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Protein

Multicilin

Gene

MCIDAS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator specifically required for multiciliate cell differentiation. Acts in a multiprotein complex containing E2F4 and E2F5 that binds and activates genes required for centriole biogenesis. Required for the deuterosome-mediated acentriolar pathway (PubMed:25048963). Plays a role in mitotic cell cycle progression by promoting cell cycle exit. Modulates GMNN activity by reducing its affinity for CDT1 (PubMed:21543332, PubMed:24064211).By similarity3 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. transcription coactivator activity Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. centriole assembly Source: UniProtKB
  3. cilium assembly Source: UniProtKB
  4. motile cilium assembly Source: UniProtKB
  5. multi-ciliated epithelial cell differentiation Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. regulation of DNA replication Source: InterPro
  8. regulation of mitotic cell cycle Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Cilium biogenesis/degradation, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Multicilin
Alternative name(s):
Multiciliate differentiation and DNA synthesis-associated cell cycle protein
Protein Idas
Gene namesi
Name:MCIDAS
Synonyms:IDAS, MCI, MCIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:40050. MCIDAS.

Subcellular locationi

Nucleus 1 Publication
Note: Excluded from the nucleolus.1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Ciliary dyskinesia, primary (CILDN): A disorder characterized by abnormalities of motile cilia. Chronic recurrent infections of the upper (rhinitis, otitis media, nasal polyps and sinusitis) and lower airways (recurrent pneumonia, bronchiectasis, chronic obstructive airway disease caused by mucociliary clearance). The disease is caused by mutations affecting the gene represented in this entry. Respiratory epithelial cells carry only one or two cilia per cell.

Keywords - Diseasei

Ciliopathy, Disease mutation, Primary ciliary dyskinesia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385MulticilinPRO_0000411076Add
BLAST

Proteomic databases

MaxQBiD6RGH6.

Expressioni

Developmental stagei

Probable target of the anaphase promoting complex/cyclosome (APC/C) which regulates its level in the cell during the mitotic cell cycle. Highly expressed during interphase and early mitosis. Expression decreases during anaphase to become undetectable during telophase and cytokinesis.1 Publication

Gene expression databases

ExpressionAtlasiD6RGH6. baseline and differential.

Organism-specific databases

HPAiHPA049981.

Interactioni

Subunit structurei

Heterodimer (via coiled-coil domain) with GMNN (via coiled-coil domain); targets GMNN to the nucleus. Can form homodimers (in vitro, via coiled-coil domain), but these are much less stable than the heterodimer formed with GMNN.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-3954372,EBI-3954372
GMNNO754967EBI-3954372,EBI-371669

Protein-protein interaction databases

IntActiD6RGH6. 1 interaction.

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi178 – 22548Combined sources
Helixi227 – 24115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BRYX-ray2.89B173-245[»]
ProteinModelPortaliD6RGH6.
SMRiD6RGH6. Positions 176-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 130130Necessary and sufficient for its degradation during the cell cycleAdd
BLAST
Regioni131 – 385255Necessary and sufficient for proper nuclear localizationAdd
BLAST
Regioni173 – 24573Necessary and sufficient for interaction with GMNN and sufficient for homodimerizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili179 – 227491 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the geminin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00730000111470.
HOGENOMiHOG000133078.
InParanoidiD6RGH6.
KOiK10749.
OMAiGYKFRWV.
PhylomeDBiD6RGH6.

Family and domain databases

InterProiIPR022786. Geminin/Multicilin.
IPR029699. Multicilin/Idas.
[Graphical view]
PANTHERiPTHR13372:SF3. PTHR13372:SF3. 1 hit.
PfamiPF07412. Geminin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D6RGH6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQACGGGAAG RRAFDSICPN RMLALPGRAL LCKPGKPERK FAPPRKFFPG
60 70 80 90 100
CTGGSPVSVY EDPPDAEPTA LPALTTIDLQ DLADCSSLLG SDAPPGGDLA
110 120 130 140 150
ASQNHSHQTE ADFNLQDFRD TVDDLISDSS SMMSPTLASG DFPFSPCDIS
160 170 180 190 200
PFGPCLSPPL DPRALQSPPL RPPDVPPPEQ YWKEVADQNQ RALGDALVEN
210 220 230 240 250
NQLHVTLTQK QEEIASLKER NVQLKELASR TRHLASVLDK LMITQSRDCG
260 270 280 290 300
AAAEPFLLKA KAKRSLEELV SAAGQDCAEV DAILREISER CDEALQSRDP
310 320 330 340 350
KRPRLLPEPA NTDTRPGNLH GAFRGLRTDC SRSALNLSHS ELEEGGSFST
360 370 380
RIRSHSTIRT LAFPQGNAFT IRTANGGYKF RWVPS
Length:385
Mass (Da):41,720
Last modified:July 13, 2010 - v1
Checksum:iD52A35B926E75723
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti366 – 3661G → D in CILDN. 1 Publication
VAR_071800
Natural varianti381 – 3811R → H in CILDN. 1 Publication
VAR_071801

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR854393 mRNA. Translation: CCA89438.1.
AC091977 Genomic DNA. No translation available.
CCDSiCCDS54853.1.
RefSeqiNP_001177716.1. NM_001190787.1.
UniGeneiHs.394578.

Genome annotation databases

EnsembliENST00000513312; ENSP00000426359; ENSG00000234602.
GeneIDi345643.
KEGGihsa:345643.
UCSCiuc021xyp.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR854393 mRNA. Translation: CCA89438.1.
AC091977 Genomic DNA. No translation available.
CCDSiCCDS54853.1.
RefSeqiNP_001177716.1. NM_001190787.1.
UniGeneiHs.394578.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BRYX-ray2.89B173-245[»]
ProteinModelPortaliD6RGH6.
SMRiD6RGH6. Positions 176-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiD6RGH6. 1 interaction.

Proteomic databases

MaxQBiD6RGH6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000513312; ENSP00000426359; ENSG00000234602.
GeneIDi345643.
KEGGihsa:345643.
UCSCiuc021xyp.1. human.

Organism-specific databases

CTDi345643.
GeneCardsiGC05M054521.
HGNCiHGNC:40050. MCIDAS.
HPAiHPA049981.
MIMi614086. gene.
neXtProtiNX_D6RGH6.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00730000111470.
HOGENOMiHOG000133078.
InParanoidiD6RGH6.
KOiK10749.
OMAiGYKFRWV.
PhylomeDBiD6RGH6.

Miscellaneous databases

GenomeRNAii345643.
NextBioi98889.
PROiD6RGH6.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiD6RGH6. baseline and differential.

Family and domain databases

InterProiIPR022786. Geminin/Multicilin.
IPR029699. Multicilin/Idas.
[Graphical view]
PANTHERiPTHR13372:SF3. PTHR13372:SF3. 1 hit.
PfamiPF07412. Geminin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Idas, a novel phylogenetically conserved geminin-related protein, binds to geminin and is required for cell cycle progression."
    Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E., Kyrousi C., Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.
    J. Biol. Chem. 286:23234-23246(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GMNN, HOMODIMERIZATION, SUBUNIT, DEVELOPMENTAL STAGE.
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The Geminin and Idas coiled coils preferentially form a heterodimer that inhibits Geminin function in DNA replication licensing."
    Caillat C., Pefani E.D., Gillespie P.J., Taraviras S., Blow J.J., Lygerou Z., Perrakis A.
    J. Biol. Chem. 288:31624-31634(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 173-245 IN COMPLEX WITH GMNN, FUNCTION, COILED-COIL DOMAIN, SUBUNIT.
  4. Cited for: INVOLVEMENT IN CILDN, VARIANTS CILDN ASP-366 AND HIS-381.

Entry informationi

Entry nameiMCIN_HUMAN
AccessioniPrimary (citable) accession number: D6RGH6
Secondary accession number(s): C9JGY3, D6R920, F8KGQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 13, 2010
Last modified: January 7, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Was named Idas in reference to the cousin of the Gemini in ancient Greek mythology.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.