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Q2NKJ3 (CTC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CST complex subunit CTC1
Alternative name(s):
Conserved telomere maintenance component 1
HBV DNAPTP1-transactivated protein B
Gene names
Name:CTC1
Synonyms:C17orf68
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites. Ref.6 Ref.7

Subunit structure

Component of the CST complex, composed of TEN1/C17orf106, CTC1/C17orf68 and STN1/OBFC1. Interacts with STN1/OBFC1; the interaction is direct. Ref.6

Subcellular location

Nucleus. Chromosometelomere. Note: A transmembrane region is predicted by sequence analysis tools (ESKW, MEMSAT and Phobius); however, given the telomeric localization of the protein, the relevance of the transmembrane region is unsure in vivo. Ref.6

Involvement in disease

Cerebroretinal microangiopathy with calcifications and cysts (CRMCC) [MIM:612199]: An autosomal recessive pleiomorphic disorder characterized primarily by intracranial calcifications, leukodystrophy, and brain cysts, resulting in spasticity, ataxia, dystonia, seizures, and cognitive decline. Patients also have retinal telangiectasia and exudates (Coats disease) as well as extraneurologic manifestations, including osteopenia with poor bone healing and a high risk of gastrointestinal bleeding and portal hypertension caused by vasculature ectasias in the stomach, small intestine, and liver. Some individuals also have hair, skin, and nail changes, as well as anemia and thrombocytopenia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9

Sequence similarities

Belongs to the CTC1 family.

Sequence caution

The sequence BAB15247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAD38600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandDNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone marrow development

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

hematopoietic stem cell proliferation

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

replicative senescence

Inferred from electronic annotation. Source: Ensembl

spleen development

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Inferred from mutant phenotype Ref.7. Source: UniProtKB

telomere maintenance via telomere lengthening

Inferred from electronic annotation. Source: Ensembl

thymus development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentStn1-Ten1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromosome, telomeric region

Inferred from direct assay Ref.6. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

single-stranded DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OBFC1Q9H6686EBI-2562802,EBI-746930

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q2NKJ3-1)

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: Q2NKJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     217-251: Missing.
     1053-1066: GKCTRLGSTCPTQT → APGGGWDCRSRGDL
     1067-1217: Missing.
Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12171217CST complex subunit CTC1
PRO_0000287181

Natural variations

Alternative sequence217 – 25135Missing in isoform 2.
VSP_025351
Alternative sequence1053 – 106614GKCTR…CPTQT → APGGGWDCRSRGDL in isoform 2.
VSP_025352
Alternative sequence1067 – 1217151Missing in isoform 2.
VSP_025353
Natural variant2271A → V in CRMCC. Ref.8
VAR_067369
Natural variant2591V → M in CRMCC. Ref.9
VAR_067370
Natural variant5031G → R in CRMCC. Ref.9
VAR_067371
Natural variant6651V → G in CRMCC. Ref.8
VAR_067372
Natural variant8201I → V.
Corresponds to variant rs3027238 [ dbSNP | Ensembl ].
VAR_032282
Natural variant8401R → W in CRMCC. Ref.9
VAR_067373
Natural variant8711V → M in CRMCC. Ref.9
VAR_067374
Natural variant9751R → G in CRMCC. Ref.8 Ref.9
VAR_067375
Natural variant9851Missing in CRMCC. Ref.8 Ref.9
VAR_067376
Natural variant9871R → W in CRMCC. Ref.9
VAR_067377
Natural variant10051I → V. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs3826543 [ dbSNP | Ensembl ].
VAR_032283
Natural variant11421L → H in CRMCC. Ref.8
VAR_067378
Natural variant1196 – 12027Missing in CRMCC.
VAR_067379

Experimental info

Sequence conflict411L → V in CAD38600. Ref.2
Sequence conflict4251L → P in CAD38600. Ref.2
Sequence conflict6681S → I in ABE02809. Ref.1
Sequence conflict6681S → I in BAG52278. Ref.3
Sequence conflict8641S → G in CAD38600. Ref.2
Sequence conflict9001A → T in AAI10374. Ref.5
Sequence conflict9641G → E in CAD38600. Ref.2

Sequences

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

Last modified March 23, 2010. Version 2.
Checksum: EF6B3985C72FDA6E

FASTA1,217134,609
        10         20         30         40         50         60 
MAAGRAQVPS SEQAWLEDAQ VFIQKTLCPA VKEPNVQLTP LVIDCVKTVW LSQGRNQGST 

        70         80         90        100        110        120 
LPLSYSFVSV QDLKTHQRLP CCSHLSWSSS AYQAWAQEAG PNGNPLPREQ LLLLGTLTDL 

       130        140        150        160        170        180 
SADLEQECRN GSLYVRDNTG VLSCELIDLD LSWLGHLFLF PRWSYLPPAR WNSSGEGHLE 

       190        200        210        220        230        240 
LWDAPVPVFP LTISPGPVTP IPVLYPESAS CLLRLRNKLR GVQRNLAGSL VRLSALVKSK 

       250        260        270        280        290        300 
QKAYFILSLG RSHPAVTHVS IIVQVPAQLV WHRALRPGTA YVLTELRVSK IRGQRQHVWM 

       310        320        330        340        350        360 
TSQSSRLLLL KPECVQELEL ELEGPLLEAD PKPLPMPSNS EDKKDPESLV RYSRLLSYSG 

       370        380        390        400        410        420 
AVTGVLNEPA GLYELDGQLG LCLAYQQFRG LRRVMRPGVC LQLQDVHLLQ SVGGGTRRPV 

       430        440        450        460        470        480 
LAPCLRGAVL LQSFSRQKPG AHSSRQAYGA SLYEQLVWER QLGLPLYLWA TKALEELACK 

       490        500        510        520        530        540 
LCPHVLRHHQ FLQHSSPGSP SLGLQLLAPT LDLLAPPGSP VRNAHNEILE EPHHCPLQKY 

       550        560        570        580        590        600 
TRLQTPSSFP TLATLKEEGQ RKAWASFDPK ALLPLPEASY LPSCQLNRRL AWSWLCLLPS 

       610        620        630        640        650        660 
AFCPAQVLLG VLVASSHKGC LQLRDQSGSL PCLLLAKHSQ PLSDPRLIGC LVRAERFQLI 

       670        680        690        700        710        720 
VERDVRSSFP SWKELSMPGF IQKQQARVYV QFFLADALIL PVPRPCLHSA TPSTPQTDPT 

       730        740        750        760        770        780 
GPEGPHLGQS RLFLLCHKEA LMKRNFCVPP GASPEVPKPA LSFYVLGSWL GGTQRKEGTG 

       790        800        810        820        830        840 
WGLPEPQGND DNDQKVHLIF FGSSVRWFEF LHPGQVYRLI APGPATPMLF EKDGSSCISR 

       850        860        870        880        890        900 
RPLELAGCAS CLTVQDNWTL ELESSQDIQD VLDANKSLPE SSLTDLLSDN FTDSLVSFSA 

       910        920        930        940        950        960 
EILSRTLCEP LVASLWMKLG NTGAMRRCVK LTVALETAEC EFPPHLDVYI EDPHLPPSLG 

       970        980        990       1000       1010       1020 
LLPGARVHFS QLEKRVSRSH NVYCCFRSST YVQVLSFPPE TTISIPLPHI YLAELLQGGQ 

      1030       1040       1050       1060       1070       1080 
SPFQATASCH IVSVFSLQLF WVCAYCTSIC RQGKCTRLGS TCPTQTAISQ AIIRLLVEDG 

      1090       1100       1110       1120       1130       1140 
TAEAVVTCRN HHVAAALGLC PREWASLLDF VQVPGRVVLQ FAGPGAQLES SARVDEPMTM 

      1150       1160       1170       1180       1190       1200 
FLWTLCTSPS VLRPIVLSFE LERKPSKIVP LEPPRLQRFQ CGELPFLTHV NPRLRLSCLS 

      1210 
IRESEYSSSL GILASSC 

« Hide

Isoform 2 [UniParc].

Checksum: 4FDB851CDB123E45
Show »

FASTA1,031114,142

References

« Hide 'large scale' references
[1]Lun Y.Z., Cheng J., Guo J., Zhang L.Y., Zhao B.C.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-1005.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT VAL-1005.
Tissue: Skeletal muscle.
[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), VARIANT VAL-1005.
Tissue: Corpus callosum and Kidney epithelium.
[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]"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] (ISOFORM 1), VARIANT VAL-1005.
Tissue: Lung carcinoma and Uterine adenocarcinoma.
[6]"RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway."
Miyake Y., Nakamura M., Nabetani A., Shimamura S., Tamura M., Yonehara S., Saito M., Ishikawa F.
Mol. Cell 36:193-206(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CST COMPLEX, SUBCELLULAR LOCATION.
[7]"Conserved telomere maintenance component 1 interacts with STN1 and maintains chromosome ends in higher eukaryotes."
Surovtseva Y.V., Churikov D., Boltz K.A., Song X., Lamb J.C., Warrington R., Leehy K., Heacock M., Price C.M., Shippen D.E.
Mol. Cell 36:207-218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Mutations in CTC1, encoding the CTS telomere maintenance complex component 1, cause cerebroretinal microangiopathy with calcifications and cysts."
Polvi A., Linnankivi T., Kivela T., Herva R., Keating J.P., Makitie O., Pareyson D., Vainionpaa L., Lahtinen J., Hovatta I., Pihko H., Lehesjoki A.E.
Am. J. Hum. Genet. 90:540-549(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRMCC VAL-227; GLY-665; GLY-975; CYS-985 DEL; HIS-1142 AND 1196-LEU--ARG-1202 DEL.
[9]"Mutations in CTC1, encoding conserved telomere maintenance component 1, cause Coats plus."
Anderson B.H., Kasher P.R., Mayer J., Szynkiewicz M., Jenkinson E.M., Bhaskar S.S., Urquhart J.E., Daly S.B., Dickerson J.E., O'Sullivan J., Leibundgut E.O., Muter J., Abdel-Salem G.M., Babul-Hirji R., Baxter P., Berger A., Bonafe L., Brunstom-Hernandez J.E. expand/collapse author list , Buckard J.A., Chitayat D., Chong W.K., Cordelli D.M., Ferreira P., Fluss J., Forrest E.H., Franzoni E., Garone C., Hammans S.R., Houge G., Hughes I., Jacquemont S., Jeannet P.Y., Jefferson R.J., Kumar R., Kutschke G., Lundberg S., Lourenco C.M., Mehta R., Naidu S., Nischal K.K., Nunes L., Ounap K., Philippart M., Prabhakar P., Risen S.R., Schiffmann R., Soh C., Stephenson J.B., Stewart H., Stone J., Tolmie J.L., van der Knaap M.S., Vieira J.P., Vilain C.N., Wakeling E.L., Wermenbol V., Whitney A., Lovell S.C., Meyer S., Livingston J.H., Baerlocher G.M., Black G.C., Rice G.I., Crow Y.J.
Nat. Genet. 44:338-342(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRMCC MET-259; ARG-503; TRP-840; MET-871; GLY-975; CYS-985 DEL; TRP-987 AND 1196-LEU--ARG-1202 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ451688 mRNA. Translation: ABE02809.1.
AL831955 mRNA. Translation: CAD38600.1. Different initiation.
AK091077 mRNA. Translation: BAG52278.1.
AC135178 Genomic DNA. No translation available.
BC026057 mRNA. Translation: AAH26057.2.
BC110373 mRNA. Translation: AAI10374.1.
BC111783 mRNA. Translation: AAI11784.1.
AK025823 mRNA. Translation: BAB15247.1. Different initiation.
CCDSCCDS42259.1. [Q2NKJ3-1]
RefSeqNP_079375.3. NM_025099.5. [Q2NKJ3-1]
UniGeneHs.156055.

3D structure databases

ProteinModelPortalQ2NKJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123155. 2 interactions.
DIPDIP-56900N.
IntActQ2NKJ3. 3 interactions.
STRING9606.ENSP00000313759.

PTM databases

PhosphoSiteQ2NKJ3.

Polymorphism databases

DMDM292495002.

Proteomic databases

MaxQBQ2NKJ3.
PaxDbQ2NKJ3.
PRIDEQ2NKJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315684; ENSP00000313759; ENSG00000178971. [Q2NKJ3-1]
ENST00000449476; ENSP00000396018; ENSG00000178971. [Q2NKJ3-2]
GeneID80169.
KEGGhsa:80169.
UCSCuc002gkq.4. human. [Q2NKJ3-1]

Organism-specific databases

CTD80169.
GeneCardsGC17M008174.
H-InvDBHIX0019337.
HGNCHGNC:26169. CTC1.
HPAHPA044349.
MIM612199. phenotype.
613129. gene.
neXtProtNX_Q2NKJ3.
Orphanet313838. Coats plus syndrome.
1775. Dyskeratosis congenita.
PharmGKBPA142672251.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39921.
HOVERGENHBG097256.
InParanoidQ2NKJ3.
OMARLAWSWL.
OrthoDBEOG79CXXP.
PhylomeDBQ2NKJ3.
TreeFamTF335866.

Gene expression databases

ArrayExpressQ2NKJ3.
BgeeQ2NKJ3.
CleanExHS_C17orf68.
GenevestigatorQ2NKJ3.

Family and domain databases

InterProIPR029156. CTC1.
[Graphical view]
PfamPF15489. CTC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTC1. human.
GenomeRNAi80169.
NextBio70483.
PROQ2NKJ3.
SOURCESearch...

Entry information

Entry nameCTC1_HUMAN
AccessionPrimary (citable) accession number: Q2NKJ3
Secondary accession number(s): B3KR66 expand/collapse secondary AC list , C9JEX5, Q1PCD1, Q2TBE3, Q8N3S6, Q9H6L0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 70 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 17

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