CLASP2
entrez
23122
canonical
uniprot
O75122
canonical
ensembl
ENSG00000163539
resolver
ensp
ENSP00000382297
resolver
ensp
ENSP00000417518
resolver
ensp
ENSP00000419305
resolver
ensp
ENSP00000419974
resolver
ensp
ENSP00000489023
resolver
ensp
ENSP00000498272
resolver
ensp
ENSP00000507498
resolver
ensp
ENSP00000565745
resolver
ensp
ENSP00000582597
resolver
ensp
ENSP00000582598
resolver
enst
ENST00000399362
resolver
enst
ENST00000468888
resolver
enst
ENST00000635664
resolver
enst
ENST00000650653
resolver
enst
ENST00000682230
resolver
genesymbol
CLASP2
resolver
genesymbol_syn
KIAA0627
resolver
hgnc
HGNC:17078
resolver
uniprot
A0A0U1RQI6
resolver
uniprot
A0A804HJG7
resolver
uniprot
B2RTR1
resolver
uniprot
E7ERI8
resolver
uniprot
E7EW49
resolver
uniprot
F5H604
resolver
uniprot
J3KR49
resolver
uniprot
Q7L8F6
resolver
uniprot
Q8N6R6
resolver
uniprot
Q9BQT3
resolver
uniprot
Q9BQT4
resolver
uniprot
Q9H7A3
resolver
uniprot
Q9NSZ2
resolver
uniprot_entry
A0A0U1RQI6_HUMAN
resolver
uniprot_entry
A0A804HJG7_HUMAN
resolver
uniprot_entry
CLAP2_HUMAN
resolver
uniprot_entry
E7ERI8_HUMAN
resolver
uniprot_entry
E7EW49_HUMAN
resolver
uniprot_entry
J3KR49_HUMAN
resolver
uniprot_sec
B2RTR1
resolver
uniprot_sec
F5H604
resolver
uniprot_sec
Q7L8F6
resolver
uniprot_sec
Q8N6R6
resolver
uniprot_sec
Q9BQT3
resolver
uniprot_sec
Q9BQT4
resolver
uniprot_sec
Q9H7A3
resolver
uniprot_sec
Q9NSZ2
resolver
amino_acid_sequence
MAMGDDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQSDRSSSSSQESLNRPFSSKWSTANPSTVAGRVSAGSSKASSLPGSLQRSRSDIDVNAAAGAKAHHAAGQSVRSGRLGAGALNAGSYASLEDTSDKLDGTASEDGRVRAKLSAPLAGMGNAKADSRGRSRTKMVSQSQPGSRSGSPGRVLTTTALSTVSSGVQRVLVNSASAQKRSKIPRSQGCSREASPSRLSVARSSRIPRPSVSQGCSREASRESSRDTSPVRSFQPLASRHHSRSTGALYAPEVYGASGPGYGISQSSRLSSSVSAMRVLNTGSDVEEAVADALKKPARRRYESYGMHSDDDANSDASSACSERSYSSRNGSIPTYMRQTEDVAEVLNRCASSNWSERKEGLLGLQNLLKNQRTLSRVELKRLCEIFTRMFADPHGKRVFSMFLETLVDFIQVHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRESFPNDLQFNILMRFTVDQTQTPSLKVKVAILKYIETLAKQMDPGDFINSSETRLAVSRVITWTTEPKSSDVRKAAQSVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLRNTGNGTQSSMGSPLTRPTPRSPANWSSPLTSPTNTSQNTLSPSAFDYDTENMNSEDIYSSLRGVTEAIQNFSFRSQEDMNEPLKRDSKKDDGDSMCGGPGMSDPRAGGDATDSSQTALDNKASLLHSMPTHSSPRSRDYNPYNYSDSISPFNKSALKEAMFDDDADQFPDDLSLDHSDLVAELLKELSNHNERVEERKIALYELMKLTQEESFSVWDEHFKTILLLLLETLGDKEPTIRALALKVLREILRHQPARFKNYAELTVMKTLEAHKDPHKEVVRSAEEAASVLATSISPEQCIKVLCPIIQTADYPINLAAIKMQTKVIERVSKETLNLLLPEIMPGLIQGYDNSESSVRKACVFCLVAVHAVIGDELKPHLSQLTGSKMKLLNLYIKRAQTGSGGADPTTDVSGQS
uniprot
proteins
function
FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). 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 (PubMed:16824950). 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 (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. {ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.
uniprot
proteins
mass_dalton
141064
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="W->E: Decreases affinity for microtubules; when associated with A-191; E-667; E-833; A-838 and A-839."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 191; /note="K->A: Decreases affinity for microtubules; when associated with E-106; E-667; E-833; A-838 and A-839."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 496..497; /note="IP->AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 519-A-A-520."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 496..497; /note="IP->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."; /evidence="ECO:0000269|PubMed:19632184"; MUTAGEN 499; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-503; D-507; D-525; D-529; D-533; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 503; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-507; D-525; D-529; D-533; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 507; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-525; D-529; D-533; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 519..520; /note="IP->AA: No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 496-A-A-497."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 519..520; /note="IP->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."; /evidence="ECO:0000269|PubMed:19632184"; MUTAGEN 525; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-529; D-533; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 529; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-533; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 533; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-537 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 537; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-541."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 541; /note="S->D: Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-537."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 667; /note="W->E: Decreases affinity for microtubules; when associated with E-106; A-191; E-833; A-838 and A-839."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 833; /note="K->E: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; A-838 and A-839."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 838; /note="R->A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-839."; /evidence="ECO:0000269|PubMed:26003921"; MUTAGEN 839; /note="K->A: Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-838."; /evidence="ECO:0000269|PubMed:26003921
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. {ECO:0000269|PubMed:15955847, ECO:0000305|PubMed:26003921}.
uniprot
proteins
protein_family
CLASP family
uniprot
proteins
pubmed
11290329
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15207236
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15631994
uniprot
proteins
pubmed
15955847
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16824950
uniprot
proteins
pubmed
16866869
uniprot
proteins
pubmed
16914514
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17543864
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19632184
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20937854
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26003921
uniprot
proteins
pubmed
27410476
uniprot
proteins
pubmed
33587225
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1294
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Golgi apparatus {ECO:0000250|UniProtKB:Q8BRT1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17543864}. Cell membrane {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane {ECO:0000269|PubMed:20937854}. Cytoplasm, cell cortex {ECO:0000269|PubMed:27410476}. Note=Localizes to microtubule plus ends (PubMed:15631994). Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase (PubMed:16866869, PubMed:16914514). 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 (PubMed:16824950). Colocalizes with KANK1 at the cell cortex, likely recruited in cortical microtubule stabilization complexes (CMSC) at focal adhesions rims (PubMed:27410476). The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane. {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:27410476}.
uniprot
proteins