Q69YQ0 · CYTSA_HUMAN
- ProteinCytospin-A
- GeneSPECC1L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1117 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in cytokinesis and spindle organization. May play a role in actin cytoskeleton organization and microtubule stabilization and hence required for proper cell adhesion and migration.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytoplasm | |
Cellular Component | filamentous actin | |
Cellular Component | gap junction | |
Cellular Component | microtubule organizing center | |
Cellular Component | spindle | |
Biological Process | actin cytoskeleton organization | |
Biological Process | cell adhesion | |
Biological Process | cell division |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytospin-A
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ69YQ0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with acetylated alpha-tubulin, gamma-tubulin and F-actin. Also observed in a ring around gamma-tubulin containing centrioles possibly in the microtubule organizing center.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Facial clefting, oblique, 1 (OBLFC1)
- Note
- DescriptionA rare form of facial clefting. A facial cleft is any of the fissures between the embryonic prominences that normally unite to form the face.
- See alsoMIM:600251
Natural variants in OBLFC1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_066873 | 415 | Q>P | in OBLFC1; severely impairs the stabilization of microtubules; dbSNP:rs387907108 |
Teebi hypertelorism syndrome 1 (TBHS1)
- Note
- DescriptionA form of Teebi hypertelorism syndrome, a syndrome characterized by an abnormally increased distance between ocular orbits, and facial features that can resemble craniofrontonasal dysplasia such as prominent forehead, widow's peak, heavy and broad eyebrows, long palpebral fissures, ptosis, high and broad nasal bridge, short nose, low-set ears, natal teeth, thin upper lip and a grooved chin. Some affected individuals have limb, urogenital, umbilical and cardiac defects. Developmental delay and/or impaired intellectual development have been observed in some patients. TBHS1 inheritance is autosomal dominant.
- See alsoMIM:145420
Natural variants in TBHS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073384 | 397 | T>P | in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules; dbSNP:rs786201030 | |
VAR_081478 | 400-401 | missing | in TBHS1; uncertain significance | |
VAR_081479 | 420 | E>D | in TBHS1; uncertain significance | |
VAR_073385 | 1083 | G>S | in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules; dbSNP:rs786201031 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_066872 | 190 | no effect on the stabilization of microtubules; dbSNP:rs142144652 | |||
Sequence: T → M | ||||||
Natural variant | VAR_060448 | 301 | in dbSNP:rs204710 | |||
Sequence: G → D | ||||||
Natural variant | VAR_073384 | 397 | in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules; dbSNP:rs786201030 | |||
Sequence: T → P | ||||||
Natural variant | VAR_081478 | 400-401 | in TBHS1; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_066873 | 415 | in OBLFC1; severely impairs the stabilization of microtubules; dbSNP:rs387907108 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_081479 | 420 | in TBHS1; uncertain significance | |||
Sequence: E → D | ||||||
Natural variant | VAR_060449 | 712 | in dbSNP:rs5760340 | |||
Sequence: S → F | ||||||
Natural variant | VAR_060450 | 717 | in dbSNP:rs6004132 | |||
Sequence: T → A | ||||||
Natural variant | VAR_060451 | 943 | in dbSNP:rs11704759 | |||
Sequence: V → A | ||||||
Natural variant | VAR_060452 | 951 | in dbSNP:rs204718 | |||
Sequence: V → M | ||||||
Natural variant | VAR_073385 | 1083 | in TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules; dbSNP:rs786201031 | |||
Sequence: G → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,216 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_0000231018 | 1-1117 | UniProt | Cytospin-A | |||
Sequence: MKKASRSVGSVPKVSAISKTQTAEKIKPENSSSASTGGKLVKPGTAASLSKTKSSDDLLAGMAGGVTVTNGVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKESSSTRERLRERTRLNQSKKLPSAGQGANDMALAKRSRSRTATECDVRMSKSKSDNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTSSDDALDAPSSSESEGIPSIERSRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRPNYGEIPVQEHLLRTSSASRPASLPRVPAMESAKTLSVSRRSSEEVKRDISAQEGASPASLMAMGTTSPQLSLSSSPTASVTPTTRSRIREERKDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 384 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 385 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 392 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 831 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 832 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 835 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 868 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 868 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 870 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 881 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 881 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 887 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 889 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 893 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 922 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 928 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 973 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 981 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
May interact with both microtubules and actin cytoskeleton.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q69YQ0 | EFCAB3 Q8N7B9-2 | 3 | EBI-351113, EBI-11958551 | |
BINARY | Q69YQ0 | ELOA Q14241 | 3 | EBI-351113, EBI-742350 | |
BINARY | Q69YQ0 | G2E3 Q7L622 | 2 | EBI-351113, EBI-751757 | |
BINARY | Q69YQ0 | PPP1R12C Q9BZL4 | 3 | EBI-351113, EBI-721802 | |
BINARY | Q69YQ0 | SNW1 Q13573 | 3 | EBI-351113, EBI-632715 | |
BINARY | Q69YQ0 | ZFHX3 Q15911-2 | 3 | EBI-351113, EBI-10237226 | |
BINARY | Q69YQ0 | ZNF250 P15622-3 | 3 | EBI-351113, EBI-10177272 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-176 | Disordered | ||||
Sequence: MKKASRSVGSVPKVSAISKTQTAEKIKPENSSSASTGGKLVKPGTAASLSKTKSSDDLLAGMAGGVTVTNGVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKESSSTRERLRERTRLNQSKKLPSAGQGANDMALAKRSRSRTATECDVRMSKSKSDNQIS | ||||||
Compositional bias | 11-39 | Polar residues | ||||
Sequence: VPKVSAISKTQTAEKIKPENSSSASTGGK | ||||||
Compositional bias | 71-119 | Polar residues | ||||
Sequence: GVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKES | ||||||
Compositional bias | 120-134 | Basic and acidic residues | ||||
Sequence: SSTRERLRERTRLNQ | ||||||
Compositional bias | 154-176 | Basic and acidic residues | ||||
Sequence: SRSRTATECDVRMSKSKSDNQIS | ||||||
Coiled coil | 168-280 | |||||
Sequence: KSKSDNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQ | ||||||
Region | 293-323 | Disordered | ||||
Sequence: SLSPEITPGNQSDGGGTLTSSVEGSAPGSVE | ||||||
Region | 358-390 | Disordered | ||||
Sequence: SSDDALDAPSSSESEGIPSIERSRKGSSGNASE | ||||||
Coiled coil | 394-449 | |||||
Sequence: ACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESL | ||||||
Coiled coil | 487-807 | |||||
Sequence: RYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRV | ||||||
Region | 920-997 | Disordered | ||||
Sequence: TSSASRPASLPRVPAMESAKTLSVSRRSSEEVKRDISAQEGASPASLMAMGTTSPQLSLSSSPTASVTPTTRSRIREE | ||||||
Compositional bias | 965-990 | Polar residues | ||||
Sequence: SLMAMGTTSPQLSLSSSPTASVTPTT | ||||||
Domain | 1011-1116 | Calponin-homology (CH) | ||||
Sequence: GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFE |
Sequence similarities
Belongs to the cytospin-A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q69YQ0-1
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
- Length1,117
- Mass (Da)124,544
- Last updated2022-02-23 v3
- Checksum9FA1BB5B2DC92C96
Q69YQ0-2
- Name2
- Differences from canonical
- 1030-1068: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J8U1 | C9J8U1_HUMAN | SPECC1L | 788 | ||
C9JLY8 | C9JLY8_HUMAN | SPECC1L | 175 | ||
A0A494C1J1 | A0A494C1J1_HUMAN | SPECC1L | 1136 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-39 | Polar residues | ||||
Sequence: VPKVSAISKTQTAEKIKPENSSSASTGGK | ||||||
Compositional bias | 71-119 | Polar residues | ||||
Sequence: GVKGKKSTCPSAAPSASAPAMTTVENKSKISTGTASSTKRSTSTGNKES | ||||||
Compositional bias | 120-134 | Basic and acidic residues | ||||
Sequence: SSTRERLRERTRLNQ | ||||||
Compositional bias | 154-176 | Basic and acidic residues | ||||
Sequence: SRSRTATECDVRMSKSKSDNQIS | ||||||
Sequence conflict | 375 | in Ref. 1; AAX84184 and 2; CAH10609 | ||||
Sequence: P → L | ||||||
Compositional bias | 965-990 | Polar residues | ||||
Sequence: SLMAMGTTSPQLSLSSSPTASVTPTT | ||||||
Alternative sequence | VSP_047359 | 1030-1068 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1041 | in Ref. 4; BAA21574 | ||||
Sequence: N → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY884293 EMBL· GenBank· DDBJ | AAX84184.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301482 EMBL· GenBank· DDBJ | BAH13494.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832425 EMBL· GenBank· DDBJ | CAH10609.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000354 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AP000355 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AB002374 EMBL· GenBank· DDBJ | BAA21574.1 EMBL· GenBank· DDBJ | mRNA |