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Q66K74

- MAP1S_HUMAN

UniProt

Q66K74 - MAP1S_HUMAN

Protein

Microtubule-associated protein 1S

Gene

MAP1S

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    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

    1. actin filament binding Source: HGNC
    2. beta-tubulin binding Source: HGNC
    3. DNA binding Source: HGNC
    4. hydrolase activity Source: InterPro
    5. microtubule binding Source: HGNC
    6. protein binding Source: UniProtKB
    7. tubulin binding Source: HGNC

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: BHF-UCL
    2. brain development Source: HGNC
    3. execution phase of apoptosis Source: BHF-UCL
    4. microtubule bundle formation Source: HGNC
    5. mitochondrion transport along microtubule Source: HGNC
    6. nervous system development Source: HGNC
    7. neuron projection morphogenesis Source: HGNC

    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
    Variable charge Y chromosome 2-interacting protein 1
    Short name:
    VCY2-interacting protein 1
    Short name:
    VCY2IP-1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MAP1S
    Synonyms:BPY2IP1, C19orf5, MAP8, VCY2IP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:15715. MAP1S.

    Subcellular locationi

    Nucleus. Cytoplasmcytosol. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonspindle
    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.By similarity

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. cell projection Source: UniProtKB
    3. cytoplasm Source: HPA
    4. cytosol Source: HGNC
    5. dendrite Source: HGNC
    6. microtubule Source: UniProtKB
    7. neuronal cell body Source: HGNC
    8. nucleolus Source: HPA
    9. nucleus Source: HGNC
    10. perinuclear region of cytoplasm Source: HGNC
    11. spindle Source: UniProtKB-SubCell
    12. synapse Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38031.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10591059Microtubule-associated protein 1SPRO_0000311379Add
    BLAST
    Chaini1 – 829829MAP1S heavy chainPRO_0000311380Add
    BLAST
    Chaini830 – 1059230MAP1S light chainPRO_0000311381Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei472 – 4721Phosphoserine3 Publications
    Modified residuei640 – 6401Phosphoserine1 Publication
    Modified residuei657 – 6571Phosphoserine2 Publications
    Modified residuei759 – 7591Phosphoserine5 Publications
    Modified residuei809 – 8091Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ66K74.
    PaxDbiQ66K74.
    PRIDEiQ66K74.

    PTM databases

    PhosphoSiteiQ66K74.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiQ66K74.
    BgeeiQ66K74.
    GenevestigatoriQ66K74.

    Organism-specific databases

    HPAiHPA050934.
    HPA054637.

    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 (via C-terminus) with GAN (via Kelch domains) By similarity. Interacts with ESR1, LRPPRC, RASSF1 isoform A and isoform C, microtubules and VCY2. Interacts with WDR47 (via N-terminus of light chain).By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BPY2BO145993EBI-2133734,EBI-2133713
    SOCS3O145436EBI-2133734,EBI-714146

    Protein-protein interaction databases

    BioGridi120498. 16 interactions.
    IntActiQ66K74. 17 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66K74.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 797797Necessary for the microtubule-organizing center localizationAdd
    BLAST
    Regioni666 – 1059394Necessary for interaction with RASSF1 isoform A and isoform CAdd
    BLAST
    Regioni714 – 966253Necessary for association with microtubulesAdd
    BLAST
    Regioni960 – 1059100Necessary for association with actinBy similarityAdd
    BLAST
    Regioni967 – 99125Necessary for the mitochondrial aggregation and genome destructionAdd
    BLAST

    Compositional bias

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

    Domaini

    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.By similarity

    Sequence similaritiesi

    Belongs to the MAP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG108117.
    InParanoidiQ66K74.
    KOiK10429.
    OMAiPCEFEHR.
    OrthoDBiEOG773XKP.
    PhylomeDBiQ66K74.
    TreeFamiTF350229.

    Family and domain databases

    Gene3Di3.60.15.10. 2 hits.
    InterProiIPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    [Graphical view]
    PANTHERiPTHR13843. PTHR13843. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q66K74-1) [UniParc]FASTAAdd to Basket

    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

    MAAVAGSGAA AAPSSLLLVV GSEFGSPGLL TYVLEELERG IRSWDVDPGV     50
    CNLDEQLKVF VSRHSATFSS IVKGQRSLHH RGDNLETLVL LNPSDKSLYD 100
    ELRNLLLDPA SHKLLVLAGP CLEETGELLL QTGGFSPHHF LQVLKDREIR 150
    DILATTPPPV QPPILTITCP TFGDWAQLAP AVPGLQGALR LQLRLNPPAQ 200
    LPNSEGLCEF LEYVAESLEP PSPFELLEPP TSGGFLRLGR PCCYIFPGGL 250
    GDAAFFAVNG FTVLVNGGSN PKSSFWKLVR HLDRVDAVLV THPGADSLPG 300
    LNSLLRRKLA ERSEVAAGGG SWDDRLRRLI SPNLGVVFFN ACEAASRLAR 350
    GEDEAELALS LLAQLGITPL PLSRGPVPAK PTVLFEKMGV GRLDMYVLHP 400
    PSAGAERTLA SVCALLVWHP AGPGEKVVRV LFPGCTPPAC LLDGLVRLQH 450
    LRFLREPVVT PQDLEGPGRA ESKESVGSRD SSKREGLLAT HPRPGQERPG 500
    VARKEPARAE APRKTEKEAK TPRELKKDPK PSVSRTQPRE VRRAASSVPN 550
    LKKTNAQAAP KPRKAPSTSH SGFPPVANGP RSPPSLRCGE ASPPSAACGS 600
    PASQLVATPS LELGPIPAGE EKALELPLAA SSIPRPRTPS PESHRSPAEG 650
    SERLSLSPLR GGEAGPDASP TVTTPTVTTP SLPAEVGSPH STEVDESLSV 700
    SFEQVLPPSA PTSEAGLSLP LRGPRARRSA SPHDVDLCLV SPCEFEHRKA 750
    VPMAPAPASP GSSNDSSARS QERAGGLGAE ETPPTSVSES LPTLSDSDPV 800
    PLAPGAADSD EDTEGFGVPR HDPLPDPLKV PPPLPDPSSI CMVDPEMLPP 850
    KTARQTENVS RTRKPLARPN SRAAAPKATP VAAAKTKGLA GGDRASRPLS 900
    ARSEPSEKGG RAPLSRKSST PKTATRGPSG SASSRPGVSA TPPKSPVYLD 950
    LAYLPSGSSA HLVDEEFFQR VRALCYVISG QDQRKEEGMR AVLDALLASK 1000
    QHWDRDLQVT LIPTFDSVAM HTWYAETHAR HQALGITVLG SNSMVSMQDD 1050
    AFPACKVEF 1059
    Length:1,059
    Mass (Da):112,211
    Last modified:November 13, 2007 - v2
    Checksum:i30AB33FFE26DDF91
    GO
    Isoform 2 (identifier: Q66K74-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: MAAVAGSGAAAAPSSLLLVVGSEFGSPGLLTYVLEELER → MAGMIDRFSPANT

    Note: No experimental confirmation available.

    Show »
    Length:1,033
    Mass (Da):109,788
    Checksum:i0CCD0392292B2B08
    GO

    Sequence cautioni

    The sequence AAH07253.1 differs from that shown. Reason: Contaminating sequence. At the N-terminus.
    The sequence BAB55242.1 differs from that shown. Reason: Frameshift at position 851.
    The sequence AAH07253.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH67115.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91743.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB14415.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB93493.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAD38911.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201P → L in CAD29574. (PubMed:14627543)Curated
    Sequence conflicti120 – 1201P → L in BAB55242. (PubMed:14702039)Curated
    Sequence conflicti178 – 1781L → P in CAD29574. (PubMed:14627543)Curated
    Sequence conflicti178 – 1781L → P in BAB55242. (PubMed:14702039)Curated
    Sequence conflicti440 – 4401C → Y in CAD38911. (PubMed:17974005)Curated
    Sequence conflicti521 – 5211T → A in BAB93493. 1 PublicationCurated
    Sequence conflicti526 – 5261K → R in CAD29574. (PubMed:14627543)Curated
    Sequence conflicti526 – 5261K → R in BAB55242. (PubMed:14702039)Curated
    Sequence conflicti967 – 9671F → L in BAB14415. (PubMed:14702039)Curated
    Sequence conflicti1043 – 10431S → G in BAA91743. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti372 – 3721L → V.
    Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
    VAR_050023
    Natural varianti411 – 4111S → C.1 Publication
    Corresponds to variant rs17710707 [ dbSNP | Ensembl ].
    VAR_037236
    Natural varianti538 – 5381P → Q.
    Corresponds to variant rs7252905 [ dbSNP | Ensembl ].
    VAR_037237

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939MAAVA…EELER → MAGMIDRFSPANT in isoform 2. 1 PublicationVSP_056043Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ440784 mRNA. Translation: CAD29574.1.
    DQ387861 mRNA. Translation: ABD47682.1.
    AK027623 mRNA. Translation: BAB55242.1. Frameshift.
    AK001531 mRNA. Translation: BAA91743.1. Different initiation.
    AK023118 mRNA. Translation: BAB14415.1. Different initiation.
    AK294936 mRNA. Translation: BAG58014.1.
    AL834233 mRNA. Translation: CAD38911.1. Different initiation.
    AC008761 Genomic DNA. No translation available.
    BC006358 mRNA. Translation: AAH06358.2.
    BC007253 mRNA. Translation: AAH07253.1. Different initiation.
    BC008806 mRNA. Translation: AAH08806.2.
    BC067115 mRNA. Translation: AAH67115.1. Different initiation.
    BC080547 mRNA. Translation: AAH80547.1.
    BC113952 mRNA. Translation: AAI13953.1.
    AB062430 mRNA. Translation: BAB93493.1. Different initiation.
    CCDSiCCDS32954.1.
    RefSeqiNP_060644.4. NM_018174.4.
    UniGeneiHs.66048.

    Genome annotation databases

    EnsembliENST00000324096; ENSP00000325313; ENSG00000130479.
    ENST00000544059; ENSP00000439243; ENSG00000130479.
    GeneIDi55201.
    KEGGihsa:55201.
    UCSCiuc002nhe.1. human.

    Polymorphism databases

    DMDMi160410004.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ440784 mRNA. Translation: CAD29574.1 .
    DQ387861 mRNA. Translation: ABD47682.1 .
    AK027623 mRNA. Translation: BAB55242.1 . Frameshift.
    AK001531 mRNA. Translation: BAA91743.1 . Different initiation.
    AK023118 mRNA. Translation: BAB14415.1 . Different initiation.
    AK294936 mRNA. Translation: BAG58014.1 .
    AL834233 mRNA. Translation: CAD38911.1 . Different initiation.
    AC008761 Genomic DNA. No translation available.
    BC006358 mRNA. Translation: AAH06358.2 .
    BC007253 mRNA. Translation: AAH07253.1 . Different initiation.
    BC008806 mRNA. Translation: AAH08806.2 .
    BC067115 mRNA. Translation: AAH67115.1 . Different initiation.
    BC080547 mRNA. Translation: AAH80547.1 .
    BC113952 mRNA. Translation: AAI13953.1 .
    AB062430 mRNA. Translation: BAB93493.1 . Different initiation.
    CCDSi CCDS32954.1.
    RefSeqi NP_060644.4. NM_018174.4.
    UniGenei Hs.66048.

    3D structure databases

    ProteinModelPortali Q66K74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120498. 16 interactions.
    IntActi Q66K74. 17 interactions.

    PTM databases

    PhosphoSitei Q66K74.

    Polymorphism databases

    DMDMi 160410004.

    Proteomic databases

    MaxQBi Q66K74.
    PaxDbi Q66K74.
    PRIDEi Q66K74.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324096 ; ENSP00000325313 ; ENSG00000130479 .
    ENST00000544059 ; ENSP00000439243 ; ENSG00000130479 .
    GeneIDi 55201.
    KEGGi hsa:55201.
    UCSCi uc002nhe.1. human.

    Organism-specific databases

    CTDi 55201.
    GeneCardsi GC19P017832.
    H-InvDB HIX0014899.
    HGNCi HGNC:15715. MAP1S.
    HPAi HPA050934.
    HPA054637.
    MIMi 607573. gene.
    neXtProti NX_Q66K74.
    PharmGKBi PA38031.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG108117.
    InParanoidi Q66K74.
    KOi K10429.
    OMAi PCEFEHR.
    OrthoDBi EOG773XKP.
    PhylomeDBi Q66K74.
    TreeFami TF350229.

    Miscellaneous databases

    ChiTaRSi MAP1S. human.
    GeneWikii MAP1S.
    GenomeRNAii 55201.
    NextBioi 59090.
    PROi Q66K74.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q66K74.
    Bgeei Q66K74.
    Genevestigatori Q66K74.

    Family and domain databases

    Gene3Di 3.60.15.10. 2 hits.
    InterProi IPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    [Graphical view ]
    PANTHERi PTHR13843. PTHR13843. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a VCY2 interacting protein-1; VCY2IP-1, a MAP-like protein."
      Wong E.Y., Tse J.Y., Yao K.-M., Lui V.C., Tam P.-C., Yeung W.S.
      Biol. Reprod. 70:775-784(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VCY2, TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "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] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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., Yamazaki M., 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., Watanabe M., 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., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Amygdala.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1), VARIANT CYS-411.
      Tissue: Brain, Lung, Lymph and Muscle.
    7. "Identification of immuno-peptidmics that recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059 (ISOFORM 1/2).
    8. "Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
      Liu L., McKeehan W.L.
      Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRPPRC, TISSUE SPECIFICITY.
    9. "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."
      Liu L., Amy V., Liu G., McKeehan W.L.
      In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRPPRC, SUBCELLULAR LOCATION.
    10. "RASSF1A interacts with microtubule-associated proteins and modulates microtubule dynamics."
      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.
      Cancer Res. 64:4112-4116(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF1.
    11. "Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein."
      Liu L., Vo A., Liu G., McKeehan W.L.
      Biochem. Biophys. Res. Commun. 332:670-676(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRPPRC, DNA-BINDING.
    12. "Specificity of the methylation-suppressed A isoform of candidate tumor suppressor RASSF1 for microtubule hyperstabilization is determined by cell death inducer C19ORF5."
      Liu L., Vo A., McKeehan W.L.
      Cancer Res. 65:1830-1838(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASSF1, SUBCELLULAR LOCATION.
    13. "Distinct structural domains within C19ORF5 support association with stabilized microtubules and mitochondrial aggregation and genome destruction."
      Liu L., Vo A., Liu G., McKeehan W.L.
      Cancer Res. 65:4191-4201(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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, TISSUE SPECIFICITY.
    16. "Depletion of the Ras association domain family 1, isoform A-associated novel microtubule-associated protein, C19ORF5/MAP1S, causes mitotic abnormalities."
      Dallol A., Cooper W.N., Al-Mulla F., Agathanggelou A., Maher E.R., Latif F.
      Cancer Res. 67:492-500(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    17. "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site."
      Zou B., Yan H., Kawasaki F., Ordway R.W.
      Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-640; SER-657 AND SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-657; SER-759 AND SER-809, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: INTERACTION WITH WDR47.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAP1S_HUMAN
    AccessioniPrimary (citable) accession number: Q66K74
    Secondary accession number(s): B4DH53
    , Q27QB1, Q6NXF1, Q8N3L8, Q8N3W5, Q8NI88, Q96H94, Q96IT4, Q96SP8, Q9BRC6, Q9H928, Q9NVK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3