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Q9ULC4 (MCTS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malignant T-cell-amplified sequence 1

Short name=MCT-1
Alternative name(s):
Multiple copies T-cell malignancies
Gene names
Name:MCTS1
Synonyms:MCT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anti-oncogene that play a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constituvely expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Plays a role as translation enhancer; Recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; Up-regulates protein levels of BCL2L2, TFDP1, MRE11A, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiples chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion of angiogenesis through the decline of inhibitory THBS1/thrombospondin-1, and inhibition of apoptosis. Involved in the process of proteasome degradation to down-regulate Tumor suppressor p53/TP53 in breast cancer cell; Positively regulates phosphorylation of MAPK1 and MAPK3. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

Interacts (via PUA domain) with DENR. Ref.12

Subcellular location

Cytoplasm. Note: Nuclear relocalization after DNA damage. Ref.8 Ref.12

Tissue specificity

Ubiquitous. Over-expressed in T-cell lymphoid cell lines and in non-Hodgkin lymphoma cell lines as well as in a subset of primary large B-cell lymphomas. Ref.1

Induction

By DNA damaging agents such as gamma irradiation, adriamycin or taxol in lymphoid cells, but not by stress stimuli such as heat shock. This induction of protein expression does not occur at the RNA level, and does not require new protein synthesis. Ref.8

Domain

The PUA RNA-binding domain is critical for cap binding, but not sufficient for translation enhancer function. MCT1 N-terminal region is required to enhance translation possibly through interaction with other proteins. Ref.12

Post-translational modification

Phosphorylation is critical for stabilization and promotion of cell proliferation.

Sequence similarities

Belongs to the MCTS1 family.

Contains 1 PUA domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ULC4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ULC4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MFKKFDEKENVSNCIQLKTSVI → MENYSFLDKE
Isoform 3 (identifier: Q9ULC4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MFKK → MGKGR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Malignant T-cell-amplified sequence 1
PRO_0000344786

Regions

Domain92 – 17180PUA

Amino acid modifications

Modified residue811Phosphothreonine; by MAPK1 and MAPK3 Ref.14
Modified residue1181Phosphoserine; by CDK1 Ref.14

Natural variations

Alternative sequence1 – 2222MFKKF…KTSVI → MENYSFLDKE in isoform 2.
VSP_034856
Alternative sequence1 – 44MFKK → MGKGR in isoform 3.
VSP_041352
Natural variant1061L → H.
Corresponds to variant rs2233110 [ dbSNP | Ensembl ].
VAR_045632

Experimental info

Mutagenesis811T → A: No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction. Ref.14
Mutagenesis1181S → A: No phosphorylation by CDK1; No cell growth alteration. Ref.14
Sequence conflict251I → L in AAH95461. Ref.6

Secondary structure

...................................... 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2FC00C7A992E24EB

FASTA18120,555
        10         20         30         40         50         60 
MFKKFDEKEN VSNCIQLKTS VIKGIKNQLI EQFPGIEPWL NQIMPKKDPV KIVRCHEHIE 

        70         80         90        100        110        120 
ILTVNGELLF FRQREGPFYP TLRLLHKYPF ILPHQQVDKG AIKFVLSGAN IMCPGLTSPG 

       130        140        150        160        170        180 
AKLYPAAVDT IVAIMAEGKQ HALCVGVMKM SAEDIEKVNK GIGIENIHYL NDGLWHMKTY 


K 

« Hide

Isoform 2 [UniParc].

Checksum: 4EC881C03823737A
Show »

FASTA16919,229
Isoform 3 [UniParc].

Checksum: 89F724E4C7657902
Show »

FASTA18220,550

References

« Hide 'large scale' references
[1]"A novel candidate oncogene, MCT-1, is involved in cell cycle progression."
Prosniak M., Dierov J., Okami K., Tilton B., Jameson B., Sawaya B.E., Gartenhaus R.B.
Cancer Res. 58:4233-4237(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
[2]"NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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] (ISOFORMS 1 AND 3).
Tissue: Brain.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Chondrosarcoma and Eye.
[7]"Increased G1 cyclin/cdk activity in cells overexpressing the candidate oncogene, MCT-1."
Dierov J., Prosniak M., Gallia G., Gartenhaus R.B.
J. Cell. Biochem. 74:544-550(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Expression and stabilization of the MCT-1 protein by DNA damaging agents."
Herbert G.B., Shi B., Gartenhaus R.B.
Oncogene 20:6777-6783(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[9]"Expression of the candidate MCT-1 oncogene in B- and T-cell lymphoid malignancies."
Shi B., Hsu H.-L., Evens A.M., Gordon L.I., Gartenhaus R.B.
Blood 102:297-302(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"MCT-1 oncogene contributes to increased in vivo tumorigenicity of MCF7 cells by promotion of angiogenesis and inhibition of apoptosis."
Levenson A.S., Thurn K.E., Simons L.A., Veliceasa D., Jarrett J., Osipo C., Jordan V.C., Volpert O.V., Satcher R.L. Jr., Gartenhaus R.B.
Cancer Res. 65:10651-10656(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The MCT-1 oncogene product impairs cell cycle checkpoint control and transforms human mammary epithelial cells."
Hsu H.-L., Shi B., Gartenhaus R.B.
Oncogene 24:4956-4964(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"MCT-1 protein interacts with the cap complex and modulates messenger RNA translational profiles."
Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E., He H., Gartenhaus R.B.
Cancer Res. 66:8994-9001(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PUA, INTERACTION WITH DENR.
[13]"MCT-1 oncogene downregulates p53 and destabilizes genome structure in the response to DNA double-strand damage."
Hsu H.-L., Choy C.O., Kasiappan R., Shih H.-J., Sawyer J.R., Shu C.-L., Chu K.-L., Chen Y.-R., Hsu H.-F., Gartenhaus R.B.
DNA Repair 6:1319-1332(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Phosphorylation of MCT-1 by p44/42 MAPK is required for its stabilization in response to DNA damage."
Nandi S., Reinert L.S., Hachem A., Mazan-Mamczarz K., Hagner P., He H., Gartenhaus R.B.
Oncogene 26:2283-2289(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT THR-81 AND SER-118, MUTAGENESIS OF THR-81 AND SER-118.
[15]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB034206 mRNA. Translation: BAA86055.1.
AY364258 mRNA. Translation: AAQ76817.1.
AK294834 mRNA. Translation: BAG57943.1.
AK311993 mRNA. Translation: BAG34931.1.
AC011890 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11874.1.
BC001013 mRNA. Translation: AAH01013.1.
BC095461 mRNA. Translation: AAH95461.1.
RefSeqNP_001131026.1. NM_001137554.1.
NP_054779.1. NM_014060.2.
UniGeneHs.102696.
Hs.670803.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R90X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-181[»]
ProteinModelPortalQ9ULC4.
SMRQ9ULC4. Positions 1-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118806. 25 interactions.
IntActQ9ULC4. 1 interaction.
MINTMINT-1405141.
STRING9606.ENSP00000360365.

PTM databases

PhosphoSiteQ9ULC4.

Polymorphism databases

DMDM74735052.

Proteomic databases

PaxDbQ9ULC4.
PeptideAtlasQ9ULC4.
PRIDEQ9ULC4.

Protocols and materials databases

DNASU28985.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371315; ENSP00000360365; ENSG00000232119. [Q9ULC4-3]
ENST00000371317; ENSP00000360367; ENSG00000232119. [Q9ULC4-1]
GeneID28985.
KEGGhsa:28985.
UCSCuc004esx.3. human. [Q9ULC4-1]
uc011mub.2. human. [Q9ULC4-3]
uc022cdn.1. human. [Q9ULC4-2]

Organism-specific databases

CTD28985.
GeneCardsGC0XP119727.
HGNCHGNC:23357. MCTS1.
HPAHPA001045.
MIM300587. gene.
neXtProtNX_Q9ULC4.
PharmGKBPA128394649.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2016.
HOGENOMHOG000223988.
HOVERGENHBG105551.
KOK07575.
OMAGSNIMCP.
OrthoDBEOG7S7SG1.
PhylomeDBQ9ULC4.
TreeFamTF315123.

Gene expression databases

BgeeQ9ULC4.
CleanExHS_MCTS1.
GenevestigatorQ9ULC4.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
InterProIPR002478. PUA.
IPR015947. PUA-like_domain.
IPR016437. Transl_RNA-bd_prd.
IPR004521. Uncharacterised_CHP00451.
[Graphical view]
PANTHERPTHR22798. PTHR22798. 1 hit.
PfamPF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF005067. Tma_RNA-bind_prd. 1 hit.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00451. unchar_dom_2. 1 hit.
PROSITEPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi28985.
NextBio51887.
PROQ9ULC4.
SOURCESearch...

Entry information

Entry nameMCTS1_HUMAN
AccessionPrimary (citable) accession number: Q9ULC4
Secondary accession number(s): B4DGY2, Q502X6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 114 of the entry and version 1 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 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 X

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