Human protein: IPI00296485 * 112211 Da * MAP1S Microtubule-associated protein 1S - Liebel-Lab @ KIT
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>MAP1S Microtubule-associated protein 1S - Length: 1059 AS 
MAAVAGSGAAAAPSSLLLVVGSEFGSPGLLTYVLEELERGIRSWDVDPGVCNLDEQLKVFVSRHSATFSSIVKGQRSLHH
RGDNLETLVLLNPSDKSLYDELRNLLLDPASHKLLVLAGPCLEETGELLLQTGGFSPHHFLQVLKDREIRDILATTPPPV
QPPILTITCPTFGDWAQLAPAVPGLQGALRLQLRLNPPAQLPNSEGLCEFLEYVAESLEPPSPFELLEPPTSGGFLRLGR
PCCYIFPGGLGDAAFFAVNGFTVLVNGGSNPKSSFWKLVRHLDRVDAVLVTHPGADSLPGLNSLLRRKLAERSEVAAGGG
SWDDRLRRLISPNLGVVFFNACEAASRLARGEDEAELALSLLAQLGITPLPLSRGPVPAKPTVLFEKMGVGRLDMYVLHP
PSAGAERTLASVCALLVWHPAGPGEKVVRVLFPGCTPPACLLDGLVRLQHLRFLREPVVTPQDLEGPGRAESKESVGSRD
SSKREGLLATHPRPGQERPGVARKEPARAEAPRKTEKEAKTPRELKKDPKPSVSRTQPREVRRAASSVPNLKKTNAQAAP
KPRKAPSTSHSGFPPVANGPRSPPSLRCGEASPPSAACGSPASQLVATPSLELGPIPAGEEKALELPLAASSIPRPRTPS
PESHRSPAEGSERLSLSPLRGGEAGPDASPTVTTPTVTTPSLPAEVGSPHSTEVDESLSVSFEQVLPPSAPTSEAGLSLP
LRGPRARRSASPHDVDLCLVSPCEFEHRKAVPMAPAPASPGSSNDSSARSQERAGGLGAEETPPTSVSESLPTLSDSDPV
PLAPGAADSDEDTEGFGVPRHDPLPDPLKVPPPLPDPSSICMVDPEMLPPKTARQTENVSRTRKPLARPNSRAAAPKATP
VAAAKTKGLAGGDRASRPLSARSEPSEKGGRAPLSRKSSTPKTATRGPSGSASSRPGVSATPPKSPVYLDLAYLPSGSSA
HLVDEEFFQRVRALCYVISGQDQRKEEGMRAVLDALLASKQHWDRDLQVTLIPTFDSVAMHTWYAETHARHQALGITVLG
SNSMVSMQDDAFPACKVEF
Linkouts to other data resources: BioCompare * Entrez * PolyMeta * GeneCard * imaGenes * GenomeBrowser * Google Scholar * Mitocheck
AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
ACTIVATE: SMART analysis
NameBeginEndE-value
low complexity221-
low complexity122134-
low complexity184195-
low complexity216232-
low complexity352365-
low complexity502514-
low complexity591603-
low complexity670680-
low complexity750770-
low complexity822837-
low complexity873887-
low complexity923936-


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AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page

AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page


AceView - BLAST - CDD - ensEMBL - EntrezGene - GoPubMed - H-Inv - IHOP - Localisation - MINT - OMIM - ProteinWiki - SMART - UNIPROT - STRING - crosslinks top of page
General information
Entry name MAP1S_HUMAN
Accession number Q66K74, Q27QB1, Q6NXF1, Q8N3L8, Q8N3W5, Q8NI88, Q96H94, Q96IT4, Q96SP8, Q9BRC6, Q9H928, Q9NVK7
Integrated 13-NOV-2007, UniProtKB/Swiss-Prot.
Sequence update 13-NOV-2007, sequence version 2
Annotation update 25-NOV-2008, entry version 32
UniSave Q66K74, Q27QB1, Q6NXF1, Q8N3L8, Q8N3W5, Q8NI88, Q96H94, Q96IT4, Q96SP8, Q9BRC6, Q9H928, Q9NVK7
UniRef100 UniRef100_Q66K74
UniParc UPI00002036F9
Description and origin of the Protein
Description Recommended
Full=Microtubule-associated protein 1S;
Short=MAP-1S;
Synonym
Full=BPY2-interacting protein 1;
Full=Microtubule-associated protein 8;
Full=Variable charge Y chromosome 2-interacting protein 1;
Short=VCY2-interacting protein 1;
Short=Protein VCY2IP-1;
Contains Recommended
Full=MAP1S heavy chain;
Contains Recommended
Full=MAP1S light chain;
Gene name(s) MAP1S
Synonym(s) BPY2IP1 C19orf5 MAP8 VCY2IP1
Organism source Homo sapiens (Human).
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
NCBI TaxID 9606
References
[1] Wong,E.Y., Tse,J.Y., Yao,K.-M., Lui,V.C., Tam,P.-C., Yeung,W.S.,
Identification and characterization of a VCY2 interacting protein-1; VCY2IP-1, a MAP-like protein.
(2004) Biol. Reprod. 70:775-784
Position NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VCY2, AND TISSUE SPECIFICITY.
Comments TISSUE=Testis;
DOI 10.1095/biolreprod.103.018531;
PubMed
14627543 FreeClick to get it from BioOne Subscription requiredClick to get it from BioOne Subscription requiredClick to get it from BioOne FreeClick to get it from intl.biolreprod.org Free after 12 monthsClick to get it from intl.biolreprod.org Free after 12 monthsClick to get it from intl.biolreprod.org Subscription requiredClick to get it from Highwire Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[2] Ding,J., Valle,A., Allen,E., Wang,W., Nardine,T., Zhang,Y., Peng,L., Yang,Y.,
Microtubule-associated protein 8 contains two microtubule binding sites.
(2006) Biochem. Biophys. Res. Commun. 339:172-179
Position NUCLEOTIDE SEQUENCE [MRNA].
DOI 10.1016/j.bbrc.2005.10.199;
PubMed
16297881 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[3]
Submitted JUL-2002 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Comments TISSUE=Amygdala;
[4] Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R., Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H., Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T., Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y., Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M., Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H., Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T., Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K., Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H., Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M., Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S., Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A., Hara,H., Tanase,T.-O., Nomura,Y., Togiya,S., Komai,F., Hara,R., Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A., Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T., Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S., Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H., Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T., Sugiyama,A., Takemoto,M., Kawakami,B., Watanabe,K., Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M., Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y., Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N., Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T., Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K., Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T., Oyama,M., Hata,H., Komatsu,T., Mizushima-Sugano,J., Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K., Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R., Nakai,K., Yada,T., Ohara,O., Isogai,T., Sugano,S.,
Complete sequencing and characterization of 21,243 full-length human cDNAs.
(2004) Nat. Genet. 36:40-45
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI 10.1038/ng1285;
PubMed
14702039 Subscription requiredClick to get it from nature.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[5]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
(2004) Genome Res. 14:2121-2127
Position NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-411.
Comments TISSUE=Brain, Lung, Lymph, and Muscle;
DOI 10.1101/gr.2596504;
PubMed
15489334 Free after 6 monthsClick to get it from www.genome.org Free after 6 monthsClick to get it from www.genome.org FreeClick to get it from www.genome.org Subscription requiredClick to get it from DOI Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral CiteXplore
[6] Shichijo,S., Itoh,K.,
Identification of immuno-peptidmics that recognized by tumor-reactive CTL generated from TIL of colon cancer patients.
Submitted MAY-2001 to the EMBL GenBank DDBJ databases
Position NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059.
[7] Liu,L., McKeehan,W.L.,
Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity.
(2002) Genomics 79:124-136
Position INTERACTION WITH LRPPRC, AND TISSUE SPECIFICITY.
Medline 21686162
DOI 10.1006/geno.2001.6679;
PubMed
11827465 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[8] Liu,L., Amy,V., Liu,G., McKeehan,W.L.,
Novel complex integrating mitochondria and the microtubular cytoskeleton with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico homology analysis, interaction cloning in yeast, and colocalization in cultured cells.
(2002) In Vitro Cell. Dev. Biol. Anim. 38:582-594
Position INTERACTION WITH LRPPRC, AND SUBCELLULAR LOCATION.
PubMed
12762840 Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[9] Dallol,A., Agathanggelou,A., Fenton,S.L., Ahmed-Choudhury,J., Hesson,L., Vos,M.D., Clark,G.J., Downward,J., Maher,E.R., Latif,F.,
RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics.
(2004) Cancer Res. 64:4112-4116
Position INTERACTION WITH RASSF1.
DOI 10.1158/0008-5472.CAN-04-0267;
PubMed
15205320 Free after 12 monthsClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from aacrjournals.org Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[10] Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E., Villen,J., Li,J., Cohn,M.A., Cantley,L.C., Gygi,S.P.,
Large-scale characterization of HeLa cell nuclear phosphoproteins.
(2004) Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135
Position PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-638; SER-640; SER-657 AND SER-759, AND MASS SPECTROMETRY.
Comments TISSUE=Epithelium;
DOI 10.1073/pnas.0404720101;
PubMed
15302935 Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Subscription requiredClick to get it from www.pnas.org CiteXplore
[11] Liu,L., Vo,A., Liu,G., McKeehan,W.L.,
Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein.
(2005) Biochem. Biophys. Res. Commun. 332:670-676
Position INTERACTION WITH LRPPRC, AND DNA-BINDING.
DOI 10.1016/j.bbrc.2005.05.006;
PubMed
15907802 Subscription requiredClick to get it from ScienceDirect CiteXplore
[12] Liu,L., Vo,A., McKeehan,W.L.,
Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5.
(2005) Cancer Res. 65:1830-1838
Position INTERACTION WITH RASSF1, AND SUBCELLULAR LOCATION.
DOI 10.1158/0008-5472.CAN-04-3896;
PubMed
15753381 Free after 12 monthsClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from aacrjournals.org CiteXplore
[13] Liu,L., Vo,A., Liu,G., McKeehan,W.L.,
Distinct structural domains within C19ORF5 support association with stabilized microtubules and mitochondrial aggregation and genome destruction.
(2005) Cancer Res. 65:4191-4201
Position FUNCTION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
DOI 10.1158/0008-5472.CAN-04-3865;
PubMed
15899810 Free after 12 monthsClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Subscription requiredClick to get it from aacrjournals.org Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[14] Olsen,J.V., Blagoev,B., Gnad,F., Macek,B., Kumar,C., Mortensen,P., Mann,M.,
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
(2006) Cell 127:635-648
Position PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-729 AND SER-731, AND MASS SPECTROMETRY.
Comments TISSUE=Epithelium;
DOI 10.1016/j.cell.2006.09.026;
PubMed
17081983 Subscription requiredClick to get it from www.cell.com Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[15] Eriksson,M., Samuelsson,H., Samuelsson,E.-B., Liu,L., McKeehan,W.L., Benedikz,E., Sundstroem,E.,
The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain.
(2007) Biochem. Biophys. Res. Commun. 361:127-132
Position INTERACTION WITH ESR1, AND TISSUE SPECIFICITY.
DOI 10.1016/j.bbrc.2007.06.179;
PubMed
17658481 Subscription requiredClick to get it from PaperBase@EBI Subscription requiredClick to get it from ScienceDirect CiteXplore
[16] Dallol,A., Cooper,W.N., Al-Mulla,F., Agathanggelou,A., Maher,E.R., Latif,F.,
Depletion of the Ras association domain family 1, isoform A- associated novel microtubule-associated protein, C19ORF5/MAP1S, causes mitotic abnormalities.
(2007) Cancer Res. 67:492-500
Position FUNCTION, AND SUBCELLULAR LOCATION.
DOI 10.1158/0008-5472.CAN-06-3604;
PubMed
17234756 Free after 12 monthsClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from cancerres.aacrjournals.org FreeClick to get it from cancerres.aacrjournals.org Free after 12 monthsClick to get it from aacrjournals.org Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[17] Molina,H., Horn,D.M., Tang,N., Mathivanan,S., Pandey,A.,
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.
(2007) Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204
Position PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, AND MASS SPECTROMETRY.
DOI 10.1073/pnas.0611217104;
PubMed
17287340 Subscription requiredClick to get it from PaperBase@EBI FreeClick to get it from PubMedCentral FreeClick to get it from PubMedCentral FreeClick to get it from UK_PubMedCentral FreeClick to get it from UK_PubMedCentral Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Subscription requiredClick to get it from www.pnas.org CiteXplore
[18] Cantin,G.T., Yi,W., Lu,B., Park,S.K., Xu,T., Lee,J.-D., Yates,J.R. III,
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
(2008) J. Proteome Res. 7:1346-1351
Position PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731 AND SER-759, AND MASS SPECTROMETRY.
DOI 10.1021/pr0705441;
PubMed
18220336 Subscription requiredClick to get it from pubs.acs.com Subscription requiredClick to get it from PaperBase@EBI CiteXplore
[19] Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E., Elledge,S.J., Gygi,S.P.,
A quantitative atlas of mitotic phosphorylation.
(2008) Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767
Position PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-475; THR-638; SER-640; SER-657; SER-729; SER-731; SER-741 AND SER-759, AND MASS SPECTROMETRY.
DOI 10.1073/pnas.0805139105;
PubMed
18669648 Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Free after 6 monthsClick to get it from www.pnas.org Subscription requiredClick to get it from www.pnas.org CiteXplore
Comments
FUNCTION 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).
SUBUNIT 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 (By similarity). Interacts with ESR1, LRPPRC, RASSF1 isoform A and isoform C, microtubules and VCY2.
SUBCELLULAR LOCATION Nucleus. Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Note=Detected in filopodia-like protrusions and synapses (By similarity). 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 isoform A. 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.
TISSUE SPECIFICITY Expressed in neurons (at protein level). Expressed in spermatocytes, spermatids and spermatozoa. Expressed in the cerebral cortex. Highly expressed in testis. Moderately expressed in the brain, colon, heart, kidney, liver, lung, placenta, small intestine, spleen and stomach. Weakly expressed in muscle.
DOMAIN The N-terminus of the heavy chain associates with the C- terminus of the light chain to form the heterodimer complex (By similarity). Its C-terminal part of the heavy chain interacts with ESR1.
MISCELLANEOUS Depletion of MAP1S by RNAi causes mitotic abnormalities that consist of failure to form a stable metaphase plate, premature sister chromatid separation, lagging chromosomes, and multipolar spindles.
SIMILARITY Belongs to the MAP1 family.
SEQUENCE CAUTION Sequence=AAH07253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus; Sequence=BAB55242.1; Type=Frameshift; Positions=851;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms Distributed under the Creative Commons Attribution-NoDerivs License
Database cross-references
EMBL
AJ440784; CAD29574.1; -; mRNA.
DQ387861; ABD47682.1; -; mRNA.
AL834233; CAD38911.1; ALT_INIT; mRNA.
AK001531; BAA91743.1; ALT_INIT; mRNA.
AK023118; BAB14415.1; ALT_INIT; mRNA.
AK027623; BAB55242.1; ALT_FRAME; mRNA.
BC006358; AAH06358.2; -; mRNA.
BC007253; AAH07253.1; ALT_INIT; mRNA.
BC008806; AAH08806.2; -; mRNA.
BC067115; AAH67115.1; ALT_INIT; mRNA.
BC080547; AAH80547.1; -; mRNA.
BC113952; AAI13953.1; -; mRNA.
AB062430; BAB93493.1; ALT_INIT; mRNA.
RefSeq
NP_060644.4; -.
UniGene
Hs.66048; -.
PhosphoSite
Q66K74; -.
Ensembl
ENSG00000130479; Homo sapiens.
GeneID
55201; -.
KEGG
hsa:55201; -.
HGNC
HGNC:15715; MAP1S.
MIM
607573; gene.
HOVERGEN
Q66K74; -.
NextBio
59090; -.
ArrayExpress
Q66K74; -.
GO
GO:0043025; C:cell soma; ISS:HGNC.
GO:0005829; C:cytosol; IDA:HGNC.
GO:0030425; C:dendrite; ISS:HGNC.
GO:0005874; C:microtubule; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:HGNC.
GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
GO:0045202; C:synapse; IDA:UniProtKB.
GO:0051015; F:actin filament binding; IDA:HGNC.
GO:0048487; F:beta-tubulin binding; IDA:HGNC.
GO:0003677; F:DNA binding; IDA:HGNC.
GO:0008017; F:microtubule binding; IDA:HGNC.
GO:0006915; P:apoptosis; IDA:HGNC.
GO:0007420; P:brain development; ISS:HGNC.
GO:0001578; P:microtubule bundle formation; IMP:HGNC.
GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
GO:0048812; P:neurite morphogenesis; IEP:HGNC.
Protein Existence
1: Evidence at protein level;
Keywords
Apoptosis; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Nucleus; Phosphoprotein; Polymorphism;
CHAIN: 1 1059, Microtubule-associated protein 1S. /FTId=PRO_0000311379. CHAIN: 1 ?, MAP1S heavy chain. /FTId=PRO_0000311380. CHAIN: ? 1059, MAP1S light chain. /FTId=PRO_0000311381. REGION: 1 797, Necessary for the microtubule-organizing center localization. REGION: 666 1059, Necessary for interaction with RASSF1 isoform A and isoform C. REGION: 714 966, Necessary for association with microtubules. REGION: 960 1059, Necessary for association with actin (By similarity). REGION: 967 991, Necessary for the mitochondrial aggregation and genome destruction. COMPBIAS: 560 850, Pro-rich. MOD_RES: 472 472, Phosphoserine. MOD_RES: 475 475, Phosphoserine. MOD_RES: 638 638, Phosphothreonine. MOD_RES: 640 640, Phosphoserine. MOD_RES: 657 657, Phosphoserine. MOD_RES: 729 729, Phosphoserine. MOD_RES: 731 731, Phosphoserine. MOD_RES: 741 741, Phosphoserine. MOD_RES: 759 759, Phosphoserine. MOD_RES: 900 900, Phosphoserine. VARIANT: 411 411, S -> C (in dbSNP:rs17710707). /FTId=VAR_037236. VARIANT: 538 538, P -> Q (in dbSNP:rs7252905). /FTId=VAR_037237. CONFLICT: 120 120, P -> L (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 178 178, L -> P (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 440 440, C -> Y (in Ref. 3; CAD38911). CONFLICT: 521 521, T -> A (in Ref. 6; BAB93493). CONFLICT: 526 526, K -> R (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 967 967, F -> L (in Ref. 4; BAB14415). CONFLICT: 1043 1043, S -> G (in Ref. 4; BAA91743). CHAIN: 1 1059, Microtubule-associated protein 1S. /FTId=PRO_0000311379. CHAIN: 1 ?, MAP1S heavy chain. /FTId=PRO_0000311380. CHAIN: ? 1059, MAP1S light chain. /FTId=PRO_0000311381. REGION: 1 797, Necessary for the microtubule-organizing center localization. REGION: 666 1059, Necessary for interaction with RASSF1 isoform A and isoform C. REGION: 714 966, Necessary for association with microtubules. REGION: 960 1059, Necessary for association with actin (By similarity). REGION: 967 991, Necessary for the mitochondrial aggregation and genome destruction. COMPBIAS: 560 850, Pro-rich. MOD_RES: 472 472, Phosphoserine. MOD_RES: 475 475, Phosphoserine. MOD_RES: 638 638, Phosphothreonine. MOD_RES: 640 640, Phosphoserine. MOD_RES: 657 657, Phosphoserine. MOD_RES: 729 729, Phosphoserine. MOD_RES: 731 731, Phosphoserine. MOD_RES: 741 741, Phosphoserine. MOD_RES: 759 759, Phosphoserine. MOD_RES: 900 900, Phosphoserine. VARIANT: 411 411, S -> C (in dbSNP:rs17710707). /FTId=VAR_037236. VARIANT: 538 538, P -> Q (in dbSNP:rs7252905). /FTId=VAR_037237. CONFLICT: 120 120, P -> L (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 178 178, L -> P (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 440 440, C -> Y (in Ref. 3; CAD38911). CONFLICT: 521 521, T -> A (in Ref. 6; BAB93493). CONFLICT: 526 526, K -> R (in Ref. 1; CAD29574 and 4; BAB55242). CONFLICT: 967 967, F -> L (in Ref. 4; BAB14415). CONFLICT: 1043 1043, S -> G (in Ref. 4; BAA91743).
Key Begin End Length Description RESID
  CHAIN 1 1059 1059 Microtubule-associated protein 1S. /FTId=PRO_0000311379.
  CHAIN 1 ? 0 MAP1S heavy chain. /FTId=PRO_0000311380.
  CHAIN ? 1059 0 MAP1S light chain. /FTId=PRO_0000311381.
  REGION 1 797 797 Necessary for the microtubule-organizing center localization.
  REGION 666 1059 394 Necessary for interaction with RASSF1 isoform A and isoform C.
  REGION 714 966 253 Necessary for association with microtubules.
  REGION 960 1059 100 Necessary for association with actin (By similarity).
  REGION 967 991 25 Necessary for the mitochondrial aggregation and genome destruction.
  COMPBIAS 560 850 291 Pro-rich.
  MOD_RES 472 472 1 Phosphoserine. RESID:AA0037
  MOD_RES 475 475 1 Phosphoserine. RESID:AA0037
  MOD_RES 638 638 1 Phosphothreonine. RESID:AA0038
  MOD_RES 640 640 1 Phosphoserine. RESID:AA0037
  MOD_RES 657 657 1 Phosphoserine. RESID:AA0037
  MOD_RES 729 729 1 Phosphoserine. RESID:AA0037
  MOD_RES 731 731 1 Phosphoserine. RESID:AA0037
  MOD_RES 741 741 1 Phosphoserine. RESID:AA0037
  MOD_RES 759 759 1 Phosphoserine. RESID:AA0037
  MOD_RES 900 900 1 Phosphoserine. RESID:AA0037
  VARIANT 411 411 1 S -> C (in dbSNP:rs17710707). /FTId=VAR_037236.
  VARIANT 538 538 1 P -> Q (in dbSNP:rs7252905). /FTId=VAR_037237.
  CONFLICT 120 120 1 P -> L (in Ref. 1; CAD29574 and 4; BAB55242).
  CONFLICT 178 178 1 L -> P (in Ref. 1; CAD29574 and 4; BAB55242).
  CONFLICT 440 440 1 C -> Y (in Ref. 3; CAD38911).
  CONFLICT 521 521 1 T -> A (in Ref. 6; BAB93493).
  CONFLICT 526 526 1 K -> R (in Ref. 1; CAD29574 and 4; BAB55242).
  CONFLICT 967 967 1 F -> L (in Ref. 4; BAB14415).
  CONFLICT 1043 1043 1 S -> G (in Ref. 4; BAA91743).


IPI crosslinks:
SP Q66K74 IPI00296485 A8K940;B4DH53; ENSP00000325313; VALIDATED:NP_060644; HIT000265816; ABD47682; 15715,MAP1S; 55201,MAP1S; UPI00002036F9 Hs.66048; CCDS32954.1; GI:50428935; OTTHUMP00000078237;
IPI gene crosslinks:
19 17691291 17706322 1 19p13.12 ENSG00000130479 15715,MAP1S 55201,MAP1S IPI00296485; Q66K74; A8K940;B4DH53; ENSP00000325313; VALIDATED:NP_060644; HIT000265816; Hs.66048; CCDS32954.1; GI:50428935; OTTHUMG00000071832; OTTHUMP00000078237;