MNDA_HUMAN
ID MNDA_HUMAN Reviewed; 407 AA.
AC P41218;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Myeloid cell nuclear differentiation antigen;
GN Name=MNDA;
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].
RX PubMed=1644857; DOI=10.1002/jcb.240490114;
RA Briggs J.A., Burrus G.R., Stickney B.D., Briggs R.C.;
RT "Cloning and expression of the human myeloid cell nuclear differentiation
RT antigen: regulation by interferon alpha.";
RL J. Cell. Biochem. 49:82-92(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=1377701; DOI=10.1002/jcb.240480210;
RA Burrus G.R., Briggs J.A., Briggs R.C.;
RT "Characterization of the human myeloid cell nuclear differentiation
RT antigen: relationship to interferon-inducible proteins.";
RL J. Cell. Biochem. 48:190-202(1992).
RN [4]
RP INDUCTION.
RX PubMed=7512843;
RA Briggs R.C., Briggs J.A., Ozer J., Sealy L., Dworkin L.L., Kingsmore S.F.,
RA Seldin M.F., Kaur G.P., Athwal R.S., Dessypris E.N.;
RT "The human myeloid cell nuclear differentiation antigen gene is one of at
RT least two related interferon-inducible genes located on chromosome 1q that
RT are expressed specifically in hematopoietic cells.";
RL Blood 83:2153-2162(1994).
RN [5]
RP TISSUE SPECIFICITY OF ALPHA-INTERFERON INDUCTION.
RX PubMed=8175894; DOI=10.1002/jcb.240540208;
RA Briggs R., Dworkin L., Briggs J., Dessypris E., Stein J., Stein G.,
RA Lian J.;
RT "Interferon alpha selectively affects expression of the human myeloid cell
RT nuclear differentiation antigen in late stage cells in the monocytic but
RT not the granulocytic lineage.";
RL J. Cell. Biochem. 54:198-206(1994).
RN [6]
RP CHROMOSOMAL LOCATION, AND TISSUE SPECIFIC INDUCTION.
RX PubMed=7806273; DOI=10.1007/bf00188431;
RA Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R.,
RA Baker E.;
RT "The closely linked genes encoding the myeloid nuclear differentiation
RT antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression.";
RL Immunogenetics 41:40-43(1995).
RN [7]
RP INTERACTION.
RX PubMed=9712147;
RX DOI=10.1002/(sici)1097-4644(19980915)70:4<489::aid-jcb6>3.0.co;2-f;
RA Xie J., Briggs J.A., Briggs R.C.;
RT "Human hematopoietic cell specific nuclear protein MNDA interacts with the
RT multifunctional transcription factor YY1 and stimulates YY1 DNA binding.";
RL J. Cell. Biochem. 70:489-506(1998).
RN [8]
RP STRUCTURE BY NMR OF 1-90.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pyrin (PAAD-DAPIN) domain in human myeloid cell
RT nuclear differentiation antigen.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: May act as a transcriptional activator/repressor in the
CC myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific
CC response to interferon. Stimulates the DNA binding of the
CC transcriptional repressor protein YY1.
CC -!- SUBUNIT: Participates in a ternary complex with YY1 and the YY1 target
CC DNA element. Binds nucleolin and nucleophosmin/NPM/B23.
CC -!- INTERACTION:
CC P41218; P01023: A2M; NbExp=3; IntAct=EBI-2829677, EBI-640741;
CC P41218; P50570-2: DNM2; NbExp=3; IntAct=EBI-2829677, EBI-10968534;
CC P41218; P28799: GRN; NbExp=3; IntAct=EBI-2829677, EBI-747754;
CC P41218; P42858: HTT; NbExp=18; IntAct=EBI-2829677, EBI-466029;
CC P41218; Q92993: KAT5; NbExp=3; IntAct=EBI-2829677, EBI-399080;
CC P41218; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2829677, EBI-11742507;
CC P41218; P08581: MET; NbExp=3; IntAct=EBI-2829677, EBI-1039152;
CC P41218; P49821: NDUFV1; NbExp=3; IntAct=EBI-2829677, EBI-748312;
CC P41218; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-2829677, EBI-3390132;
CC P41218; O43933: PEX1; NbExp=3; IntAct=EBI-2829677, EBI-988601;
CC P41218; P49810: PSEN2; NbExp=3; IntAct=EBI-2829677, EBI-2010251;
CC P41218; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2829677, EBI-9090795;
CC P41218; O14656-2: TOR1A; NbExp=3; IntAct=EBI-2829677, EBI-25847109;
CC P41218; P02766: TTR; NbExp=3; IntAct=EBI-2829677, EBI-711909;
CC P41218; P61981: YWHAG; NbExp=3; IntAct=EBI-2829677, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Uniformly distributed
CC throughout the interphase cell nucleus. Associates with chromatin.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in cells of the myeloid
CC lineage. Found in promyelocyte stage cells as well as in all other
CC stage cells including peripheral blood monocytes and granulocytes. Also
CC appears in myeloblast cells in some cases of acute myeloid Leukemia.
CC {ECO:0000269|PubMed:8175894}.
CC -!- INDUCTION: Strongly induced by alpha interferon which selectively
CC affects expression in late stage cells in the monocytic but not the
CC granulocytic lineage. Induced in vitro by dimethylsulfoxide and 1,25
CC dihydroxyvitamin D3. {ECO:0000269|PubMed:7512843}.
CC -!- DOMAIN: Its N-terminal half (200 amino acids) is sufficient for maximum
CC enhancement of YY1 DNA binding and a portion of this sequence is
CC responsible for binding YY1.
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DR EMBL; M81750; AAA69696.1; -; mRNA.
DR EMBL; BC032319; AAH32319.1; -; mRNA.
DR CCDS; CCDS1177.1; -.
DR PIR; I55525; I55525.
DR RefSeq; NP_002423.1; NM_002432.2.
DR PDB; 2DBG; NMR; -; A=1-90.
DR PDB; 5H7Q; X-ray; 1.45 A; A=4-98.
DR PDB; 5WPZ; X-ray; 2.00 A; A/B/C/D/E/F=4-98.
DR PDBsum; 2DBG; -.
DR PDBsum; 5H7Q; -.
DR PDBsum; 5WPZ; -.
DR AlphaFoldDB; P41218; -.
DR SMR; P41218; -.
DR BioGRID; 110475; 178.
DR IntAct; P41218; 177.
DR MINT; P41218; -.
DR STRING; 9606.ENSP00000357123; -.
DR iPTMnet; P41218; -.
DR PhosphoSitePlus; P41218; -.
DR BioMuta; MNDA; -.
DR DMDM; 730038; -.
DR EPD; P41218; -.
DR jPOST; P41218; -.
DR MassIVE; P41218; -.
DR PaxDb; P41218; -.
DR PeptideAtlas; P41218; -.
DR PRIDE; P41218; -.
DR ProteomicsDB; 55422; -.
DR Antibodypedia; 34254; 333 antibodies from 30 providers.
DR DNASU; 4332; -.
DR Ensembl; ENST00000368141.5; ENSP00000357123.4; ENSG00000163563.8.
DR GeneID; 4332; -.
DR KEGG; hsa:4332; -.
DR MANE-Select; ENST00000368141.5; ENSP00000357123.4; NM_002432.3; NP_002423.1.
DR CTD; 4332; -.
DR DisGeNET; 4332; -.
DR GeneCards; MNDA; -.
DR HGNC; HGNC:7183; MNDA.
DR HPA; ENSG00000163563; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 159553; gene.
DR neXtProt; NX_P41218; -.
DR OpenTargets; ENSG00000163563; -.
DR PharmGKB; PA30895; -.
DR VEuPathDB; HostDB:ENSG00000163563; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR GeneTree; ENSGT00390000013296; -.
DR HOGENOM; CLU_020123_2_0_1; -.
DR InParanoid; P41218; -.
DR OMA; HNIKCEE; -.
DR OrthoDB; 1304994at2759; -.
DR PhylomeDB; P41218; -.
DR TreeFam; TF337385; -.
DR PathwayCommons; P41218; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P41218; -.
DR BioGRID-ORCS; 4332; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; MNDA; human.
DR EvolutionaryTrace; P41218; -.
DR GeneWiki; MNDA; -.
DR GenomeRNAi; 4332; -.
DR Pharos; P41218; Tbio.
DR PRO; PR:P41218; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P41218; protein.
DR Bgee; ENSG00000163563; Expressed in monocyte and 185 other tissues.
DR ExpressionAtlas; P41218; baseline and differential.
DR Genevisible; P41218; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IBA:GO_Central.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.40.50.140; -; 2.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 1.
DR Pfam; PF02760; HIN; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..407
FT /note="Myeloid cell nuclear differentiation antigen"
FT /id="PRO_0000153724"
FT DOMAIN 1..88
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 196..394
FT /note="HIN-200"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 108..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..137
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 130..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 156
FT /note="S -> R (in dbSNP:rs35417083)"
FT /id="VAR_034107"
FT VARIANT 286
FT /note="V -> L (in dbSNP:rs1056771)"
FT /id="VAR_012055"
FT VARIANT 357
FT /note="H -> Y (in dbSNP:rs2276403)"
FT /id="VAR_020483"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5H7Q"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:5H7Q"
SQ SEQUENCE 407 AA; 45836 MW; F4943C38033C5A83 CRC64;
MVNEYKKILL LKGFELMDDY HFTSIKSLLA YDLGLTTKMQ EEYNRIKITD LMEKKFQGVA
CLDKLIELAK DMPSLKNLVN NLRKEKSKVA KKIKTQEKAP VKKINQEEVG LAAPAPTARN
KLTSEARGRI PVAQKRKTPN KEKTEAKRNK VSQEQSKPPG PSGASTSAAV DHPPLPQTSS
STPSNTSFTP NQETQAQRQV DARRNVPQND PVTVVVLKAT APFKYESPEN GKSTMFHATV
ASKTQYFHVK VFDINLKEKF VRKKVITISD YSECKGVMEI KEASSVSDFN QNFEVPNRII
EIANKTPKIS QLYKQASGTM VYGLFMLQKK SVHKKNTIYE IQDNTGSMDV VGSGKWHNIK
CEKGDKLRLF CLQLRTVDRK LKLVCGSHSF IKVIKAKKNK EGPMNVN
