Q99439 · CNN2_HUMAN
- ProteinCalponin-2
- GeneCNN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids309 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalponin-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99439
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 470 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000204773 | 2-309 | UniProt | Calponin-2 | |||
Sequence: SSTQFNKGPSYGLSAEVKNRLLSKYDPQKEAELRTWIEGLTGLSIGPDFQKGLKDGTILCTLMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMNPVDLFEANDLFESGNMTQVQVSLLALAGKAKTKGLQSGVDIGVKYSEKQERNFDDATMKAGQCVIGLQMGTNKCASQSGMTAYGTRRHLYDPKNHILPPMDHSTISLQMGTNKCASQVGMTAPGTRRHIYDTKLGTDKCDNSSMSLQMGYTQGANQSGQVFGLGRQIYDPKYCPQGTVADGAPSGTGDCPDPGEVPEYPPYYQEEAGY | |||||||
Modified residue | 8 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 12 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 138 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 184 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Heart and smooth muscle.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-132 | Calponin-homology (CH) | ||||
Sequence: PQKEAELRTWIEGLTGLSIGPDFQKGLKDGTILCTLMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMNPVDLFEANDLFESGNMTQVQVSLLALAGKAK | ||||||
Repeat | 166-191 | Calponin-like 1 | ||||
Sequence: IGLQMGTNKCASQSGMTAYGTRRHLY | ||||||
Repeat | 206-231 | Calponin-like 2 | ||||
Sequence: ISLQMGTNKCASQVGMTAPGTRRHIY | ||||||
Repeat | 245-269 | Calponin-like 3 | ||||
Sequence: MSLQMGYTQGANQSGQVFGLGRQIY | ||||||
Region | 283-309 | Disordered | ||||
Sequence: APSGTGDCPDPGEVPEYPPYYQEEAGY |
Sequence similarities
Belongs to the calponin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q99439-1
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
- Length309
- Mass (Da)33,697
- Last updated2007-01-23 v4
- Checksum0D767E9040190A5F
Q99439-2
- Name2
- Differences from canonical
- 131-169: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BVI6 | H3BVI6_HUMAN | CNN2 | 261 | ||
B4DUT8 | B4DUT8_HUMAN | CNN2 | 330 | ||
H3BQH0 | H3BQH0_HUMAN | CNN2 | 154 | ||
B4DDF4 | B4DDF4_HUMAN | CNN2 | 298 | ||
U3KPS3 | U3KPS3_HUMAN | CNN2 | 103 | ||
K7ES69 | K7ES69_HUMAN | CNN2 | 148 | ||
A0A087X271 | A0A087X271_HUMAN | CNN2 | 179 | ||
A0A087X1X5 | A0A087X1X5_HUMAN | CNN2 | 191 | ||
A0A087WV51 | A0A087WV51_HUMAN | CNN2 | 66 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 52 | in Ref. 6; BAA20887 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_042941 | 131-169 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 142 | in Ref. 6; BAA20887 | ||||
Sequence: I → V | ||||||
Sequence conflict | 165 | in Ref. 6; BAA20887 | ||||
Sequence: V → G | ||||||
Sequence conflict | 182-183 | in Ref. 6; BAA20887 | ||||
Sequence: TA → HL | ||||||
Sequence conflict | 187-202 | in Ref. 6; BAA20887 | ||||
Sequence: RRHLYDPKNHILPPMD → AGISMTPRTISCPPWT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D83735 EMBL· GenBank· DDBJ | BAA12090.1 EMBL· GenBank· DDBJ | mRNA | ||
AK126391 EMBL· GenBank· DDBJ | BAG54322.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004528 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011558 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471139 EMBL· GenBank· DDBJ | EAW69565.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471139 EMBL· GenBank· DDBJ | EAW69567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471139 EMBL· GenBank· DDBJ | EAW69570.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC141818 EMBL· GenBank· DDBJ | AAI41819.1 EMBL· GenBank· DDBJ | mRNA | ||
BC141833 EMBL· GenBank· DDBJ | AAI41834.1 EMBL· GenBank· DDBJ | mRNA | ||
D86059 EMBL· GenBank· DDBJ | BAA20887.1 EMBL· GenBank· DDBJ | mRNA |