Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Microtubule-associated protein 1S

Gene

Map1s

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis (By similarity). Involved in the formation of microtubule bundles.By similarity1 Publication

GO - Molecular functioni

  • actin filament binding Source: HGNC
  • beta-tubulin binding Source: HGNC
  • DNA binding Source: HGNC
  • identical protein binding Source: MGI
  • microtubule binding Source: HGNC
  • tubulin binding Source: HGNC

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • brain development Source: HGNC
  • microtubule bundle formation Source: HGNC
  • microtubule cytoskeleton organization Source: MGI
  • nervous system development Source: HGNC
  • neuron projection morphogenesis Source: HGNC
  • regulation of chromatin disassembly Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1S
Short name:
MAP-1S
Alternative name(s):
BPY2-interacting protein 1
Microtubule-associated protein 8
Cleaved into the following 2 chains:
Gene namesi
Name:Map1s
Synonyms:Bpy2ip1, Map8, Mtap1s
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2443304. Map1s.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmcytosol By similarity
  • Cytoplasmcytoskeleton 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication

  • Note: Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the nucleus in cells exhibiting apoptosis. Associated specifically with microtubules stabilized by paclitaxel and colocalizes with RASSF1. In interphase cells, shows a diffuse cytoplasmic staining with partial localization to the microtubules. During the different stages of mitosis detected at the spindle microtubules. Detected in filopodia-like protrusions and synapses (By similarity).By similarity

GO - Cellular componenti

  • cell junction Source: MGI
  • cell projection Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: HGNC
  • dendrite Source: HGNC
  • microtubule Source: MGI
  • microtubule cytoskeleton Source: MGI
  • neuronal cell body Source: HGNC
  • nucleolus Source: MGI
  • nucleus Source: HGNC
  • perinuclear region of cytoplasm Source: HGNC
  • spindle Source: UniProtKB-SubCell
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 973973Microtubule-associated protein 1SPRO_0000311382Add
BLAST
Chaini1 – 742742MAP1S heavy chainPRO_0000311383Add
BLAST
Chaini743 – 973231MAP1S light chainPRO_0000311384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei586 – 5861PhosphoserineBy similarity
Modified residuei591 – 5911PhosphoserineBy similarity
Modified residuei593 – 5931PhosphoserineBy similarity
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei684 – 6841PhosphoserineBy similarity
Modified residuei724 – 7241PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8C052.
MaxQBiQ8C052.
PaxDbiQ8C052.
PeptideAtlasiQ8C052.
PRIDEiQ8C052.

PTM databases

iPTMnetiQ8C052.
PhosphoSiteiQ8C052.

Expressioni

Tissue specificityi

Expressed in ventral and dorsal horns of the spinal cord, hippocampus, cerebral cortex, molecular, Purkinje and granular cell layers of the cerebellum and in dorsal root ganglia of the PNS (at protein level). Expressed in brain, testis, heart, lung, kidney and liver.2 Publications

Developmental stagei

Expressed in embryo at 10 dpc onwards (at protein level).1 Publication

Gene expression databases

BgeeiQ8C052.
CleanExiMM_MTAP1S.
GenevisibleiQ8C052. MM.

Interactioni

Subunit structurei

Heterodimer of a heavy and a light chain. Interacts with microtubules and actin. Both MAP1S heavy and light chains interact with microtubules. MAP1S light chain interacts with actin. Interacts with ESR1, LRPPRC, RASSF1, microtubules and VCY2. Interacts with WDR47 (via N-terminus of light chain) (By similarity). Interacts (via C-terminus) with GAN (via Kelch domains).By similarity3 Publications

GO - Molecular functioni

  • actin filament binding Source: HGNC
  • beta-tubulin binding Source: HGNC
  • identical protein binding Source: MGI
  • microtubule binding Source: HGNC
  • tubulin binding Source: HGNC

Protein-protein interaction databases

IntActiQ8C052. 2 interactions.
MINTiMINT-4113762.
STRINGi10090.ENSMUSP00000019405.

Structurei

3D structure databases

ProteinModelPortaliQ8C052.
SMRiQ8C052. Positions 245-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 716716Necessary for the microtubule-organizing center localizationBy similarityAdd
BLAST
Regioni601 – 973373Necessary for interaction with RASSF1By similarityAdd
BLAST
Regioni645 – 880236Necessary for association with microtubulesAdd
BLAST
Regioni875 – 97399Necessary for association with actinAdd
BLAST
Regioni881 – 90525Necessary for the mitochondrial aggregation and genome destructionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi560 – 850291Pro-richAdd
BLAST

Domaini

Its C-terminal part of the heavy chain interacts with ESR1 (By similarity). The N-terminus of the heavy chain associates with the C-terminus of the light chain to form the heterodimer complex.By similarity

Sequence similaritiesi

Belongs to the MAP1 family.Curated

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000072716.
HOVERGENiHBG108117.
InParanoidiQ8C052.
KOiK10429.
OMAiPCEFEHR.
OrthoDBiEOG773XKP.
TreeFamiTF350229.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027322. MAP1S.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF11. PTHR13843:SF11. 1 hit.
SUPFAMiSSF56281. SSF56281. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8C052-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVMAAPEA VEAPSSLLLL VVGGECGCPG LLAYVMEELE RGVRSWEDVD
60 70 80 90 100
PAVCSLDEQL KAFVSRHSAT FSSIVKGQRS LHHRGETLET LVLLNPSDKS
110 120 130 140 150
LCDELRNLLM DPAPHKLLVL AGPCLEETGE LLLQTGGFSA HHFLQVLGDK
160 170 180 190 200
EVQDALASAP AAPALTVSCP TFGDWALLGP VPGLQLRLNP PAQLPASEGL
210 220 230 240 250
RAFLEYVAES LEPPSPFELL EPPAAGGFLR LARPCCYVFP GGLGDAAFFA
260 270 280 290 300
VNGFTVLVNG GSNPKSSFWK LVRHLDRVDA VLVTHAGADS LPGLNSLLRR
310 320 330 340 350
KLAEREAAAG PQGQHEERLR RLLSPALGVV FLNAREAASR LRGGEDEAVC
360 370 380 390 400
ARSLLRSLGI APLPLQRGPQ PSCPTVLFEK LGVGRLELFV LHPPPGDPAA
410 420 430 440 450
PACALLVWQP AAPGDKVVRV LFPGRTPPAR LLDGLQRLQH LPCLRRPVVT
460 470 480 490 500
THDLEAPSRA NSQDSLASRD SARKEPVRGT VGSIANRSTV RREPALATRD
510 520 530 540 550
QKKDTRSGPT QPTARDTRRS GPGVVNTKPR VSQNGPRAPV LAAPLTAPVA
560 570 580 590 600
ECPGEAENIL ESERPPAPSP TLSPAQSPPP TAPGNSPERL SLSPLRPEPA
610 620 630 640 650
PDASPSATTP TLTTPSLPAE LGSPHSTEVD ESLSVSFEQV LPAGDPGLSL
660 670 680 690 700
PLRLARRSTS PHDVDLCLVS PCEFSHRKPP PPASPGSSDS SARSQERPPE
710 720 730 740 750
TPPTSVSESL PTLSDSDPVP VADSDDDAGS ESAARDPPPT PRVPPPLPDV
760 770 780 790 800
PGICMVDPEA LPPRARQPLN TTNPSRSRKA PARPSSASAT PRAATVAAKT
810 820 830 840 850
KGPAGDRNRP LSARSEPADR PGRVPLTRKP SVPKTVPKMA SATRLSSGPS
860 870 880 890 900
GRPAPLAAGS PVYLDLAYLP GGGAGHLDQN FFLRVRALCY VISGQGQRQE
910 920 930 940 950
EGLRAVLDAL LAGKRQWDLD LQVTLIPTFD SAVMHRWYEE THAQHQALGI
960 970
RVLGSGSLVS MQDEAFPACK VEF
Length:973
Mass (Da):102,939
Last modified:July 27, 2011 - v2
Checksum:i3DD3E1A43F70E8DD
GO

Sequence cautioni

The sequence AAH52828.1 differs from that shown.Contaminating sequence. At the N-terminus.Curated
The sequence AAH52828.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti475 – 4751E → G in AAH52828 (PubMed:15489334).Curated
Sequence conflicti680 – 6801P → T in ABD47683 (PubMed:16297881).Curated
Sequence conflicti680 – 6801P → T in BAC27800 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ387862 mRNA. Translation: ABD47683.1.
AK032300 mRNA. Translation: BAC27800.1.
AK162124 mRNA. Translation: BAE36739.1.
AC019302 Genomic DNA. No translation available.
BC052828 mRNA. Translation: AAH52828.1. Different initiation.
CCDSiCCDS22387.1.
RefSeqiNP_766601.2. NM_173013.3.
UniGeneiMm.248559.

Genome annotation databases

EnsembliENSMUST00000019405; ENSMUSP00000019405; ENSMUSG00000019261.
GeneIDi270058.
KEGGimmu:270058.
UCSCiuc009mcd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ387862 mRNA. Translation: ABD47683.1.
AK032300 mRNA. Translation: BAC27800.1.
AK162124 mRNA. Translation: BAE36739.1.
AC019302 Genomic DNA. No translation available.
BC052828 mRNA. Translation: AAH52828.1. Different initiation.
CCDSiCCDS22387.1.
RefSeqiNP_766601.2. NM_173013.3.
UniGeneiMm.248559.

3D structure databases

ProteinModelPortaliQ8C052.
SMRiQ8C052. Positions 245-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8C052. 2 interactions.
MINTiMINT-4113762.
STRINGi10090.ENSMUSP00000019405.

PTM databases

iPTMnetiQ8C052.
PhosphoSiteiQ8C052.

Proteomic databases

EPDiQ8C052.
MaxQBiQ8C052.
PaxDbiQ8C052.
PeptideAtlasiQ8C052.
PRIDEiQ8C052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019405; ENSMUSP00000019405; ENSMUSG00000019261.
GeneIDi270058.
KEGGimmu:270058.
UCSCiuc009mcd.2. mouse.

Organism-specific databases

CTDi55201.
MGIiMGI:2443304. Map1s.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
GeneTreeiENSGT00550000074593.
HOGENOMiHOG000072716.
HOVERGENiHBG108117.
InParanoidiQ8C052.
KOiK10429.
OMAiPCEFEHR.
OrthoDBiEOG773XKP.
TreeFamiTF350229.

Miscellaneous databases

PROiQ8C052.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C052.
CleanExiMM_MTAP1S.
GenevisibleiQ8C052. MM.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027322. MAP1S.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PANTHERiPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF11. PTHR13843:SF11. 1 hit.
SUPFAMiSSF56281. SSF56281. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Microtubule-associated protein 8 contains two microtubule binding sites."
    Ding J., Valle A., Allen E., Wang W., Nardine T., Zhang Y., Peng L., Yang Y.
    Biochem. Biophys. Res. Commun. 339:172-179(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH MICROTUBULES AND ACTIN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Egg and Olfactory bulb.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 380-973.
    Strain: C57BL/6NCr.
    Tissue: Hematopoietic stem cell.
  5. "Microtubule-associated protein 1S, a short and ubiquitously expressed member of the microtubule-associated protein 1 family."
    Orban-Nemeth Z., Simader H., Badurek S., Trancikova A., Propst F.
    J. Biol. Chem. 280:2257-2265(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH MICROTUBULES AND ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Gene targeting of GAN in mouse causes a toxic accumulation of microtubule-associated protein 8 and impaired retrograde axonal transport."
    Ding J., Allen E., Wang W., Valle A., Wu C., Nardine T., Cui B., Yi J., Taylor A., Jeon N.L., Chu S., So Y., Vogel H., Tolwani R., Mobley W., Yang Y.
    Hum. Mol. Genet. 15:1451-1463(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAN.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-660 AND SER-724, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMAP1S_MOUSE
AccessioniPrimary (citable) accession number: Q8C052
Secondary accession number(s): E9QKR8, Q3TSD6, Q7TMW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.