P27546 · MAP4_MOUSE

  • Protein
    Microtubule-associated protein 4
  • Gene
    Map4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Non-neuronal microtubule-associated protein. Promotes microtubule assembly.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaxon
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Cellular Componentmicrotubule organizing center
Cellular Componentmitotic spindle
Cellular Componentneuron projection
Cellular Componentpostsynaptic density
Molecular Functionmicrotubule binding
Biological Processcell division
Biological Processestablishment of spindle orientation
Biological Processmicrotubule cytoskeleton organization
Biological Processmicrotubule sliding
Biological Processmitotic spindle organization
Biological Processneuron projection development

Names & Taxonomy

Protein names

  • Recommended name
    Microtubule-associated protein 4
  • Short names
    MAP-4

Gene names

    • Name
      Map4
    • Synonyms
      Mtap4

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • C3H/He
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P27546
  • Secondary accessions
    • Q05BJ2
    • Q3UIS2
    • Q3UUH5
    • Q3UY36
    • Q7TPC6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000727522-1125Microtubule-associated protein 4
Modified residue5Phosphoserine
Modified residue60Phosphoserine
Modified residue99Phosphoserine
Modified residue254Phosphoserine
Modified residue260Phosphothreonine
Modified residue277Phosphothreonine
Modified residue333In isoform P27546-4; Phosphoserine
Modified residue334In isoform P27546-4; Phosphoserine
Modified residue349Phosphothreonine
Modified residue381Phosphoserine
Modified residue410Phosphothreonine
Modified residue447Phosphothreonine
Modified residue475Phosphoserine
Modified residue494Phosphothreonine
Modified residue503Phosphothreonine
Modified residue506Phosphoserine
Modified residue511Phosphothreonine
Modified residue512Phosphoserine
Modified residue517Phosphoserine
Modified residue519Phosphoserine
Modified residue598Phosphoserine
Modified residue617Phosphoserine
Modified residue658Phosphothreonine
Modified residue667Phosphoserine
Modified residue684Phosphoserine
Modified residue694Phosphoserine
Modified residue760Phosphoserine
Modified residue798Phosphoserine
Cross-link811Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue826Phosphoserine
Modified residue901Phosphoserine
Modified residue914Phosphoserine
Modified residue915Phosphothreonine
Modified residue973Phosphoserine
Modified residue1046Phosphoserine
Modified residue1118Phosphoserine
Modified residue1124Phosphoserine

Post-translational modification

Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity).
Phosphorylation on Ser-760 negatively regulates MAP4 activity to promote microtubule assembly. Isoform 4 is phosphorylated on Ser-333 and Ser-334 (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Testis, striated and cardiac muscle.

Gene expression databases

Interaction

Subunit

Interacts with SEPTIN2; this interaction impedes tubulin-binding. Interacts with TRAF3IP1 (PubMed:26487268).
Interacts with KNSTRN (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, repeat.

TypeIDPosition(s)Description
Compositional bias49-63Basic and acidic residues
Region49-103Disordered
Region245-265Disordered
Compositional bias247-263Polar residues
Region315-361Disordered
Region455-478Disordered
Region508-529Disordered
Region563-964Disordered
Compositional bias567-581Basic and acidic residues
Compositional bias582-596Polar residues
Compositional bias623-638Polar residues
Compositional bias677-711Polar residues
Compositional bias777-808Polar residues
Compositional bias827-854Polar residues
Compositional bias862-917Polar residues
Repeat896-926Tau/MAP 1
Compositional bias923-937Basic and acidic residues
Repeat965-995Tau/MAP 2
Repeat996-1026Tau/MAP 3
Repeat1027-1058Tau/MAP 4
Region1047-1125Disordered
Compositional bias1095-1125Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

P27546-1

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.

  • Length
    1,125
  • Mass (Da)
    117,429
  • Last updated
    2007-06-12 v3
  • Checksum
    E948B7F1F5B903E9
MADLSLVDALTEPPPEIEGEIKRDFMAALEAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTDTTPGPDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVVLPSDPITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNADLHSGTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQKETPGSQPSEPCSGVSRQEEAKAAVGVTGNDITTPPNKEPPPSPEKKAKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTSGGLNKKPMSLASGSVPAAPHKRPAAATATARPSTLPARDVKPKPITEAKVAEKRTSPSKPSSAPALKPGPKTTPTVSKATSPSTLVSTGPSSRSPATTLPKRPTSIKTEGKPADVKRMTAKSASADLSRSKTTSASSVKRNTTPTGAAPPAGMTSTRVKPMSAPSRSSGALSVDKKPTSTKPSSSAPRVSRLATTVSAPDLKSVRSKVGSTENIKHQPGGGRAKVEKKTEAATTAGKPEPNAVTKAAGSIASAQKPPAGKVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGNVQIQNKKVDISKVSSKCGSKANIKHKPGGGDVKIESQKLNFKEKAQAKVGSLDNVGHLPAGGAVKTEGGGSEALPCPGPPAGEEPVIPEAAPDAGAPTSASGLSGHTTLSGGGDQREPQTLDSQIQETSI

P27546-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P27546-3

P27546-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-26: MADLSLVDALTEPPPEIEGEIKRDFM → MSLPEKQPAALT
    • 30-259: EAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDTSQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYPDYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADLLFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQEWSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKEQLPAKALETMAEQTTDVVHSPSTDT → AAEDEQLSKGNPPECGMDSRKEIGQDGFEWQRTEGKLNEIGLNVSMDGQLKDRLVKNSSFLEQNKLGFFEGKLDKELSIEKPNKAYQETSGHLESGYVISGTCQPSEGNLVHQKAAEFHPGLTEGKDKAATVQGKVAGKSGLEIKSQPDLNFPGAADTLTQHGEEQETSAWNANFYSVTQSPQAA
    • 263-419: PDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMELLTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTTSPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEIEEALAKNDESSAEIPVAQETVVSETEVVLATEVV → KEKNGLVSSCSVTGVMSDNSGQLNNKSPLLVAITHPDPTSEHLPTTSPPITMVEFTQENLNAGQDKELEKLRSSEEGPMLDQVPQQKKAIRRALSECYHLSVPPAVNLVDKYPELPAREE
    • 424-531: PITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPTETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPLSEEEVTSVKDMSPSAETEAPLAKNAD → LLPPTSSPMPSPMPRKLGVPAMRRSMTVAEDQSASCRLSAGELASLSASQVPTALTFEEPVAKEREEQIHFSNDSNSSGKKELGIAGLY
    • 535-625: GTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKPREDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAPSPLENLEQK → KLEQIPEGSHKGKGQKNTGETRVDSCPFICLGGEKQLMALAGKKEIEVTATQSIPSLLLE
    • 629-637: GSQPSEPCS → RD
    • 927-964: Missing
    • 965-995: Missing
    • 1124-1125: SI → N

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A140T8T5A0A140T8T5_MOUSEMap4414
E9PZ43E9PZ43_MOUSEMap4933
Q78TF3Q78TF3_MOUSEMap499
A0A0G2JFH2A0A0G2JFH2_MOUSEMap41441
A0A0G2JFK3A0A0G2JFK3_MOUSEMap4207
A0A0G2JFT4A0A0G2JFT4_MOUSEMap4276
A0A0G2JG35A0A0G2JG35_MOUSEMap4290
A0A0G2JDY5A0A0G2JDY5_MOUSEMap4220
A0A0G2JDU1A0A0G2JDU1_MOUSEMap4116
A0A0G2JE57A0A0G2JE57_MOUSEMap481
A0A0G2JDN7A0A0G2JDN7_MOUSEMap4902

Sequence caution

The sequence AAH42645.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAE27434.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0260891-26in isoform 4
Alternative sequenceVSP_02609030-259in isoform 4
Compositional bias49-63Basic and acidic residues
Sequence conflict225in Ref. 3; AAH55364
Compositional bias247-263Polar residues
Sequence conflict252in Ref. 3; AAH55364
Alternative sequenceVSP_026091263-419in isoform 4
Sequence conflict394-395in Ref. 1; AAA16372
Sequence conflict416in Ref. 3; AAH55332
Alternative sequenceVSP_026092424-531in isoform 4
Sequence conflict435In isoform P27546-4; in Ref. 2; BAE23650/BAE22377
Alternative sequenceVSP_026093535-625in isoform 4
Compositional bias567-581Basic and acidic residues
Compositional bias582-596Polar residues
Compositional bias623-638Polar residues
Alternative sequenceVSP_026094629-637in isoform 4
Compositional bias677-711Polar residues
Compositional bias777-808Polar residues
Compositional bias827-854Polar residues
Compositional bias862-917Polar residues
Compositional bias923-937Basic and acidic residues
Alternative sequenceVSP_026095927-964in isoform 3 and isoform 4
Sequence conflict955in Ref. 3; AAH55364
Alternative sequenceVSP_026096965-995in isoform 4
Sequence conflict982in Ref. 1; AAA16372
Sequence conflict993in Ref. 1; AAA16372
Sequence conflict1053in Ref. 1; AAA16372
Sequence conflict1060in Ref. 3; AAH44654/AAH55364
Sequence conflict1089in Ref. 1; AAA16372
Compositional bias1095-1125Polar residues
Alternative sequenceVSP_0260971124-1125in isoform 2, isoform 3 and isoform 4

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M72414
EMBL· GenBank· DDBJ
AAA16372.1
EMBL· GenBank· DDBJ
mRNA
AK134996
EMBL· GenBank· DDBJ
BAE22377.1
EMBL· GenBank· DDBJ
mRNA
AK138416
EMBL· GenBank· DDBJ
BAE23650.1
EMBL· GenBank· DDBJ
mRNA
AK146790
EMBL· GenBank· DDBJ
BAE27434.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC042645
EMBL· GenBank· DDBJ
AAH42645.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC044654
EMBL· GenBank· DDBJ
AAH44654.1
EMBL· GenBank· DDBJ
mRNA
BC050893
EMBL· GenBank· DDBJ
AAH50893.1
EMBL· GenBank· DDBJ
mRNA
BC055332
EMBL· GenBank· DDBJ
AAH55332.1
EMBL· GenBank· DDBJ
mRNA
BC055364
EMBL· GenBank· DDBJ
AAH55364.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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