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P14174 (MIF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage migration inhibitory factor

Short name=MIF
EC=5.3.2.1
Alternative name(s):
Glycosylation-inhibiting factor
Short name=GIF
L-dopachrome isomerase
L-dopachrome tautomerase
EC=5.3.3.12
Phenylpyruvate tautomerase
Gene names
Name:MIF
Synonyms:GLIF, MMIF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.23 Ref.24 Ref.36

Catalytic activity

Keto-phenylpyruvate = enol-phenylpyruvate. Ref.33 Ref.35 Ref.36

L-dopachrome = 5,6-dihydroxyindole-2-carboxylate. Ref.33 Ref.35 Ref.36

Subunit structure

Homotrimer. Interacts with CXCR2 extracellular domain By similarity. Interacts with the CD74 extracellular domain, COPS5 and BNIPL. Ref.18 Ref.21 Ref.22 Ref.25 Ref.34 Ref.35 Ref.36

Subcellular location

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. Ref.1 Ref.2 Ref.18 Ref.23 Ref.25

Induction

Up-regulated in concanavalin-A-treated lymphocytes. Up-regulated in macrophages upon exposure to M.tuberculosis antigens. Ref.1 Ref.23

Involvement in disease

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.

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.

Sequence similarities

Belongs to the MIF family.

Biophysicochemical properties

Kinetic parameters:

KM=249 µM for phenylpyruvate Ref.20

KM=168 µM for p-hydroxyphenylpyruvate

Vmax=2113 µmol/min/mg enzyme toward phenylpyruvate

Vmax=524 µmol/min/mg enzyme toward p-hydroxyphenylpyruvate

Ontologies

Keywords
   Biological processImmunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Isomerase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

carboxylic acid metabolic process

Inferred from direct assay Ref.22. Source: BHF-UCL

cell aging

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from direct assay Ref.22. Source: UniProtKB

cell surface receptor signaling pathway

Inferred from direct assay Ref.22. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from direct assay Ref.22. Source: UniProtKB

negative regulation of cell aging

Inferred from direct assay PubMed 10562313. Source: BHF-UCL

negative regulation of cell cycle arrest

Inferred from direct assay PubMed 10562313. Source: BHF-UCL

negative regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from direct assay PubMed 10562313. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

negative regulation of mature B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of myeloid cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive chemotaxis

Inferred from direct assay PubMed 19602265. Source: GOC

positive regulation of B cell proliferation

Inferred from direct assay Ref.22. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.22PubMed 17045821. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine (C-X-C motif) ligand 2 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from direct assay PubMed 19602265. Source: BHF-UCL

positive regulation of fibroblast proliferation

Inferred from direct assay Ref.22. Source: BHF-UCL

positive regulation of lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of myeloid leukocyte cytokine production involved in immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

positive regulation of phosphorylation

Inferred from direct assay Ref.22. Source: BHF-UCL

positive regulation of prostaglandin secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase A signaling

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

prostaglandin biosynthetic process

Inferred from direct assay Ref.22. Source: UniProtKB

protein homotrimerization

Inferred from physical interaction Ref.34. Source: UniProtKB

regulation of macrophage activation

Non-traceable author statement Ref.22. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay Ref.22. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from direct assay Ref.22. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

   Molecular_functionchemoattractant activity

Inferred from direct assay PubMed 19602265. Source: BHF-UCL

cytokine activity

Inferred from direct assay Ref.22. Source: UniProtKB

cytokine receptor binding

Inferred from physical interaction PubMed 17045821. Source: BHF-UCL

dopachrome isomerase activity

Inferred from direct assay Ref.34. Source: UniProtKB

phenylpyruvate tautomerase activity

Inferred from direct assay PubMed 16285950. Source: MGI

protein binding

Inferred from physical interaction Ref.21. Source: UniProtKB

receptor binding

Inferred from physical interaction Ref.22. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL2L11O43521-25EBI-372712,EBI-526420

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14 Ref.15
Chain2 – 115114Macrophage migration inhibitory factor
PRO_0000158062

Sites

Active site21Proton acceptor; via imino nitrogen
Binding site331Substrate
Binding site651Substrate; via amide nitrogen
Binding site981Substrate

Amino acid modifications

Modified residue781N6-acetyllysine; alternate Ref.26
Modified residue781N6-succinyllysine; alternate By similarity

Experimental info

Mutagenesis1111N → C: Causes formation of interchain disulfide bonds with Cys-81 from another subunit. Ref.36
Sequence conflict57 – 593CAL → WAF in ABQ95571. Ref.6
Sequence conflict671K → R in CAG46452. Ref.9
Sequence conflict791L → Q in CAG46452. Ref.9
Sequence conflict811C → F in ABQ95571. Ref.6
Sequence conflict1061N → S in AAA36315. Ref.1
Sequence conflict1131T → P in ABQ95571. Ref.6

Secondary structure

......................... 115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14174 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 56D51107C05286B2

FASTA11512,476
        10         20         30         40         50         60 
MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC 

        70         80         90        100        110 
SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA 

« Hide

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1."
Kleemann R., Hausser A., Geiger G., Mischke R., Burger-Kentischer A., Flieger O., Johannes F.-J., Roger T., Calandra T., Kapurniotu A., Grell M., Finkelmeier D., Brunner H., Bernhagen J.
Nature 408:211-216(2000) [PubMed] [Europe PMC] [Abstract]
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]"Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis."
Tan T.H.P., Edgerton S.A.V., Kumari R., McAlister M.S.B., Roe S.M., Nagl S., Pearl L.H., Selkirk M.E., Bianco A.E., Totty N.F., Engwerda C., Gray C.A., Meyer D.J., Rowe S.M.
Biochem. J. 357:373-383(2001) [PubMed] [Europe PMC] [Abstract]
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]"MIF signal transduction initiated by binding to CD74."
Leng L., Metz C.N., Fang Y., Xu J., Donnelly S., Baugh J., Delohery T., Chen Y., Mitchell R.A., Bucala R.
J. Exp. Med. 197:1467-1476(2003) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13819.1.
PIRA48793.
RefSeqNP_002406.1. NM_002415.1.
UniGeneHs.407995.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP14174.
SMRP14174. Positions 2-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110428. 22 interactions.
DIPDIP-31137N.
IntActP14174. 17 interactions.
MINTMINT-5000040.
STRING9606.ENSP00000215754.

Chemistry

BindingDBP14174.
ChEMBLCHEMBL2085.

PTM databases

PhosphoSiteP14174.

Polymorphism databases

DMDM1170955.

2D gel databases

SWISS-2DPAGEP14174.

Proteomic databases

MaxQBP14174.
PaxDbP14174.
PeptideAtlasP14174.
PRIDEP14174.

Protocols and materials databases

DNASU4282.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215754; ENSP00000215754; ENSG00000240972.
GeneID4282.
KEGGhsa:4282.
UCSCuc002zyr.1. human.

Organism-specific databases

CTD4282.
GeneCardsGC22P024236.
H-InvDBHIX0041297.
HGNCHGNC:7097. MIF.
HPACAB005284.
HPA003868.
MIM153620. gene.
604302. phenotype.
neXtProtNX_P14174.
Orphanet85414. Systemic-onset juvenile idiopathic arthritis.
PharmGKBPA30819.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG08790.
HOGENOMHOG000112325.
HOVERGENHBG003240.
InParanoidP14174.
KOK07253.
OMAKPERYVM.
OrthoDBEOG7GXPDN.
PhylomeDBP14174.
TreeFamTF313853.

Gene expression databases

BgeeP14174.
CleanExHS_MIF.
GenevestigatorP14174.

Family and domain databases

InterProIPR001398. Macrophage_inhib_fac.
IPR019829. Macrophage_inhib_fac_CS.
IPR014347. Tautomerase/MIF_sf.
[Graphical view]
PANTHERPTHR11954. PTHR11954. 1 hit.
PfamPF01187. MIF. 1 hit.
[Graphical view]
ProDomPD004816. Macrophage_inhib_fac. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF55331. SSF55331. 1 hit.
PROSITEPS01158. MIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14174.
GeneWikiMacrophage_migration_inhibitory_factor.
GenomeRNAi4282.
NextBio16845.
PROP14174.
SOURCESearch...

Entry information

Entry nameMIF_HUMAN
AccessionPrimary (citable) accession number: P14174
Secondary accession number(s): A5Z1R8 expand/collapse secondary AC list , B2R4S3, Q2V4Y5, Q6FHV0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 173 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM