MYPOP_HUMAN
ID MYPOP_HUMAN Reviewed; 399 AA.
AC Q86VE0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Myb-related transcription factor, partner of profilin;
DE AltName: Full=Myb-related protein p42POP;
DE AltName: Full=Partner of profilin;
GN Name=MYPOP; Synonyms=P42POP;
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=Blood;
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 [2]
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).
CC -!- FUNCTION: Transcriptional repressor; DNA-binding protein that
CC specifically recognizes the core sequence 5'-YAAC[GT]G-3'. Dimerization
CC with PFN1 reduces its DNA-binding capacity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PFN1. Homodimer and heterodimer with PFN1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q86VE0; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-2858213, EBI-357530;
CC Q86VE0; O95429: BAG4; NbExp=3; IntAct=EBI-2858213, EBI-2949658;
CC Q86VE0; Q96PG8: BBC3; NbExp=3; IntAct=EBI-2858213, EBI-17289784;
CC Q86VE0; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2858213, EBI-3866279;
CC Q86VE0; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-2858213, EBI-741528;
CC Q86VE0; A0PJX0: CIB4; NbExp=3; IntAct=EBI-2858213, EBI-12868028;
CC Q86VE0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2858213, EBI-3867333;
CC Q86VE0; Q13643: FHL3; NbExp=3; IntAct=EBI-2858213, EBI-741101;
CC Q86VE0; P31943: HNRNPH1; NbExp=3; IntAct=EBI-2858213, EBI-351590;
CC Q86VE0; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2858213, EBI-7060731;
CC Q86VE0; P49639: HOXA1; NbExp=3; IntAct=EBI-2858213, EBI-740785;
CC Q86VE0; O75525: KHDRBS3; NbExp=3; IntAct=EBI-2858213, EBI-722504;
CC Q86VE0; Q92845: KIFAP3; NbExp=3; IntAct=EBI-2858213, EBI-954040;
CC Q86VE0; Q6A162: KRT40; NbExp=3; IntAct=EBI-2858213, EBI-10171697;
CC Q86VE0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2858213, EBI-11749135;
CC Q86VE0; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-2858213, EBI-10172290;
CC Q86VE0; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2858213, EBI-10171774;
CC Q86VE0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-2858213, EBI-10172052;
CC Q86VE0; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-2858213, EBI-10176379;
CC Q86VE0; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-2858213, EBI-1048945;
CC Q86VE0; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-2858213, EBI-12805508;
CC Q86VE0; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-2858213, EBI-9996449;
CC Q86VE0; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-2858213, EBI-10250562;
CC Q86VE0; Q99750: MDFI; NbExp=3; IntAct=EBI-2858213, EBI-724076;
CC Q86VE0; Q5JR59-3: MTUS2; NbExp=5; IntAct=EBI-2858213, EBI-11522433;
CC Q86VE0; O43639: NCK2; NbExp=3; IntAct=EBI-2858213, EBI-713635;
CC Q86VE0; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-2858213, EBI-10172876;
CC Q86VE0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2858213, EBI-22310682;
CC Q86VE0; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-2858213, EBI-3957793;
CC Q86VE0; P79522: PRR3; NbExp=3; IntAct=EBI-2858213, EBI-2803328;
CC Q86VE0; P98179: RBM3; NbExp=3; IntAct=EBI-2858213, EBI-2949699;
CC Q86VE0; P38159: RBMX; NbExp=3; IntAct=EBI-2858213, EBI-743526;
CC Q86VE0; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-2858213, EBI-11994018;
CC Q86VE0; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-2858213, EBI-11987469;
CC Q86VE0; P21673: SAT1; NbExp=3; IntAct=EBI-2858213, EBI-711613;
CC Q86VE0; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-2858213, EBI-11123832;
CC Q86VE0; P22735: TGM1; NbExp=3; IntAct=EBI-2858213, EBI-2562368;
CC Q86VE0; Q63HR2: TNS2; NbExp=3; IntAct=EBI-2858213, EBI-949753;
CC Q86VE0; P62995: TRA2B; NbExp=3; IntAct=EBI-2858213, EBI-725485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The proline-rich region is required for PFN1 interaction.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC044311; AAH44311.2; -; mRNA.
DR CCDS; CCDS33055.1; -.
DR RefSeq; NP_001012661.1; NM_001012643.3.
DR AlphaFoldDB; Q86VE0; -.
DR SMR; Q86VE0; -.
DR BioGRID; 130870; 52.
DR IntAct; Q86VE0; 40.
DR STRING; 9606.ENSP00000325402; -.
DR iPTMnet; Q86VE0; -.
DR PhosphoSitePlus; Q86VE0; -.
DR BioMuta; MYPOP; -.
DR DMDM; 74759426; -.
DR EPD; Q86VE0; -.
DR jPOST; Q86VE0; -.
DR MassIVE; Q86VE0; -.
DR MaxQB; Q86VE0; -.
DR PaxDb; Q86VE0; -.
DR PeptideAtlas; Q86VE0; -.
DR PRIDE; Q86VE0; -.
DR ProteomicsDB; 69990; -.
DR Antibodypedia; 45635; 22 antibodies from 10 providers.
DR DNASU; 339344; -.
DR Ensembl; ENST00000322217.6; ENSP00000325402.4; ENSG00000176182.6.
DR GeneID; 339344; -.
DR KEGG; hsa:339344; -.
DR MANE-Select; ENST00000322217.6; ENSP00000325402.4; NM_001012643.4; NP_001012661.1.
DR UCSC; uc002pdt.4; human.
DR CTD; 339344; -.
DR DisGeNET; 339344; -.
DR GeneCards; MYPOP; -.
DR HGNC; HGNC:20178; MYPOP.
DR HPA; ENSG00000176182; Low tissue specificity.
DR MIM; 617861; gene.
DR neXtProt; NX_Q86VE0; -.
DR OpenTargets; ENSG00000176182; -.
DR PharmGKB; PA164723403; -.
DR VEuPathDB; HostDB:ENSG00000176182; -.
DR eggNOG; ENOG502RV5V; Eukaryota.
DR GeneTree; ENSGT00450000040421; -.
DR HOGENOM; CLU_046143_2_0_1; -.
DR InParanoid; Q86VE0; -.
DR OMA; QEGGCPR; -.
DR OrthoDB; 1378970at2759; -.
DR PhylomeDB; Q86VE0; -.
DR TreeFam; TF338618; -.
DR PathwayCommons; Q86VE0; -.
DR SignaLink; Q86VE0; -.
DR BioGRID-ORCS; 339344; 12 hits in 1081 CRISPR screens.
DR GenomeRNAi; 339344; -.
DR Pharos; Q86VE0; Tdark.
DR PRO; PR:Q86VE0; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q86VE0; protein.
DR Bgee; ENSG00000176182; Expressed in oocyte and 113 other tissues.
DR Genevisible; Q86VE0; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR028002; Myb_DNA-bind_5.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF13873; Myb_DNA-bind_5; 1.
DR SMART; SM00717; SANT; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..399
FT /note="Myb-related transcription factor, partner of
FT profilin"
FT /id="PRO_0000344799"
FT DOMAIN 12..84
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 87..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..86
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 382..385
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 390..393
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 155..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..332
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..399
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 42508 MW; F949A70588E0C454 CRC64;
MASAAAGEAE ETTRLRKPRF SFEENQILIR EVRAHYPQLY GAQSRRVSVA ERRRVWDGIA
AKINGITSWK RTGQEVQKRW NDFKRRTKEK LARVPHSTQG AGPAAEDAFS AEEETIFAIL
GPGVAAPGAG AGAEEPPAAP SSQPPPPSAC PQRYVLSEDR REDRRADTSA HSKAGSSSPE
PWARPSCTPQ EGGCPRPKER ESPPPSALQP VQLPRLALSP PPPAPPLPPP PPLAQVAPSP
PSPPPPPRPP PTLSASDPSL DFLRAQQETA NAIRELAGTL RQGLAKLSEA LSALLPLLPG
TPVDSLPPPL PPPPPPPPPP RPVLPPPAPK VEITPEPVSV VAAVVDGAVV AARGVIIAPR
SEEGAPRPPP APLPPHDSPP HKRRKGFPTR KRRGRWKSP