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Q8BRT1

- CLAP2_MOUSE

UniProt

Q8BRT1 - CLAP2_MOUSE

Protein

CLIP-associating protein 2

Gene

Clasp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex By similarity.By similarity

    GO - Molecular functioni

    1. microtubule binding Source: MGI
    2. microtubule plus-end binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: MGI
    2. establishment or maintenance of cell polarity Source: MGI
    3. meiotic nuclear division Source: UniProtKB-KW
    4. microtubule anchoring Source: UniProtKB
    5. microtubule nucleation Source: UniProtKB
    6. microtubule organizing center organization Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB-KW
    8. negative regulation of microtubule depolymerization Source: MGI
    9. regulation of microtubule-based process Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CLIP-associating protein 2
    Alternative name(s):
    Cytoplasmic linker-associated protein 2
    Gene namesi
    Name:Clasp2
    Synonyms:Kiaa0627
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1923749. Clasp2.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Golgi apparatus. Golgi apparatustrans-Golgi network By similarity. Cell membrane By similarity. Cell projectionruffle membrane By similarity
    Note: Localizes to microtubule plus ends. Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase. In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella. Localizes to the cell cortex and this requires ERC1 and PHLDB2 By similarity. Also localizes to meiotic spindle poles. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane By similarity.By similarity

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. Golgi apparatus Source: MGI
    3. microtubule Source: UniProtKB
    4. microtubule organizing center Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB
    6. ruffle membrane Source: UniProtKB
    7. spindle pole Source: UniProtKB-SubCell
    8. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Membrane, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61C → S: Impairs Golgi localization; when associated with S-10. 1 Publication
    Mutagenesisi10 – 101C → S: Impairs Golgi localization; when associated with S-6. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12861286CLIP-associating protein 2PRO_0000089850Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141PhosphoserineBy similarity
    Modified residuei376 – 3761PhosphoserineBy similarity
    Modified residuei461 – 4611PhosphoserineBy similarity
    Modified residuei531 – 5311PhosphoserineBy similarity
    Modified residuei535 – 5351PhosphoserineBy similarity
    Modified residuei581 – 5811PhosphoserineBy similarity
    Modified residuei1021 – 10211PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. Isoform 2 is phosphorylated on Ser-241.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BRT1.
    PaxDbiQ8BRT1.
    PRIDEiQ8BRT1.

    PTM databases

    PhosphoSiteiQ8BRT1.

    Expressioni

    Tissue specificityi

    Highly expressed in brain and at low levels in heart, kidney and lung.1 Publication

    Developmental stagei

    Expressed in oocytes and early embryos.1 Publication

    Gene expression databases

    CleanExiMM_CLASP2.
    GenevestigatoriQ8BRT1.

    Interactioni

    Subunit structurei

    Interacts with ERC1, MAPRE3, microtubules and PHLDB2. The interaction with ERC1 may be mediated by PHLDB2. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with GCC2; recruits CLASP2 to the Golgi membranes By similarity. Interacts with CLIP2 and RSN. Interacts with MACF1.By similarity2 Publications

    Protein-protein interaction databases

    IntActiQ8BRT1. 5 interactions.
    MINTiMINT-4112101.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BRT1.
    SMRiQ8BRT1. Positions 70-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati179 – 21436HEAT 1Add
    BLAST
    Repeati215 – 25137HEAT 2Add
    BLAST
    Repeati764 – 80138HEAT 3Add
    BLAST
    Repeati1090 – 112738HEAT 4Add
    BLAST
    Repeati1208 – 124538HEAT 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4040Golgi localizationAdd
    BLAST
    Regioni450 – 565116Interaction with microtubules, MAPRE1 and MAPRE3By similarityAdd
    BLAST
    Regioni864 – 1286423Interaction with RSN and localization to the Golgi and kinetochoresBy similarityAdd
    BLAST
    Regioni1009 – 1286278Required for cortical localizationBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1047 – 107630Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi500 – 5034Microtubule tip localization signal
    Motifi523 – 5264Microtubule tip localization signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi459 – 572114Ser-richAdd
    BLAST

    Domaini

    The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.By similarity

    Sequence similaritiesi

    Belongs to the CLASP family.Curated
    Contains 5 HEAT repeats.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG81443.
    HOGENOMiHOG000185856.
    HOVERGENiHBG079692.
    KOiK16578.
    PhylomeDBiQ8BRT1.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR024395. CLASP_N_dom.
    [Graphical view]
    PfamiPF12348. CLASP_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 4 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BRT1-1) [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

    MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK     50
    PGSAGGPKVG GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS SRELEETLNK 100
    IREILSDDKH DWDQRANALK KIRSLLVAGA AQYDCFFQHL RLLDGALKLS 150
    AKDLRSQVVR EACITVAHLS TVLGNKFDHG AEAIVPTLFN LVPNSAKVMA 200
    TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE FLDLLLQEWQ 250
    THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN 300
    SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP 350
    STVAGRVSVG GSKANPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR 400
    LGAGALNPGS YASLEDTSDK MDGTASDDGR VRAKLSTPLV AVGNAKTDSR 450
    GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS TVSSGAQRVL VNSASAQKRS 500
    KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR ESSRDTSPVR 550
    SFQPLGPGYG ISQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK 600
    KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE 650
    VLNRCASSNW SERKEGLLGL QNLLKNQRTL SRIELKRLCE IFTRMFADPH 700
    GKVFSMFLET LVDFIQVHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ 750
    KALDITRESF PNDLQFNILM RFTVDQTQTP SLKVKVAILK YIETLAKQMD 800
    PRDFTNSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL FELNTPEFTM 850
    LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP 900
    LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED 950
    MSEPVRRDPK KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM 1000
    PLHSSPRSRD YNPYNYSDSI SPFNKSALKE AMFDDDADQF PDDLSLDHSD 1050
    LVAELLKELS NHNERIEERK IALYELMKLT QEESFSVWDE HFKTILLLLL 1100
    ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT LEAHKDPHKE 1150
    VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER 1200
    VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH 1250
    LSQLTGSKMK LLNLYIKRAQ TGSAGADPTA DVSGQS 1286
    Length:1,286
    Mass (Da):140,739
    Last modified:March 1, 2003 - v1
    Checksum:i5B208D8F4E90CB93
    GO
    Isoform 2 (identifier: Q8BRT1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: MRRLICKRICDY → MEPRGAEYFC...GGMILSVCKD
         142-1054: Missing.

    Show »
    Length:600
    Mass (Da):66,370
    Checksum:iF7ADD06A38B893D3
    GO
    Isoform 3 (identifier: Q8BRT1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: MRRLICKRICDY → MAMGDD
         119-173: LKKIRSLLVA...ITVAHLSTVL → CMSCSLVASE...SPVSSAFVQH
         174-1286: Missing.

    Show »
    Length:167
    Mass (Da):18,021
    Checksum:i5512515D37A0CF08
    GO

    Sequence cautioni

    The sequence BAC41436.2 differs from that shown. Reason: Frameshift at position 737.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti657 – 6571S → T in BAC41436. (PubMed:12465718)Curated
    Sequence conflicti683 – 6831I → V in BAC41436. (PubMed:12465718)Curated
    Sequence conflicti699 – 6991P → L in BAC41436. (PubMed:12465718)Curated
    Sequence conflicti702 – 7021K → KR in BAC41436. (PubMed:12465718)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1212MRRLI…RICDY → MEPRGAEYFCAQVLQKDVSG RLQAGEELLLCLGTPGAIPD LEDDPSRLAKTVDALTRWVG SSNYRVSLLGLEILSAFVDR LSTRFKSYVTMVTTALIDRM GDVKDKVREEAQNLTLKLMD EVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGT QPLVISKLVPHLCVLFGDSN SQVRNAALSAVVEIYRHVGE KLRIDLCKRDIPPARLEMVL AKFDEVQNSGGMILSVCKD in isoform 2. 1 PublicationVSP_015808Add
    BLAST
    Alternative sequencei1 – 1212MRRLI…RICDY → MAMGDD in isoform 3. 2 PublicationsVSP_015809Add
    BLAST
    Alternative sequencei119 – 17355LKKIR…LSTVL → CMSCSLVASEVERALAWPLW SHLATYQHHCHCTLSHEDLP EKRLTSPVSSAFVQH in isoform 3. 2 PublicationsVSP_015810Add
    BLAST
    Alternative sequencei142 – 1054913Missing in isoform 2. 1 PublicationVSP_015811Add
    BLAST
    Alternative sequencei174 – 12861113Missing in isoform 3. 2 PublicationsVSP_015812Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ276961 mRNA. Translation: CAC35161.1.
    AK043551 mRNA. Translation: BAC31579.1.
    AK005146 mRNA. Translation: BAB23842.1.
    BC030468 mRNA. Translation: AAH30468.1.
    AB093252 Transcribed RNA. Translation: BAC41436.2. Frameshift.
    CCDSiCCDS52948.1. [Q8BRT1-1]
    RefSeqiNP_001273528.1. NM_001286599.1.
    NP_001273529.1. NM_001286600.1.
    NP_001273530.1. NM_001286601.1.
    NP_001273531.1. NM_001286602.1.
    NP_001273532.1. NM_001286603.1. [Q8BRT1-6]
    UniGeneiMm.222272.

    Genome annotation databases

    GeneIDi76499.
    KEGGimmu:76499.
    UCSCiuc009rwt.1. mouse. [Q8BRT1-6]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ276961 mRNA. Translation: CAC35161.1 .
    AK043551 mRNA. Translation: BAC31579.1 .
    AK005146 mRNA. Translation: BAB23842.1 .
    BC030468 mRNA. Translation: AAH30468.1 .
    AB093252 Transcribed RNA. Translation: BAC41436.2 . Frameshift.
    CCDSi CCDS52948.1. [Q8BRT1-1 ]
    RefSeqi NP_001273528.1. NM_001286599.1.
    NP_001273529.1. NM_001286600.1.
    NP_001273530.1. NM_001286601.1.
    NP_001273531.1. NM_001286602.1.
    NP_001273532.1. NM_001286603.1. [Q8BRT1-6 ]
    UniGenei Mm.222272.

    3D structure databases

    ProteinModelPortali Q8BRT1.
    SMRi Q8BRT1. Positions 70-312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BRT1. 5 interactions.
    MINTi MINT-4112101.

    PTM databases

    PhosphoSitei Q8BRT1.

    Proteomic databases

    MaxQBi Q8BRT1.
    PaxDbi Q8BRT1.
    PRIDEi Q8BRT1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 76499.
    KEGGi mmu:76499.
    UCSCi uc009rwt.1. mouse. [Q8BRT1-6 ]

    Organism-specific databases

    CTDi 23122.
    MGIi MGI:1923749. Clasp2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG81443.
    HOGENOMi HOG000185856.
    HOVERGENi HBG079692.
    KOi K16578.
    PhylomeDBi Q8BRT1.

    Miscellaneous databases

    PROi Q8BRT1.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CLASP2.
    Genevestigatori Q8BRT1.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR024395. CLASP_N_dom.
    [Graphical view ]
    Pfami PF12348. CLASP_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts."
      Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F., Galjart N.
      Cell 104:923-935(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH CLIP2 AND RSN, MUTAGENESIS OF CYS-6 AND CYS-10.
    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] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Brain cortex and Cerebellum.
    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] (ISOFORM 3).
      Tissue: Eye.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
      DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1286 (ISOFORM 1).
    5. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. "PAR-1 and the microtubule-associated proteins CLASP2 and dynactin-p50 have specific localisation on mouse meiotic and first mitotic spindles."
      Moore C.A., Zernicka-Goetz M.
      Reproduction 130:311-320(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    8. "Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by regulating spindle and kinetochore function."
      Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L., Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T., Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.
      Mol. Biol. Cell 17:4526-4542(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity."
      Wu X., Kodama A., Fuchs E.
      Cell 135:137-148(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MACF1.

    Entry informationi

    Entry nameiCLAP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BRT1
    Secondary accession number(s): Q8CHE3, Q99JI3, Q9DB80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 110 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3