Q8NEM0 · MCPH1_HUMAN
- ProteinMicrocephalin
- GeneMCPH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids835 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex.
Miscellaneous
MCPH1 deficient cells exhibit a delay in post-mitotic chromosome decondensation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleoplasm | |
Molecular Function | identical protein binding | |
Biological Process | bone development | |
Biological Process | cerebral cortex development | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | mitotic cell cycle | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | neuronal stem cell population maintenance | |
Biological Process | protein localization to centrosome | |
Biological Process | regulation of centrosome cycle | |
Biological Process | regulation of chromosome condensation | |
Biological Process | regulation of inflammatory response |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrocephalin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8NEM0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Microcephaly 1, primary, autosomal recessive (MCPH1)
- Note
- DescriptionA disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals have mild to severe intellectual disability. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder. Some MCHP1 patients also present growth retardation, short stature, and misregulated chromosome condensation as indicated by a high number of prophase-like cells detected in routine cytogenetic preparations and poor-quality metaphase G-banding.
- See alsoMIM:251200
Natural variants in MCPH1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_046745 | 27 | T>R | in MCPH1; mild phenotype; dbSNP:rs199422124 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046745 | 27 | in MCPH1; mild phenotype; dbSNP:rs199422124 | |||
Sequence: T → R | ||||||
Natural variant | VAR_046746 | 171 | in dbSNP:rs2442513 | |||
Sequence: R → S | ||||||
Natural variant | VAR_046747 | 212 | in dbSNP:rs2922828 | |||
Sequence: A → T | ||||||
Natural variant | VAR_046748 | 264 | in dbSNP:rs34121009 | |||
Sequence: I → V | ||||||
Natural variant | VAR_046749 | 288 | in dbSNP:rs35590577 | |||
Sequence: P → H | ||||||
Natural variant | VAR_046750 | 304 | in dbSNP:rs2083914 | |||
Sequence: R → I | ||||||
Natural variant | VAR_046751 | 314 | in dbSNP:rs930557 | |||
Sequence: D → H | ||||||
Natural variant | VAR_046752 | 392 | in dbSNP:rs2515569 | |||
Sequence: D → G | ||||||
Natural variant | VAR_046753 | 580 | in dbSNP:rs17076894 | |||
Sequence: S → G | ||||||
Natural variant | VAR_046754 | 602 | in dbSNP:rs34418490 | |||
Sequence: L → F | ||||||
Natural variant | VAR_046755 | 682 | in dbSNP:rs12674488 | |||
Sequence: T → N | ||||||
Natural variant | VAR_046756 | 761 | in dbSNP:rs1057090 | |||
Sequence: A → V | ||||||
Natural variant | VAR_046757 | 828 | in dbSNP:rs1057091 | |||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,445 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000096296 | 1-835 | UniProt | Microcephalin | |||
Sequence: MAAPILKDVVAYVEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHIDESLFPAANMNEHLSSLIKKKRKCMQPKDFNFKTPENDKRFQKKFEKMAKELQRQKTNLDDDVPILLFESNGSLIYTPTIEINSRHHSAMEKRLQEMKEKRENLSPTSSQMIQQSHDNPSNSLCEAPLNISRDTLCSDEYFAGGLHSSFDDLCGNSGCGNQERKLEGSINDIKSDVCISSLVLKANNIHSSPSFTHLDKSSPQKFLSNLSKEEINLQRNIAGKVVTPDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSIMPRLQLCRSEDRLQHVAGPALEALSCGESSYDDYFSPDNLKERYSENLPPESQLPSSPAQLSCRSLSKKERTSIFEMSDFSCVGKKTRTVDITNFTAKTISSPRKTGNGEGRATSSCVTSAPEEALRCCRQAGKEDACPEGNGFSYTIEDPALPKGHDDDLTPLEGSLEEMKEAVGLKSTQNKGTTSKISNSSEGEAQSEHEPCFIVDCNMETSTEEKENLPGGYSGSVKNRPTRHDVLDDSCDGFKDLIKPHEELKKSGRGKKPTRTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWISEEPFELSHHFPAAPLCRSECHLSAGPYRGTLFADQPAMFVSPASSPPVAKLCELVHLCGGRVSQVPRQASIVIGPYSGKKKATVKYLSEKWVLDSITQHKVCAPENYLLSQ | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 254 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 287 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 296 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 322 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 333 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 335 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 335 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 543 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 548 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 548 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 623 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with CDC27 and maybe other components of the APC/C complex. Interacts with histone variant H2AX under DNA damage conditions.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8NEM0 | CRACR2A Q9BSW2 | 2 | EBI-1565483, EBI-739773 | |
BINARY | Q8NEM0 | E2F1 Q01094 | 6 | EBI-1565483, EBI-448924 | |
BINARY | Q8NEM0 | MCPH1 Q8NEM0 | 2 | EBI-1565483, EBI-1565483 | |
BINARY | Q8NEM0 | TERF2 Q15554 | 5 | EBI-1565483, EBI-706637 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-93 | BRCT 1 | ||||
Sequence: MAAPILKDVVAYVEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQSTWDKAQKRGVKLVSVLWVEKCRTAGAHIDESLFPA | ||||||
Region | 313-381 | Disordered | ||||
Sequence: PDQKQAAGMSQETFEEKYRLSPTLSSTKGHLLIHSRPRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRSI | ||||||
Compositional bias | 316-346 | Polar residues | ||||
Sequence: KQAAGMSQETFEEKYRLSPTLSSTKGHLLIH | ||||||
Compositional bias | 349-380 | Basic residues | ||||
Sequence: PRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRS | ||||||
Region | 419-443 | Disordered | ||||
Sequence: DNLKERYSENLPPESQLPSSPAQLS | ||||||
Region | 555-584 | Disordered | ||||
Sequence: AVGLKSTQNKGTTSKISNSSEGEAQSEHEP | ||||||
Compositional bias | 559-579 | Polar residues | ||||
Sequence: KSTQNKGTTSKISNSSEGEAQ | ||||||
Domain | 640-730 | BRCT 2 | ||||
Sequence: SGRGKKPTRTLVMTSMPSEKQNVVIQVVDKLKGFSIAPDVCETTTHVLSGKPLRTLNVLLGIARGCWVLSYDWVLWSLELGHWISEEPFEL | ||||||
Domain | 751-833 | BRCT 3 | ||||
Sequence: YRGTLFADQPAMFVSPASSPPVAKLCELVHLCGGRVSQVPRQASIVIGPYSGKKKATVKYLSEKWVLDSITQHKVCAPENYLL |
Domain
BRCT domain 1 is required to prevent abnormal chromosome condensation. It binds directly to the SWI-SNF chromatin remodeling complex (PubMed:19925808).
BRCT domains 2 and 3 recognize phosphoserine/phosphothreonine marks on proteins with high selectivity, and mediate interaction with phosphorylated CDC27. They also mediate the dual recognition of phosphoserine and phosphotyrosine in the C-terminal tail of histone H2AX (PubMed:22139841, PubMed:22908299).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8NEM0-1
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.
- Name1
- Length835
- Mass (Da)92,849
- Last updated2017-05-10 v4
- ChecksumD17961B94EC240A3
Q8NEM0-2
- Name2
Q8NEM0-3
- Name3
Computationally mapped potential isoform sequences
There are 21 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QKY7 | A0A8I5QKY7_HUMAN | MCPH1 | 667 | ||
A0A8I5QKX9 | A0A8I5QKX9_HUMAN | MCPH1 | 506 | ||
A0A8I5QJK3 | A0A8I5QJK3_HUMAN | MCPH1 | 365 | ||
A0A8I5KPV6 | A0A8I5KPV6_HUMAN | MCPH1 | 871 | ||
A0A8I5KRS3 | A0A8I5KRS3_HUMAN | MCPH1 | 46 | ||
A0A8I5KSF2 | A0A8I5KSF2_HUMAN | MCPH1 | 39 | ||
A0A8I5KQZ4 | A0A8I5KQZ4_HUMAN | MCPH1 | 100 | ||
A0A8I5KR97 | A0A8I5KR97_HUMAN | MCPH1 | 742 | ||
A0A8I5KR64 | A0A8I5KR64_HUMAN | MCPH1 | 608 | ||
A0A8I5KQQ3 | A0A8I5KQQ3_HUMAN | MCPH1 | 79 | ||
A0A8I5KRI7 | A0A8I5KRI7_HUMAN | MCPH1 | 580 | ||
A0A8I5KV10 | A0A8I5KV10_HUMAN | MCPH1 | 875 | ||
A0A8I5KTK9 | A0A8I5KTK9_HUMAN | MCPH1 | 57 | ||
A0A8I5KW78 | A0A8I5KW78_HUMAN | MCPH1 | 830 | ||
A0A8I5KX36 | A0A8I5KX36_HUMAN | MCPH1 | 890 | ||
A0A8I5KWR1 | A0A8I5KWR1_HUMAN | MCPH1 | 180 | ||
A0A8I5KYD2 | A0A8I5KYD2_HUMAN | MCPH1 | 166 | ||
A0A8I5KYX6 | A0A8I5KYX6_HUMAN | MCPH1 | 113 | ||
A0A8I5KZ89 | A0A8I5KZ89_HUMAN | MCPH1 | 744 | ||
A0A8I5KXP9 | A0A8I5KXP9_HUMAN | MCPH1 | 121 | ||
A0A8I5KXJ5 | A0A8I5KXJ5_HUMAN | MCPH1 | 450 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_046135 | 146-194 | in isoform 2 | |||
Sequence: DDDVPILLFESNGSLIYTPTIEINSRHHSAMEKRLQEMKEKRENLSPTS → A | ||||||
Compositional bias | 316-346 | Polar residues | ||||
Sequence: KQAAGMSQETFEEKYRLSPTLSSTKGHLLIH | ||||||
Compositional bias | 349-380 | Basic residues | ||||
Sequence: PRSSSVKRKRVSHGSHSPPKEKCKRKRSTRRS | ||||||
Compositional bias | 559-579 | Polar residues | ||||
Sequence: KSTQNKGTTSKISNSSEGEAQ | ||||||
Alternative sequence | VSP_046136 | 610 | in isoform 2 and isoform 3 | |||
Sequence: V → M | ||||||
Alternative sequence | VSP_046137 | 611-835 | in isoform 2 and isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AX087870 EMBL· GenBank· DDBJ | CAC34661.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022909 EMBL· GenBank· DDBJ | BAB14304.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301702 EMBL· GenBank· DDBJ | BAG63174.1 EMBL· GenBank· DDBJ | mRNA | ||
AC016065 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC018398 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AF287957 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877206 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877207 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC030702 EMBL· GenBank· DDBJ | AAH30702.2 EMBL· GenBank· DDBJ | mRNA | ||
BK004076 EMBL· GenBank· DDBJ | DAA04567.1 EMBL· GenBank· DDBJ | mRNA |