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Q7Z460

- CLAP1_HUMAN

UniProt

Q7Z460 - CLAP1_HUMAN

Protein

CLIP-associating protein 1

Gene

CLASP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 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.6 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell division Source: MGI
    3. establishment of spindle orientation Source: MGI
    4. establishment or maintenance of cell polarity Source: UniProtKB
    5. exit from mitosis Source: UniProtKB
    6. G2/M transition of mitotic cell cycle Source: Reactome
    7. microtubule anchoring Source: UniProtKB
    8. microtubule bundle formation Source: UniProtKB
    9. microtubule cytoskeleton organization Source: UniProtKB
    10. microtubule nucleation Source: UniProtKB
    11. microtubule organizing center organization Source: UniProtKB
    12. mitotic cell cycle Source: Reactome
    13. negative regulation of microtubule depolymerization Source: UniProtKB
    14. negative 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_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CLIP-associating protein 1
    Alternative name(s):
    Cytoplasmic linker-associated protein 1
    Multiple asters homolog 1
    Protein Orbit homolog 1
    Short name:
    hOrbit1
    Gene namesi
    Name:CLASP1
    Synonyms:KIAA0622, MAST1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17088. CLASP1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Golgi apparatustrans-Golgi network Curated
    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.

    GO - Cellular componenti

    1. cell cortex Source: MGI
    2. centrosomal corona Source: UniProtKB
    3. centrosome Source: UniProtKB
    4. condensed chromosome kinetochore Source: UniProtKB-SubCell
    5. cortical microtubule cytoskeleton Source: UniProtKB
    6. cytoplasmic microtubule Source: UniProtKB
    7. cytosol Source: Reactome
    8. extracellular vesicular exosome Source: UniProt
    9. Golgi apparatus Source: UniProtKB
    10. kinetochore Source: UniProtKB
    11. kinetochore microtubule Source: UniProtKB
    12. membrane Source: UniProtKB
    13. spindle microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38436.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15381538CLIP-associating protein 1PRO_0000089847Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei600 – 6001Phosphoserine3 Publications
    Modified residuei646 – 6461Phosphoserine4 Publications
    Modified residuei649 – 6491Phosphoserine1 Publication
    Modified residuei656 – 6561Phosphothreonine1 Publication
    Modified residuei684 – 6841Phosphoserine1 Publication
    Modified residuei688 – 6881Phosphoserine2 Publications
    Modified residuei695 – 6951Phosphoserine1 Publication
    Modified residuei711 – 7111Phosphothreonine1 Publication
    Modified residuei714 – 7141Phosphoserine1 Publication
    Modified residuei797 – 7971Phosphoserine1 Publication
    Modified residuei1091 – 10911Phosphoserine2 Publications
    Modified residuei1099 – 10991Phosphothreonine1 Publication
    Modified residuei1196 – 11961Phosphoserine1 Publication
    Modified residuei1223 – 12231Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z460.
    PaxDbiQ7Z460.
    PRIDEiQ7Z460.

    PTM databases

    PhosphoSiteiQ7Z460.

    Miscellaneous databases

    PMAP-CutDBQ7Z460.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7Z460.
    BgeeiQ7Z460.
    CleanExiHS_CLASP1.
    HS_MAST1.
    GenevestigatoriQ7Z460.

    Interactioni

    Subunit structurei

    Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules, PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP1 to Golgi membranes. Interacts with MACF1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Clip1Q9JK252EBI-913476,EBI-908338From a different organism.
    Clip2O551563EBI-913476,EBI-349416From a different organism.
    KIF1BO603333EBI-913476,EBI-465633
    SPAG5Q96R063EBI-913476,EBI-413317

    Protein-protein interaction databases

    BioGridi116919. 10 interactions.
    IntActiQ7Z460. 13 interactions.
    MINTiMINT-1683081.
    STRINGi9606.ENSP00000263710.

    Structurei

    Secondary structure

    1
    1538
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi297 – 30610
    Helixi317 – 33115
    Helixi338 – 35316
    Helixi356 – 3583
    Helixi362 – 3676
    Helixi370 – 3778
    Helixi382 – 39918
    Helixi400 – 4034
    Helixi404 – 41512
    Turni416 – 4194
    Helixi423 – 43917
    Helixi445 – 4517
    Helixi452 – 4543
    Helixi458 – 47417
    Helixi477 – 4793
    Turni480 – 4823
    Helixi484 – 49512
    Helixi500 – 51617
    Helixi518 – 52710
    Helixi530 – 5378

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4K92X-ray2.00A/B284-552[»]
    ProteinModelPortaliQ7Z460.
    SMRiQ7Z460. Positions 5-227, 296-538.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati87 – 12438HEAT 1Add
    BLAST
    Repeati163 – 20038HEAT 2Add
    BLAST
    Repeati405 – 44036HEAT 3Add
    BLAST
    Repeati441 – 47737HEAT 4Add
    BLAST
    Repeati974 – 101138HEAT 5Add
    BLAST
    Repeati1342 – 137938HEAT 6Add
    BLAST
    Repeati1460 – 149738HEAT 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni662 – 785124Interaction with microtubules, MAPRE1 and MAPRE3Add
    BLAST
    Regioni1254 – 1538285Interaction with CLIP2By similarityAdd
    BLAST
    Regioni1254 – 1538285Interaction with PHLDB2 and RSNAdd
    BLAST
    Regioni1256 – 1538283Localization to kinetochoresAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1299 – 133032Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi530 – 765236Ser-richAdd
    BLAST
    Compositional biasi1526 – 15327Poly-Ser

    Sequence similaritiesi

    Belongs to the CLASP family.Curated
    Contains 7 HEAT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG81443.
    HOGENOMiHOG000236347.
    HOVERGENiHBG079692.
    InParanoidiQ7Z460.
    KOiK16578.
    OMAiSGNMIQS.
    PhylomeDBiQ7Z460.
    TreeFamiTF101155.

    Family and domain databases

    Gene3Di1.25.10.10. 4 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR028399. CLASP_metazoan.
    IPR024395. CLASP_N_dom.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view]
    PANTHERiPTHR21567:SF28. PTHR21567:SF28. 1 hit.
    PfamiPF12348. CLASP_N. 1 hit.
    PF02985. HEAT. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.
    PROSITEiPS50077. HEAT_REPEAT. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z460-1) [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

    MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL     50
    VDGLATSWVN SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL 100
    GDAKDSVREQ DQTLLLKIMD QAANPQYVWD RMLGGFKHKN FRTREGICLC 150
    LIATLNASGA QTLTLSKIVP HICNLLGDPN SQVRDAAINS LVEIYRHVGE 200
    RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN FDDEDSVDGN 250
    RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 300
    DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS 350
    LLLAGAAEYD NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG 400
    NKFDHGAEAI MPTIFNLIPN SAKIMATSGV VAVRLIIRHT HIPRLIPVIT 450
    SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL ERHISVLAET IKKGIHDADS 500
    EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL KNSDSIVSLP 550
    QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 600
    DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA 650
    TNVASTPDNR GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL 700
    TGGSSRGPPV TPSSEKRSKI PRSQGCSRET SPNRIGLARS SRIPRPSMSQ 750
    GCSRDTSRES SRDTSPARGF PPLDRFGLGQ PGRIPGSVNA MRVLSTSTDL 800
    EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY GSRNGGIPHY 850
    LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI 900
    FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD 950
    LLGSVQAKVQ KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK 1000
    YIESLARQMD PTDFVNSSET RLAVSRIITW TTEPKSSDVR KAAQIVLISL 1050
    FELNTPEFTM LLGALPKTFQ DGATKLLHNH LKNSSNTSVG SPSNTIGRTP 1100
    SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP PFSQPNSIPT 1150
    APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL 1200
    NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT 1250
    QPPRAFPGPR ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH 1300
    SDLVADLLKE LSNHNERVEE RKGALLELLK ITREDSLGVW EEHFKTILLL 1350
    LLETLGDKDH SIRALALRVL REILRNQPAR FKNYAELTIM KTLEAHKDSH 1400
    KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL AAIKMQTKVV 1450
    ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK 1500
    PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS 1538
    Length:1,538
    Mass (Da):169,451
    Last modified:October 1, 2003 - v1
    Checksum:i6E03BD948C227F8D
    GO
    Isoform 2 (identifier: Q7Z460-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         737-772: Missing.
         808-808: L → LLLGDSRSK
         1123-1161: Missing.

    Show »
    Length:1,471
    Mass (Da):162,110
    Checksum:iF027A39E35F82BA2
    GO
    Isoform 3 (identifier: Q7Z460-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         737-772: Missing.
         808-808: L → LLLGDSRSK
         911-911: K → KIADSEAECEDKEGNLFPSEVSCT
         1123-1161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,494
    Mass (Da):164,566
    Checksum:i0B69865E7CD5A48F
    GO
    Isoform 4 (identifier: Q7Z460-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         637-637: L → LESRHMREDMEYIGLDS
         673-682: RSRSANPAGA → P
         737-772: Missing.
         808-808: L → LLLGDSRS
         1123-1161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,477
    Mass (Da):163,061
    Checksum:i7C56388FDF06760C
    GO

    Sequence cautioni

    The sequence AAH32563.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAX88872.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511R → G in CAI46251. (PubMed:17974005)Curated
    Sequence conflicti556 – 5561S → F in CAI46251. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331I → T.
    Corresponds to variant rs17761055 [ dbSNP | Ensembl ].
    VAR_053818

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei637 – 6371L → LESRHMREDMEYIGLDS in isoform 4. 1 PublicationVSP_054412
    Alternative sequencei673 – 68210RSRSANPAGA → P in isoform 4. 1 PublicationVSP_054413
    Alternative sequencei737 – 77236Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_022386Add
    BLAST
    Alternative sequencei808 – 8081L → LLLGDSRSK in isoform 2 and isoform 3. 2 PublicationsVSP_022387
    Alternative sequencei808 – 8081L → LLLGDSRS in isoform 4. 1 PublicationVSP_054414
    Alternative sequencei911 – 9111K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3. 1 PublicationVSP_022388
    Alternative sequencei1123 – 116139Missing in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_022389Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF347693 mRNA. Translation: AAQ15051.1.
    AC012447 Genomic DNA. No translation available.
    AC013399 Genomic DNA. Translation: AAX88872.1. Sequence problems.
    AC018737 Genomic DNA. No translation available.
    AC079449 Genomic DNA. No translation available.
    BC032563 mRNA. Translation: AAH32563.1. Different initiation.
    BC112940 mRNA. Translation: AAI12941.1.
    BC144107 mRNA. Translation: AAI44108.1.
    AJ288057 mRNA. Translation: CAC35156.1.
    CR933722 mRNA. Translation: CAI46251.1.
    AB014522 mRNA. Translation: BAA31597.1.
    PIRiT00387.
    RefSeqiNP_001135745.1. NM_001142273.1.
    NP_001135746.1. NM_001142274.1. [Q7Z460-2]
    NP_001193980.1. NM_001207051.1. [Q7Z460-4]
    NP_056097.1. NM_015282.2. [Q7Z460-1]
    UniGeneiHs.469840.
    Hs.708183.

    Genome annotation databases

    EnsembliENST00000263710; ENSP00000263710; ENSG00000074054. [Q7Z460-1]
    ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
    ENST00000541377; ENSP00000441625; ENSG00000074054. [Q7Z460-4]
    GeneIDi23332.
    KEGGihsa:23332.
    UCSCiuc002tnc.3. human. [Q7Z460-1]
    uc010yza.2. human. [Q7Z460-2]

    Polymorphism databases

    DMDMi74723323.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF347693 mRNA. Translation: AAQ15051.1 .
    AC012447 Genomic DNA. No translation available.
    AC013399 Genomic DNA. Translation: AAX88872.1 . Sequence problems.
    AC018737 Genomic DNA. No translation available.
    AC079449 Genomic DNA. No translation available.
    BC032563 mRNA. Translation: AAH32563.1 . Different initiation.
    BC112940 mRNA. Translation: AAI12941.1 .
    BC144107 mRNA. Translation: AAI44108.1 .
    AJ288057 mRNA. Translation: CAC35156.1 .
    CR933722 mRNA. Translation: CAI46251.1 .
    AB014522 mRNA. Translation: BAA31597.1 .
    PIRi T00387.
    RefSeqi NP_001135745.1. NM_001142273.1.
    NP_001135746.1. NM_001142274.1. [Q7Z460-2 ]
    NP_001193980.1. NM_001207051.1. [Q7Z460-4 ]
    NP_056097.1. NM_015282.2. [Q7Z460-1 ]
    UniGenei Hs.469840.
    Hs.708183.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4K92 X-ray 2.00 A/B 284-552 [» ]
    ProteinModelPortali Q7Z460.
    SMRi Q7Z460. Positions 5-227, 296-538.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116919. 10 interactions.
    IntActi Q7Z460. 13 interactions.
    MINTi MINT-1683081.
    STRINGi 9606.ENSP00000263710.

    PTM databases

    PhosphoSitei Q7Z460.

    Polymorphism databases

    DMDMi 74723323.

    Proteomic databases

    MaxQBi Q7Z460.
    PaxDbi Q7Z460.
    PRIDEi Q7Z460.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263710 ; ENSP00000263710 ; ENSG00000074054 . [Q7Z460-1 ]
    ENST00000409078 ; ENSP00000386442 ; ENSG00000074054 . [Q7Z460-2 ]
    ENST00000541377 ; ENSP00000441625 ; ENSG00000074054 . [Q7Z460-4 ]
    GeneIDi 23332.
    KEGGi hsa:23332.
    UCSCi uc002tnc.3. human. [Q7Z460-1 ]
    uc010yza.2. human. [Q7Z460-2 ]

    Organism-specific databases

    CTDi 23332.
    GeneCardsi GC02M122095.
    HGNCi HGNC:17088. CLASP1.
    MIMi 605852. gene.
    neXtProti NX_Q7Z460.
    PharmGKBi PA38436.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81443.
    HOGENOMi HOG000236347.
    HOVERGENi HBG079692.
    InParanoidi Q7Z460.
    KOi K16578.
    OMAi SGNMIQS.
    PhylomeDBi Q7Z460.
    TreeFami TF101155.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_19230. Role of Abl in Robo-Slit signaling.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi CLASP1. human.
    GeneWikii CLASP1.
    GenomeRNAii 23332.
    NextBioi 45259.
    PMAP-CutDB Q7Z460.
    PROi Q7Z460.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z460.
    Bgeei Q7Z460.
    CleanExi HS_CLASP1.
    HS_MAST1.
    Genevestigatori Q7Z460.

    Family and domain databases

    Gene3Di 1.25.10.10. 4 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR028399. CLASP_metazoan.
    IPR024395. CLASP_N_dom.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view ]
    PANTHERi PTHR21567:SF28. PTHR21567:SF28. 1 hit.
    Pfami PF12348. CLASP_N. 1 hit.
    PF02985. HEAT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    PROSITEi PS50077. HEAT_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Full length cDNA of a human homologue of Drosophila melanogaster multiple asters (MAST) gene."
      Maiato H., Sunkel C.E., Earnshaw W.C.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2).
      Tissue: Eye.
    4. "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 1-266, FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3).
      Tissue: Testis.
    6. "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] OF 250-1538.
      Tissue: Brain.
    7. "Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics."
      Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E., Earnshaw W.C.
      Cell 113:891-904(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Microtubule bundle formation and cell death induced by the human CLASP/Orbit N-terminal fragment."
      Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N., Matsukage A.
      Cell Struct. Funct. 30:7-13(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
    9. "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.
    10. Cited for: INTERACTION WITH ERC1 AND PHLDB2, 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.
    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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-649; THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, 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. "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-600; SER-646; SER-688; SER-797 AND SER-1091, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-646 AND SER-1223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-600; SER-646 AND SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCLAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z460
    Secondary accession number(s): B7ZLX3
    , O75118, Q2KHQ9, Q5H9P0, Q8N5B8, Q9BQT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2005
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3