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O15205 (UBD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Ubiquitin D
Alternative name(s):
Diubiquitin
Ubiquitin-like protein FAT10
Gene names
Name:UBD
Synonyms:FAT10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1L-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN). Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Subunit structure

Interact directly with the 26S proteasome. The interaction with NUB1L vie the N-terminal ubiquitin domain facilitates the linking of UBD-conjugated target protein to the proteasome complex and accelerates its own degradation and that of its conjugates. Interacts with the spindle checkpoint protein MAD2L1 during mitosis. Present in aggresomes of proteasome inhibited cells. Interacts with HDAC6 under proteasome impairment conditions. Forms a thioester with UBA6 in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg). Ref.2 Ref.7 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Accumulates in aggresomes under proteasome inhibition conditions. Ref.6 Ref.15

Tissue specificity

Constitutively expressed in mature dendritic cells and B-cells. Mostly expressed in the reticuloendothelial system (e.g. thymus, spleen), the gastrointestinal system, kidney, lung and prostate gland. Ref.1 Ref.6

Induction

Rapidly degraded by the proteasome. Cell-cycle regulation with highest expression during the S-phase (at protein level). Induced during dendritic cell maturation. Negatively regulated by p53/TP53. High levels in various gastrointestinal and gynecological cancer cells. Induced in RTECs in common renal diseases including diabetic nephropathy (DN), IgA nephropathy (IgAN), and hypertensive nephrosclerosis (HN), as well as in hepatocellular carcinoma (HCC) and during HIVAN. Inducible by the proinflammatory cytokines IFNG/IFN-gamma and TNF in cancers of liver and colon. Repressed by NUB1L (at protein level). Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21

Post-translational modification

Can be acetylated. Ref.15

Miscellaneous

Common types of chronic kidney disease are associated with tubulointerstitial up-regulation of FAT10. FAT10 may mediate NF-kappa-B activation and may promote tubulointerstitial inflammation in chronic kidney diseases.

Sequence similarities

Contains 2 ubiquitin-like domains.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaggresome assembly

Inferred from direct assay Ref.15. Source: UniProtKB

myeloid dendritic cell differentiation

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

protein modification by small protein conjugation

Non-traceable author statement Ref.1. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.8Ref.14. Source: UniProtKB

proteolysis

Non-traceable author statement Ref.1. Source: UniProtKB

response to interferon-gamma

Inferred from expression pattern Ref.14. Source: UniProtKB

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from expression pattern Ref.14. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

   Cellular_componentaggresome

Inferred from direct assay Ref.15. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionproteasome binding

Inferred from direct assay Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.7Ref.11Ref.12Ref.14Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBE2ZQ9H8322EBI-6657186,EBI-720977

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 165165Ubiquitin D
PRO_0000114893

Regions

Domain6 – 8176Ubiquitin-like 1
Domain90 – 16374Ubiquitin-like 2

Sites

Site164 – 1652Activation by thioester intermediate formation with UBA6

Natural variations

Natural variant511L → S.
Corresponds to variant rs2076484 [ dbSNP | Ensembl ].
VAR_024273
Natural variant681I → T.
Corresponds to variant rs2076485 [ dbSNP | Ensembl ].
VAR_024274
Natural variant951S → P.
Corresponds to variant rs2076486 [ dbSNP | Ensembl ].
VAR_024275
Natural variant991A → G.
Corresponds to variant rs2076487 [ dbSNP | Ensembl ].
VAR_025401
Natural variant1201E → K.
Corresponds to variant rs17184290 [ dbSNP | Ensembl ].
VAR_052693
Natural variant1601C → S. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs8337 [ dbSNP | Ensembl ].
VAR_025402
Natural variant1621C → F.
Corresponds to variant rs7757931 [ dbSNP | Ensembl ].
VAR_024276

Experimental info

Mutagenesis164 – 1652GG → AA: Impaired thioester formation-mediated activation by UBA6. Ref.14

Sequences

Sequence LengthMass (Da)Tools
O15205 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 40BE415049920CC6

FASTA16518,473
        10         20         30         40         50         60 
MAPNASCLCV HVRSEEWDLM TFDANPYDSV KKIKEHVRSK TKVPVQDQVL LLGSKILKPR 

        70         80         90        100        110        120 
RSLSSYGIDK EKTIHLTLKV VKPSDEELPL FLVESGDEAK RHLLQVRRSS SVAQVKAMIE 

       130        140        150        160 
TKTGIIPETQ IVTCNGKRLE DGKMMADYGI RKGNLLFLAC YCIGG 

« Hide

References

« Hide 'large scale' references
[1]"Identification and analysis of a novel member of the ubiquitin family expressed in dendritic cells and mature B cells."
Bates E.E.M., Ravel O., Dieu M.-C., Ho S., Guret C., Bridon J.-M., Ait-Yahia S., Briere F., Caux C., Banchereau J., Lebecque S.
Eur. J. Immunol. 27:2471-2477(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-160, TISSUE SPECIFICITY.
[2]"A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2."
Liu Y.-C., Pan J., Zhang C., Fan W., Collinge M., Bender J.R., Weissman S.M.
Proc. Natl. Acad. Sci. U.S.A. 96:4313-4318(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MAD2L1, VARIANT SER-160.
Tissue: Spleen.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-160.
[4]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], VARIANT SER-160.
[5]"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: Urinary bladder.
[6]"Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers."
Lee C.G.L., Ren J., Cheong I.S.Y., Ban K.H.K., Ooi L.L.P.J., Yong Tan S., Kan A., Nuchprayoon I., Jin R., Lee K.-H., Choti M., Lee L.A.
Oncogene 22:2592-2603(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION IN HEPATOCELLULAR CARCINOMA.
[7]"NEDD8 ultimate buster-1L interacts with the ubiquitin-like protein FAT10 and accelerates its degradation."
Hipp M.S., Raasi S., Groettrup M., Schmidtke G.
J. Biol. Chem. 279:16503-16510(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUB1L, INDUCTION BY NUB1L.
[8]"FAT10, a ubiquitin-independent signal for proteasomal degradation."
Hipp M.S., Kalveram B., Raasi S., Groettrup M., Schmidtke G.
Mol. Cell. Biol. 25:3483-3491(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"FAT10, a gene up-regulated in various cancers, is cell-cycle regulated."
Lim C.-B., Zhang D., Lee C.G.
Cell Div. 1:20-20(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY CELL CYCLE.
[10]"Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal disease."
Ross M.J., Wosnitzer M.S., Ross M.D., Granelli B., Gusella G.L., Husain M., Kaufman L., Vasievich M., D'Agati V.D., Wilson P.D., Klotman M.E., Klotman P.E.
J. Am. Soc. Nephrol. 17:996-1004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION IN HIVAN.
[11]"FAT10 plays a role in the regulation of chromosomal stability."
Ren J., Kan A., Leong S.H., Ooi L.L.P.J., Jeang K.-T., Chong S.S., Kon O.L., Lee C.G.L.
J. Biol. Chem. 281:11413-11421(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAD2L1.
[12]"The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10."
Schmidtke G., Kalveram B., Weber E., Bochtler P., Lukasiak S., Hipp M.S., Groettrup M.
J. Biol. Chem. 281:20045-20054(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUB1L AND PROTEASOME.
[13]"p53 negatively regulates the expression of FAT10, a gene upregulated in various cancers."
Zhang D.W., Jeang K.-T., Lee C.G.
Oncogene 25:2318-2327(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY TP53.
[14]"E1-L2 activates both ubiquitin and FAT10."
Chiu Y.-H., Sun Q., Chen Z.J.
Mol. Cell 27:1014-1023(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBA6, THIOESTER FORMATION, INDUCTION BY TNF AND IFNG, MUTAGENESIS OF 164-GLY-GLY-165.
[15]"The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition."
Kalveram B., Schmidtke G., Groettrup M.
J. Cell Sci. 121:4079-4088(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HDAC6, SUBCELLULAR LOCATION, ACETYLATION.
[16]"Proinflammatory cytokines cause FAT10 upregulation in cancers of liver and colon."
Lukasiak S., Schiller C., Oehlschlaeger P., Schmidtke G., Krause P., Legler D.F., Autschbach F., Schirmacher P., Breuhahn K., Groettrup M.
Oncogene 27:6068-6074(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY CYTOKINES.
[17]"Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L."
Schmidtke G., Kalveram B., Groettrup M.
FEBS Lett. 583:591-594(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system."
Ebstein F., Lange N., Urban S., Seifert U., Krueger E., Kloetzel P.-M.
Int. J. Biochem. Cell Biol. 41:1205-1215(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[19]"FAT10: a novel mediator of Vpr-induced apoptosis in human immunodeficiency virus-associated nephropathy."
Snyder A., Alsauskas Z., Gong P., Rosenstiel P.E., Klotman M.E., Klotman P.E., Ross M.J.
J. Virol. 83:11983-11988(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[20]"FAT10 level in human gastric cancer and its relation with mutant p53 level, lymph node metastasis and TNM staging."
Ji F., Jin X., Jiao C.-H., Xu Q.-W., Wang Z.-W., Chen Y.-L.
World J. Gastroenterol. 15:2228-2233(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[21]"The ubiquitin-like protein FAT10 mediates NF-kappa-B activation."
Gong P., Canaan A., Wang B., Leventhal J., Snyder A., Nair V., Cohen C.D., Kretzler M., D'Agati V., Weissman S., Ross M.J.
J. Am. Soc. Nephrol. 21:316-326(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12653 mRNA. Translation: CAA73200.1.
AF123050 mRNA. Translation: AAD52982.1.
AL031983 Genomic DNA. Translation: CAA21458.1.
AL662826 Genomic DNA. Translation: CAI17384.1.
AL645936 Genomic DNA. Translation: CAI18010.1.
CR759766, CR942274 Genomic DNA. Translation: CAQ06603.1.
CR759770 Genomic DNA. Translation: CAQ10041.1.
CR942274, CR759766 Genomic DNA. Translation: CAQ10316.1.
CH471081 Genomic DNA. Translation: EAX03201.1.
BC012472 mRNA. Translation: AAH12472.1.
CCDSCCDS4662.1.
RefSeqNP_006389.2. NM_006398.3.
UniGeneHs.44532.

3D structure databases

ProteinModelPortalO15205.
SMRO15205. Positions 10-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115791. 667 interactions.
IntActO15205. 4 interactions.
STRING9606.ENSP00000366249.

PTM databases

PhosphoSiteO15205.

Proteomic databases

MaxQBO15205.
PaxDbO15205.
PRIDEO15205.

Protocols and materials databases

DNASU10537.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377050; ENSP00000366249; ENSG00000213886.
ENST00000383547; ENSP00000373039; ENSG00000206468.
ENST00000421519; ENSP00000396152; ENSG00000231968.
ENST00000432676; ENSP00000410416; ENSG00000228913.
GeneID10537.
KEGGhsa:10537.
UCSCuc003nmo.3. human.

Organism-specific databases

CTD10537.
GeneCardsGC06M029525.
GC06Mj29519.
GC06Mk29523.
GC06Mm29523.
HGNCHGNC:18795. UBD.
HPAHPA043710.
MIM606050. gene.
neXtProtNX_O15205.
PharmGKBPA38682.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG101094.
InParanoidO15205.
KOK12157.
OMAEINIFFL.
OrthoDBEOG75TMDT.
PhylomeDBO15205.

Gene expression databases

BgeeO15205.
CleanExHS_UBD.
GenevestigatorO15205.

Family and domain databases

InterProIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00240. ubiquitin. 2 hits.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMSSF54236. SSF54236. 2 hits.
PROSITEPS50053. UBIQUITIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBD. human.
GeneWikiUbiquitin_D.
GenomeRNAi10537.
NextBio39977.
PROO15205.
SOURCESearch...

Entry information

Entry nameUBD_HUMAN
AccessionPrimary (citable) accession number: O15205
Secondary accession number(s): B0UZT6 expand/collapse secondary AC list , Q5STL2, Q5SUK2, Q96EC7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: November 24, 2009
Last modified: July 9, 2014
This is version 119 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM