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P61956 (SUMO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small ubiquitin-related modifier 2

Short name=SUMO-2
Alternative name(s):
HSMT3
SMT3 homolog 2
SUMO-3
Sentrin-2
Ubiquitin-like protein SMT3A
Short name=Smt3A
Gene names
Name:SUMO2
Synonyms:SMT3A, SMT3H2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length95 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Ref.7 Ref.15 Ref.16

Subunit structure

Homotrimer Potential. Crystal packing analysis suggests a possible trimeric assembly, of which the biological significance remains to be determined. Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Ref.11 Ref.14 Ref.15 Ref.19 Ref.21

Subcellular location

Nucleus. NucleusPML body Ref.7 Ref.10 Ref.18.

Tissue specificity

Broadly expressed. Ref.7

Post-translational modification

Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4.

Cleavage of precursor form by SENP1 or SENP2 is necessary for function.

Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.

Sequence similarities

Belongs to the ubiquitin family. SUMO subfamily.

Contains 1 ubiquitin-like domain.

Caution

Frequently wrongly assigned as SMT3B in many databases and publications. However, according to initial nomenclature, SUMO2 corresponds to SMT3A (Ref.8).

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61956-1)

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: P61956-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-74: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9393Small ubiquitin-related modifier 2
PRO_0000035949
Propeptide94 – 952
PRO_0000035950

Regions

Domain16 – 9580Ubiquitin-like

Amino acid modifications

Modified residue111N6-acetyllysine; alternate By similarity
Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.9 Ref.16 Ref.17
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-link93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Natural variations

Alternative sequence51 – 7424Missing in isoform 2.
VSP_042351
Natural variant161D → N. Ref.6
Corresponds to variant rs17850328 [ dbSNP | Ensembl ].
VAR_047508

Experimental info

Mutagenesis111K → R: Abolishes the formation of poly(SUMO) chains. Ref.9

Secondary structure

........................ 95
Helix Strand Turn

Details...

Sequences

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

Last modified February 22, 2012. Version 3.
Checksum: F8F0426849BEF08B

FASTA9510,871
        10         20         30         40         50         60 
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER QGLSMRQIRF 

        70         80         90 
RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY 

« Hide

Isoform 2 [UniParc].

Checksum: 96014B2763D7E899
Show »

FASTA718,111

References

« Hide 'large scale' references
[1]"Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene."
Mannen H., Tseng H.M., Cho C.L., Li S.S.-L.
Biochem. Biophys. Res. Commun. 222:178-180(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family."
Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C.
Genomics 40:362-367(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[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] (ISOFORM 1).
Tissue: Cerebellum.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [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 (JUL-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), VARIANT ASN-16.
Tissue: Blood vessel, Bone, Bone marrow, Brain, Lung, Skin and Testis.
[7]"Characterization of a second member of the sentrin family of ubiquitin-like proteins."
Kamitani T., Kito K., Nguyen H.P., Fukuda-Kamitani T., Yeh E.T.H.
J. Biol. Chem. 273:11349-11353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3."
Saitoh H., Hinchey J.
J. Biol. Chem. 275:6252-6258(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[9]"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-11, MUTAGENESIS OF LYS-11.
[10]"Molecular features of human ubiquitin-like SUMO genes and their encoded proteins."
Su H.-L., Li S.S.-L.
Gene 296:65-73(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
Biochemistry 42:9959-9969(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2I.
[12]"A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex."
Reverter D., Lima C.D.
Structure 12:1519-1531(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE.
[13]"Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
Xu Z., Au S.W.N.
Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE.
[14]"NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression."
Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G.
Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[15]"Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25."
Meulmeester E., Kunze M., Hsiao H.H., Urlaub H., Melchior F.
Mol. Cell 30:610-619(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SUMOYLATION OF USP25, INTERACTION WITH USP25.
[16]"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, POLYUBIQUITINATION AT LYS-11 BY RNF4.
[17]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-11.
Tissue: Cervix carcinoma.
[18]"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"PolySUMO-binding proteins identified through a string search."
Sun H., Hunter T.
J. Biol. Chem. 287:42071-42083(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF REPEAT SUMO-INTERACTING MOTIF, INTERACTION WITH SIMC1; CASP8AP2; RNF111 AND SOBP.
[20]"Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT MET-1.
[21]"Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins."
Huang W.-C., Ko T.-P., Li S.S.-L., Wang A.H.-J.
Eur. J. Biochem. 271:4114-4122(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 9-93, SUBUNIT.
[22]"Solution structure of human SUMO-2 (SMT3B), a ubiquitin-like protein."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-93.
[23]"Crystal structure of SUMO-3-modified thymine-DNA glycosylase."
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K., Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.
J. Mol. Biol. 359:137-147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-93 CONJUGATED TO TDG.
[24]"Solution structure of human small ubiquitin-like modifier protein isoform 2 (SUMO-2)."
Chang C.K., Wang Y.H., Chung T.L., Chang C.F., Li S.S.L., Huang T.H.
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-95.
+Additional computationally mapped references.

Web resources

Wikipedia

SUMO protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L76416 mRNA. Translation: AAD45399.1.
X99585 mRNA. Translation: CAA67897.1.
AK311837 mRNA. Translation: BAG34779.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89249.1.
BC008450 mRNA. Translation: AAH08450.1.
BC016775 mRNA. Translation: AAH16775.1.
BC022340 mRNA. Translation: AAH22340.1.
BC062713 mRNA. Translation: AAH62713.1.
BC068465 mRNA. Translation: AAH68465.1.
BC070159 mRNA. Translation: AAH70159.1.
BC071645 mRNA. Translation: AAH71645.1.
BC071646 mRNA. Translation: AAH71646.1.
BC107853 mRNA. Translation: AAI07854.1.
BF978876 mRNA. No translation available.
PIRJC4760.
RefSeqNP_001005849.1. NM_001005849.1.
NP_008868.3. NM_006937.3.
UniGeneHs.380973.
Hs.546298.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WM2X-ray1.60A12-89[»]
1WM3X-ray1.20A17-88[»]
1WZ0NMR-A1-91[»]
1Z5Qmodel-B15-93[»]
2AWTNMR-A1-95[»]
2CKHX-ray3.20B15-93[»]
2D07X-ray2.10B1-93[»]
2IO0X-ray2.30B15-95[»]
2IO3X-ray3.20B15-93[»]
2IYDX-ray3.20B15-95[»]
2RPQNMR-A1-93[»]
3UINX-ray2.60B14-93[»]
3UIOX-ray2.60B14-93[»]
3ZO5X-ray2.15B16-95[»]
4BKGX-ray2.11A12-93[»]
ProteinModelPortalP61956.
SMRP61956. Positions 1-95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112497. 1257 interactions.
DIPDIP-29253N.
IntActP61956. 51 interactions.
MINTMINT-1373938.
STRING9606.ENSP00000405965.

Chemistry

ChEMBLCHEMBL2146301.

PTM databases

PhosphoSiteP61956.

Polymorphism databases

DMDM378405233.

Proteomic databases

PaxDbP61956.
PRIDEP61956.

Protocols and materials databases

DNASU6613.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314523; ENSP00000400886; ENSG00000188612. [P61956-2]
ENST00000420826; ENSP00000405965; ENSG00000188612. [P61956-1]
GeneID6613.
KEGGhsa:6613.
UCSCuc002jne.3. human. [P61956-1]
uc002jnf.3. human. [P61956-2]

Organism-specific databases

CTD6613.
GeneCardsGC17M073163.
H-InvDBHIX0056267.
HGNCHGNC:11125. SUMO2.
HPACAB037314.
MIM603042. gene.
neXtProtNX_P61956.
PharmGKBPA134914683.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5227.
HOVERGENHBG053025.
KOK12160.
OMADAYCKKQ.
PhylomeDBP61956.
TreeFamTF315116.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP61956.
BgeeP61956.
CleanExHS_SUMO2.
GenevestigatorP61956.

Family and domain databases

InterProIPR022617. Rad60/SUMO_like.
IPR027218. SUMO_chordates.
IPR000626. Ubiquitin-like.
[Graphical view]
PANTHERPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP61956.
GeneWikiSUMO2.
GenomeRNAi6613.
NextBio25747.
PMAP-CutDBP61956.
PROP61956.
SOURCESearch...

Entry information

Entry nameSUMO2_HUMAN
AccessionPrimary (citable) accession number: P61956
Secondary accession number(s): B2R4I2 expand/collapse secondary AC list , P55855, Q32Q42, Q6IPZ6, Q96HK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: February 22, 2012
Last modified: April 16, 2014
This is version 118 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 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 17

Human chromosome 17: entries, gene names and cross-references to MIM