A0A7I2V2N8 · A0A7I2V2N8_HUMAN
- Proteinnon-specific serine/threonine protein kinase
- GeneMARK3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids726 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site.
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 | dendrite | |
Molecular Function | ATP binding | |
Molecular Function | protein serine/threonine kinase activity |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namenon-specific serine/threonine protein kinase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A7I2V2N8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 666 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 42 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 356 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 359 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 360 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 372 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 382 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 420 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 451 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 473 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 489 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 522 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 525 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 527 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 531 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 545 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 546 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 565 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 567 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 569 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 697 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MSTRTPLPTVNERDTENHTSHGDGRQEVTSRTSRSG | ||||||
Compositional bias | 14-28 | Basic and acidic residues | ||||
Sequence: DTENHTSHGDGRQEV | ||||||
Domain | 56-289 | Protein kinase | ||||
Sequence: YRLLKTIGKGNFAKVKLARHILTGRELFREVRIMKILNHPNIVKLFEVIETEKTLYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRFLVLNPIKRGTLEQIMKDRWI | ||||||
Domain | 308-347 | UBA | ||||
Sequence: ISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLG | ||||||
Compositional bias | 352-400 | Polar residues | ||||
Sequence: ELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRY | ||||||
Region | 352-628 | Disordered | ||||
Sequence: ELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRYSDHAGPAIPSVVAYPKRSQTSTADSDLKEDGISSRKSSGSAVGGKGIAPASPMLGNASNPNKADIPERKKSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAATPDRIRFPRGTASRSTFHGQPRERRTATYNGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLTRRLPTEYERNGRYEGSSRNVSAEQKDENKEAKP | ||||||
Compositional bias | 470-530 | Polar residues | ||||
Sequence: KSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAA | ||||||
Compositional bias | 560-595 | Polar residues | ||||
Sequence: NGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLT | ||||||
Compositional bias | 596-628 | Basic and acidic residues | ||||
Sequence: RRLPTEYERNGRYEGSSRNVSAEQKDENKEAKP | ||||||
Domain | 677-726 | KA1 | ||||
Sequence: DGHAENLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length726
- Mass (Da)81,256
- Last updated2021-04-07 v1
- ChecksumF52C0D2F672E127D
Computationally mapped potential isoform sequences
There are 35 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P27448 | MARK3_HUMAN | MARK3 | 753 | ||
J3KNR0 | J3KNR0_HUMAN | MARK3 | 776 | ||
H0YNV4 | H0YNV4_HUMAN | MARK3 | 643 | ||
H0YKP9 | H0YKP9_HUMAN | MARK3 | 623 | ||
H0YJI9 | H0YJI9_HUMAN | MARK3 | 789 | ||
H0YIY6 | H0YIY6_HUMAN | MARK3 | 505 | ||
A0A7I2YQ84 | A0A7I2YQ84_HUMAN | MARK3 | 108 | ||
A0A7I2YQ91 | A0A7I2YQ91_HUMAN | MARK3 | 113 | ||
A0A7I2YQF4 | A0A7I2YQF4_HUMAN | MARK3 | 640 | ||
A0A7I2YQF7 | A0A7I2YQF7_HUMAN | MARK3 | 738 | ||
A0A7I2YQJ7 | A0A7I2YQJ7_HUMAN | MARK3 | 102 | ||
A0A7I2V2E3 | A0A7I2V2E3_HUMAN | MARK3 | 622 | ||
A0A7I2V2I9 | A0A7I2V2I9_HUMAN | MARK3 | 554 | ||
A0A7I2V2J6 | A0A7I2V2J6_HUMAN | MARK3 | 115 | ||
A0A7I2V2U9 | A0A7I2V2U9_HUMAN | MARK3 | 790 | ||
A0A7I2V3B9 | A0A7I2V3B9_HUMAN | MARK3 | 665 | ||
A0A7I2V3C6 | A0A7I2V3C6_HUMAN | MARK3 | 529 | ||
A0A7I2V3I9 | A0A7I2V3I9_HUMAN | MARK3 | 682 | ||
A0A7I2V3K2 | A0A7I2V3K2_HUMAN | MARK3 | 507 | ||
A0A7I2V3Q1 | A0A7I2V3Q1_HUMAN | MARK3 | 99 | ||
A0A7I2V409 | A0A7I2V409_HUMAN | MARK3 | 796 | ||
A0A7I2V3P5 | A0A7I2V3P5_HUMAN | MARK3 | 535 | ||
A0A7I2V3X7 | A0A7I2V3X7_HUMAN | MARK3 | 115 | ||
A0A7I2V483 | A0A7I2V483_HUMAN | MARK3 | 111 | ||
A0A7I2V4K8 | A0A7I2V4K8_HUMAN | MARK3 | 781 | ||
A0A7I2V4L1 | A0A7I2V4L1_HUMAN | MARK3 | 373 | ||
A0A7I2V4G7 | A0A7I2V4G7_HUMAN | MARK3 | 647 | ||
A0A7I2V549 | A0A7I2V549_HUMAN | MARK3 | 664 | ||
A0A7I2V4T2 | A0A7I2V4T2_HUMAN | MARK3 | 621 | ||
A0A7I2V4T5 | A0A7I2V4T5_HUMAN | MARK3 | 100 | ||
A0A7I2V5G3 | A0A7I2V5G3_HUMAN | MARK3 | 674 | ||
A0A7I2V5H7 | A0A7I2V5H7_HUMAN | MARK3 | 157 | ||
A0A7I2V602 | A0A7I2V602_HUMAN | MARK3 | 655 | ||
A0A7I2V639 | A0A7I2V639_HUMAN | MARK3 | 689 | ||
A0A7I2V5Z7 | A0A7I2V5Z7_HUMAN | MARK3 | 36 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 14-28 | Basic and acidic residues | ||||
Sequence: DTENHTSHGDGRQEV | ||||||
Compositional bias | 352-400 | Polar residues | ||||
Sequence: ELDASDSSSSSNLSLAKVRPSSDLNNSTGQSPHHKVQRSVSSSQKQRRY | ||||||
Compositional bias | 470-530 | Polar residues | ||||
Sequence: KSSTVPSSNTASGGMTRRNTYVCSERTTADRHSVIQNGKENSTIPDQRTPVASTHSISSAA | ||||||
Compositional bias | 560-595 | Polar residues | ||||
Sequence: NGPPASPSLSHEATPLSQTRSRGSTNLFSKLTSKLT | ||||||
Compositional bias | 596-628 | Basic and acidic residues | ||||
Sequence: RRLPTEYERNGRYEGSSRNVSAEQKDENKEAKP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL133367 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF456011 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |