Q9UHD1 · CHRD1_HUMAN
- ProteinCysteine and histidine-rich domain-containing protein 1
- GeneCHORDC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids332 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755).
Proposed to act as co-chaperone for HSP90 (PubMed:20230755).
May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755).
In vitro, has intrinsic chaperone activity (PubMed:20230755).
This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755).
Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105).
Involved in stress response (PubMed:20230755).
Prevents tumorigenesis (PubMed:20230755).
Proposed to act as co-chaperone for HSP90 (PubMed:20230755).
May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755).
In vitro, has intrinsic chaperone activity (PubMed:20230755).
This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755).
Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105).
Involved in stress response (PubMed:20230755).
Prevents tumorigenesis (PubMed:20230755).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 5 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 10 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 24 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 27 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 42 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 43 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 59 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 64 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 157 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 162 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 176 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 194 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 195 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 211 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 216 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H |
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 | |
---|---|---|
Molecular Function | ADP binding | |
Molecular Function | ATP binding | |
Molecular Function | Hsp90 protein binding | |
Molecular Function | zinc ion binding | |
Biological Process | centrosome duplication | |
Biological Process | chaperone-mediated protein folding | |
Biological Process | regulation of cellular response to heat | |
Biological Process | regulation of centrosome duplication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCysteine and histidine-rich domain-containing protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UHD1
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_038676 | 329 | in dbSNP:rs1045861 | |||
Sequence: A → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 590 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000317770 | 2-332 | UniProt | Cysteine and histidine-rich domain-containing protein 1 | |||
Sequence: ALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDATTD | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 47 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 51 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 137 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Underexpressed in many breast and lung cancers.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with HSP90AA1, ROCK1 and ROCK2. Interacts with HSP90AB1 and PPP5C (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UHD1 | HSP90AA1 P07900 | 8 | EBI-2550959, EBI-296047 | |
BINARY | Q9UHD1 | HSP90AB1 P08238 | 6 | EBI-2550959, EBI-352572 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-77 | Interaction with PPP5C | ||||
Sequence: ALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEV | ||||||
Domain | 5-64 | CHORD 1 | ||||
Sequence: CYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRH | ||||||
Region | 65-316 | Interaction with HSP90AA1 and HSP90AB1 | ||||
Sequence: NSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLE | ||||||
Domain | 157-216 | CHORD 2 | ||||
Sequence: CKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKH | ||||||
Domain | 227-316 | CS | ||||
Sequence: VVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9UHD1-1
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
- Length332
- Mass (Da)37,490
- Last updated2008-02-05 v2
- Checksum3142D8EC8A879155
Q9UHD1-2
- Name2
- Differences from canonical
- 39-57: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031150 | 39-57 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 234 | in Ref. 1; AAF18437 | ||||
Sequence: W → L | ||||||
Sequence conflict | 267 | in Ref. 1; AAF18437 | ||||
Sequence: H → I |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF192466 EMBL· GenBank· DDBJ | AAF18437.1 EMBL· GenBank· DDBJ | mRNA | ||
AF123249 EMBL· GenBank· DDBJ | AAG43237.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290231 EMBL· GenBank· DDBJ | BAF82920.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312663 EMBL· GenBank· DDBJ | BAG35545.1 EMBL· GenBank· DDBJ | mRNA | ||
AP002364 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471065 EMBL· GenBank· DDBJ | EAW66868.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471065 EMBL· GenBank· DDBJ | EAW66870.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC017789 EMBL· GenBank· DDBJ | AAH17789.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC072461 EMBL· GenBank· DDBJ | AAH72461.1 EMBL· GenBank· DDBJ | mRNA |