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O75122

- CLAP2_HUMAN

UniProt

O75122 - CLAP2_HUMAN

Protein

CLIP-associating protein 2

Gene

CLASP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (11 Oct 2005)
      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.7 Publications

    GO - Molecular functioni

    1. galactoside 2-alpha-L-fucosyltransferase activity Source: UniProtKB
    2. microtubule plus-end binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. establishment or maintenance of cell polarity Source: UniProtKB
    3. fucosylation Source: GOC
    4. microtubule anchoring Source: UniProtKB
    5. microtubule nucleation Source: UniProtKB
    6. microtubule organizing center organization Source: UniProtKB
    7. mitotic cell cycle Source: Reactome
    8. mitotic nuclear division Source: UniProtKB-KW
    9. negative regulation of microtubule depolymerization Source: UniProtKB
    10. regulation of microtubule-based process Source: UniProtKB
    11. regulation of microtubule polymerization or depolymerization Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CLIP-associating protein 2
    Alternative name(s):
    Cytoplasmic linker-associated protein 2
    Protein Orbit homolog 2
    Short name:
    hOrbit2
    Gene namesi
    Name:CLASP2
    Synonyms:KIAA0627
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:17078. CLASP2.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Golgi apparatus. Golgi apparatustrans-Golgi network. Cell membrane. Cell projectionruffle membrane
    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. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.

    GO - Cellular componenti

    1. cell cortex Source: MGI
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. cytoplasmic microtubule Source: UniProtKB
    5. cytosol Source: Reactome
    6. Golgi apparatus Source: UniProtKB
    7. kinetochore microtubule Source: UniProtKB
    8. membrane Source: UniProtKB
    9. microtubule Source: UniProtKB
    10. microtubule organizing center Source: UniProtKB-SubCell
    11. plasma membrane Source: UniProtKB
    12. ruffle membrane Source: UniProtKB
    13. 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
    Mutagenesisi496 – 4972IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 519-S-S-520. 1 Publication
    Mutagenesisi519 – 5202IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 496-S-S-497. 1 Publication

    Organism-specific databases

    PharmGKBiPA38435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12941294CLIP-associating protein 2PRO_0000089849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine2 Publications
    Modified residuei370 – 3701Phosphoserine4 Publications
    Modified residuei455 – 4551Phosphoserine2 Publications
    Modified residuei525 – 5251Phosphoserine2 Publications
    Modified residuei529 – 5291Phosphoserine2 Publications
    Modified residuei596 – 5961Phosphoserine4 Publications
    Modified residuei1029 – 10291Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75122.
    PaxDbiO75122.
    PRIDEiO75122.

    PTM databases

    PhosphoSiteiO75122.

    Expressioni

    Tissue specificityi

    Brain-specific.

    Gene expression databases

    ArrayExpressiO75122.
    BgeeiO75122.
    CleanExiHS_CLASP2.
    GenevestigatoriO75122.

    Interactioni

    Subunit structurei

    Interacts with CLIP2, ERC1, MAPRE3, microtubules, PHLDB2 and RSN. 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 Golgi membranes. Interacts with MACF1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Clip2O551563EBI-913524,EBI-349416From a different organism.

    Protein-protein interaction databases

    BioGridi116743. 21 interactions.
    DIPiDIP-36804N.
    IntActiO75122. 12 interactions.
    MINTiMINT-4526878.
    STRINGi9606.ENSP00000352581.

    Structurei

    3D structure databases

    ProteinModelPortaliO75122.
    SMRiO75122. Positions 64-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati173 – 20836HEAT 1Add
    BLAST
    Repeati209 – 24537HEAT 2Add
    BLAST
    Repeati772 – 80938HEAT 3Add
    BLAST
    Repeati1098 – 113538HEAT 4Add
    BLAST
    Repeati1216 – 125338HEAT 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni444 – 580137Interaction with microtubules, MAPRE1 and MAPRE3Add
    BLAST
    Regioni872 – 1294423Interaction with RSN and localization to the Golgi and kinetochoresAdd
    BLAST
    Regioni1017 – 1294278Required for cortical localizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1055 – 108430Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi494 – 4974Microtubule tip localization signal
    Motifi517 – 5204Microtubule tip localization signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi310 – 587278Ser-richAdd
    BLAST
    Compositional biasi1104 – 11085Poly-Leu

    Domaini

    The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.1 Publication

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG81443.
    HOGENOMiHOG000236347.
    HOVERGENiHBG079692.
    InParanoidiO75122.
    KOiK16578.
    PhylomeDBiO75122.

    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. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms exist.

    Isoform 1 (identifier: O75122-1) [UniParc]FASTAAdd to Basket

    Also known as: CLASP2 gamma

    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

    MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG     50
    PKVGGASKEG GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS 100
    DDKHDWDQRA NALKKIRSLL VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS 150
    QVVREACITV AHLSTVLGNK FDHGAEAIVP TLFNLVPNSA KVMATSGCAA 200
    IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL QEWQTHSLER 250
    HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY 300
    QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR 350
    VSAGSSKASS LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL 400
    NAGSYASLED TSDKLDGTAS EDGRVRAKLS APLAGMGNAK ADSRGRSRTK 450
    MVSQSQPGSR SGSPGRVLTT TALSTVSSGV QRVLVNSASA QKRSKIPRSQ 500
    GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT SPVRSFQPLA 550
    SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE 600
    AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR 650
    QTEDVAEVLN RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT 700
    RMFADPHGKR VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL 750
    GSVQAKVQKA LDVTRESFPN DLQFNILMRF TVDQTQTPSL KVKVAILKYI 800
    ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA AQSVLISLFE 850
    LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR 900
    SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN 950
    FSFRSQEDMN EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN 1000
    KASLLHSMPT HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD 1050
    DLSLDHSDLV AELLKELSNH NERVEERKIA LYELMKLTQE ESFSVWDEHF 1100
    KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY AELTVMKTLE 1150
    AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK 1200
    MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV 1250
    IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS 1294
    Length:1,294
    Mass (Da):141,133
    Last modified:October 11, 2005 - v2
    Checksum:iE4FF7E06049E65E5
    GO
    Isoform 2 (identifier: O75122-2) [UniParc]FASTAAdd to Basket

    Also known as: CLASP2 beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MAMGDD → MRRLICKRICDY
         410-425: DTSDKLDGTASEDGRV → CEAFWRSGRTAKLYSV
         426-1294: Missing.

    Show »
    Length:431
    Mass (Da):46,585
    Checksum:i5C5C731ECD32FFEB
    GO

    Sequence cautioni

    The sequence BAA31602.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB14995.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti392 – 3921R → S in BAA31602. (PubMed:9734811)Curated
    Sequence conflicti392 – 3921R → S in AAH29035. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MAMGDD → MRRLICKRICDY in isoform 2. 2 PublicationsVSP_015805
    Alternative sequencei410 – 42516DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2. 2 PublicationsVSP_015806Add
    BLAST
    Alternative sequencei426 – 1294869Missing in isoform 2. 2 PublicationsVSP_015807Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014527 mRNA. Translation: BAA31602.2. Different initiation.
    BC029035 mRNA. Translation: AAH29035.1.
    AJ288058 mRNA. Translation: CAC35157.1.
    AJ288059 mRNA. Translation: CAC35158.1.
    AL137636 mRNA. Translation: CAB70852.1.
    AK024770 mRNA. Translation: BAB14995.1. Different initiation.
    PIRiT00386.
    RefSeqiNP_001193973.1. NM_001207044.1.
    NP_055912.2. NM_015097.2.
    UniGeneiHs.108614.

    Genome annotation databases

    EnsembliENST00000313350; ENSP00000324364; ENSG00000163539.
    GeneIDi23122.
    KEGGihsa:23122.
    UCSCiuc021wvb.1. human. [O75122-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014527 mRNA. Translation: BAA31602.2 . Different initiation.
    BC029035 mRNA. Translation: AAH29035.1 .
    AJ288058 mRNA. Translation: CAC35157.1 .
    AJ288059 mRNA. Translation: CAC35158.1 .
    AL137636 mRNA. Translation: CAB70852.1 .
    AK024770 mRNA. Translation: BAB14995.1 . Different initiation.
    PIRi T00386.
    RefSeqi NP_001193973.1. NM_001207044.1.
    NP_055912.2. NM_015097.2.
    UniGenei Hs.108614.

    3D structure databases

    ProteinModelPortali O75122.
    SMRi O75122. Positions 64-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116743. 21 interactions.
    DIPi DIP-36804N.
    IntActi O75122. 12 interactions.
    MINTi MINT-4526878.
    STRINGi 9606.ENSP00000352581.

    PTM databases

    PhosphoSitei O75122.

    Proteomic databases

    MaxQBi O75122.
    PaxDbi O75122.
    PRIDEi O75122.

    Protocols and materials databases

    DNASUi 23122.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313350 ; ENSP00000324364 ; ENSG00000163539 .
    GeneIDi 23122.
    KEGGi hsa:23122.
    UCSCi uc021wvb.1. human. [O75122-1 ]

    Organism-specific databases

    CTDi 23122.
    GeneCardsi GC03M033537.
    HGNCi HGNC:17078. CLASP2.
    MIMi 605853. gene.
    neXtProti NX_O75122.
    PharmGKBi PA38435.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81443.
    HOGENOMi HOG000236347.
    HOVERGENi HBG079692.
    InParanoidi O75122.
    KOi K16578.
    PhylomeDBi O75122.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi CLASP2. human.
    GeneWikii CLASP2.
    GenomeRNAii 23122.
    NextBioi 44351.
    PROi O75122.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75122.
    Bgeei O75122.
    CleanExi HS_CLASP2.
    Genevestigatori O75122.

    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. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "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 2).
      Tissue: Brain.
    3. "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] OF 1-9 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 939-1294 (ISOFORM 1).
      Tissue: Testis.
    5. "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] OF 1128-1294 (ISOFORM 1).
    6. "The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream of the tyrosine kinase Abl in mediating axon guidance."
      Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.
      Neuron 42:913-926(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex."
      Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C., Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A.
      J. Cell Biol. 168:141-153(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, SUBCELLULAR LOCATION.
    8. "Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta in migrating epithelial cells."
      Wittmann T., Waterman-Storer C.M.
      J. Cell Biol. 169:929-939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION BY GSK3B.
    9. Erratum
      Wittmann T., Waterman-Storer C.M.
      J. Cell Biol. 171:393-393(2005)
    10. Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERC1; PHLDB2 AND RSN, SUBCELLULAR LOCATION.
    11. "Mammalian CLASPs are required for mitotic spindle organization and kinetochore alignment."
      Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A., Tsukita S., Vorobjev I.
      Genes Cells 11:845-857(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "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.
    13. Cited for: FUNCTION, INTERACTION WITH GCC2, SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-525; SER-529; SER-596 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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].
    18. Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF 496-ILE-PRO-497 AND 519-ILE-PRO-520.
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-596 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
      Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
      Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    21. "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-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-8; SER-370; SER-455 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCLAP2_HUMAN
    AccessioniPrimary (citable) accession number: O75122
    Secondary accession number(s): Q7L8F6
    , Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 123 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3