MYCBP_HUMAN
ID MYCBP_HUMAN Reviewed; 103 AA.
AC Q99417; B2R4N0; Q5TA64; Q96HE2;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=c-Myc-binding protein {ECO:0000305};
DE AltName: Full=Associate of Myc 1;
DE Short=AMY-1;
GN Name=MYCBP {ECO:0000312|HGNC:HGNC:7554}; Synonyms=AMY1;
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 [MRNA].
RC TISSUE=Placenta;
RX PubMed=9797456; DOI=10.1046/j.1365-2443.1998.00206.x;
RA Taira T., Maeda J., Ohishi T., Kitaura H., Yoshida S., Kato H., Ikeda M.,
RA Tamai K., Iguchi-Ariga S.M.M., Ariga H.;
RT "AMY-1, a novel C-MYC binding protein that stimulates transcription
RT activity of C-MYC.";
RL Genes Cells 3:549-565(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP INTERACTION WITH AKAP1.
RX PubMed=11483602; DOI=10.1074/jbc.m103885200;
RA Furusawa M., Ohnishi T., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT "AMY-1, a c-Myc-binding protein, is localized in the mitochondria of sperm
RT by association with S-AKAP84, an anchor protein of cAMP-dependent protein
RT kinase.";
RL J. Biol. Chem. 276:36647-36651(2001).
RN [9]
RP INTERACTION WITH MYCBPAP.
RX PubMed=12151104; DOI=10.1016/s0167-4781(02)00411-6;
RA Yukitake H., Furusawa M., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT "AMAP-1, a novel testis-specific AMY-1-binding protein, is differentially
RT expressed during the course of spermatogenesis.";
RL Biochim. Biophys. Acta 1577:126-132(2002).
RN [10]
RP INTERACTION WITH CFAP91.
RC TISSUE=Testis;
RX PubMed=12223483; DOI=10.1074/jbc.m206201200;
RA Yukitake H., Furusawa M., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT "AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary
RT complex between AMY-1, A-kinase anchor protein 84 and a regulatory subunit
RT of cAMP-dependent protein kinase and is phosphorylated by its kinase.";
RL J. Biol. Chem. 277:45480-45492(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-94.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of c-myc-1 binding protein domain from Homo sapiens.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: May control the transcriptional activity of MYC. Stimulates
CC the activation of E box-dependent transcription by MYC.
CC -!- SUBUNIT: Binds via its C-terminal region to the N-terminal region of
CC MYC. Associates with AKAP1/S-AKAP84. Interacts with MYCBPAP. Interacts
CC with CFAP91 (PubMed:12223483). {ECO:0000269|PubMed:11483602,
CC ECO:0000269|PubMed:12151104, ECO:0000269|PubMed:12223483}.
CC -!- INTERACTION:
CC Q99417; Q92667-2: AKAP1; NbExp=2; IntAct=EBI-716185, EBI-2120060;
CC Q99417; Q9Y6D6: ARFGEF1; NbExp=3; IntAct=EBI-716185, EBI-1044254;
CC Q99417; Q9Y6D5: ARFGEF2; NbExp=5; IntAct=EBI-716185, EBI-2837511;
CC Q99417; Q7Z4T9-3: CFAP91; NbExp=5; IntAct=EBI-716185, EBI-17172567;
CC Q99417; Q8TBZ2: MYCBPAP; NbExp=4; IntAct=EBI-716185, EBI-1391585;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion.
CC Note=Translocates into the nucleus in the S phase of the cell cycle
CC upon an increase of MYC expression. Found in the mitochondria when
CC associated with AKAP1.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, pancreas,
CC skeletal muscle and kidney. Also present at low levels in lung.
CC -!- SIMILARITY: Belongs to the AMY1 family. {ECO:0000305}.
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DR EMBL; D50692; BAA09338.1; -; mRNA.
DR EMBL; BT007109; AAP35773.1; -; mRNA.
DR EMBL; AB007191; BAA22408.1; -; mRNA.
DR EMBL; AB451287; BAG70101.1; -; mRNA.
DR EMBL; AB451419; BAG70233.1; -; mRNA.
DR EMBL; AK311886; BAG34827.1; -; mRNA.
DR EMBL; AL139260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008686; AAH08686.1; -; mRNA.
DR CCDS; CCDS431.1; -.
DR RefSeq; NP_036465.2; NM_012333.4.
DR PDB; 2YY0; X-ray; 2.40 A; A/B/C/D=42-94.
DR PDBsum; 2YY0; -.
DR AlphaFoldDB; Q99417; -.
DR SMR; Q99417; -.
DR BioGRID; 117673; 86.
DR CORUM; Q99417; -.
DR IntAct; Q99417; 55.
DR MINT; Q99417; -.
DR STRING; 9606.ENSP00000380702; -.
DR GlyGen; Q99417; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99417; -.
DR PhosphoSitePlus; Q99417; -.
DR BioMuta; MYCBP; -.
DR EPD; Q99417; -.
DR jPOST; Q99417; -.
DR MassIVE; Q99417; -.
DR MaxQB; Q99417; -.
DR PaxDb; Q99417; -.
DR PeptideAtlas; Q99417; -.
DR PRIDE; Q99417; -.
DR ProteomicsDB; 78257; -.
DR TopDownProteomics; Q99417; -.
DR Antibodypedia; 17669; 227 antibodies from 28 providers.
DR DNASU; 26292; -.
DR Ensembl; ENST00000397572.5; ENSP00000380702.2; ENSG00000214114.9.
DR GeneID; 26292; -.
DR KEGG; hsa:26292; -.
DR MANE-Select; ENST00000397572.5; ENSP00000380702.2; NM_012333.5; NP_036465.2.
DR UCSC; uc001ccs.4; human.
DR CTD; 26292; -.
DR DisGeNET; 26292; -.
DR GeneCards; MYCBP; -.
DR HGNC; HGNC:7554; MYCBP.
DR HPA; ENSG00000214114; Low tissue specificity.
DR MIM; 606535; gene.
DR neXtProt; NX_Q99417; -.
DR OpenTargets; ENSG00000214114; -.
DR PharmGKB; PA31354; -.
DR VEuPathDB; HostDB:ENSG00000214114; -.
DR eggNOG; ENOG502S2IC; Eukaryota.
DR GeneTree; ENSGT00390000017974; -.
DR HOGENOM; CLU_135895_0_1_1; -.
DR InParanoid; Q99417; -.
DR OMA; QYEPLQE; -.
DR OrthoDB; 1497203at2759; -.
DR PhylomeDB; Q99417; -.
DR TreeFam; TF329224; -.
DR PathwayCommons; Q99417; -.
DR SignaLink; Q99417; -.
DR BioGRID-ORCS; 26292; 55 hits in 1038 CRISPR screens.
DR EvolutionaryTrace; Q99417; -.
DR GeneWiki; MYCBP; -.
DR GenomeRNAi; 26292; -.
DR Pharos; Q99417; Tbio.
DR PRO; PR:Q99417; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99417; protein.
DR Bgee; ENSG00000214114; Expressed in olfactory segment of nasal mucosa and 155 other tissues.
DR ExpressionAtlas; Q99417; baseline and differential.
DR Genevisible; Q99417; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR InterPro; IPR026060; AMY1.
DR PANTHER; PTHR13168; PTHR13168; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Mitochondrion; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..103
FT /note="c-Myc-binding protein"
FT /id="PRO_0000220980"
FT CONFLICT 65
FT /note="L -> V (in Ref. 1; BAA09338/BAA22408)"
FT /evidence="ECO:0000305"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:2YY0"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2YY0"
FT HELIX 60..90
FT /evidence="ECO:0007829|PDB:2YY0"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2YY0"
SQ SEQUENCE 103 AA; 11967 MW; 72B9BD179A6808D0 CRC64;
MAHYKAADSK REQFRRYLEK SGVLDTLTKV LVALYEEPEK PNSALDFLKH HLGAATPENP
EIELLRLELA EMKEKYEAIV EENKKLKAKL AQYEPPQEEK RAE
