P49589 · SYCC_HUMAN
- ProteinCysteine--tRNA ligase, cytoplasmic
- GeneCARS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids748 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys)This reaction proceeds in the forward direction.
Cofactor
Kinetics
Isoform 1
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.4 μM | tRNA(Cys) |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
18000 pmol/sec/mg | for tRNA(Cys) |
Isoform 2
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.4 μM | tRNA(Cys) |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
4000 pmol/sec/mg | for tRNA(Cys) |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 55 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | L-cysteine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 96 | L-cysteine (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 348 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 373 | L-cysteine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 373 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 377 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 409 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-tRNA ligase activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | tRNA binding | |
Biological Process | cysteinyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCysteine--tRNA ligase, cytoplasmic
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP49589
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Microcephaly, developmental delay, and brittle hair syndrome (MDBH)
- Note
- DescriptionAn autosomal recessive disorder characterized by developmental delay, motor and cognitive disabilities, brittle hair and nails, failure to thrive, and short stature.
- See alsoMIM:618891
Natural variants in MDBH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084305 | 341 | R>H | in MDBH; 50% reduction of cysteine-tRNA ligase activity | |
VAR_084306 | 359 | S>L | in MDBH; 84% reduction of cysteine-tRNA ligase activity | |
VAR_084307 | 380-748 | missing | in MDBH; undetectable mutant protein in patient cells; loss-of-function variant unable to rescue viability defects in a yeast complementation assay | |
VAR_084308 | 400 | L>Q | in MDBH; loss-of-function variant unable to rescue viability defects in a yeast complementation assay |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_084305 | 341 | in MDBH; 50% reduction of cysteine-tRNA ligase activity | |||
Sequence: R → H | ||||||
Natural variant | VAR_084306 | 359 | in MDBH; 84% reduction of cysteine-tRNA ligase activity | |||
Sequence: S → L | ||||||
Natural variant | VAR_084307 | 380-748 | in MDBH; undetectable mutant protein in patient cells; loss-of-function variant unable to rescue viability defects in a yeast complementation assay | |||
Sequence: Missing | ||||||
Natural variant | VAR_084308 | 400 | in MDBH; loss-of-function variant unable to rescue viability defects in a yeast complementation assay | |||
Sequence: L → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,397 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
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_0000159550 | 2-748 | UniProt | Cysteine--tRNA ligase, cytoplasmic | |||
Sequence: ADSSGQQGKGRRVQPQWSPPAGTQPCRLHLYNSLTRNKEVFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLKDYFKFDVFYCMNITDIDDKIIKRARQNHLFEQYREKRPEAAQLLEDVQAALKPFSVKLNETTDPDKKQMLERIQHAVQLATEPLEKAVQSRLTGEEVNSCVEVLLEEAKDLLSDWLDSTLGCDVTDNSIFSKLPKFWEGDFHRDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYVSNGSVYFDTAKFASSEKHSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKGRPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHLTIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQYEKFLNEFFLNVKDILRAPVDITGQFEKWGEEEAELNKNFYDKKTAIHKALCDNVDTRTVMEEMRALVSQCNLYMAARKAVRKRPNQALLENIALYLTHMLKIFGAVEEDSSLGFPVGGPGTSLSLEATVMPYLQVLSEFREGVRKIAREQKVPEILQLSDALRDNILPELGVRFEDHEGLPTVVKLVDRNTLLKEREEKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIPPSEMFLSETDKYSKFDENGLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ | |||||||
Modified residue | 19 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 36 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 79 | UniProt | In isoform P49589-3; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 260 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 305 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 307 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 503 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 746 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 746 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MADSSGQQGKGRRVQPQWSPPA | ||||||
Region | 1-25 | Disordered | ||||
Sequence: MADSSGQQGKGRRVQPQWSPPAGTQ | ||||||
Motif | 57-67 | 'HIGH' region | ||||
Sequence: PTVYDASHMGH | ||||||
Motif | 101-104 | 'KIIK' region | ||||
Sequence: KIIK | ||||||
Motif | 406-410 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Compositional bias | 653-679 | Basic and acidic residues | ||||
Sequence: EKRRVEEEKRKKKEEAARRKQEQEAAK | ||||||
Region | 653-686 | Disordered | ||||
Sequence: EKRRVEEEKRKKKEEAARRKQEQEAAKLAKMKIP |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P49589-1
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
- Length748
- Mass (Da)85,473
- Last updated2002-01-31 v3
- ChecksumD0B7A29EC03AA87F
P49589-2
- Name2
- NoteFound in 20% of the mRNAs.
- Differences from canonical
- 705-748: GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ → VSMVCPHMTWRAKSSAKGKPRS
P49589-3
- Name3
- Differences from canonical
- 9-9: G → APDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPQLFHVARWFRHIEALLGSPCGKGQPCRLQAS
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MADSSGQQGKGRRVQPQWSPPA | ||||||
Alternative sequence | VSP_043571 | 9 | in isoform 3 | |||
Sequence: G → APDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLSAPPADPQLFHVARWFRHIEALLGSPCGKGQPCRLQAS | ||||||
Compositional bias | 653-679 | Basic and acidic residues | ||||
Sequence: EKRRVEEEKRKKKEEAARRKQEQEAAK | ||||||
Alternative sequence | VSP_006312 | 705-748 | in isoform 2 | |||
Sequence: GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ → VSMVCPHMTWRAKSSAKGKPRS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L06845 EMBL· GenBank· DDBJ | AAA73901.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF288206 EMBL· GenBank· DDBJ | AAG00578.1 EMBL· GenBank· DDBJ | mRNA | ||
AF288207 EMBL· GenBank· DDBJ | AAG00579.1 EMBL· GenBank· DDBJ | mRNA | ||
BT009913 EMBL· GenBank· DDBJ | AAP88915.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302644 EMBL· GenBank· DDBJ | BAG63885.1 EMBL· GenBank· DDBJ | mRNA | ||
BX647906 EMBL· GenBank· DDBJ | CAI46108.1 EMBL· GenBank· DDBJ | mRNA | ||
AC108448 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC131971 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471158 EMBL· GenBank· DDBJ | EAX02541.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002880 EMBL· GenBank· DDBJ | AAH02880.1 EMBL· GenBank· DDBJ | mRNA |