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Protein

Microtubule-associated protein 1S

Gene

Map1s

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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. Involved in the formation of microtubule bundles (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

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
Cleaved into the following 2 chains:
Gene namesi
Name:Map1s
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1308266. Map1s.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 972972Microtubule-associated protein 1SPRO_0000311385Add
BLAST
Chaini1 – 741741MAP1S heavy chainPRO_0000311386Add
BLAST
Chaini742 – 972231MAP1S light chainPRO_0000311387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei462 – 4621PhosphoserineCombined sources
Modified residuei585 – 5851PhosphoserineCombined sources
Modified residuei590 – 5901PhosphoserineBy similarity
Modified residuei592 – 5921PhosphoserineBy similarity
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei683 – 6831PhosphoserineBy similarity
Modified residuei723 – 7231PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0C5W1.
PRIDEiP0C5W1.

PTM databases

iPTMnetiP0C5W1.
PhosphoSiteiP0C5W1.

Expressioni

Tissue specificityi

Expressed in cortex cerebellum, dorsal root ganglia, frontal cortex, hippocampus, hypothalamus, mesencephalon, medulla oblongata, occipital cortex, pons, spinal cord, striatum of the brain, neurons, heart, testis and skeletal muscle (at protein level).1 Publication

Gene expression databases

GenevisibleiP0C5W1. RN.

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 LRPPRC, RASSF1, microtubules and VCY2. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts with WDR47 (via N-terminus of light chain) (By similarity). Interacts with ESR1.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025385.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 715715Necessary for the microtubule-organizing center localizationBy similarityAdd
BLAST
Regioni600 – 972373Necessary for interaction with RASSF1By similarityAdd
BLAST
Regioni644 – 879236Necessary for association with microtubulesBy similarityAdd
BLAST
Regioni874 – 97299Necessary for association with actinBy similarityAdd
BLAST
Regioni880 – 90425Necessary for the mitochondrial aggregation and genome destructionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi535 – 767233Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the MAP1A/MAP1B/MAP1S family.Curated

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000072716.
HOVERGENiHBG108117.
InParanoidiP0C5W1.
KOiK10429.
OMAiPCEFEHR.
OrthoDBiEOG773XKP.
PhylomeDBiP0C5W1.
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.

P0C5W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVMAAPEP AEAPSSLLLL VVGGECGCPG LLAYVLEELE RGVRSWEDVD
60 70 80 90 100
PDVCSLDEQL KAFVSRHSAT FSSIVKGQRS LHHRGETLET LVLLNPSDKS
110 120 130 140 150
LCDELRNLLM DPAPHKLLVL AGPCLEETGE LLLQTGGFSA HHFLQVLGDK
160 170 180 190 200
EVQDALASAP AAPALTVSCP TFGDWALLGP APGLRLRLNP PARLPSSEGL
210 220 230 240 250
RAFLEYVAES LEPPSPFELL EPPATGGFLR LARPCCYVFP GGLGDAAFFA
260 270 280 290 300
VNGFTVLVNG GSNPKSSFWK LVRHLDRVDA VLVTHAGADS LPGLNSLLRR
310 320 330 340 350
KLAEREAAAG PQGQHEERLR RLLSPALGVV FLNAREAGSR LRGGEDEAVC
360 370 380 390 400
ARSLLRSLGI VPLPLQRGPQ PSCPTVLFEK LGVGRLELFV LHPPPGDPAA
410 420 430 440 450
PACALLVWQP AAPGDKVVRV LFPGRTPPAR LLDGLQRLQH LPCLRRPVVT
460 470 480 490 500
TQDLEVPSRA NSQDSLASRD STRKEPVRGT VGATSRSAVR REPALATRDQ
510 520 530 540 550
KKDTKPGPTR STVRDVRRSG PGVVTTKPRV SQNGPRAPVP AAPPAAPAPE
560 570 580 590 600
FPGEAENIVE SERPPAPSPT LSPAQSPPPT APGNSPERLS LSPLRPEPAP
610 620 630 640 650
DASPSATTPT LTTPSLPAEL GSPHSTEVDE SLSVSFEQVL PAGDAGLSLP
660 670 680 690 700
LRLARRSTSP HDVDLCLVSP CEFSHRKPPP PASPGSSDSS ARSQERPPET
710 720 730 740 750
PPTSVSESLP TLSDSDPVPV ADSDDDAGSE SAARDPLPTP RVPPPLPDAP
760 770 780 790 800
GICMVDPEAL PPRARQPLST ANSSRGRKAP ARPSSASAAP RAATVAAKTK
810 820 830 840 850
GPVGDRSRPL SARSEPADKP GRVPLTRKPS VPKTVPKMAS ATRNSSGPSS
860 870 880 890 900
RPAPLAAGSP VYLDLAYLPG GGAGHLDQNF FLRVRALCYV ISGQGQRQEE
910 920 930 940 950
GLRGVLDALL AGKRQWDLDL QVTLIPTFDS AVMHRWYEET HEQHQALGIR
960 970
VLGSGSLVSM QDEAFPACKV EF
Length:972
Mass (Da):102,806
Last modified:November 13, 2007 - v1
Checksum:i7C666A9BA457E678
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03102209 Genomic DNA. No translation available.
AABR03103182 Genomic DNA. No translation available.
RefSeqiNP_001099540.1. NM_001106070.1.
UniGeneiRn.38446.

Genome annotation databases

GeneIDi290640.
KEGGirno:290640.
UCSCiRGD:1308266. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03102209 Genomic DNA. No translation available.
AABR03103182 Genomic DNA. No translation available.
RefSeqiNP_001099540.1. NM_001106070.1.
UniGeneiRn.38446.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025385.

PTM databases

iPTMnetiP0C5W1.
PhosphoSiteiP0C5W1.

Proteomic databases

PaxDbiP0C5W1.
PRIDEiP0C5W1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi290640.
KEGGirno:290640.
UCSCiRGD:1308266. rat.

Organism-specific databases

CTDi55201.
RGDi1308266. Map1s.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000072716.
HOVERGENiHBG108117.
InParanoidiP0C5W1.
KOiK10429.
OMAiPCEFEHR.
OrthoDBiEOG773XKP.
PhylomeDBiP0C5W1.
TreeFamiTF350229.

Miscellaneous databases

PROiP0C5W1.

Gene expression databases

GenevisibleiP0C5W1. RN.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain."
    Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L., Benedikz E., Sundstroem E.
    Biochem. Biophys. Res. Commun. 361:127-132(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ESR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "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-462; SER-585 AND SER-723, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1S_RAT
AccessioniPrimary (citable) accession number: P0C5W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: July 6, 2016
This is version 61 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, 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.