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Protein

CLIP-associating protein 2

Gene

Clasp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.By similarity

GO - Molecular functioni

  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Gene namesi
Name:Clasp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi619789. Clasp2.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Chromosomecentromerekinetochore By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • 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 phosphorylated form to the cell membrane (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000898511 – 1286CLIP-associating protein 2Add BLAST1286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineCombined sources1
Modified residuei20PhosphoserineCombined sources1
Modified residuei322PhosphoserineBy similarity1
Modified residuei333PhosphoserineCombined sources1
Modified residuei336PhosphoserineBy similarity1
Modified residuei374PhosphoserineBy similarity1
Modified residuei376PhosphoserineBy similarity1
Modified residuei413PhosphoserineCombined sources1
Modified residuei461PhosphoserineBy similarity1
Modified residuei465PhosphoserineBy similarity1
Modified residuei469PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei495PhosphoserineBy similarity1
Modified residuei513PhosphoserineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei535PhosphoserineCombined sources1
Modified residuei570PhosphoserineBy similarity1
Modified residuei572PhosphoserineBy similarity1
Modified residuei581PhosphoserineCombined sources1
Modified residuei614PhosphoserineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei779PhosphothreonineBy similarity1
Modified residuei884PhosphoserineBy similarity1
Modified residuei944PhosphoserineBy similarity1
Modified residuei947PhosphoserineCombined sources1
Modified residuei1005PhosphoserineBy similarity1
Modified residuei1021PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99JD4.
PRIDEiQ99JD4.

PTM databases

iPTMnetiQ99JD4.
PhosphoSitePlusiQ99JD4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000009161.
ExpressionAtlasiQ99JD4. baseline and differential.
GenevisibleiQ99JD4. RN.

Interactioni

Subunit structurei

Interacts with microtubules. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with CLIP2, ERC1, MAPRE3, PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP2 to Golgi membranes (By similarity). Interacts with MACF1 (By similarity).By similarity

GO - Molecular functioni

  • microtubule binding Source: RGD
  • microtubule plus-end binding Source: UniProtKB

Protein-protein interaction databases

BioGridi250360. 1 interactor.
MINTiMINT-4579893.
STRINGi10116.ENSRNOP00000012545.

Structurei

3D structure databases

ProteinModelPortaliQ99JD4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati179 – 214HEAT 1Sequence analysisAdd BLAST36
Repeati215 – 251HEAT 2Sequence analysisAdd BLAST37
Repeati256 – 293HEAT 3Sequence analysisAdd BLAST38
Repeati702 – 739HEAT 4Sequence analysisAdd BLAST38
Repeati764 – 801HEAT 5Sequence analysisAdd BLAST38
Repeati1046 – 1083HEAT 6Sequence analysisAdd BLAST38
Repeati1090 – 1127HEAT 7Sequence analysisAdd BLAST38
Repeati1208 – 1245HEAT 8Sequence analysisAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 40Golgi localizationBy similarityAdd BLAST40
Regioni66 – 317TOG 1By similarityAdd BLAST252
Regioni450 – 565Interaction with microtubules, MAPRE1 and MAPRE3By similarityAdd BLAST116
Regioni642 – 873TOG 2By similarityAdd BLAST232
Regioni864 – 1286Interaction with RSN and localization to the Golgi and kinetochoresBy similarityAdd BLAST423
Regioni1009 – 1286Required for cortical localizationBy similarityAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi500 – 503SXIP motif 1; mediates interaction with MAPRE1 and targeting to microtubule plus endsBy similarity4
Motifi523 – 526SXIP motif 2; mediates interaction with MAPRE1 and targeting to microtubule plus endsBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi316 – 572Ser-richAdd BLAST257
Compositional biasi1096 – 1100Poly-Leu5

Domaini

The two SXIP sequence motifs mediate interaction with MAPRE1; this is necessary for targeting to the growing microtubule plus ends.By similarity
Two TOG regions display structural characteristics similar to HEAT repeat domains and mediate interaction with microtubules.By similarity

Sequence similaritiesi

Belongs to the CLASP family.Curated
Contains 8 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
GeneTreeiENSGT00390000001762.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiQ99JD4.
KOiK16578.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q99JD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVNSARK
60 70 80 90 100
PGSAGGPKAG GTSKEGGAGA VDEDDFIKAF TDVPSIQIYS SRELEETLNK
110 120 130 140 150
IREILSDDKH DWDQRANALK KIRSLLVAGA AQYDCFFQHL RLLDGALKLS
160 170 180 190 200
AKDLRSQVVR EACITVAHLS TVLGNKFDHG AEAIVPTLFN LVPNSAKVMA
210 220 230 240 250
TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE FLDLLLQEWQ
260 270 280 290 300
THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN
310 320 330 340 350
SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP
360 370 380 390 400
SAVAGRVSVG GSKASPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR
410 420 430 440 450
LGAGALNPGS YASLEDTSDK MDGTASEDGR VRAKLSTPLV AVGNAKTDSR
460 470 480 490 500
GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS TVSSGAQRIL VNSASAQKRS
510 520 530 540 550
KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR ESSRDTSPVR
560 570 580 590 600
SFQPLGPGYG MSQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
610 620 630 640 650
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE
660 670 680 690 700
VLNRCASSNW SERKEGLLGL QNLLKNQRTL SRVELKRLCE IFTRMFADPH
710 720 730 740 750
GKVFSMFLET LVDFIQVHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ
760 770 780 790 800
KALDVTRESF PNDLQFNILM RFTVDQTQTP SLKVKVAILK YIETLAKQMD
810 820 830 840 850
PGDFINSSET RLAVSRVITW TTEPKSSDVR KAAQSVLISL FELNTPEFTM
860 870 880 890 900
LLGALPKTFQ DGATKLLHNH LRNTGNGTQS SMGSPLTRPT PRSPANWSSP
910 920 930 940 950
LTSPTNTSQN TLSPSAFDYD TENMNSEDIY SSLRGVTEAI QNFSFRSQED
960 970 980 990 1000
MSEPLKRDPK KEDGDTVCSG PGMSDPRAGG DAPDSSQPAL DNKASLLHSV
1010 1020 1030 1040 1050
PLHSSPRSRD YNPYNYSDSI SPFNKSALKE AMFDDDADQF PDDLSLDHSD
1060 1070 1080 1090 1100
LVAELLKELS NHNERIEERK IALYELMKLT QEESFSVWDE HFKTILLLLL
1110 1120 1130 1140 1150
ETLGDKEPTI RALALKVLKE ILRHQPARFK NYAELTVMKT LEAHKDPHKE
1160 1170 1180 1190 1200
VVRSAEEAAS VLATSISPEQ CIKVLCPIIQ TADYPINLAA IKMQTKVIER
1210 1220 1230 1240 1250
VSKETLNLLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH
1260 1270 1280
LSQLTGSKMK LLNLYIKRAQ TGSAGADPTT DVSGQS
Length:1,286
Mass (Da):140,638
Last modified:June 1, 2001 - v1
Checksum:iC1742635DADC3F09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ288060 mRNA. Translation: CAC35166.1.
RefSeqiNP_446174.1. NM_053722.2.
UniGeneiRn.19943.

Genome annotation databases

EnsembliENSRNOT00000012545; ENSRNOP00000012545; ENSRNOG00000009161.
GeneIDi114514.
KEGGirno:114514.
UCSCiRGD:619789. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ288060 mRNA. Translation: CAC35166.1.
RefSeqiNP_446174.1. NM_053722.2.
UniGeneiRn.19943.

3D structure databases

ProteinModelPortaliQ99JD4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250360. 1 interactor.
MINTiMINT-4579893.
STRINGi10116.ENSRNOP00000012545.

PTM databases

iPTMnetiQ99JD4.
PhosphoSitePlusiQ99JD4.

Proteomic databases

PaxDbiQ99JD4.
PRIDEiQ99JD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012545; ENSRNOP00000012545; ENSRNOG00000009161.
GeneIDi114514.
KEGGirno:114514.
UCSCiRGD:619789. rat.

Organism-specific databases

CTDi23122.
RGDi619789. Clasp2.

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
GeneTreeiENSGT00390000001762.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiQ99JD4.
KOiK16578.

Enzyme and pathway databases

ReactomeiR-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-68877. Mitotic Prometaphase.

Miscellaneous databases

PROiQ99JD4.

Gene expression databases

BgeeiENSRNOG00000009161.
ExpressionAtlasiQ99JD4. baseline and differential.
GenevisibleiQ99JD4. RN.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCLAP2_RAT
AccessioniPrimary (citable) accession number: Q99JD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.