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Q99JD4 (CLAP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Gene names
Name:Clasp2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1286 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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 By similarity. Interacts with MACF1 By similarity.

Subcellular location

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

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the CLASP family.

Contains 5 HEAT repeats.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCell membrane
Cell projection
Centromere
Chromosome
Cytoplasm
Cytoskeleton
Golgi apparatus
Kinetochore
Membrane
Microtubule
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell migration

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

microtubule anchoring

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule nucleation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule organizing center organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of microtubule depolymerization

Inferred from direct assay Ref.1. Source: RGD

regulation of microtubule-based process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic microtubule

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from direct assay Ref.1. Source: RGD

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from direct assay Ref.1. Source: RGD

microtubule plus-end binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12861286CLIP-associating protein 2
PRO_0000089851

Regions

Repeat179 – 21436HEAT 1
Repeat215 – 25137HEAT 2
Repeat764 – 80138HEAT 3
Repeat1090 – 112738HEAT 4
Repeat1208 – 124538HEAT 5
Region1 – 4040Golgi localization By similarity
Region450 – 565116Interaction with microtubules, MAPRE1 and MAPRE3 By similarity
Region864 – 1286423Interaction with RSN and localization to the Golgi and kinetochores By similarity
Region1009 – 1286278Required for cortical localization By similarity
Coiled coil1047 – 107630 Potential
Motif500 – 5034Microtubule tip localization signal
Motif523 – 5264Microtubule tip localization signal
Compositional bias316 – 572257Ser-rich
Compositional bias1096 – 11005Poly-Leu

Amino acid modifications

Modified residue141Phosphoserine By similarity
Modified residue3761Phosphoserine By similarity
Modified residue4611Phosphoserine By similarity
Modified residue5311Phosphoserine By similarity
Modified residue5351Phosphoserine By similarity
Modified residue5811Phosphoserine By similarity
Modified residue10211Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99JD4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: C1742635DADC3F09

FASTA1,286140,638
        10         20         30         40         50         60 
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVNSARK PGSAGGPKAG 

        70         80         90        100        110        120 
GTSKEGGAGA VDEDDFIKAF TDVPSIQIYS SRELEETLNK IREILSDDKH DWDQRANALK 

       130        140        150        160        170        180 
KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG 

       190        200        210        220        230        240 
AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE 

       250        260        270        280        290        300 
FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN 

       310        320        330        340        350        360 
SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP SAVAGRVSVG 

       370        380        390        400        410        420 
GSKASPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR LGAGALNPGS YASLEDTSDK 

       430        440        450        460        470        480 
MDGTASEDGR VRAKLSTPLV AVGNAKTDSR GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS 

       490        500        510        520        530        540 
TVSSGAQRIL VNSASAQKRS KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR 

       550        560        570        580        590        600 
ESSRDTSPVR SFQPLGPGYG MSQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK 

       610        620        630        640        650        660 
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE VLNRCASSNW 

       670        680        690        700        710        720 
SERKEGLLGL QNLLKNQRTL SRVELKRLCE IFTRMFADPH GKVFSMFLET LVDFIQVHKD 

       730        740        750        760        770        780 
DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ KALDVTRESF PNDLQFNILM RFTVDQTQTP 

       790        800        810        820        830        840 
SLKVKVAILK YIETLAKQMD PGDFINSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL 

       850        860        870        880        890        900 
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP 

       910        920        930        940        950        960 
LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED MSEPLKRDPK 

       970        980        990       1000       1010       1020 
KEDGDTVCSG PGMSDPRAGG DAPDSSQPAL DNKASLLHSV PLHSSPRSRD YNPYNYSDSI 

      1030       1040       1050       1060       1070       1080 
SPFNKSALKE AMFDDDADQF PDDLSLDHSD LVAELLKELS NHNERIEERK IALYELMKLT 

      1090       1100       1110       1120       1130       1140 
QEESFSVWDE HFKTILLLLL ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT 

      1150       1160       1170       1180       1190       1200 
LEAHKDPHKE VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER 

      1210       1220       1230       1240       1250       1260 
VSKETLNLLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK 

      1270       1280 
LLNLYIKRAQ TGSAGADPTT DVSGQS 

« Hide

References

[1]"Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts."
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F., Galjart N.
Cell 104:923-935(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ288060 mRNA. Translation: CAC35166.1.
RefSeqNP_446174.1. NM_053722.2.
UniGeneRn.19943.

3D structure databases

ProteinModelPortalQ99JD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250360. 1 interaction.
MINTMINT-4579893.
STRING10116.ENSRNOP00000063775.

PTM databases

PhosphoSiteQ99JD4.

Proteomic databases

PaxDbQ99JD4.
PRIDEQ99JD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012545; ENSRNOP00000012545; ENSRNOG00000009161.
GeneID114514.
KEGGrno:114514.
UCSCRGD:619789. rat.

Organism-specific databases

CTD23122.
RGD619789. Clasp2.

Phylogenomic databases

eggNOGNOG81443.
GeneTreeENSGT00390000001762.
HOGENOMHOG000236347.
HOVERGENHBG079692.
InParanoidQ99JD4.
KOK16578.
OMAPLAGMGN.
OrthoDBEOG780RKK.

Gene expression databases

GenevestigatorQ99JD4.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

NextBio618631.
PROQ99JD4.

Entry information

Entry nameCLAP2_RAT
AccessionPrimary (citable) accession number: Q99JD4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families