBF1 At1g32640 F6N18.4] Transcription factor MYC2 (AtMYC2) (Basic helix-loop-helix protein 6) (AtbHLH6) (bHLH 6) (Protein JASMONATE INSENSITIVE 1) (R-homologous Arabidopsis protein 1) (RAP-1) (Transcription factor EN 38) (Z-box binding factor 1 protein) (bHLH transcription factor bHLH006) (rd22BP1)
[Mycbp2 Pam Phr1] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Pam/highwire/rpm-1 protein) (Protein Magellan) (Protein associated with Myc)
[ENO1 ENO1L1 MBPB1 MPB1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)
[BIN1 AMPHL] Myc box-dependent-interacting protein 1 (Amphiphysin II) (Amphiphysin-like protein) (Box-dependent myc-interacting protein 1) (Bridging integrator 1)
[Max Myn] Protein max (Myc-associated factor X) (Myc-binding novel HLH/LZ protein) (Protein myn)
[MYCBP2 KIAA0916 PAM] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Protein associated with Myc)
[GL3 BHLH1 EN31 MYC6 SST At5g41315 MYC6.2] Transcription factor GLABRA 3 (Basic helix-loop-helix protein 1) (AtMYC6) (AtbHLH1) (bHLH 1) (Protein SHAPESHIFTER) (Transcription factor EN 31) (bHLH transcription factor bHLH001)
[Myc dm CG10798] Myc protein (Diminutive protein) (dMyc1)
[MYC BHLHE39] Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64)
[ZBTB17 MIZ1 ZNF151 ZNF60] Zinc finger and BTB domain-containing protein 17 (Myc-interacting zinc finger protein 1) (Miz-1) (Zinc finger protein 151) (Zinc finger protein 60)
[BHLH2 EGL1 EGL3 EN30 MYC146 At1g63650 F24D7.16] Transcription factor EGL1 (Basic helix-loop-helix protein 2) (AtMYC146) (AtbHLH2) (bHLH 2) (Protein ENHANCER OF GLABRA 3) (Transcription factor EN 30) (bHLH transcription factor bHLH002)
[RIOX1 C14orf169 MAPJD NO66] Ribosomal oxygenase 1 (60S ribosomal protein L8 histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.-) (EC 1.14.11.27) (Histone lysine demethylase NO66) (Myc-associated protein with JmjC domain) (Nucleolar protein 66) (hsNO66) (Ribosomal oxygenase NO66) (ROX)
[Dnph1 Rcl] 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (EC 3.2.2.-) (Deoxyribonucleoside 5'-monophosphate N-glycosidase) (c-Myc-responsive protein Rcl)
[NME2 NM23B] Nucleoside diphosphate kinase B (NDK B) (NDP kinase B) (EC 2.7.4.6) (C-myc purine-binding transcription factor PUF) (Histidine protein kinase NDKB) (EC 2.7.13.3) (nm23-H2)
[RIOX2 MDIG MINA MINA53 NO52] Ribosomal oxygenase 2 (60S ribosomal protein L27a histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.-) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Mineral dust-induced gene protein) (Nucleolar protein 52) (Ribosomal oxygenase MINA) (ROX)
[mycbp2] E3 ubiquitin-protein ligase MYCBP2 (EC 2.3.2.-) (Myc-binding protein 2) (Protein Esrom)
[NMI] N-myc-interactor (Nmi) (N-myc and STAT interactor)
[Mnt Rox] Max-binding protein MNT (Myc antagonist MNT) (Protein ROX)
[DNPH1 C6orf108 RCL] 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (EC 3.2.2.-) (c-Myc-responsive protein RCL)
[MAX BHLHD4] Protein max (Class D basic helix-loop-helix protein 4) (bHLHd4) (Myc-associated factor X)
[MYCN BHLHE37 NMYC] N-myc proto-oncogene protein (Class E basic helix-loop-helix protein 37) (bHLHe37)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Max] Protein max (Myc-associated factor X)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]

Bibliography :
[16866877] AMY-1 (associate of Myc-1) localization to the trans-Golgi network through interacting with BIG2, a guanine-nucleotide exchange factor for ADP-ribosylation factors.
[11483602] AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm by association with S-AKAP84, an anchor protein of cAMP-dependent protein kinase.
[9797456] AMY-1, a novel C-MYC binding protein that stimulates transcription activity of C-MYC.