O15021 · MAST4_HUMAN

  • Protein
    Microtubule-associated serine/threonine-protein kinase 4
  • Gene
    MAST4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site.

126232004006008001,0001,2001,4001,6001,8002,0002,2002,4002,600
Type
IDPosition(s)Description
Binding site576-584ATP (UniProtKB | ChEBI)
Binding site599ATP (UniProtKB | ChEBI)
Active site693Proton acceptor

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-phosphoinositide-dependent protein kinase activity
Molecular FunctionAMP-activated protein kinase activity
Molecular FunctionATP binding
Molecular FunctionDNA-dependent protein kinase activity
Molecular Functioneukaryotic translation initiation factor 2alpha kinase activity
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionhistone H2AS121 kinase activity
Molecular Functionhistone H2AT120 kinase activity
Molecular Functionhistone H2AXS139 kinase activity
Molecular Functionhistone H2BS14 kinase activity
Molecular Functionhistone H2BS36 kinase activity
Molecular Functionhistone H3S10 kinase activity
Molecular Functionhistone H3S28 kinase activity
Molecular Functionhistone H3S57 kinase activity
Molecular Functionhistone H3T11 kinase activity
Molecular Functionhistone H3T3 kinase activity
Molecular Functionhistone H3T45 kinase activity
Molecular Functionhistone H3T6 kinase activity
Molecular Functionhistone H4S1 kinase activity
Molecular Functionmagnesium ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular FunctionRho-dependent protein serine/threonine kinase activity
Molecular Functionribosomal protein S6 kinase activity
Biological Processcytoskeleton organization
Biological Processintracellular signal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Microtubule-associated serine/threonine-protein kinase 4
  • EC number

Gene names

    • Name
      MAST4
    • Synonyms
      KIAA0303

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O15021
  • Secondary accessions
    • A6NL49
    • B5ME48
    • E7EWQ5
    • J3QT34
    • Q05EE6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_05976877in dbSNP:rs6867856
Natural variantVAR_040787920
Natural variantVAR_0407881954
Natural variantVAR_0407892198in dbSNP:rs752429440
Natural variantVAR_0407902290
Natural variantVAR_0407912467in a lung squamous cell carcinoma sample; somatic mutation

Variants

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

Type
IDPosition(s)Source
Description
ChainPRO_00002522561-2623UniProtMicrotubule-associated serine/threonine-protein kinase 4
Modified residue (large scale data)137PRIDEPhosphoserine
Modified residue (large scale data)166PRIDEPhosphoserine
Modified residue206UniProtPhosphoserine
Modified residue (large scale data)206PRIDEPhosphoserine
Modified residue213UniProtPhosphoserine
Modified residue (large scale data)213PRIDEPhosphoserine
Modified residue (large scale data)248PRIDEPhosphoserine
Modified residue (large scale data)257PRIDEPhosphoserine
Modified residue (large scale data)261PRIDEPhosphoserine
Modified residue (large scale data)266PRIDEPhosphoserine
Modified residue270UniProtPhosphoserine
Modified residue (large scale data)270PRIDEPhosphoserine
Modified residue (large scale data)285PRIDEPhosphoserine
Modified residue (large scale data)288PRIDEPhosphoserine
Modified residue (large scale data)355PRIDEPhosphoserine
Modified residue (large scale data)357PRIDEPhosphoserine
Modified residue (large scale data)864PRIDEPhosphoserine
Modified residue914UniProtPhosphoserine
Modified residue (large scale data)922PRIDEPhosphoserine
Modified residue (large scale data)1290PRIDEPhosphoserine
Modified residue1292UniProtPhosphoserine
Modified residue (large scale data)1292PRIDEPhosphoserine
Modified residue (large scale data)1296PRIDEPhosphoserine
Modified residue (large scale data)1300PRIDEPhosphoserine
Modified residue1370UniProtPhosphoserine
Modified residue (large scale data)1370PRIDEPhosphoserine
Modified residue (large scale data)1377PRIDEPhosphoserine
Modified residue1384UniProtPhosphoserine
Modified residue (large scale data)1384PRIDEPhosphoserine
Modified residue (large scale data)1386PRIDEPhosphothreonine
Modified residue (large scale data)1390PRIDEPhosphothreonine
Modified residue (large scale data)1395PRIDEPhosphoserine
Modified residue1397UniProtPhosphoserine
Modified residue (large scale data)1397PRIDEPhosphoserine
Modified residue1419UniProtPhosphoserine
Modified residue (large scale data)1419PRIDEPhosphoserine
Modified residue (large scale data)1432PRIDEPhosphoserine
Modified residue (large scale data)1438PRIDEPhosphoserine
Modified residue (large scale data)1446PRIDEPhosphoserine
Modified residue1467UniProtPhosphoserine
Modified residue (large scale data)1467PRIDEPhosphoserine
Modified residue1523UniProtPhosphoserine
Modified residue (large scale data)1523PRIDEPhosphoserine
Modified residue (large scale data)1652PRIDEPhosphoserine
Modified residue1779UniProtPhosphoserine
Modified residue (large scale data)1779PRIDEPhosphoserine
Modified residue1822UniProtPhosphoserine
Modified residue (large scale data)1822PRIDEPhosphoserine
Modified residue (large scale data)1828PRIDEPhosphoserine
Modified residue (large scale data)1860PRIDEPhosphoserine
Modified residue1909UniProtPhosphoserine
Modified residue (large scale data)1909PRIDEPhosphoserine
Modified residue (large scale data)1947PRIDEPhosphoserine
Modified residue (large scale data)2357PRIDEPhosphoserine
Modified residue (large scale data)2440PRIDEPhosphoserine
Modified residue2442UniProtPhosphoserine
Modified residue (large scale data)2442PRIDEPhosphoserine
Modified residue (large scale data)2518PRIDEPhosphoserine
Modified residue2520UniProtPhosphoserine
Modified residue (large scale data)2520PRIDEPhosphoserine
Modified residue2552UniProtPhosphoserine
Modified residue (large scale data)2552PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in most normal human tissues, with an exception of in testis, small intestine, colon and peripheral blood leukocyte.

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-76Disordered
Region93-165Disordered
Compositional bias95-108Pro residues
Compositional bias227-240Polar residues
Region227-269Disordered
Compositional bias254-264Polar residues
Compositional bias289-299Polar residues
Region289-312Disordered
Region536-560Disordered
Compositional bias539-558Polar residues
Domain570-843Protein kinase
Domain844-916AGC-kinase C-terminal
Region921-1082Disordered
Compositional bias935-964Polar residues
Compositional bias1049-1062Polar residues
Compositional bias1069-1078Basic and acidic residues
Region1107-1143Disordered
Domain1141-1229PDZ
Region1227-1262Disordered
Compositional bias1241-1256Basic residues
Region1289-1527Disordered
Compositional bias1444-1460Basic and acidic residues
Compositional bias1540-1552Basic and acidic residues
Region1540-1561Disordered
Region1609-1671Disordered
Compositional bias1625-1638Basic and acidic residues
Compositional bias1662-1671Basic and acidic residues
Region1714-1741Disordered
Region1764-1795Disordered
Compositional bias1780-1792Basic and acidic residues
Region1809-1864Disordered
Compositional bias1844-1864Polar residues
Region1876-2386Disordered
Compositional bias1914-1923Polar residues
Compositional bias1924-1934Basic and acidic residues
Compositional bias1963-1975Basic and acidic residues
Compositional bias1982-1997Basic and acidic residues
Compositional bias2006-2015Polar residues
Compositional bias2043-2055Basic and acidic residues
Compositional bias2068-2083Basic and acidic residues
Compositional bias2114-2126Basic and acidic residues
Compositional bias2365-2375Basic and acidic residues
Region2398-2623Disordered
Compositional bias2441-2451Polar residues
Compositional bias2599-2614Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

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.

  • Length
    2,623
  • Mass (Da)
    284,097
  • Last updated
    2018-03-28 v4
  • MD5 Checksum
    9D21F5BF4D5D60D4CD1C40B6E61A6D8F
MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSFCRTSNRKSLIGNGQSPALPRPHSPLSAHAGNSPQDSPRNFSPSASAHFSFARRTDGRRWSLASLPSSGYGTNTPSSTVSSSCSSQEKLHQLPYQPTPDELHFLSKHFCTTESIATENRCRNTPMRPRSRSLSPGRSPACCDHEIIMMNHVYKERFPKATAQMEERLKEIITSYSPDNVLPLADGVLSFTHHQIIELARDCLDKSHQGLITSRYFLELQHKLDKLLQEAHDRSESGELAFIKQLVRKILIVIARPARLLECLEFDPEEFYYLLEAAEGHAKEGQGIKTDIPRYIISQLGLNKDPLEEMAHLGNYDSGTAETPETDESVSSSNASLKLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYEGHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFDTRSEKYHHMETEEEDDTNDEDFNVEIRQFSSCSHRFSKVFSSIDRITQNSAEEKEDSVDKTKSTTLPSTETLSWSSEYSEMQQLSTSNSSDTESNRHKLSSGLLPKLAISTEGEQDEAASCPGDPHEEPGKPALPPEECAQEEPEVTTPASTISSSTLSVGSFSEHLDQINGRSECVDSTDNSSKPSSEPASHMARQRLESTEKKKISGKVTKSLSASALSLMIPGDMFAVSPLGSPMSPHSLSSDPSSSRDSSPSRDSSAASASPHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSITTTPFENTSIKTGPARRNSYKSRMVRRSKKSKKKESLERRRSLFKKLAKQPSPLLHTSRSFSCLNRSLSSGESLPGSPTHSLSPRSPTPSYRSTPDFPSGTNSSQSSSPSSSAPNSPAGSGHIRPSTLHGLAPKLGGQRYRSGRRKSAGNIPLSPLARTPSPTPQPTSPQRSPSPLLGHSLGNSKIAQAFPSKMHSPPTIVRHIVRPKSAEPPRSPLLKRVQSEEKLSPSYGSDKKHLCSRKHSLEVTQEEVQREQSQREAPLQSLDENVCDVPPLSRARPVEQGCLKRPVSRKVGRQESVDDLDRDKLKAKVVVKKADGFPEKQESHQKSHGPGSDLENFALFKLEEREKKVYPKAVERSSTFENKASMQEAPPLGSLLKDALHKQASVRASEGAMSDGRVPAEHRQGGGDFRRAPAPGTLQDGLCHSLDRGISGKGEGTEKSSQAKELLRCEKLDSKLANIDYLRKKMSLEDKEDNLCPVLKPKMTAGSHECLPGNPVRPTGGQQEPPPASESRAFVSSTHAAQMSAVSFVPLKALTGRVDSGTEKPGLVAPESPVRKSPSEYKLEGRSVSCLKPIEGTLDIALLSGPQASKTELPSPESAQSPSPSGDVRASVPPVLPSSSGKKNDTTSARELSPSSLKMNKSYLLEPWFLPPSRGLQNSPAVSLPDPEFKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQDHTTDPKLLTCLGQNLHSPDLARPRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNLLSVGRTHPDFYTQTQAMEKAWAPGGKTNHKDGPGEARPPPRDNSSLHSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIESEKSEKLSSFPSLQKDGAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSPSHASGREPGAKPSTAEPSSSPQDPPKPVAAHSESSSHKPRPGPDPGPPKTKHPDRSLSSQKPSVGATKGKEPATQSLGGSSREGKGHSKSGPDVFPATPGSQNKASDGIGQGEGGPSVPLHTDRAPLDAKPQPTSGGRPLEVLEKPVHLPRPGHPGPSEPADQKLSAVGEKQTLSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPAANTDRRAEGKKCTEALYAPAEGDKLEAGLSFVHSENRLKGAERPAAGVGKGFPEARGKGPGPQKPPTEADKPNGMKRSPSATGQSSFRSTALPEKSLSCSSSFPETRAGVREASAASSDTSSAKAAGGMLELPAPSNRDHRKAQPAGEGRTHMTKSDSLPSFRVSTLPLESHHPDPNTMGGASHRDRALSVTATVGETKGKDPAPAQPPPARKQNVGRDVTKPSPAPNTDRPISLSNEKDFVVRQRRGKESLRSSPHKKAL

O15021-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-225: MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF → MDMSDPNFWTVLSNFTLPHLRSGNRLRRTQS

O15021-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 225-250: FCRTSNRKSLIGNGQSPALPRPHSPL → LIDSQKWNCLVKRPVCPNAGRTSPLG
    • 251-2623: Missing

O15021-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-225: MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF → MDESSILRRRGLQKELSLPRRGSLIDSQKWNCLVKR

O15021-6

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-225: MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSF → MKAQRERLQIPGLTLDLTPRSLSPTPSSPGSPCSPLLAFHFWS
    • 277-277: R → RRND

Computationally mapped potential isoform sequences

There are 12 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J249C9J249_HUMANMAST4167
E7EX28E7EX28_HUMANMAST4238
F8WBH1F8WBH1_HUMANMAST4166
D6RAK1D6RAK1_HUMANMAST4350
C9JKM7C9JKM7_HUMANMAST459
B5MC73B5MC73_HUMANMAST456
H7C3S4H7C3S4_HUMANMAST4122
H7C2V7H7C2V7_HUMANMAST499
H7C2A9H7C2A9_HUMANMAST458
H7C1I9H7C1I9_HUMANMAST41680
H7C146H7C146_HUMANMAST466
H7C0U3H7C0U3_HUMANMAST480

Sequence caution

The sequence AK131421 differs from that shown. Reason: Frameshift

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0208881-225in isoform 2
Alternative sequenceVSP_0231091-225in isoform 3
Alternative sequenceVSP_0593731-225in isoform 5
Compositional bias95-108Pro residues
Alternative sequenceVSP_035852225-250in isoform 4
Compositional bias227-240Polar residues
Alternative sequenceVSP_035853251-2623in isoform 4
Compositional bias254-264Polar residues
Alternative sequenceVSP_059374277in isoform 5
Compositional bias289-299Polar residues
Sequence conflict350in Ref. 4; AK131421
Compositional bias539-558Polar residues
Sequence conflict662in Ref. 4; AK131421
Sequence conflict674-678in Ref. 4; BAB71532
Compositional bias935-964Polar residues
Compositional bias1049-1062Polar residues
Compositional bias1069-1078Basic and acidic residues
Compositional bias1241-1256Basic residues
Compositional bias1444-1460Basic and acidic residues
Compositional bias1540-1552Basic and acidic residues
Sequence conflict1624in Ref. 1; AAW52510 and 5; BAA20762
Compositional bias1625-1638Basic and acidic residues
Compositional bias1662-1671Basic and acidic residues
Compositional bias1780-1792Basic and acidic residues
Sequence conflict1799in Ref. 1; AAW52510 and 5; BAA20762
Compositional bias1844-1864Polar residues
Compositional bias1914-1923Polar residues
Compositional bias1924-1934Basic and acidic residues
Compositional bias1963-1975Basic and acidic residues
Compositional bias1982-1997Basic and acidic residues
Compositional bias2006-2015Polar residues
Compositional bias2043-2055Basic and acidic residues
Compositional bias2068-2083Basic and acidic residues
Compositional bias2114-2126Basic and acidic residues
Compositional bias2365-2375Basic and acidic residues
Compositional bias2441-2451Polar residues
Compositional bias2599-2614Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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