O15021 · MAST4_HUMAN
- ProteinMicrotubule-associated serine/threonine-protein kinase 4
- GeneMAST4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2623 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 576-584 | ATP (UniProtKB | ChEBI) | |||
Binding site | 599 | ATP (UniProtKB | ChEBI) | |||
Active site | 693 | Proton acceptor | |||
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMicrotubule-associated serine/threonine-protein kinase 4
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15021
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | VAR_059768 | 77 | in dbSNP:rs6867856 | ||
Natural variant | VAR_040787 | 920 | |||
Natural variant | VAR_040788 | 1954 | |||
Natural variant | VAR_040789 | 2198 | in dbSNP:rs752429440 | ||
Natural variant | VAR_040790 | 2290 | |||
Natural variant | VAR_040791 | 2467 | in a lung squamous cell carcinoma sample; somatic mutation | ||
Variants
![](/variants.8e7f84.jpg)
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,918 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Chain | PRO_0000252256 | 1-2623 | UniProt | Microtubule-associated serine/threonine-protein kinase 4 | ||
Modified residue (large scale data) | 137 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | |||
Modified residue | 206 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 206 | PRIDE | Phosphoserine | |||
Modified residue | 213 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 213 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 257 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 261 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | |||
Modified residue | 270 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 270 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 355 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 357 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 864 | PRIDE | Phosphoserine | |||
Modified residue | 914 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 922 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1290 | PRIDE | Phosphoserine | |||
Modified residue | 1292 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1292 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1296 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1300 | PRIDE | Phosphoserine | |||
Modified residue | 1370 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1370 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1377 | PRIDE | Phosphoserine | |||
Modified residue | 1384 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1384 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1386 | PRIDE | Phosphothreonine | |||
Modified residue (large scale data) | 1390 | PRIDE | Phosphothreonine | |||
Modified residue (large scale data) | 1395 | PRIDE | Phosphoserine | |||
Modified residue | 1397 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1397 | PRIDE | Phosphoserine | |||
Modified residue | 1419 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1419 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1432 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1438 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1446 | PRIDE | Phosphoserine | |||
Modified residue | 1467 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1467 | PRIDE | Phosphoserine | |||
Modified residue | 1523 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1523 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1652 | PRIDE | Phosphoserine | |||
Modified residue | 1779 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1779 | PRIDE | Phosphoserine | |||
Modified residue | 1822 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1822 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1828 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1860 | PRIDE | Phosphoserine | |||
Modified residue | 1909 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 1909 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 1947 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 2357 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 2440 | PRIDE | Phosphoserine | |||
Modified residue | 2442 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 2442 | PRIDE | Phosphoserine | |||
Modified residue (large scale data) | 2518 | PRIDE | Phosphoserine | |||
Modified residue | 2520 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 2520 | PRIDE | Phosphoserine | |||
Modified residue | 2552 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 2552 | PRIDE | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-76 | Disordered | |||
Region | 93-165 | Disordered | |||
Compositional bias | 95-108 | Pro residues | |||
Compositional bias | 227-240 | Polar residues | |||
Region | 227-269 | Disordered | |||
Compositional bias | 254-264 | Polar residues | |||
Compositional bias | 289-299 | Polar residues | |||
Region | 289-312 | Disordered | |||
Region | 536-560 | Disordered | |||
Compositional bias | 539-558 | Polar residues | |||
Domain | 570-843 | Protein kinase | |||
Domain | 844-916 | AGC-kinase C-terminal | |||
Region | 921-1082 | Disordered | |||
Compositional bias | 935-964 | Polar residues | |||
Compositional bias | 1049-1062 | Polar residues | |||
Compositional bias | 1069-1078 | Basic and acidic residues | |||
Region | 1107-1143 | Disordered | |||
Domain | 1141-1229 | PDZ | |||
Region | 1227-1262 | Disordered | |||
Compositional bias | 1241-1256 | Basic residues | |||
Region | 1289-1527 | Disordered | |||
Compositional bias | 1444-1460 | Basic and acidic residues | |||
Compositional bias | 1540-1552 | Basic and acidic residues | |||
Region | 1540-1561 | Disordered | |||
Region | 1609-1671 | Disordered | |||
Compositional bias | 1625-1638 | Basic and acidic residues | |||
Compositional bias | 1662-1671 | Basic and acidic residues | |||
Region | 1714-1741 | Disordered | |||
Region | 1764-1795 | Disordered | |||
Compositional bias | 1780-1792 | Basic and acidic residues | |||
Region | 1809-1864 | Disordered | |||
Compositional bias | 1844-1864 | Polar residues | |||
Region | 1876-2386 | Disordered | |||
Compositional bias | 1914-1923 | Polar residues | |||
Compositional bias | 1924-1934 | Basic and acidic residues | |||
Compositional bias | 1963-1975 | Basic and acidic residues | |||
Compositional bias | 1982-1997 | Basic and acidic residues | |||
Compositional bias | 2006-2015 | Polar residues | |||
Compositional bias | 2043-2055 | Basic and acidic residues | |||
Compositional bias | 2068-2083 | Basic and acidic residues | |||
Compositional bias | 2114-2126 | Basic and acidic residues | |||
Compositional bias | 2365-2375 | Basic and acidic residues | |||
Region | 2398-2623 | Disordered | |||
Compositional bias | 2441-2451 | Polar residues | |||
Compositional bias | 2599-2614 | Basic and acidic residues | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
O15021-5
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
- Length2,623
- Mass (Da)284,097
- Last updated2018-03-28 v4
- MD5 Checksum9D21F5BF4D5D60D4CD1C40B6E61A6D8F
O15021-2
- Name2
- Differences from canonical
- 1-225: MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF → MDMSDPNFWTVLSNFTLPHLRSGNRLRRTQS
O15021-4
- Name4
O15021-3
- Name3
- Differences from canonical
- 1-225: MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF → MDESSILRRRGLQKELSLPRRGSLIDSQKWNCLVKR
O15021-6
- Name5
- Differences from canonical
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9J249 | C9J249_HUMAN | MAST4 | 167 | ||
E7EX28 | E7EX28_HUMAN | MAST4 | 238 | ||
F8WBH1 | F8WBH1_HUMAN | MAST4 | 166 | ||
D6RAK1 | D6RAK1_HUMAN | MAST4 | 350 | ||
C9JKM7 | C9JKM7_HUMAN | MAST4 | 59 | ||
B5MC73 | B5MC73_HUMAN | MAST4 | 56 | ||
H7C3S4 | H7C3S4_HUMAN | MAST4 | 122 | ||
H7C2V7 | H7C2V7_HUMAN | MAST4 | 99 | ||
H7C2A9 | H7C2A9_HUMAN | MAST4 | 58 | ||
H7C1I9 | H7C1I9_HUMAN | MAST4 | 1680 | ||
H7C146 | H7C146_HUMAN | MAST4 | 66 | ||
H7C0U3 | H7C0U3_HUMAN | MAST4 | 80 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_020888 | 1-225 | in isoform 2 | ||
Alternative sequence | VSP_023109 | 1-225 | in isoform 3 | ||
Alternative sequence | VSP_059373 | 1-225 | in isoform 5 | ||
Compositional bias | 95-108 | Pro residues | |||
Alternative sequence | VSP_035852 | 225-250 | in isoform 4 | ||
Compositional bias | 227-240 | Polar residues | |||
Alternative sequence | VSP_035853 | 251-2623 | in isoform 4 | ||
Compositional bias | 254-264 | Polar residues | |||
Alternative sequence | VSP_059374 | 277 | in isoform 5 | ||
Compositional bias | 289-299 | Polar residues | |||
Sequence conflict | 350 | in Ref. 4; AK131421 | |||
Compositional bias | 539-558 | Polar residues | |||
Sequence conflict | 662 | in Ref. 4; AK131421 | |||
Sequence conflict | 674-678 | in Ref. 4; BAB71532 | |||
Compositional bias | 935-964 | Polar residues | |||
Compositional bias | 1049-1062 | Polar residues | |||
Compositional bias | 1069-1078 | Basic and acidic residues | |||
Compositional bias | 1241-1256 | Basic residues | |||
Compositional bias | 1444-1460 | Basic and acidic residues | |||
Compositional bias | 1540-1552 | Basic and acidic residues | |||
Sequence conflict | 1624 | in Ref. 1; AAW52510 and 5; BAA20762 | |||
Compositional bias | 1625-1638 | Basic and acidic residues | |||
Compositional bias | 1662-1671 | Basic and acidic residues | |||
Compositional bias | 1780-1792 | Basic and acidic residues | |||
Sequence conflict | 1799 | in Ref. 1; AAW52510 and 5; BAA20762 | |||
Compositional bias | 1844-1864 | Polar residues | |||
Compositional bias | 1914-1923 | Polar residues | |||
Compositional bias | 1924-1934 | Basic and acidic residues | |||
Compositional bias | 1963-1975 | Basic and acidic residues | |||
Compositional bias | 1982-1997 | Basic and acidic residues | |||
Compositional bias | 2006-2015 | Polar residues | |||
Compositional bias | 2043-2055 | Basic and acidic residues | |||
Compositional bias | 2068-2083 | Basic and acidic residues | |||
Compositional bias | 2114-2126 | Basic and acidic residues | |||
Compositional bias | 2365-2375 | Basic and acidic residues | |||
Compositional bias | 2441-2451 | Polar residues | |||
Compositional bias | 2599-2614 | Basic and acidic residues | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY830839 EMBL· GenBank· DDBJ | AAW52510.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008872 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC008920 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC016634 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC034208 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC044799 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092349 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092373 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC113365 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877001 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877010 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC033215 EMBL· GenBank· DDBJ | AAH33215.1 EMBL· GenBank· DDBJ | mRNA | ||
AK057601 EMBL· GenBank· DDBJ | BAB71532.1 EMBL· GenBank· DDBJ | mRNA | ||
AK131421 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AB002301 EMBL· GenBank· DDBJ | BAA20762.1 EMBL· GenBank· DDBJ | mRNA |