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Protein

Microtubule-associated protein 6

Gene

Map6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 6
Short name:
MAP-6
Alternative name(s):
145-kDa STOP
Short name:
STOP145
Stable tubule-only polypeptide
Short name:
STOP
Gene namesi
Name:Map6
Synonyms:Mtap6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61804. Map6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 952952Microtubule-associated protein 6PRO_0000344046Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi5 – 51S-palmitoyl cysteineBy similarity
Lipidationi10 – 101S-palmitoyl cysteineBy similarity
Lipidationi11 – 111S-palmitoyl cysteineBy similarity
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei141 – 1411PhosphotyrosineBy similarity
Modified residuei185 – 1851PhosphoserineCombined sources
Modified residuei207 – 2071PhosphoserineBy similarity
Modified residuei590 – 5901PhosphoserineCombined sources
Modified residuei681 – 6811PhosphoserineCombined sources
Modified residuei736 – 7361PhosphoserineCombined sources
Modified residuei951 – 9511PhosphoserineCombined sources

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ63560.
PRIDEiQ63560.

PTM databases

iPTMnetiQ63560.
PhosphoSiteiQ63560.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Isoform 2 is expressed in embryonic brain.1 Publication

Interactioni

Subunit structurei

Interacts with calmodulin (via C-terminus); the interaction is dependent on Ca2+ (PubMed:8700896, PubMed:11413126). Interacts with TMEM106B (By similarity). Interacts with ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17 (via ANK repeats) (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Tmem106bQ6AYA56EBI-1638469,EBI-9316198

Protein-protein interaction databases

BioGridi248100. 1 interaction.
IntActiQ63560. 3 interactions.
STRINGi10116.ENSRNOP00000032018.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati222 – 26746Mc-1Add
BLAST
Repeati268 – 31346Mc-2Add
BLAST
Repeati314 – 35946Mc-3Add
BLAST
Repeati360 – 40546Mc-4Add
BLAST
Repeati406 – 45146Mc-5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 1515Calmodulin-bindingAdd
BLAST
Regioni116 – 13924Mn 1Add
BLAST
Regioni124 – 13815Calmodulin-bindingAdd
BLAST
Regioni151 – 17424Mn 2Add
BLAST
Regioni160 – 17415Calmodulin-bindingAdd
BLAST
Regioni187 – 20115Calmodulin-bindingAdd
BLAST
Regioni222 – 4512305 X approximate tandem repeat McAdd
BLAST
Regioni235 – 24915Calmodulin-bindingAdd
BLAST
Regioni280 – 29415Calmodulin-bindingAdd
BLAST
Regioni325 – 33915Calmodulin-bindingAdd
BLAST
Regioni373 – 38715Calmodulin-bindingAdd
BLAST
Regioni421 – 43515Calmodulin-bindingAdd
BLAST
Regioni473 – 49624Mn 3Add
BLAST
Regioni481 – 49515Calmodulin-bindingAdd
BLAST
Regioni532 – 54615Calmodulin-bindingAdd
BLAST
Regioni559 – 57315Calmodulin-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the STOP family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IIA0. Eukaryota.
ENOG4110KV2. LUCA.
HOGENOMiHOG000113479.
HOVERGENiHBG053112.
InParanoidiQ63560.
KOiK10432.
PhylomeDBiQ63560.

Family and domain databases

InterProiIPR007882. MAP6.
[Graphical view]
PANTHERiPTHR14759. PTHR14759. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q63560-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAWPCITRAC CIARFWNQLD KADIAVPLVF TKYSEATEHP GAPPQPPAPP
60 70 80 90 100
QPGLAPPSRA VAIETQPAQG ESDAVARATG PAPGPSGDRE TAAAPGRSGL
110 120 130 140 150
GLGAASGSTS GSGPADSVMR QDYRAWKVQR PEPSCRPRSE YQPSDAPFER
160 170 180 190 200
ETQYQKDFRA WPLPRRGDHP WIPKPVQIPA TSQPSPPVLG MPKRRPQSQE
210 220 230 240 250
RGPIQLSADA RDPEGAGGAG VPAAGKASGA DQRDTRRKAG PAWMVTRTEG
260 270 280 290 300
HEEKPLPPAQ SQTQEGGPAA GKASGADQRD TRRKAGPAWM VTRTEGHEEK
310 320 330 340 350
PLPPAQSQTQ EGGPAAGKAS GADQRDTRRK AGPAWMVTRT EGHEETPLPP
360 370 380 390 400
AQSQTQEGGP AAGKASGADQ RDTRRKAGPA WMVTRTEGHE ETPLPPAQSQ
410 420 430 440 450
TQEGGPAAGK ASGADERDTR RKAGPAWMVR RSEGHEQTTA AHAQGTGPEG
460 470 480 490 500
GKGRAVADAL NRQIREEVTS TVSSSYRNEF RAWTDIKPVK PIKAKPQYKP
510 520 530 540 550
PDDKMVHETS YSAQFKGEAS KPTTADNKVV DRRRIRSLYS EPFKESPKVE
560 570 580 590 600
KPSVQSSKPK KTSTSQKPLR KAKDKQVASG QAAKKKTTES PSATKPDDKE
610 620 630 640 650
QSKEMNNKLA EAKESRVKPT SDKNQGPVAK EPHKDQGPVA PGLPKGQGPA
660 670 680 690 700
VQEPLKDQGP MVPGLPKDQA PVVPGSLKGQ SPTAPGPPKD QGAVLLGPMK
710 720 730 740 750
DLGPVAPASV KDQDHMASEL LKNKDSVPLA PAKAQSPLLP EPLKNQSPVV
760 770 780 790 800
PARAKDQSFP APAPTPLKDP GPVIPEPEKD GAPMVPERRK DQNASIMASL
810 820 830 840 850
KNEAPVASES VKNQGLGGPE PAKDTGTDLK GHGSVFVAPV KSQGPVVPEP
860 870 880 890 900
TKGQDPIIPA LAKDQGPILP EPPKNQGPPV VLGPIKNQDP VIPVPLKGQD
910 920 930 940 950
PVVPAPTKDP GPTAPDPLKS QGPRGPQLPT VSPSPPVMIP TVPHAEYIEG

SP
Length:952
Mass (Da):100,485
Last modified:November 1, 1996 - v1
Checksum:i3599A5069096FA73
GO
Isoform 2 (identifier: Q63560-2) [UniParc]FASTAAdd to basket

Also known as: E-STOP, Early STOP

The sequence of this isoform differs from the canonical sequence as follows:
     325-325: R → RDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQR
     615-952: Missing.

Show »
Length:660
Mass (Da):70,622
Checksum:iBCB5494CC1734875
GO

Sequence cautioni

The sequence AAH78848.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei325 – 3251R → RDTRRKAGPAWMVTRTEGHE EKPLPPAQSQTQEGGPAAGK ASGADQR in isoform 2. 2 PublicationsVSP_034728
Alternative sequencei615 – 952338Missing in isoform 2. 2 PublicationsVSP_034729Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93495 mRNA. Translation: CAA63762.1.
AJ002556 mRNA. Translation: CAA05555.1.
BC078848 mRNA. Translation: AAH78848.1. Sequence problems.
RefSeqiNP_058900.1. NM_017204.1. [Q63560-1]
UniGeneiRn.37490.

Genome annotation databases

GeneIDi29457.
KEGGirno:29457.
UCSCiRGD:61804. rat. [Q63560-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93495 mRNA. Translation: CAA63762.1.
AJ002556 mRNA. Translation: CAA05555.1.
BC078848 mRNA. Translation: AAH78848.1. Sequence problems.
RefSeqiNP_058900.1. NM_017204.1. [Q63560-1]
UniGeneiRn.37490.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248100. 1 interaction.
IntActiQ63560. 3 interactions.
STRINGi10116.ENSRNOP00000032018.

PTM databases

iPTMnetiQ63560.
PhosphoSiteiQ63560.

Proteomic databases

PaxDbiQ63560.
PRIDEiQ63560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29457.
KEGGirno:29457.
UCSCiRGD:61804. rat. [Q63560-1]

Organism-specific databases

CTDi4135.
RGDi61804. Map6.

Phylogenomic databases

eggNOGiENOG410IIA0. Eukaryota.
ENOG4110KV2. LUCA.
HOGENOMiHOG000113479.
HOVERGENiHBG053112.
InParanoidiQ63560.
KOiK10432.
PhylomeDBiQ63560.

Miscellaneous databases

PROiQ63560.

Family and domain databases

InterProiIPR007882. MAP6.
[Graphical view]
PANTHERiPTHR14759. PTHR14759. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and properties of the microtubule-stabilizing protein STOP."
    Bosc C., Cronk J.D., Pirollet F., Watterson D.M., Haiech J., Job D., Margolis R.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:2125-2130(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH CALMODULIN, SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells."
    Guillaud L., Bosc C., Fourest-Lieuvin A., Denarier E., Pirollet F., Lafanechere L., Job D.
    J. Cell Biol. 142:167-179(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  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] OF 1-613 (ISOFORM 2).
    Tissue: Testis.
  4. "Purification and assay of a 145-kDa protein (STOP145) with microtubule-stabilizing and motility behavior."
    Margolis R.L., Rauch C.T., Job D.
    Proc. Natl. Acad. Sci. U.S.A. 83:639-643(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins."
    Bosc C., Frank R., Denarier E., Ronjat M., Schweitzer A., Wehland J., Job D.
    J. Biol. Chem. 276:30904-30913(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALMODULIN.
  6. "STOP (stable-tubule-only-polypeptide) is preferentially associated with the stable domain of axonal microtubules."
    Slaughter T., Black M.M.
    J. Neurocytol. 32:399-413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-590; SER-681; SER-736 AND SER-951, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP6_RAT
AccessioniPrimary (citable) accession number: Q63560
Secondary accession number(s): O88748, Q6AYX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.