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Q7TSJ2 (MAP6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 6

Short name=MAP-6
Alternative name(s):
Stable tubule-only polypeptide
Short name=STOP
Gene names
Name:Map6
Synonyms:Mtap6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in microtubule stabilization in many cell types, including neuronal cells. Specifically has microtubule cold stabilizing activity. Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B. Ref.2

Subunit structure

Interacts with calmodulin (via C-terminus); the interaction is dependent on Ca2+. Interacts with TMEM106B By similarity. Ref.5

Subcellular location

Cytoplasmcytoskeleton. Golgi apparatus. Note: Isoform 1 and isoform 2 associate with axonal microtubules in neurons. Isoform 3 associates with microtubules in fibroblasts. Ref.2 Ref.8

Tissue specificity

Isoform 1 is specifically expressed in adult brain. Isoform 2 is predominantly expressed in embryonic brain; expression persists at low levels in the adult brain. Isoform 3 is expressed at high levels in lung and at lower levels in testis, heart, muscle and kidney (at protein level). Oligodendrocytes express a major isoform of89 kDa (O-STOP). Astrocytes also express an isoform of60 kDa (A-STOP). Ref.6 Ref.7

Developmental stage

Isoform 2 is expressed in embryonic brain. Ref.6

Disruption phenotype

Mice are devoid of cold-stable microtubules and show no detectable defects in brain anatomy but show synaptic defects, with depleted synaptic vesicle pools and impaired synaptic plasticity, associated with severe behavioral disorders, including a disorganized activity with disruption of normal behavioral sequences and episodes of hyperlocomotion or apparent prostration, anxiety, severe social withdrawal and complete nurturing defects. The behavioral defects are alleviated by long-term treatment with neuroleptics. Ref.4

Sequence similarities

Belongs to the STOP family.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: Comment: Additional isoforms seem to exist.
Isoform 1 (identifier: Q7TSJ2-1)

Also known as: N-STOP; Neuronal STOP;

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: Q7TSJ2-2)

Also known as: E-STOP; Early STOP;

The sequence of this isoform differs from the canonical sequence as follows:
     569-906: Missing.
Note: Produced by alternative splicing of isoform 1.
Isoform 3 (identifier: Q7TSJ2-3)

Also known as: F-STOP; Fibroblastic STOP;

The sequence of this isoform differs from the canonical sequence as follows:
     1-203: Missing.
     503-509: VEKPSVQ → EPGQTHQ
     510-906: Missing.
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 906906Microtubule-associated protein 6
PRO_0000344045

Regions

Repeat222 – 26746Mc-1
Repeat268 – 31346Mc-2
Repeat314 – 35946Mc-3
Repeat360 – 40546Mc-4
Region1 – 1515Calmodulin-binding By similarity
Region116 – 13924Mn 1 By similarity
Region124 – 13815Calmodulin-binding By similarity
Region151 – 17424Mn 2 By similarity
Region160 – 17415Calmodulin-binding By similarity
Region187 – 20115Calmodulin-binding By similarity
Region222 – 4051844 X approximate tandem repeat Mc
Region235 – 24915Calmodulin-binding By similarity
Region280 – 29415Calmodulin-binding By similarity
Region325 – 33915Calmodulin-binding By similarity
Region375 – 38915Calmodulin-binding By similarity
Region427 – 45024Mn 3 By similarity
Region435 – 44915Calmodulin-binding By similarity
Region486 – 50015Calmodulin-binding By similarity
Region513 – 52715Calmodulin-binding By similarity

Amino acid modifications

Modified residue1411Phosphotyrosine Ref.10
Lipidation51S-palmitoyl cysteine By similarity
Lipidation101S-palmitoyl cysteine By similarity
Lipidation111S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence1 – 203203Missing in isoform 3.
VSP_034724
Alternative sequence503 – 5097VEKPSVQ → EPGQTHQ in isoform 3.
VSP_034725
Alternative sequence510 – 906397Missing in isoform 3.
VSP_034726
Alternative sequence569 – 906338Missing in isoform 2.
VSP_034727

Experimental info

Sequence conflict811P → L in CAA75049. Ref.1
Sequence conflict871V → G in CAA75930. Ref.1
Sequence conflict3441E → K in CAA75930. Ref.1
Sequence conflict3441E → K in CAA75989. Ref.2
Sequence conflict4051G → S in CAA75049. Ref.1
Sequence conflict755 – 7573MVP → VVH in CAA75930. Ref.1
Sequence conflict7551M → V in CAA75049. Ref.1
Sequence conflict8251P → S in CAA75930. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (N-STOP) (Neuronal STOP) [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: F3CED1FCF1E2CD83

FASTA90696,450
        10         20         30         40         50         60 
MAWPCITRAC CIARFWNQLD KADIAVPLVF TKYSEATEHP GAPPQPPAPL QPALAPPSRA 

        70         80         90        100        110        120 
VAIETQPAQG ESDAVARATG PAPGPSVDRE TVAAPGRSGL GLGAASASTS GSGPADSVMR 

       130        140        150        160        170        180 
QDYRAWKVQR PEPSCRPRSE YQPSDAPFER ETQYQKDFRA WPLPRRGDHP WIPKPVQIPA 

       190        200        210        220        230        240 
TSQPSQPVLG VPKRRPQSQE RGPMQLSADA RDPEGAGGAG VLAAGKASGV DQRDTRRKAG 

       250        260        270        280        290        300 
PAWMVTRNEG HEEKPLPPAQ SQTQEGGPAA GKASGADQRD TRRKAGPAWM VTRSEGHEEK 

       310        320        330        340        350        360 
PLPPAQSQTQ EGGPAAGKAS GADQRDTRRK AGPAWMVTRT EGHEETPLPP AQSQTQEGGP 

       370        380        390        400        410        420 
AAGKASGADE RDTRRKAGPA WMVRRSEGHE QTPAAHAQGT GPEGGKGRAV ADALNRQIRE 

       430        440        450        460        470        480 
EVASTVSSSY RNEFRAWTDI KPVKPIKAKP QYKPPDDKMV HETSYSAQFK GEANKPSAAD 

       490        500        510        520        530        540 
NKAMDRRRIR SLYSEPFKEC PKVEKPSVQS SKPKKTSTSH KPPRKAKDKQ VVSGQAAKKK 

       550        560        570        580        590        600 
TTEGPSATKP DDKEQSKEMN NKLAEAKESR VKPTSDASKN RGPVTKEPHK DQGSVAPGLP 

       610        620        630        640        650        660 
KGQEPLKDQG PVVPGLPKDQ VPVVPGSLKG QSPTAPGPTK DQGAVLLGPV KDLGPVAPAP 

       670        680        690        700        710        720 
IKVQDHIASE LLKNKDSVPL APAKAQSPLL PEPLKNQSPV VPASTKDQSF PTPAPRKDPG 

       730        740        750        760        770        780 
PVIPEPEKDR APTVPERRKD QHVSIMASLK NEAPMVPESV KNQGLAGPEL VKDTGTDTTA 

       790        800        810        820        830        840 
PRYLKGHDSV FVAPVKNQGP VIPEPVKSQD PIIPALAKDQ GPMLPEPPKN QSPVVLGPIK 

       850        860        870        880        890        900 
NQDPIIPVPL KGQDPLVPAP TKDQGPTAPD PLKTQGPKGT QLPTVSPSPP VMIPTVPHTE 


YIEGSP 

« Hide

Isoform 2 (E-STOP) (Early STOP) [UniParc].

Checksum: 81B1DFF1B51D2658
Show »

FASTA56861,105
Isoform 3 (F-STOP) (Fibroblastic STOP) [UniParc].

Checksum: E19396DFF272B496
Show »

FASTA30632,803

References

« Hide 'large scale' references
[1]"Genomic structure and chromosomal mapping of the mouse STOP gene (Mtap6)."
Denarier E., Aguezzoul M., Jolly C., Vourc'h C., Roure A., Andrieux A., Bosc C., Job D.
Biochem. Biophys. Res. Commun. 243:791-796(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
Strain: 129/SvJ.
Tissue: Liver.
[2]"Nonneuronal isoforms of STOP protein are responsible for microtubule cold stability in mammalian fibroblasts."
Denarier E., Fourest-Lieuvin A., Bosc C., Pirollet F., Chapel A., Margolis R.L., Job D.
Proc. Natl. Acad. Sci. U.S.A. 95:6055-6060(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
Strain: Swiss Webster / NIH.
Tissue: Fibroblast.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[4]"The suppression of brain cold-stable microtubules in mice induces synaptic defects associated with neuroleptic-sensitive behavioral disorders."
Andrieux A., Salin P.A., Vernet M., Kujala P., Baratier J., Gory-Faure S., Bosc C., Pointu H., Proietto D., Schweitzer A., Denarier E., Klumperman J., Job D.
Genes Dev. 16:2350-2364(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Unusual Ca(2+)-calmodulin binding interactions of the microtubule-associated protein F-STOP."
Bouvier D., Vanhaverbeke C., Simorre J.P., Arlaud G.J., Bally I., Forge V., Margolis R.L., Gans P., Kleman J.P.
Biochemistry 42:11484-11493(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALMODULIN.
[6]"Overlap of promoter and coding sequences in the mouse STOP gene (Mtap6)."
Aguezzoul M., Andrieux A., Denarier E.
Genomics 81:623-627(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[7]"Astrocytes and oligodendrocytes express different STOP protein isoforms."
Galiano M.R., Bosc C., Schweitzer A., Andrieux A., Job D., Hallak M.E.
J. Neurosci. Res. 78:329-337(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[8]"STOP-like protein 21 is a novel member of the STOP family, revealing a Golgi localization of STOP proteins."
Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D., Franck R., Denarier E., Job D., Andrieux A.
J. Biol. Chem. 281:28387-28396(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[10]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14754, Y14755, Y14756 Genomic DNA. Translation: CAA75049.1.
Y16008 Genomic DNA. Translation: CAA75930.1.
Y16032 mRNA. Translation: CAA75989.1.
BC053039 mRNA. Translation: AAH53039.1.
PIRJC5963.
RefSeqNP_001036820.2. NM_001043355.2.
NP_001041632.1. NM_001048167.1.
NP_034967.2. NM_010837.3.
UniGeneMm.154087.

3D structure databases

ProteinModelPortalQ7TSJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201587. 4 interactions.
IntActQ7TSJ2. 5 interactions.
MINTMINT-4105179.

Proteomic databases

PaxDbQ7TSJ2.
PRIDEQ7TSJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068973; ENSMUSP00000064787; ENSMUSG00000055407. [Q7TSJ2-1]
ENSMUST00000107100; ENSMUSP00000102717; ENSMUSG00000055407. [Q7TSJ2-3]
GeneID17760.
KEGGmmu:17760.
UCSCuc009ilg.1. mouse. [Q7TSJ2-1]
uc009ili.1. mouse. [Q7TSJ2-3]

Organism-specific databases

CTD4135.
MGIMGI:1201690. Map6.

Phylogenomic databases

eggNOGNOG87903.
GeneTreeENSGT00530000063947.
HOGENOMHOG000113479.
HOVERGENHBG053112.
InParanoidQ7TSJ2.
KOK10432.
OMARKAGPAW.
OrthoDBEOG7ZWD1D.
PhylomeDBQ7TSJ2.
TreeFamTF338320.

Gene expression databases

ArrayExpressQ7TSJ2.
BgeeQ7TSJ2.
GenevestigatorQ7TSJ2.

Family and domain databases

InterProIPR007882. MAP6.
IPR024963. MAP6/FAM154.
[Graphical view]
PANTHERPTHR14759. PTHR14759. 1 hit.
PfamPF05217. STOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292441.
PROQ7TSJ2.
SOURCESearch...

Entry information

Entry nameMAP6_MOUSE
AccessionPrimary (citable) accession number: Q7TSJ2
Secondary accession number(s): O55129 expand/collapse secondary AC list , O70586, O70587, Q78DV4, Q78DV5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot