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Q8BRT1 (CLAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Synonyms:Kiaa0627
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.8

Subunit structure

Interacts with ERC1, MAPRE3, microtubules and PHLDB2. 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 the Golgi membranes By similarity. Interacts with CLIP2 and RSN. Interacts with MACF1. Ref.1 Ref.9

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Golgi apparatus. 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 By similarity. Also localizes to meiotic spindle poles. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane By similarity. Ref.1 Ref.7 Ref.8

Tissue specificity

Highly expressed in brain and at low levels in heart, kidney and lung. Ref.1

Developmental stage

Expressed in oocytes and early embryos. Ref.7

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. Isoform 2 is phosphorylated on Ser-241.

Sequence similarities

Belongs to the CLASP family.

Contains 5 HEAT repeats.

Sequence caution

The sequence BAC41436.2 differs from that shown. Reason: Frameshift at position 737.

Ontologies

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

Inferred from mutant phenotype PubMed 17113391. Source: MGI

establishment or maintenance of cell polarity

Inferred from mutant phenotype PubMed 17113391. Source: MGI

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

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

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of microtubule depolymerization

Inferred from direct assay Ref.1. Source: MGI

regulation of microtubule-based process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.1. Source: MGI

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic microtubule

Inferred from direct assay Ref.1PubMed 17113391. Source: MGI

kinetochore microtubule

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

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 pole

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: MGI

microtubule plus-end binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BRT1-1)

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.
Isoform 2 (identifier: Q8BRT1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRRLICKRICDY → MEPRGAEYFC...GGMILSVCKD
     142-1054: Missing.
Isoform 3 (identifier: Q8BRT1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRRLICKRICDY → MAMGDD
     119-173: LKKIRSLLVA...ITVAHLSTVL → CMSCSLVASE...SPVSSAFVQH
     174-1286: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12861286CLIP-associating protein 2
PRO_0000089850

Regions

Repeat179 – 21436HEAT 1
Repeat215 – 25137HEAT 2
Repeat764 – 80138HEAT 3
Repeat1090 – 112738HEAT 4
Repeat1208 – 124538HEAT 5
Region1 – 4040Golgi localization
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 bias459 – 572114Ser-rich

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

Natural variations

Alternative sequence1 – 1212MRRLI…RICDY → MEPRGAEYFCAQVLQKDVSG RLQAGEELLLCLGTPGAIPD LEDDPSRLAKTVDALTRWVG SSNYRVSLLGLEILSAFVDR LSTRFKSYVTMVTTALIDRM GDVKDKVREEAQNLTLKLMD EVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGT QPLVISKLVPHLCVLFGDSN SQVRNAALSAVVEIYRHVGE KLRIDLCKRDIPPARLEMVL AKFDEVQNSGGMILSVCKD in isoform 2.
VSP_015808
Alternative sequence1 – 1212MRRLI…RICDY → MAMGDD in isoform 3.
VSP_015809
Alternative sequence119 – 17355LKKIR…LSTVL → CMSCSLVASEVERALAWPLW SHLATYQHHCHCTLSHEDLP EKRLTSPVSSAFVQH in isoform 3.
VSP_015810
Alternative sequence142 – 1054913Missing in isoform 2.
VSP_015811
Alternative sequence174 – 12861113Missing in isoform 3.
VSP_015812

Experimental info

Mutagenesis61C → S: Impairs Golgi localization; when associated with S-10. Ref.1
Mutagenesis101C → S: Impairs Golgi localization; when associated with S-6. Ref.1
Sequence conflict6571S → T in BAC41436. Ref.4
Sequence conflict6831I → V in BAC41436. Ref.4
Sequence conflict6991P → L in BAC41436. Ref.4
Sequence conflict7021K → KR in BAC41436. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5B208D8F4E90CB93

FASTA1,286140,739
        10         20         30         40         50         60 
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK PGSAGGPKVG 

        70         80         90        100        110        120 
GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS 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 STVAGRVSVG 

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

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

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

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

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

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

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

       790        800        810        820        830        840 
SLKVKVAILK YIETLAKQMD PRDFTNSSET 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 MSEPVRRDPK 

       970        980        990       1000       1010       1020 
KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM 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 
VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH LSQLTGSKMK 

      1270       1280 
LLNLYIKRAQ TGSAGADPTA DVSGQS 

« Hide

Isoform 2 [UniParc].

Checksum: F7ADD06A38B893D3
Show »

FASTA60066,370
Isoform 3 [UniParc].

Checksum: 5512515D37A0CF08
Show »

FASTA16718,021

References

« Hide 'large scale' 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] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INTERACTION WITH CLIP2 AND RSN, MUTAGENESIS OF CYS-6 AND CYS-10.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
Tissue: Brain cortex and Cerebellum.
[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] (ISOFORM 3).
Tissue: Eye.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1286 (ISOFORM 1).
[5]Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[7]"PAR-1 and the microtubule-associated proteins CLASP2 and dynactin-p50 have specific localisation on mouse meiotic and first mitotic spindles."
Moore C.A., Zernicka-Goetz M.
Reproduction 130:311-320(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[8]"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.
[9]"ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity."
Wu X., Kodama A., Fuchs E.
Cell 135:137-148(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MACF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ276961 mRNA. Translation: CAC35161.1.
AK043551 mRNA. Translation: BAC31579.1.
AK005146 mRNA. Translation: BAB23842.1.
BC030468 mRNA. Translation: AAH30468.1.
AB093252 Transcribed RNA. Translation: BAC41436.2. Frameshift.
RefSeqNP_001273528.1. NM_001286599.1.
NP_001273529.1. NM_001286600.1.
NP_001273530.1. NM_001286601.1.
NP_001273531.1. NM_001286602.1.
NP_001273532.1. NM_001286603.1.
UniGeneMm.222272.

3D structure databases

ProteinModelPortalQ8BRT1.
SMRQ8BRT1. Positions 70-312, 1054-1270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BRT1. 5 interactions.
MINTMINT-4112101.

PTM databases

PhosphoSiteQ8BRT1.

Proteomic databases

PaxDbQ8BRT1.
PRIDEQ8BRT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID76499.
KEGGmmu:76499.
UCSCuc009rwt.1. mouse. [Q8BRT1-6]

Organism-specific databases

CTD23122.
MGIMGI:1923749. Clasp2.
RougeSearch...

Phylogenomic databases

eggNOGNOG81443.
HOGENOMHOG000185856.
HOVERGENHBG079692.
KOK16578.
PhylomeDBQ8BRT1.

Gene expression databases

CleanExMM_CLASP2.
GenevestigatorQ8BRT1.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028399. CLASP_metazoan.
IPR024395. CLASP_N_dom.
[Graphical view]
PANTHERPTHR21567:SF11. PTHR21567:SF11. 1 hit.
PfamPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

PROQ8BRT1.
SOURCESearch...

Entry information

Entry nameCLAP2_MOUSE
AccessionPrimary (citable) accession number: Q8BRT1
Secondary accession number(s): Q8CHE3, Q99JI3, Q9DB80
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 105 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot