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P14174

- MIF_HUMAN

UniProt

P14174 - MIF_HUMAN

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Protein

Macrophage migration inhibitory factor

Gene

MIF

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

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. 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
Complete GO annotation...

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-KW
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: UniProtKB
  6. vesicle Source: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiP14174. baseline.
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 – 108Combined sources
Helixi12 – 143Combined sources
Helixi19 – 3113Combined sources
Helixi35 – 373Combined sources
Beta strandi39 – 435Combined sources
Beta strandi47 – 504Combined sources
Beta strandi58 – 669Combined sources
Helixi70 – 8819Combined sources
Helixi92 – 943Combined sources
Beta strandi95 – 1017Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 1143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4K9GX-ray1.55A/B/C2-115[»]
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.
GeneTreeiENSGT00730000111101.
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

        10         20         30         40         50
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF
60 70 80 90 100
GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY
110
DMNAANVGWN NSTFA
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000613839; ENSP00000482779; ENSG00000276701.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4K9G X-ray 1.55 A/B/C 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 CHEMBL2111430.

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 .
ENST00000613839 ; ENSP00000482779 ; ENSG00000276701 .
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.
GeneTreei ENSGT00730000111101.
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.
ExpressionAtlasi P14174. baseline.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 177 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