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Protein

Myeloid cell nuclear differentiation antigen

Gene

MNDA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.

GO - Molecular functioni

GO - Biological processi

  • B cell receptor signaling pathway Source: UniProtKB
  • cellular defense response Source: ProtInc
  • cellular response to DNA damage stimulus Source: UniProtKB
  • negative regulation of B cell proliferation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloid cell nuclear differentiation antigen
Gene namesi
Name:MNDA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7183. MNDA.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Uniformly distributed throughout the interphase cell nucleus. Associates with chromatin.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30895.

Polymorphism and mutation databases

BioMutaiMNDA.
DMDMi730038.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Myeloid cell nuclear differentiation antigenPRO_0000153724Add
BLAST

Proteomic databases

MaxQBiP41218.
PaxDbiP41218.
PeptideAtlasiP41218.
PRIDEiP41218.

PTM databases

PhosphoSiteiP41218.

Expressioni

Tissue specificityi

Expressed constitutively in cells of the myeloid lineage. Found in promyelocyte stage cells as well as in all other stage cells including peripheral blood monocytes and granulocytes. Also appear in myeloblast cells in some cases of acute myeloid Leukemia.1 Publication

Inductioni

Strongly induced by alpha interferon which selectively affects expression in late stage cells in the monocytic but not the granulocytic lineage. Induced in vitro by dimethylsulfoxide and 1,25 dihydroxyvitamin D3.1 Publication

Gene expression databases

BgeeiP41218.
CleanExiHS_MNDA.
ExpressionAtlasiP41218. baseline and differential.
GenevestigatoriP41218.

Organism-specific databases

HPAiHPA034532.

Interactioni

Subunit structurei

Participates in a ternary complex with YY1 and the YY1 target DNA element. Binds nucleolin and nucleophosmin/NPM/B23.

Binary interactionsi

WithEntry#Exp.IntActNotes
WHSC1L1Q9BZ952EBI-2829677,EBI-3390132

Protein-protein interaction databases

BioGridi110475. 3 interactions.
IntActiP41218. 163 interactions.
MINTiMINT-8373462.
STRINGi9606.ENSP00000357123.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Turni12 – 165Combined sources
Helixi19 – 3315Combined sources
Helixi37 – 426Combined sources
Helixi45 – 5511Combined sources
Helixi60 – 689Combined sources
Helixi73 – 753Combined sources
Helixi76 – 8914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBGNMR-A1-90[»]
ProteinModelPortaliP41218.
SMRiP41218. Positions 1-90, 205-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41218.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888DAPINPROSITE-ProRule annotationAdd
BLAST
Domaini196 – 394199HIN-200PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 1377Nuclear localization signalSequence Analysis

Domaini

Its N-terminal half (200 amino acids) is sufficient for maximum enhancement of YY1 DNA binding and a portion of this sequence is responsible for binding YY1.

Sequence similaritiesi

Contains 1 DAPIN domain.PROSITE-ProRule annotation
Contains 1 HIN-200 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG81691.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiP41218.
OMAiGKWHNIK.
OrthoDBiEOG7ZD1V8.
PhylomeDBiP41218.
TreeFamiTF337385.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
InterProiIPR004020. DAPIN.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF02760. HIN. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
PROSITEiPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNEYKKILL LKGFELMDDY HFTSIKSLLA YDLGLTTKMQ EEYNRIKITD
60 70 80 90 100
LMEKKFQGVA CLDKLIELAK DMPSLKNLVN NLRKEKSKVA KKIKTQEKAP
110 120 130 140 150
VKKINQEEVG LAAPAPTARN KLTSEARGRI PVAQKRKTPN KEKTEAKRNK
160 170 180 190 200
VSQEQSKPPG PSGASTSAAV DHPPLPQTSS STPSNTSFTP NQETQAQRQV
210 220 230 240 250
DARRNVPQND PVTVVVLKAT APFKYESPEN GKSTMFHATV ASKTQYFHVK
260 270 280 290 300
VFDINLKEKF VRKKVITISD YSECKGVMEI KEASSVSDFN QNFEVPNRII
310 320 330 340 350
EIANKTPKIS QLYKQASGTM VYGLFMLQKK SVHKKNTIYE IQDNTGSMDV
360 370 380 390 400
VGSGKWHNIK CEKGDKLRLF CLQLRTVDRK LKLVCGSHSF IKVIKAKKNK

EGPMNVN
Length:407
Mass (Da):45,836
Last modified:February 1, 1995 - v1
Checksum:iF4943C38033C5A83
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561S → R.
Corresponds to variant rs35417083 [ dbSNP | Ensembl ].
VAR_034107
Natural varianti286 – 2861V → L.
Corresponds to variant rs1056771 [ dbSNP | Ensembl ].
VAR_012055
Natural varianti357 – 3571H → Y.
Corresponds to variant rs2276403 [ dbSNP | Ensembl ].
VAR_020483

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81750 mRNA. Translation: AAA69696.1.
BC032319 mRNA. Translation: AAH32319.1.
CCDSiCCDS1177.1.
PIRiI55525.
RefSeqiNP_002423.1. NM_002432.1.
UniGeneiHs.153837.

Genome annotation databases

EnsembliENST00000368141; ENSP00000357123; ENSG00000163563.
GeneIDi4332.
KEGGihsa:4332.
UCSCiuc001fsz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81750 mRNA. Translation: AAA69696.1.
BC032319 mRNA. Translation: AAH32319.1.
CCDSiCCDS1177.1.
PIRiI55525.
RefSeqiNP_002423.1. NM_002432.1.
UniGeneiHs.153837.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DBGNMR-A1-90[»]
ProteinModelPortaliP41218.
SMRiP41218. Positions 1-90, 205-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110475. 3 interactions.
IntActiP41218. 163 interactions.
MINTiMINT-8373462.
STRINGi9606.ENSP00000357123.

PTM databases

PhosphoSiteiP41218.

Polymorphism and mutation databases

BioMutaiMNDA.
DMDMi730038.

Proteomic databases

MaxQBiP41218.
PaxDbiP41218.
PeptideAtlasiP41218.
PRIDEiP41218.

Protocols and materials databases

DNASUi4332.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368141; ENSP00000357123; ENSG00000163563.
GeneIDi4332.
KEGGihsa:4332.
UCSCiuc001fsz.1. human.

Organism-specific databases

CTDi4332.
GeneCardsiGC01P158801.
HGNCiHGNC:7183. MNDA.
HPAiHPA034532.
MIMi159553. gene.
neXtProtiNX_P41218.
PharmGKBiPA30895.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81691.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiP41218.
OMAiGKWHNIK.
OrthoDBiEOG7ZD1V8.
PhylomeDBiP41218.
TreeFamiTF337385.

Miscellaneous databases

ChiTaRSiMNDA. human.
EvolutionaryTraceiP41218.
GeneWikiiMNDA.
GenomeRNAii4332.
NextBioi17047.
PROiP41218.
SOURCEiSearch...

Gene expression databases

BgeeiP41218.
CleanExiHS_MNDA.
ExpressionAtlasiP41218. baseline and differential.
GenevestigatoriP41218.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
InterProiIPR004020. DAPIN.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF02760. HIN. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
PROSITEiPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the human myeloid cell nuclear differentiation antigen: regulation by interferon alpha."
    Briggs J.A., Burrus G.R., Stickney B.D., Briggs R.C.
    J. Cell. Biochem. 49:82-92(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  3. "Characterization of the human myeloid cell nuclear differentiation antigen: relationship to interferon-inducible proteins."
    Burrus G.R., Briggs J.A., Briggs R.C.
    J. Cell. Biochem. 48:190-202(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
  4. "The human myeloid cell nuclear differentiation antigen gene is one of at least two related interferon-inducible genes located on chromosome 1q that are expressed specifically in hematopoietic cells."
    Briggs R.C., Briggs J.A., Ozer J., Sealy L., Dworkin L.L., Kingsmore S.F., Seldin M.F., Kaur G.P., Athwal R.S., Dessypris E.N.
    Blood 83:2153-2162(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Interferon alpha selectively affects expression of the human myeloid cell nuclear differentiation antigen in late stage cells in the monocytic but not the granulocytic lineage."
    Briggs R., Dworkin L., Briggs J., Dessypris E., Stein J., Stein G., Lian J.
    J. Cell. Biochem. 54:198-206(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY OF ALPHA-INTERFERON INDUCTION.
  6. "The closely linked genes encoding the myeloid nuclear differentiation antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression."
    Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R., Baker E.
    Immunogenetics 41:40-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL LOCATION, TISSUE SPECIFIC INDUCTION.
  7. "Human hematopoietic cell specific nuclear protein MNDA interacts with the multifunctional transcription factor YY1 and stimulates YY1 DNA binding."
    Xie J., Briggs J.A., Briggs R.C.
    J. Cell. Biochem. 70:489-506(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION.
  8. "Solution structure of the pyrin (PAAD-DAPIN) domain in human myeloid cell nuclear differentiation antigen."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-90.

Entry informationi

Entry nameiMNDA_HUMAN
AccessioniPrimary (citable) accession number: P41218
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.