Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O60907 (TBL1X_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box-like/WD repeat-containing protein TBL1X
Alternative name(s):
SMAP55
Transducin beta-like protein 1X
Transducin-beta-like protein 1, X-linked
Gene names
Name:TBL1X
Synonyms:TBL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units. Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange. Ref.10

Subunit structure

Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Probably part of other corepressor complexes, that do not contain NCOR1 and NCOR2. Interacts with histones H2B, H3a and H4. Ref.7

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitous. Ref.1

Domain

The F-box-like domain is related to the F-box domain, and apparently displays the same function as component of ubiquitin E3 ligase complexes By similarity.

Sequence similarities

Belongs to the WD repeat EBI family.

Contains 1 F-box-like domain.

Contains 1 LisH domain.

Contains 8 WD repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
   DomainRepeat
WD repeat
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 18193033. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18193033. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18193033. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

proteolysis

Inferred from mutant phenotype PubMed 18374649. Source: UniProtKB

sensory perception of sound

Inferred from mutant phenotype Ref.1. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18193033. Source: UniProtKB

spindle microtubule

Inferred from direct assay PubMed 18326024. Source: UniProtKB

transcriptional repressor complex

Inferred from direct assay Ref.9PubMed 15601853. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 18193033. Source: UniProtKB

histone binding

Inferred from direct assay PubMed 15601853. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 18374649. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.5. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.9. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 18193033. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18193033. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60907-1)

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: O60907-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577F-box-like/WD repeat-containing protein TBL1X
PRO_0000051263

Regions

Domain55 – 8733LisH
Domain92 – 13746F-box-like
Repeat230 – 26940WD 1
Repeat286 – 32540WD 2
Repeat327 – 36640WD 3
Repeat369 – 40941WD 4
Repeat410 – 44940WD 5
Repeat452 – 50049WD 6
Repeat503 – 54240WD 7
Repeat544 – 57633WD 8
Compositional bias159 – 17517Poly-Ala

Natural variations

Alternative sequence1 – 5151Missing in isoform 2.
VSP_036905

Experimental info

Sequence conflict3161T → A in BAF82098. Ref.2
Sequence conflict3901T → A in BAF83651. Ref.2

Secondary structure

........... 577
Helix Strand Turn

Details...

Sequences

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

Last modified April 14, 2009. Version 3.
Checksum: D830A37781E2A15C

FASTA57762,496
        10         20         30         40         50         60 
MTELAGASSS CCHRPAGRGA MQSVLHHFQR LRGREGGSHF INTSSPRGEA KMSITSDEVN 

        70         80         90        100        110        120 
FLVYRYLQES GFSHSAFTFG IESHISQSNI NGTLVPPAAL ISILQKGLQY VEAEISINED 

       130        140        150        160        170        180 
GTVFDGRPIE SLSLIDAVMP DVVQTRQQAF REKLAQQQAS AAAAAAAATA AATAATTTSA 

       190        200        210        220        230        240 
GVSHQNPSKN REATVNGEEN RAHSVNNHAK PMEIDGEVEI PSSKATVLRG HESEVFICAW 

       250        260        270        280        290        300 
NPVSDLLASG SGDSTARIWN LNENSNGGST QLVLRHCIRE GGHDVPSNKD VTSLDWNTNG 

       310        320        330        340        350        360 
TLLATGSYDG FARIWTEDGN LASTLGQHKG PIFALKWNRK GNYILSAGVD KTTIIWDAHT 

       370        380        390        400        410        420 
GEAKQQFPFH SAPALDVDWQ NNTTFASCST DMCIHVCRLG CDRPVKTFQG HTNEVNAIKW 

       430        440        450        460        470        480 
DPSGMLLASC SDDMTLKIWS MKQEVCIHDL QAHNKEIYTI KWSPTGPATS NPNSNIMLAS 

       490        500        510        520        530        540 
ASFDSTVRLW DIERGVCTHT LTKHQEPVYS VAFSPDGKYL ASGSFDKCVH IWNTQSGNLV 

       550        560        570 
HSYRGTGGIF EVCWNARGDK VGASASDGSV CVLDLRK 

« Hide

Isoform 2 [UniParc].

Checksum: 98922F88EC42F6E9
Show »

FASTA52657,049

References

« Hide 'large scale' references
[1]"X-linked late-onset sensorineural deafness caused by a deletion involving OA1 and a novel gene containing WD-40 repeats."
Bassi M.T., Ramesar R.S., Caciotti B., Winship I.M., De Grandi A., Riboni M., Townes P.L., Beighton P., Ballabio A., Borsani G.
Am. J. Hum. Genet. 64:1604-1616(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"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 2).
[3]"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].
[4]"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: Lymph and Pancreas.
[5]"A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness."
Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., Shiekhattar R.
Genes Dev. 14:1048-1057(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
[6]"Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3."
Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J.
EMBO J. 19:4342-4350(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR2 AND HDAC3.
[7]"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
Matsuzawa S., Reed J.C.
Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT OF A COMPLEX WITH UBE2D1; CACYBP; SIAH1 AND APC.
[8]"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2."
Zhang J., Kalkum M., Chait B.T., Roeder R.G.
Mol. Cell 9:611-623(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR1; NCOR2; GPS2; TBL1R AND HDAC3.
[9]"Purification and functional characterization of the human N-CoR complex: the roles of HDAC3, TBL1 and TBLR1."
Yoon H.-G., Chan D.W., Huang Z.-Q., Li J., Fondell J.D., Qin J., Wong J.
EMBO J. 22:1336-1346(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1R; CORO2A AND HDAC3, HISTONE-BINDING.
[10]"A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors."
Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G.
Cell 116:511-526(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RECRUITMENT OF 19S PROTEASOME COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12781 mRNA. Translation: CAA73319.1.
AK289409 mRNA. Translation: BAF82098.1.
AK290962 mRNA. Translation: BAF83651.1.
AC003036 Genomic DNA. No translation available.
BC032708 mRNA. Translation: AAH32708.1.
BC052304 mRNA. Translation: AAH52304.1.
RefSeqNP_001132938.1. NM_001139466.1.
NP_001132939.1. NM_001139467.1.
NP_001132940.1. NM_001139468.1.
NP_005638.1. NM_005647.3.
UniGeneHs.495656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XTCX-ray2.22A/B52-141[»]
2XTDX-ray3.20A/B52-122[»]
2XTEX-ray3.90A/B/C/D/E/F/G/H/I/J/K/L52-141[»]
ProteinModelPortalO60907.
SMRO60907. Positions 53-126, 228-576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112770. 40 interactions.
DIPDIP-60532N.
IntActO60907. 8 interactions.
STRING9606.ENSP00000217964.

PTM databases

PhosphoSiteO60907.

Proteomic databases

PaxDbO60907.
PRIDEO60907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217964; ENSP00000217964; ENSG00000101849. [O60907-1]
ENST00000380961; ENSP00000370348; ENSG00000101849. [O60907-2]
ENST00000407597; ENSP00000385988; ENSG00000101849. [O60907-1]
ENST00000424279; ENSP00000394097; ENSG00000101849. [O60907-2]
ENST00000536365; ENSP00000445317; ENSG00000101849. [O60907-2]
GeneID6907.
KEGGhsa:6907.
UCSCuc004csq.4. human. [O60907-1]

Organism-specific databases

CTD6907.
GeneCardsGC0XP009431.
HGNCHGNC:11585. TBL1X.
HPACAB005363.
MIM300196. gene.
neXtProtNX_O60907.
PharmGKBPA36349.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000220902.
HOVERGENHBG050240.
InParanoidO60907.
KOK04508.
OMASMKQEVC.
OrthoDBEOG79CXZ3.
PhylomeDBO60907.
TreeFamTF323190.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
SignaLinkO60907.

Gene expression databases

ArrayExpressO60907.
BgeeO60907.
CleanExHS_TBL1X.
GenevestigatorO60907.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00667. LisH. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
SSF50998. SSF50998. 1 hit.
PROSITEPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTBL1X. human.
EvolutionaryTraceO60907.
GeneWikiTBL1X.
GenomeRNAi6907.
NextBio27011.
PROO60907.
SOURCESearch...

Entry information

Entry nameTBL1X_HUMAN
AccessionPrimary (citable) accession number: O60907
Secondary accession number(s): A8K044, A8K4J7, Q86UY2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: April 14, 2009
Last modified: April 16, 2014
This is version 136 of the entry and version 3 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 X

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