Q99JD4 (CLAP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CLIP-associating protein 2

Alternative name(s):
Cytoplasmic linker-associated protein 2

Gene names

Name:

Clasp2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1286 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. Golgi apparatus By similarity. Golgi apparatus › trans-Golgi network By similarity. Cell membrane By similarity. Cell projection › ruffle 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 process	Cell cycle Cell division Mitosis
Cellular component	Cell membrane Cell projection Centromere Chromosome Cytoplasm Cytoskeleton Golgi apparatus Kinetochore Membrane Microtubule
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW cell migration Inferred from electronic annotation. Source: Compara establishment or maintenance of cell polarity Inferred from electronic annotation. Source: Compara 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: RGD
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic microtubule Inferred from electronic annotation. Source: Compara microtubule Inferred from direct assay Ref.1. Source: RGD microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell 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_function	microtubule plus-end binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1286	1286	CLIP-associating protein 2		PRO_0000089851
Regions
	Repeat	179 – 214	36	HEAT 1
	Repeat	215 – 251	37	HEAT 2
	Repeat	764 – 801	38	HEAT 3
	Repeat	1090 – 1127	38	HEAT 4
	Repeat	1208 – 1245	38	HEAT 5
	Region	1 – 40	40	Golgi localization By similarity
	Region	450 – 565	116	Interaction with microtubules, MAPRE1 and MAPRE3 By similarity
	Region	864 – 1286	423	Interaction with RSN and localization to the Golgi and kinetochores By similarity
	Region	1009 – 1286	278	Required for cortical localization By similarity
	Coiled coil	1047 – 1076	30	Potential
	Motif	500 – 503	4	Microtubule tip localization signal
	Motif	523 – 526	4	Microtubule tip localization signal
	Compositional bias	316 – 572	257	Ser-rich
	Compositional bias	1096 – 1100	5	Poly-Leu
Amino acid modifications
	Modified residue	14	1	Phosphoserine By similarity
	Modified residue	376	1	Phosphoserine By similarity
	Modified residue	461	1	Phosphoserine By similarity
	Modified residue	513	1	Phosphoserine By similarity
	Modified residue	531	1	Phosphoserine By similarity
	Modified residue	535	1	Phosphoserine By similarity
	Modified residue	581	1	Phosphoserine By similarity
	Modified residue	1021	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99JD4 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: C1742635DADC3F09	FASTA	1,286	140,638
	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

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.
IPI	IPI00195046.
RefSeq	NP_446174.1. NM_053722.2.
UniGene	Rn.19943.
3D structure databases
ProteinModelPortal	Q99JD4.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000063775.
PTM databases
PhosphoSite	Q99JD4.
Proteomic databases
PaxDb	Q99JD4.
PRIDE	Q99JD4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000012545; ENSRNOP00000012545; ENSRNOG00000009161.
GeneID	114514.
KEGG	rno:114514.
UCSC	RGD:619789. rat.
Organism-specific databases
CTD	23122.
RGD	619789. Clasp2.
Phylogenomic databases
eggNOG	NOG81443.
GeneTree	ENSGT00390000001762.
HOGENOM	HOG000236347.
HOVERGEN	HBG079692.
InParanoid	Q99JD4.
KO	K16578.
Gene expression databases
ArrayExpress	Q99JD4.
Genevestigator	Q99JD4.
GermOnline	ENSRNOG00000009161. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR024395. CLASP_N_dom. [Graphical view]
Pfam	PF12348. CLASP_N. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	618631.

Entry information

Entry name

CLAP2_RAT

Accession

Primary (citable) accession number: Q99JD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program