AF1Q_HUMAN
ID AF1Q_HUMAN Reviewed; 90 AA.
AC Q13015;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein AF1q;
GN Name=MLLT11; Synonyms=AF1Q;
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], CHROMOSOMAL REARRANGEMENT, AND TISSUE
RP SPECIFICITY.
RX PubMed=7833468;
RA Tse W., Zhu W., Chen H.S., Cohen A.;
RT "A novel gene, AF1q, fused to MLL in t(1;11)(q21;q23), is specifically
RT expressed in leukemic and immature hematopoietic cells.";
RL Blood 85:650-656(1995).
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].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and Lung;
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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 24-LEU--LEU-32,
RP UBIQUITINATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=21715312; DOI=10.1182/blood-2011-01-333179;
RA Parcelier A., Maharzi N., Delord M., Robledo-Sarmiento M., Nelson E.,
RA Belakhdar-Mekid H., Pla M., Kuranda K., Parietti V., Goodhardt M.,
RA Legrand N., Bernstein I.D., Gluckman J.C., Sigaux F., Canque B.;
RT "AF1q/MLLT11 regulates the emergence of human prothymocytes through
RT cooperative interaction with the Notch signaling pathway.";
RL Blood 118:1784-1796(2011).
RN [8]
RP INTERACTION WITH HSPA8 AND LAMP2.
RX PubMed=24880125; DOI=10.1016/j.yexcr.2014.05.013;
RA Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D., Ji C.;
RT "Degradation of AF1Q by chaperone-mediated autophagy.";
RL Exp. Cell Res. 327:48-56(2014).
RN [9]
RP FUNCTION, INTERACTION WITH TCF7, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26079538; DOI=10.18632/oncotarget.4136;
RA Park J., Schlederer M., Schreiber M., Ice R., Merkel O., Bilban M.,
RA Hofbauer S., Kim S., Addison J., Zou J., Ji C., Bunting S.T., Wang Z.,
RA Shoham M., Huang G., Bago-Horvath Z., Gibson L.F., Rojanasakul Y.,
RA Remick S., Ivanov A., Pugacheva E., Bunting K.D., Moriggl R., Kenner L.,
RA Tse W.;
RT "AF1q is a novel TCF7 co-factor which activates CD44 and promotes breast
RT cancer metastasis.";
RL Oncotarget 6:20697-20710(2015).
CC -!- FUNCTION: Cofactor for the transcription factor TCF7 (PubMed:26079538).
CC Involved in regulation of lymphoid development by driving multipotent
CC hematopoietic progenitor cells towards a T cell fate (PubMed:21715312).
CC {ECO:0000269|PubMed:21715312, ECO:0000269|PubMed:26079538}.
CC -!- SUBUNIT: Interacts with HSPA8 and LAMP2 isoform A; the interaction may
CC target MLLT11 for degradation via chaperone-mediated autophagy
CC (PubMed:24880125). Interacts with TCF7 (PubMed:26079538).
CC {ECO:0000269|PubMed:24880125, ECO:0000269|PubMed:26079538}.
CC -!- INTERACTION:
CC Q13015; P36402: TCF7; NbExp=2; IntAct=EBI-6269719, EBI-2119465;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21715312,
CC ECO:0000269|PubMed:26079538}. Cytoplasm {ECO:0000269|PubMed:21715312,
CC ECO:0000269|PubMed:26079538}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:21715312}.
CC Note=Continuous nuclear export is followed by degradation.
CC {ECO:0000269|PubMed:21715312}.
CC -!- TISSUE SPECIFICITY: Expressed in myoepithelial cells of normal breast
CC tissue (at protein level) (PubMed:26079538). Highly expressed in thymus
CC (PubMed:7833468). Expressed in colon, small intestine, prostate and
CC ovary. Not detected in peripheral blood lymphocytes and spleen
CC (PubMed:7833468). {ECO:0000269|PubMed:26079538,
CC ECO:0000269|PubMed:7833468}.
CC -!- PTM: Ubiquitinated, leading to degradation.
CC {ECO:0000269|PubMed:21715312}.
CC -!- DISEASE: Note=A chromosomal aberration involving MLLT11 is found in
CC acute leukemias. Translocation t(1;11)(q21;q23) with KMT2A/MLL1.
CC -!- SIMILARITY: Belongs to the MLLT11 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF1qID12.html";
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DR EMBL; U16954; AAA70088.1; -; mRNA.
DR EMBL; BT006799; AAP35445.1; -; mRNA.
DR EMBL; CR456879; CAG33160.1; -; mRNA.
DR EMBL; AL590133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006471; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC008445; AAH08445.1; -; mRNA.
DR EMBL; BC009624; AAH09624.1; -; mRNA.
DR EMBL; BC019253; AAH19253.1; -; mRNA.
DR EMBL; BC021703; AAH21703.1; -; mRNA.
DR EMBL; BC022448; AAH22448.1; -; mRNA.
DR CCDS; CCDS982.1; -.
DR PIR; I38889; I38889.
DR RefSeq; NP_006809.1; NM_006818.3.
DR AlphaFoldDB; Q13015; -.
DR SMR; Q13015; -.
DR BioGRID; 116161; 53.
DR IntAct; Q13015; 23.
DR MINT; Q13015; -.
DR STRING; 9606.ENSP00000357917; -.
DR iPTMnet; Q13015; -.
DR MetOSite; Q13015; -.
DR PhosphoSitePlus; Q13015; -.
DR BioMuta; MLLT11; -.
DR EPD; Q13015; -.
DR jPOST; Q13015; -.
DR MassIVE; Q13015; -.
DR PaxDb; Q13015; -.
DR PeptideAtlas; Q13015; -.
DR PRIDE; Q13015; -.
DR ProteomicsDB; 59101; -.
DR TopDownProteomics; Q13015; -.
DR Antibodypedia; 34047; 120 antibodies from 22 providers.
DR DNASU; 10962; -.
DR Ensembl; ENST00000368921.5; ENSP00000357917.3; ENSG00000213190.4.
DR GeneID; 10962; -.
DR KEGG; hsa:10962; -.
DR MANE-Select; ENST00000368921.5; ENSP00000357917.3; NM_006818.4; NP_006809.1.
DR CTD; 10962; -.
DR DisGeNET; 10962; -.
DR GeneCards; MLLT11; -.
DR HGNC; HGNC:16997; MLLT11.
DR HPA; ENSG00000213190; Tissue enhanced (brain).
DR MIM; 604684; gene.
DR neXtProt; NX_Q13015; -.
DR OpenTargets; ENSG00000213190; -.
DR PharmGKB; PA142671347; -.
DR VEuPathDB; HostDB:ENSG00000213190; -.
DR eggNOG; ENOG502S7MB; Eukaryota.
DR GeneTree; ENSGT00390000009895; -.
DR HOGENOM; CLU_2440320_0_0_1; -.
DR InParanoid; Q13015; -.
DR OMA; FNYWKEP; -.
DR OrthoDB; 1586302at2759; -.
DR PhylomeDB; Q13015; -.
DR TreeFam; TF336906; -.
DR PathwayCommons; Q13015; -.
DR SignaLink; Q13015; -.
DR SIGNOR; Q13015; -.
DR BioGRID-ORCS; 10962; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; MLLT11; human.
DR GenomeRNAi; 10962; -.
DR Pharos; Q13015; Tbio.
DR PRO; PR:Q13015; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13015; protein.
DR Bgee; ENSG00000213190; Expressed in pons and 197 other tissues.
DR ExpressionAtlas; Q13015; baseline and differential.
DR Genevisible; Q13015; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IDA:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR026778; MLLT11_fam.
DR InterPro; IPR033461; WRNPLPNID.
DR PANTHER; PTHR15404; PTHR15404; 1.
DR Pfam; PF15017; WRNPLPNID; 1.
PE 1: Evidence at protein level;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..90
FT /note="Protein AF1q"
FT /id="PRO_0000064471"
FT MOTIF 24..32
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:21715312"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97783"
FT MUTAGEN 24..32
FT /note="LSELEGLGL->ASEAEGAGA: Constitutive nuclear
FT sequestration."
FT /evidence="ECO:0000269|PubMed:21715312"
SQ SEQUENCE 90 AA; 10061 MW; B37C6F7303C9EBF8 CRC64;
MRDPVSSQYS SFLFWRMPIP ELDLSELEGL GLSDTATYKV KDSSVGKMIG QATAADQEKN
PEGDGLLEYS TFNFWRAPIA SIHSFELDLL
