Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P14174

- MIF_HUMAN

UniProt

P14174 - MIF_HUMAN

Protein

Macrophage migration inhibitory factor

Gene

MIF

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

    Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity.3 Publications

    Catalytic activityi

    Keto-phenylpyruvate = enol-phenylpyruvate.
    L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.

    Kineticsi

    1. KM=249 µM for phenylpyruvate1 Publication
    2. KM=168 µM for p-hydroxyphenylpyruvate1 Publication

    Vmax=2113 µmol/min/mg enzyme toward phenylpyruvate1 Publication

    Vmax=524 µmol/min/mg enzyme toward p-hydroxyphenylpyruvate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21Proton acceptor; via imino nitrogen
    Binding sitei33 – 331Substrate
    Binding sitei65 – 651Substrate; via amide nitrogen
    Binding sitei98 – 981Substrate

    GO - Molecular functioni

    1. chemoattractant activity Source: BHF-UCL
    2. cytokine activity Source: UniProtKB
    3. cytokine receptor binding Source: BHF-UCL
    4. dopachrome isomerase activity Source: UniProtKB
    5. phenylpyruvate tautomerase activity Source: MGI
    6. protein binding Source: UniProtKB
    7. receptor binding Source: BHF-UCL

    GO - Biological processi

    1. carboxylic acid metabolic process Source: BHF-UCL
    2. cell aging Source: Ensembl
    3. cell proliferation Source: UniProtKB
    4. cell surface receptor signaling pathway Source: UniProtKB
    5. DNA damage response, signal transduction by p53 class mediator Source: Ensembl
    6. inflammatory response Source: UniProtKB-KW
    7. innate immune response Source: UniProtKB-KW
    8. negative regulation of apoptotic process Source: UniProtKB
    9. negative regulation of cell aging Source: BHF-UCL
    10. negative regulation of cell cycle arrest Source: BHF-UCL
    11. negative regulation of cellular protein metabolic process Source: Ensembl
    12. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    13. negative regulation of gene expression Source: BHF-UCL
    14. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    15. negative regulation of mature B cell apoptotic process Source: Ensembl
    16. negative regulation of myeloid cell apoptotic process Source: Ensembl
    17. positive chemotaxis Source: GOC
    18. positive regulation of arachidonic acid secretion Source: Ensembl
    19. positive regulation of B cell proliferation Source: BHF-UCL
    20. positive regulation of chemokine (C-X-C motif) ligand 2 production Source: Ensembl
    21. positive regulation of cytokine secretion Source: BHF-UCL
    22. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    23. positive regulation of fibroblast proliferation Source: BHF-UCL
    24. positive regulation of lipopolysaccharide-mediated signaling pathway Source: Ensembl
    25. positive regulation of MAP kinase activity Source: Ensembl
    26. positive regulation of myeloid leukocyte cytokine production involved in immune response Source: Ensembl
    27. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    28. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    29. positive regulation of phosphorylation Source: BHF-UCL
    30. positive regulation of prostaglandin secretion involved in immune response Source: Ensembl
    31. positive regulation of protein kinase A signaling Source: BHF-UCL
    32. prostaglandin biosynthetic process Source: UniProtKB
    33. protein homotrimerization Source: UniProtKB
    34. regulation of macrophage activation Source: UniProtKB

    Keywords - Molecular functioni

    Cytokine, Isomerase

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage migration inhibitory factor (EC:5.3.2.1)
    Short name:
    MIF
    Alternative name(s):
    Glycosylation-inhibiting factor
    Short name:
    GIF
    L-dopachrome isomerase
    L-dopachrome tautomerase (EC:5.3.3.12)
    Phenylpyruvate tautomerase
    Gene namesi
    Name:MIF
    Synonyms:GLIF, MMIF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7097. MIF.

    Subcellular locationi

    Secreted. Cytoplasm
    Note: Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens.

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: UniProtKB-SubCell
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB-KW
    5. extracellular vesicular exosome Source: UniProt
    6. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Rheumatoid arthritis systemic juvenile (RASJ) [MIM:604302]: An inflammatory articular disorder with systemic-onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi111 – 1111N → C: Causes formation of interchain disulfide bonds with Cys-81 from another subunit. 1 Publication

    Organism-specific databases

    MIMi604302. phenotype.
    Orphaneti85414. Systemic-onset juvenile idiopathic arthritis.
    PharmGKBiPA30819.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 115114Macrophage migration inhibitory factorPRO_0000158062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei78 – 781N6-acetyllysine; alternate1 Publication
    Modified residuei78 – 781N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP14174.
    PaxDbiP14174.
    PeptideAtlasiP14174.
    PRIDEiP14174.

    2D gel databases

    SWISS-2DPAGEP14174.

    PTM databases

    PhosphoSiteiP14174.

    Expressioni

    Inductioni

    Up-regulated in concanavalin-A-treated lymphocytes. Up-regulated in macrophages upon exposure to M.tuberculosis antigens.2 Publications

    Gene expression databases

    BgeeiP14174.
    CleanExiHS_MIF.
    GenevestigatoriP14174.

    Organism-specific databases

    HPAiCAB005284.
    HPA003868.

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with CXCR2 extracellular domain By similarity. Interacts with the CD74 extracellular domain, COPS5 and BNIPL.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2L11O43521-25EBI-372712,EBI-526420

    Protein-protein interaction databases

    BioGridi110428. 23 interactions.
    DIPiDIP-31137N.
    IntActiP14174. 17 interactions.
    MINTiMINT-5000040.
    STRINGi9606.ENSP00000215754.

    Structurei

    Secondary structure

    1
    115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Helixi12 – 143
    Helixi19 – 3113
    Helixi35 – 373
    Beta strandi39 – 435
    Beta strandi47 – 504
    Beta strandi58 – 669
    Helixi70 – 8819
    Helixi92 – 943
    Beta strandi95 – 1017
    Helixi104 – 1063
    Beta strandi107 – 1093
    Beta strandi112 – 1143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CA7X-ray2.50A/B/C2-115[»]
    1CGQX-ray2.00A/B/C2-115[»]
    1GCZX-ray1.90A/B/C2-115[»]
    1GD0X-ray1.50A/B/C2-115[»]
    1GIFX-ray1.90A/B/C1-115[»]
    1LJTX-ray2.00A/B/C2-115[»]
    1MIFX-ray2.60A/B/C1-115[»]
    1P1GX-ray2.50A/B/C2-115[»]
    2OOHX-ray1.85A/B/C2-115[»]
    2OOWX-ray1.75A/B/C2-115[»]
    2OOZX-ray1.80A/B/C2-115[»]
    3B9SX-ray1.80A/B/C2-115[»]
    3CE4X-ray1.55A/B/C2-115[»]
    3DJHX-ray1.25A/B/C2-115[»]
    3DJIX-ray1.95A/B/C/D/E/F2-115[»]
    3HOFX-ray1.90A/B/C1-115[»]
    3IJGX-ray1.70A/B/C2-115[»]
    3IJJX-ray1.25A/B/C2-115[»]
    3JSFX-ray1.93A/B/C2-115[»]
    3JSGX-ray1.58A/B/C2-115[»]
    3JTUX-ray1.86A/B/C2-115[»]
    3L5PX-ray1.80A/B/C2-115[»]
    3L5RX-ray1.94A/B/C2-115[»]
    3L5SX-ray1.86A/B/C2-115[»]
    3L5TX-ray1.86A/B/C2-115[»]
    3L5UX-ray1.90A/B/C2-115[»]
    3L5VX-ray1.70A/B/C2-115[»]
    3SMBX-ray1.60A/B/C2-115[»]
    3SMCX-ray1.80A/B/C2-115[»]
    3U18X-ray1.90A/B/C2-115[»]
    3WNRX-ray2.01A/B/C2-115[»]
    3WNSX-ray1.66A/B/C2-115[»]
    3WNTX-ray2.07A/B/C2-115[»]
    4ETGX-ray1.61A/B/C2-115[»]
    4EUIX-ray1.70A/B/C2-115[»]
    4EVGX-ray1.70A/B/C2-115[»]
    4F2KX-ray1.53A/B/C2-115[»]
    4GRNX-ray1.25A/B/C2-115[»]
    4GROX-ray2.00A/B/C/D/E/F/G/H2-115[»]
    4GRPX-ray1.27A/B/C2-115[»]
    4GRQX-ray1.65A/B/C2-115[»]
    4GRRX-ray1.47A/B/C3-115[»]
    4GRUX-ray1.92A/B/C2-115[»]
    4GUMX-ray2.33A/B/C/D/E/F/G/H/I2-115[»]
    4OSFX-ray1.62A/B/C2-115[»]
    4OYQX-ray1.70A/B/C2-115[»]
    4P01X-ray2.07A/B/C2-115[»]
    4P0HX-ray1.93A/B/C2-115[»]
    ProteinModelPortaliP14174.
    SMRiP14174. Positions 2-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14174.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MIF family.Curated

    Phylogenomic databases

    eggNOGiNOG08790.
    HOGENOMiHOG000112325.
    HOVERGENiHBG003240.
    InParanoidiP14174.
    KOiK07253.
    OMAiKPERYVM.
    OrthoDBiEOG7GXPDN.
    PhylomeDBiP14174.
    TreeFamiTF313853.

    Family and domain databases

    InterProiIPR001398. Macrophage_inhib_fac.
    IPR019829. Macrophage_inhib_fac_CS.
    IPR014347. Tautomerase/MIF_sf.
    [Graphical view]
    PANTHERiPTHR11954. PTHR11954. 1 hit.
    PfamiPF01187. MIF. 1 hit.
    [Graphical view]
    ProDomiPD004816. Macrophage_inhib_fac. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF55331. SSF55331. 1 hit.
    PROSITEiPS01158. MIF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14174-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF    50
    GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY 100
    DMNAANVGWN NSTFA 115
    Length:115
    Mass (Da):12,476
    Last modified:January 23, 2007 - v4
    Checksum:i56D51107C05286B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 593CAL → WAF in ABQ95571. 1 PublicationCurated
    Sequence conflicti67 – 671K → R in CAG46452. 1 PublicationCurated
    Sequence conflicti79 – 791L → Q in CAG46452. 1 PublicationCurated
    Sequence conflicti81 – 811C → F in ABQ95571. 1 PublicationCurated
    Sequence conflicti106 – 1061N → S in AAA36315. (PubMed:2552447)Curated
    Sequence conflicti113 – 1131T → P in ABQ95571. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25639 mRNA. Translation: AAA36315.1.
    L10612 mRNA. Translation: AAA35892.1.
    Z23063 mRNA. Translation: CAA80598.1.
    L19686 Genomic DNA. Translation: AAA21814.1.
    AF469046 mRNA. Translation: AAL78635.1.
    EF611126 mRNA. Translation: ABQ95571.1.
    CR456520 mRNA. Translation: CAG30406.1.
    AK311929 mRNA. Translation: BAG34870.1.
    CR407644 mRNA. Translation: CAG28572.1.
    CR541651 mRNA. Translation: CAG46452.1.
    BT007148 mRNA. Translation: AAP35812.1.
    DQ307455 Genomic DNA. Translation: ABB96245.1.
    CH471095 Genomic DNA. Translation: EAW59620.1.
    BC000447 mRNA. Translation: AAH00447.1.
    BC007676 mRNA. Translation: AAH07676.1.
    BC008914 mRNA. Translation: AAH08914.1.
    BC013976 mRNA. Translation: AAH13976.1.
    BC022414 mRNA. Translation: AAH22414.1.
    BC053376 mRNA. Translation: AAH53376.1.
    M95775 mRNA. Translation: AAA36179.1.
    CCDSiCCDS13819.1.
    PIRiA48793.
    RefSeqiNP_002406.1. NM_002415.1.
    UniGeneiHs.407995.

    Genome annotation databases

    EnsembliENST00000215754; ENSP00000215754; ENSG00000240972.
    GeneIDi4282.
    KEGGihsa:4282.
    UCSCiuc002zyr.1. human.

    Polymorphism databases

    DMDMi1170955.

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25639 mRNA. Translation: AAA36315.1 .
    L10612 mRNA. Translation: AAA35892.1 .
    Z23063 mRNA. Translation: CAA80598.1 .
    L19686 Genomic DNA. Translation: AAA21814.1 .
    AF469046 mRNA. Translation: AAL78635.1 .
    EF611126 mRNA. Translation: ABQ95571.1 .
    CR456520 mRNA. Translation: CAG30406.1 .
    AK311929 mRNA. Translation: BAG34870.1 .
    CR407644 mRNA. Translation: CAG28572.1 .
    CR541651 mRNA. Translation: CAG46452.1 .
    BT007148 mRNA. Translation: AAP35812.1 .
    DQ307455 Genomic DNA. Translation: ABB96245.1 .
    CH471095 Genomic DNA. Translation: EAW59620.1 .
    BC000447 mRNA. Translation: AAH00447.1 .
    BC007676 mRNA. Translation: AAH07676.1 .
    BC008914 mRNA. Translation: AAH08914.1 .
    BC013976 mRNA. Translation: AAH13976.1 .
    BC022414 mRNA. Translation: AAH22414.1 .
    BC053376 mRNA. Translation: AAH53376.1 .
    M95775 mRNA. Translation: AAA36179.1 .
    CCDSi CCDS13819.1.
    PIRi A48793.
    RefSeqi NP_002406.1. NM_002415.1.
    UniGenei Hs.407995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CA7 X-ray 2.50 A/B/C 2-115 [» ]
    1CGQ X-ray 2.00 A/B/C 2-115 [» ]
    1GCZ X-ray 1.90 A/B/C 2-115 [» ]
    1GD0 X-ray 1.50 A/B/C 2-115 [» ]
    1GIF X-ray 1.90 A/B/C 1-115 [» ]
    1LJT X-ray 2.00 A/B/C 2-115 [» ]
    1MIF X-ray 2.60 A/B/C 1-115 [» ]
    1P1G X-ray 2.50 A/B/C 2-115 [» ]
    2OOH X-ray 1.85 A/B/C 2-115 [» ]
    2OOW X-ray 1.75 A/B/C 2-115 [» ]
    2OOZ X-ray 1.80 A/B/C 2-115 [» ]
    3B9S X-ray 1.80 A/B/C 2-115 [» ]
    3CE4 X-ray 1.55 A/B/C 2-115 [» ]
    3DJH X-ray 1.25 A/B/C 2-115 [» ]
    3DJI X-ray 1.95 A/B/C/D/E/F 2-115 [» ]
    3HOF X-ray 1.90 A/B/C 1-115 [» ]
    3IJG X-ray 1.70 A/B/C 2-115 [» ]
    3IJJ X-ray 1.25 A/B/C 2-115 [» ]
    3JSF X-ray 1.93 A/B/C 2-115 [» ]
    3JSG X-ray 1.58 A/B/C 2-115 [» ]
    3JTU X-ray 1.86 A/B/C 2-115 [» ]
    3L5P X-ray 1.80 A/B/C 2-115 [» ]
    3L5R X-ray 1.94 A/B/C 2-115 [» ]
    3L5S X-ray 1.86 A/B/C 2-115 [» ]
    3L5T X-ray 1.86 A/B/C 2-115 [» ]
    3L5U X-ray 1.90 A/B/C 2-115 [» ]
    3L5V X-ray 1.70 A/B/C 2-115 [» ]
    3SMB X-ray 1.60 A/B/C 2-115 [» ]
    3SMC X-ray 1.80 A/B/C 2-115 [» ]
    3U18 X-ray 1.90 A/B/C 2-115 [» ]
    3WNR X-ray 2.01 A/B/C 2-115 [» ]
    3WNS X-ray 1.66 A/B/C 2-115 [» ]
    3WNT X-ray 2.07 A/B/C 2-115 [» ]
    4ETG X-ray 1.61 A/B/C 2-115 [» ]
    4EUI X-ray 1.70 A/B/C 2-115 [» ]
    4EVG X-ray 1.70 A/B/C 2-115 [» ]
    4F2K X-ray 1.53 A/B/C 2-115 [» ]
    4GRN X-ray 1.25 A/B/C 2-115 [» ]
    4GRO X-ray 2.00 A/B/C/D/E/F/G/H 2-115 [» ]
    4GRP X-ray 1.27 A/B/C 2-115 [» ]
    4GRQ X-ray 1.65 A/B/C 2-115 [» ]
    4GRR X-ray 1.47 A/B/C 3-115 [» ]
    4GRU X-ray 1.92 A/B/C 2-115 [» ]
    4GUM X-ray 2.33 A/B/C/D/E/F/G/H/I 2-115 [» ]
    4OSF X-ray 1.62 A/B/C 2-115 [» ]
    4OYQ X-ray 1.70 A/B/C 2-115 [» ]
    4P01 X-ray 2.07 A/B/C 2-115 [» ]
    4P0H X-ray 1.93 A/B/C 2-115 [» ]
    ProteinModelPortali P14174.
    SMRi P14174. Positions 2-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110428. 23 interactions.
    DIPi DIP-31137N.
    IntActi P14174. 17 interactions.
    MINTi MINT-5000040.
    STRINGi 9606.ENSP00000215754.

    Chemistry

    BindingDBi P14174.
    ChEMBLi CHEMBL2085.

    PTM databases

    PhosphoSitei P14174.

    Polymorphism databases

    DMDMi 1170955.

    2D gel databases

    SWISS-2DPAGE P14174.

    Proteomic databases

    MaxQBi P14174.
    PaxDbi P14174.
    PeptideAtlasi P14174.
    PRIDEi P14174.

    Protocols and materials databases

    DNASUi 4282.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215754 ; ENSP00000215754 ; ENSG00000240972 .
    GeneIDi 4282.
    KEGGi hsa:4282.
    UCSCi uc002zyr.1. human.

    Organism-specific databases

    CTDi 4282.
    GeneCardsi GC22P024236.
    H-InvDB HIX0041297.
    HGNCi HGNC:7097. MIF.
    HPAi CAB005284.
    HPA003868.
    MIMi 153620. gene.
    604302. phenotype.
    neXtProti NX_P14174.
    Orphaneti 85414. Systemic-onset juvenile idiopathic arthritis.
    PharmGKBi PA30819.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG08790.
    HOGENOMi HOG000112325.
    HOVERGENi HBG003240.
    InParanoidi P14174.
    KOi K07253.
    OMAi KPERYVM.
    OrthoDBi EOG7GXPDN.
    PhylomeDBi P14174.
    TreeFami TF313853.

    Miscellaneous databases

    EvolutionaryTracei P14174.
    GeneWikii Macrophage_migration_inhibitory_factor.
    GenomeRNAii 4282.
    NextBioi 16845.
    PROi P14174.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14174.
    CleanExi HS_MIF.
    Genevestigatori P14174.

    Family and domain databases

    InterProi IPR001398. Macrophage_inhib_fac.
    IPR019829. Macrophage_inhib_fac_CS.
    IPR014347. Tautomerase/MIF_sf.
    [Graphical view ]
    PANTHERi PTHR11954. PTHR11954. 1 hit.
    Pfami PF01187. MIF. 1 hit.
    [Graphical view ]
    ProDomi PD004816. Macrophage_inhib_fac. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF55331. SSF55331. 1 hit.
    PROSITEi PS01158. MIF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding a human macrophage migration inhibitory factor."
      Weiser W.Y., Temple P.A., Witek-Giannotti J.S., Remold H.G., Clark S.C., David J.R.
      Proc. Natl. Acad. Sci. U.S.A. 86:7522-7526(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION.
    2. "Molecular cloning and functional expression of a cDNA encoding glycosylation-inhibiting factor."
      Mikayama T., Nakano T., Gomi H., Nakagawa Y., Liu Y.C., Iwamatsu A., Weiser W.Y., Ishizaka K., Sato M., Ishii Y.
      Proc. Natl. Acad. Sci. U.S.A. 90:10056-10060(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    3. "Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF)."
      Bernhagen J., Mitchell R.A., Calandra T., Voelter W., Cerami A., Bucala R.
      Biochemistry 33:14144-14155(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Cloning the human gene for macrophage migration inhibitory factor (MIF)."
      Paralkar V., Wistow G.J.
      Genomics 19:48-51(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The effect of macrophage migration inhibitory factor in the atherogenesis process."
      Shan Z.X., Yu X.Y., Lin S.G., Lin Q.X., Fu Y.H., Tan H.H.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Amplification and expression of macrophage migration inhibitory factor (MIF) in tissue of squamous carcinoma of the cervix."
      Wu S.H., Xie J., Shang H.X., Li Y., Zhang Z.
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    11. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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: Brain, Lung, Skin and Uterus.
    14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12.
      Tissue: Platelet.
    15. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11.
      Tissue: Liver.
    16. "The major binding protein of the interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor."
      Zeng F.Y., Weiser W.Y., Kratzin H., Stahl B., Karas M., Gabius H.J.
      Arch. Biochem. Biophys. 303:74-80(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-24.
    17. "A macrophage migration inhibitory factor is expressed in the differentiating cells of the eye lens."
      Wistow G.J., Shaughnessy M., Lee D.C., Hodin J., Zelenka P.S.
      Proc. Natl. Acad. Sci. U.S.A. 90:1272-1275(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-115.
      Tissue: Lens.
    18. Cited for: INTERACTION WITH COPS5, SUBCELLULAR LOCATION.
    19. "A novel 5'-flanking region polymorphism of macrophage migration inhibitory factor is associated with systemic-onset juvenile idiopathic arthritis."
      The British peadiatric rheumatology study group
      Donn R.P., Shelley E., Ollier W.E.R., Thomson W.
      Arthritis Rheum. 44:1782-1785(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO SYSTEMIC JUVENILE RHEUMATOID ARTHRITIS.
    20. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    21. "The apoptosis-associated protein BNIPL interacts with two cell proliferation-related proteins, MIF and GFER."
      Shen L., Hu J., Lu H., Wu M., Qin W., Wan D., Li Y.-Y., Gu J.
      FEBS Lett. 540:86-90(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BNIPL.
    22. Cited for: INTERACTION WITH CD74.
    23. "Macrophage migration inhibitory factor reduces the growth of virulent Mycobacterium tuberculosis in human macrophages."
      Oddo M., Calandra T., Bucala R., Meylan P.R.A.
      Infect. Immun. 73:3783-3786(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
    24. "Association between high levels of blood macrophage migration inhibitory factor, inappropriate adrenal response, and early death in patients with severe sepsis."
      Emonts M., Sweep F.C.G.J., Grebenchtchikov N., Geurts-Moespot A., Knaup M., Chanson A.L., Erard V., Renner P., Hermans P.W.M., Hazelzet J.A., Calandra T.
      Clin. Infect. Dis. 44:1321-1328(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN SEPSIS-RELATED DEATH.
    25. "The Golgi-associated protein p115 mediates the secretion of macrophage migration inhibitory factor."
      Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D., Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B., Bernhagen J., Bucala R.
      J. Immunol. 182:6896-6906(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH USO1.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1-A resolution."
      Sugimoto H., Suzuki M., Nakagawa A., Tanaka I., Nishihira J.
      FEBS Lett. 389:145-148(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    30. "The crystal structure of human glycosylation-inhibiting factor is a trimeric barrel with three 6-stranded beta-sheets."
      Kato Y., Muto T., Tomura T., Tsumura H., Watarai H., Mikayama T., Ishizaka K., Kuroki R.
      Proc. Natl. Acad. Sci. U.S.A. 93:3007-3010(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    31. "Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor."
      Sun H.W., Bernhagen J., Bucala R., Lolis E.
      Proc. Natl. Acad. Sci. U.S.A. 93:5191-5196(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    32. "Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity."
      Lubetsky J.B., Swope M., Dealwis C., Blake P., Lolis E.
      Biochemistry 38:7346-7354(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    33. "Coumarin and chromen-4-one analogues as tautomerase inhibitors of macrophage migration inhibitory factor: discovery and X-ray crystallography."
      Orita M., Yamamoto S., Katayama N., Aoki M., Takayama K., Yamagiwa Y., Seki N., Suzuki H., Kurihara H., Sakashita H., Takeuchi M., Fujita S., Yamada T., Tanaka A.
      J. Med. Chem. 44:540-547(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH TAUTOMERASE INHIBITOR, CATALYTIC ACTIVITY.
    34. "Alternative chemical modifications reverse the binding orientation of a pharmacophore scaffold in the active site of macrophage migration inhibitory factor."
      Crichlow G.V., Cheng K.F., Dabideen D., Ochani M., Aljabari B., Pavlov V.A., Miller E.J., Lolis E., Al-Abed Y.
      J. Biol. Chem. 282:23089-23095(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH CARBONYLOXIME-BASED INHIBITORS, SUBUNIT.
    35. "Structural and kinetic analyses of macrophage migration inhibitory factor active site interactions."
      Crichlow G.V., Lubetsky J.B., Leng L., Bucala R., Lolis E.J.
      Biochemistry 48:132-139(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR N-ACETYL-P-BENZOQUINONE IMINE, SUBUNIT, CATALYTIC ACTIVITY.
    36. "MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations."
      Fan C., Rajasekaran D., Syed M.A., Leng L., Loria J.P., Bhandari V., Bucala R., Lolis E.J.
      Proc. Natl. Acad. Sci. U.S.A. 110:10994-10999(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CD74, MUTAGENESIS OF ASN-111, SUBUNIT.

    Entry informationi

    Entry nameiMIF_HUMAN
    AccessioniPrimary (citable) accession number: P14174
    Secondary accession number(s): A5Z1R8
    , B2R4S3, Q2V4Y5, Q6FHV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 175 of the entry and version 4 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

    Miscellaneous

    Serum levels of MIF are elevated in patients with severe sepsis or septic shock. High levels of MIF are correlated with low survival. Drugs that inhibit tautomerase activity protect against death due to sepsis.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3