CLAP1_HUMAN
ID CLAP1_HUMAN Reviewed; 1538 AA.
AC Q7Z460; A2RU21; B7ZLX3; F5GWS0; O75118; Q2KHQ9; Q5H9P0; Q8N5B8; Q9BQT5;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CLIP-associating protein 1;
DE AltName: Full=Cytoplasmic linker-associated protein 1;
DE AltName: Full=Multiple asters homolog 1;
DE AltName: Full=Protein Orbit homolog 1;
DE Short=hOrbit1;
GN Name=CLASP1; Synonyms=KIAA0622, MAST1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Maiato H., Sunkel C.E., Earnshaw W.C.;
RT "Full length cDNA of a human homologue of Drosophila melanogaster multiple
RT asters (MAST) gene.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-266, FUNCTION, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, AND INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
RC TISSUE=Brain;
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-1538.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12837247; DOI=10.1016/s0092-8674(03)00465-3;
RA Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E.,
RA Earnshaw W.C.;
RT "Human CLASP1 is an outer kinetochore component that regulates spindle
RT microtubule dynamics.";
RL Cell 113:891-904(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=16145243; DOI=10.1247/csf.30.7;
RA Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N.,
RA Matsukage A.;
RT "Microtubule bundle formation and cell death induced by the human
RT CLASP/Orbit N-terminal fragment.";
RL Cell Struct. Funct. 30:7-13(2005).
RN [10]
RP FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15631994; DOI=10.1083/jcb.200405094;
RA Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
RA Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A.;
RT "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics
RT at the cell cortex.";
RL J. Cell Biol. 168:141-153(2005).
RN [11]
RP INTERACTION WITH ERC1 AND PHLDB2, AND SUBCELLULAR LOCATION.
RX PubMed=16824950; DOI=10.1016/j.devcel.2006.05.012;
RA Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S.,
RA Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F.,
RA Akhmanova A.;
RT "CLASPs attach microtubule plus ends to the cell cortex through a complex
RT with LL5beta.";
RL Dev. Cell 11:21-32(2006).
RN [12]
RP FUNCTION.
RX PubMed=16866869; DOI=10.1111/j.1365-2443.2006.00990.x;
RA Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A.,
RA Tsukita S., Vorobjev I.;
RT "Mammalian CLASPs are required for mitotic spindle organization and
RT kinetochore alignment.";
RL Genes Cells 11:845-857(2006).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16914514; DOI=10.1091/mbc.e06-07-0579;
RA Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
RA Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
RA Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
RT "Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
RT regulating spindle and kinetochore function.";
RL Mol. Biol. Cell 17:4526-4542(2006).
RN [14]
RP FUNCTION, INTERACTION WITH GCC2, AND SUBCELLULAR LOCATION.
RX PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
RA Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
RA Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
RA Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
RT "Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at
RT the trans-Golgi network.";
RL Dev. Cell 12:917-930(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-649;
RP THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-688;
RP SER-797 AND SER-1091, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646 AND SER-1223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646 AND SER-684, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-545; SER-558;
RP SER-559; SER-568; SER-600; SER-636; SER-646; SER-647; SER-649; SER-695;
RP SER-705; SER-787; SER-797; SER-823; SER-1091 AND SER-1196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC stabilization of dynamic microtubules. Involved in the nucleation of
CC noncentrosomal microtubules originating from the trans-Golgi network
CC (TGN). Required for the polarization of the cytoplasmic microtubule
CC arrays in migrating cells towards the leading edge of the cell. May act
CC at the cell cortex to enhance the frequency of rescue of depolymerizing
CC microtubules by attaching their plus-ends to cortical platforms
CC composed of ERC1 and PHLDB2. This cortical microtubule stabilizing
CC activity is regulated at least in part by phosphatidylinositol 3-kinase
CC signaling. Also performs a similar stabilizing function at the
CC kinetochore which is essential for the bipolar alignment of chromosomes
CC on the mitotic spindle. {ECO:0000269|PubMed:11290329,
CC ECO:0000269|PubMed:12837247, ECO:0000269|PubMed:15631994,
CC ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514,
CC ECO:0000269|PubMed:17543864}.
CC -!- SUBUNIT: Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules,
CC PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2.
CC Interacts with GCC2; recruits CLASP1 to Golgi membranes. Interacts with
CC MACF1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z460; O60333: KIF1B; NbExp=3; IntAct=EBI-913476, EBI-465633;
CC Q7Z460; Q96R06: SPAG5; NbExp=3; IntAct=EBI-913476, EBI-413317;
CC Q7Z460; Q9JK25: Clip1; Xeno; NbExp=2; IntAct=EBI-913476, EBI-908338;
CC Q7Z460; O55156: Clip2; Xeno; NbExp=3; IntAct=EBI-913476, EBI-349416;
CC Q7Z460-2; Q9NX95-5: SYBU; NbExp=3; IntAct=EBI-10967515, EBI-12816095;
CC Q7Z460-4; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-10257534, EBI-752007;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14654843}. Chromosome, centromere, kinetochore.
CC Cytoplasm, cytoskeleton, spindle. Golgi apparatus, trans-Golgi network
CC {ECO:0000305}. Note=Localizes to microtubule plus ends. Localizes to
CC centrosomes, kinetochores and the mitotic spindle from prometaphase.
CC Subsequently localizes to the spindle midzone from anaphase and to the
CC midbody from telophase. In migrating cells localizes to the plus ends
CC of microtubules within the cell body and to the entire microtubule
CC lattice within the lamella. Localizes to the cell cortex and this
CC requires ERC1 and PHLDB2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z460-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z460-2; Sequence=VSP_022386, VSP_022387, VSP_022389;
CC Name=3;
CC IsoId=Q7Z460-3; Sequence=VSP_022386, VSP_022387, VSP_022388,
CC VSP_022389;
CC Name=4;
CC IsoId=Q7Z460-4; Sequence=VSP_054412, VSP_054413, VSP_022386,
CC VSP_054414, VSP_022389;
CC Name=5;
CC IsoId=Q7Z460-5; Sequence=VSP_057272, VSP_022386, VSP_022387,
CC VSP_022389;
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32563.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAX88872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF347693; AAQ15051.1; -; mRNA.
DR EMBL; AC012447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013399; AAX88872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC018737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032563; AAH32563.1; ALT_INIT; mRNA.
DR EMBL; BC112940; AAI12941.1; -; mRNA.
DR EMBL; BC132723; AAI32724.1; -; mRNA.
DR EMBL; BC144107; AAI44108.1; -; mRNA.
DR EMBL; AJ288057; CAC35156.1; -; mRNA.
DR EMBL; CR933722; CAI46251.1; -; mRNA.
DR EMBL; AB014522; BAA31597.1; -; mRNA.
DR PIR; T00387; T00387.
DR RefSeq; NP_001135745.1; NM_001142273.1. [Q7Z460-5]
DR RefSeq; NP_001135746.1; NM_001142274.1. [Q7Z460-2]
DR RefSeq; NP_001193980.1; NM_001207051.1. [Q7Z460-4]
DR RefSeq; NP_056097.1; NM_015282.2. [Q7Z460-1]
DR RefSeq; XP_011509150.1; XM_011510848.1. [Q7Z460-3]
DR PDB; 4K92; X-ray; 2.00 A; A/B=284-552.
DR PDB; 6MQ5; X-ray; 2.15 A; A/B=1-257.
DR PDB; 6MQ7; X-ray; 1.78 A; A/B=284-552.
DR PDBsum; 4K92; -.
DR PDBsum; 6MQ5; -.
DR PDBsum; 6MQ7; -.
DR AlphaFoldDB; Q7Z460; -.
DR SMR; Q7Z460; -.
DR BioGRID; 116919; 74.
DR IntAct; Q7Z460; 50.
DR MINT; Q7Z460; -.
DR STRING; 9606.ENSP00000263710; -.
DR DrugBank; DB12010; Fostamatinib.
DR GlyGen; Q7Z460; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z460; -.
DR MetOSite; Q7Z460; -.
DR PhosphoSitePlus; Q7Z460; -.
DR SwissPalm; Q7Z460; -.
DR BioMuta; CLASP1; -.
DR DMDM; 74723323; -.
DR EPD; Q7Z460; -.
DR jPOST; Q7Z460; -.
DR MassIVE; Q7Z460; -.
DR MaxQB; Q7Z460; -.
DR PaxDb; Q7Z460; -.
DR PeptideAtlas; Q7Z460; -.
DR PRIDE; Q7Z460; -.
DR ProteomicsDB; 24199; -.
DR ProteomicsDB; 69152; -. [Q7Z460-1]
DR ProteomicsDB; 69153; -. [Q7Z460-2]
DR ProteomicsDB; 69154; -. [Q7Z460-3]
DR ProteomicsDB; 7239; -.
DR Antibodypedia; 33401; 297 antibodies from 32 providers.
DR DNASU; 23332; -.
DR Ensembl; ENST00000263710.8; ENSP00000263710.4; ENSG00000074054.20. [Q7Z460-1]
DR Ensembl; ENST00000397587.7; ENSP00000380717.4; ENSG00000074054.20. [Q7Z460-5]
DR Ensembl; ENST00000409078.8; ENSP00000386442.3; ENSG00000074054.20. [Q7Z460-2]
DR Ensembl; ENST00000541377.5; ENSP00000441625.1; ENSG00000074054.20. [Q7Z460-4]
DR GeneID; 23332; -.
DR KEGG; hsa:23332; -.
DR UCSC; uc061nlf.1; human. [Q7Z460-1]
DR CTD; 23332; -.
DR DisGeNET; 23332; -.
DR GeneCards; CLASP1; -.
DR HGNC; HGNC:17088; CLASP1.
DR HPA; ENSG00000074054; Low tissue specificity.
DR MalaCards; CLASP1; -.
DR MIM; 605852; gene.
DR neXtProt; NX_Q7Z460; -.
DR OpenTargets; ENSG00000074054; -.
DR PharmGKB; PA38436; -.
DR VEuPathDB; HostDB:ENSG00000074054; -.
DR eggNOG; KOG2956; Eukaryota.
DR GeneTree; ENSGT00940000154817; -.
DR InParanoid; Q7Z460; -.
DR OMA; MFMDTHT; -.
DR OrthoDB; 66632at2759; -.
DR PhylomeDB; Q7Z460; -.
DR TreeFam; TF101155; -.
DR PathwayCommons; Q7Z460; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q7Z460; -.
DR SIGNOR; Q7Z460; -.
DR BioGRID-ORCS; 23332; 16 hits in 325 CRISPR screens.
DR ChiTaRS; CLASP1; human.
DR GeneWiki; CLASP1; -.
DR GenomeRNAi; 23332; -.
DR Pharos; Q7Z460; Tbio.
DR PRO; PR:Q7Z460; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7Z460; protein.
DR Bgee; ENSG00000074054; Expressed in cortical plate and 201 other tissues.
DR ExpressionAtlas; Q7Z460; baseline and differential.
DR Genevisible; Q7Z460; HS.
DR GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0031592; C:centrosomal corona; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
DR GO; GO:0043515; F:kinetochore binding; IMP:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IDA:MGI.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
DR GO; GO:0051294; P:establishment of spindle orientation; IDA:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; NAS:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028399; CLASP_1.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR21567:SF28; PTHR21567:SF28; 1.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 4.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1538
FT /note="CLIP-associating protein 1"
FT /id="PRO_0000089847"
FT REPEAT 87..124
FT /note="HEAT 1"
FT REPEAT 163..200
FT /note="HEAT 2"
FT REPEAT 405..440
FT /note="HEAT 3"
FT REPEAT 441..477
FT /note="HEAT 4"
FT REPEAT 974..1011
FT /note="HEAT 5"
FT REPEAT 1342..1379
FT /note="HEAT 6"
FT REPEAT 1460..1497
FT /note="HEAT 7"
FT REGION 235..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..785
FT /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT /evidence="ECO:0000269|PubMed:15631994"
FT REGION 1080..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1538
FT /note="Interaction with CLIP2"
FT /evidence="ECO:0000250"
FT REGION 1254..1538
FT /note="Interaction with PHLDB2 and RSN"
FT /evidence="ECO:0000269|PubMed:16824950"
FT REGION 1256..1538
FT /note="Localization to kinetochores"
FT COILED 1299..1330
FT /evidence="ECO:0000255"
FT COMPBIAS 250..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 656
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 711
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1095
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT MOD_RES 1099
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT MOD_RES 1196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 637
FT /note="L -> LESRHMREDMEYIGLDS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054412"
FT VAR_SEQ 637
FT /note="L -> LDGTTTKAE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057272"
FT VAR_SEQ 673..682
FT /note="RSRSANPAGA -> P (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054413"
FT VAR_SEQ 737..772
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022386"
FT VAR_SEQ 808
FT /note="L -> LLLGDSRSK (in isoform 2, isoform 3 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022387"
FT VAR_SEQ 808
FT /note="L -> LLLGDSRS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054414"
FT VAR_SEQ 911
FT /note="K -> KIADSEAECEDKEGNLFPSEVSCT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_022388"
FT VAR_SEQ 1123..1161
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022389"
FT VARIANT 233
FT /note="I -> T (in dbSNP:rs17761055)"
FT /id="VAR_053818"
FT CONFLICT 251
FT /note="R -> G (in Ref. 5; CAI46251)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="S -> F (in Ref. 5; CAI46251)"
FT /evidence="ECO:0000305"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:6MQ5"
FT TURN 34..42
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:6MQ5"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:6MQ5"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:6MQ5"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 382..399
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:6MQ7"
FT TURN 416..419
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 423..439
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 445..450
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 484..495
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 500..516
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:6MQ7"
FT HELIX 530..537
FT /evidence="ECO:0007829|PDB:6MQ7"
SQ SEQUENCE 1538 AA; 169451 MW; 6E03BD948C227F8D CRC64;
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN
FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS
DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI
PRSQGCSRET SPNRIGLARS SRIPRPSMSQ GCSRDTSRES SRDTSPARGF PPLDRFGLGQ
PGRIPGSVNA MRVLSTSTDL EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY
GSRNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI
FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ
KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK YIESLARQMD PTDFVNSSET
RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM LLGALPKTFQ DGATKLLHNH
LKNSSNTSVG SPSNTIGRTP SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP
PFSQPNSIPT APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL
NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT QPPRAFPGPR
ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH SDLVADLLKE LSNHNERVEE
RKGALLELLK ITREDSLGVW EEHFKTILLL LLETLGDKDH SIRALALRVL REILRNQPAR
FKNYAELTIM KTLEAHKDSH KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL
AAIKMQTKVV ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK
PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS
