Q8BRT1 (CLAP2_MOUSE) 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
Synonyms:	Kiaa0627

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	1286 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole. Golgi apparatus. 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 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 process	Cell cycle Cell division Meiosis Mitosis
Cellular component	Cell membrane Cell projection Centromere Chromosome Cytoplasm Cytoskeleton Golgi apparatus Kinetochore Membrane Microtubule
Coding sequence diversity	Alternative splicing
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 mutant phenotype PubMed 17113391. Source: MGI establishment or maintenance of cell polarity Inferred from mutant phenotype PubMed 17113391. Source: MGI meiosis 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
Cellular_component	Golgi 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 microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell 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_function	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.

Note: Contains a phosphoserine at position 241.

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1286	1286	CLIP-associating protein 2		PRO_0000089850
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
	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	459 – 572	114	Ser-rich
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.12
	Modified residue	376	1	Phosphoserine By similarity
	Modified residue	461	1	Phosphoserine By similarity
	Modified residue	513	1	Phosphoserine Ref.9
	Modified residue	531	1	Phosphoserine By similarity
	Modified residue	535	1	Phosphoserine By similarity
	Modified residue	581	1	Phosphoserine Ref.6
	Modified residue	1021	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 12	12	MRRLI…RICDY → MEPRGAEYFCAQVLQKDVSG RLQAGEELLLCLGTPGAIPD LEDDPSRLAKTVDALTRWVG SSNYRVSLLGLEILSAFVDR LSTRFKSYVTMVTTALIDRM GDVKDKVREEAQNLTLKLMD EVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGT QPLVISKLVPHLCVLFGDSN SQVRNAALSAVVEIYRHVGE KLRIDLCKRDIPPARLEMVL AKFDEVQNSGGMILSVCKD in isoform 2.		VSP_015808
	Alternative sequence	1 – 12	12	MRRLI…RICDY → MAMGDD in isoform 3.		VSP_015809
	Alternative sequence	119 – 173	55	LKKIR…LSTVL → CMSCSLVASEVERALAWPLW SHLATYQHHCHCTLSHEDLP EKRLTSPVSSAFVQH in isoform 3.		VSP_015810
	Alternative sequence	142 – 1054	913	Missing in isoform 2.		VSP_015811
	Alternative sequence	174 – 1286	1113	Missing in isoform 3.		VSP_015812
Experimental info
	Mutagenesis	6	1	C → S: Impairs Golgi localization; when associated with S-10. Ref.1
	Mutagenesis	10	1	C → S: Impairs Golgi localization; when associated with S-6. Ref.1
	Sequence conflict	657	1	S → T in BAC41436. Ref.4
	Sequence conflict	683	1	I → V in BAC41436. Ref.4
	Sequence conflict	699	1	P → L in BAC41436. Ref.4
	Sequence conflict	702	1	K → KR in BAC41436. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 5B208D8F4E90CB93	FASTA	1,286	140,739
	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
	Isoform 2 [UniParc]. Checksum: F7ADD06A38B893D3	FASTA	600	66,370
	10 20 30 40 50 60 MEPRGAEYFC AQVLQKDVSG RLQAGEELLL CLGTPGAIPD LEDDPSRLAK TVDALTRWVG 70 80 90 100 110 120 SSNYRVSLLG LEILSAFVDR LSTRFKSYVT MVTTALIDRM GDVKDKVREE AQNLTLKLMD 130 140 150 160 170 180 EVAPPMYIWE QLASGFKHKN FRSREGVCLC LIETLNIFGT QPLVISKLVP HLCVLFGDSN 190 200 210 220 230 240 SQVRNAALSA VVEIYRHVGE KLRIDLCKRD IPPARLEMVL AKFDEVQNSG GMILSVCKDK 250 260 270 280 290 300 SFDDEESVDG NRPSSAASAF KVPAPKTPGN PVSSARKPGS AGGPKVGGPS KEGGAGAVDE 310 320 330 340 350 360 DDFIKAFTDV PSVQIYSSRE LEETLNKIRE ILSDDKHDWD QRANALKKIR SLLVAGAAQY 370 380 390 400 410 420 DCFFQHLRLL KELSNHNERI EERKIALYEL MKLTQEESFS VWDEHFKTIL LLLLETLGDK 430 440 450 460 470 480 EPTIRALALK VLKEILRHQP ARFKNYAELT VMKTLEAHKD PHKEVVRSAE EAASVLATSI 490 500 510 520 530 540 SPEQCIKVLC PIIQTADYPI NLAAIKMQTK VIERVSKETL NMLLPEIMPG LIQGYDNSES 550 560 570 580 590 600 SVRKACVFCL VAVHAVIGDE LKPHLSQLTG SKMKLLNLYI KRAQTGSAGA DPTADVSGQS
	Isoform 3 [UniParc]. Checksum: 5512515D37A0CF08	FASTA	167	18,021
	10 20 30 40 50 60 MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTPGNPVS SARKPGSAGG PKVGGPSKEG 70 80 90 100 110 120 GAGAVDEDDF IKAFTDVPSV QIYSSRELEE TLNKIREILS DDKHDWDQRA NACMSCSLVA 130 140 150 160 SEVERALAWP LWSHLATYQH HCHCTLSHED LPEKRLTSPV SSAFVQH

References

	« Hide 'large scale' referencesShow '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. , 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581, MASS SPECTROMETRY. 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]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Liver.
[11]	"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.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Melanoma.
+	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.
IPI	IPI00654284. IPI00875254. IPI00985608.
UniGene	Mm.222272.
3D structure databases
ProteinModelPortal	Q8BRT1.
SMR	Q8BRT1. Positions 1096-1123.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BRT1. 4 interactions.
PTM databases
PhosphoSite	Q8BRT1.
Proteomic databases
PaxDb	Q8BRT1.
PRIDE	Q8BRT1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc009rwt.1. mouse. uc009rwv.1. mouse.
Organism-specific databases
MGI	MGI:1923749. Clasp2.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG81443.
HOGENOM	HOG000185856.
HOVERGEN	HBG079692.
Gene expression databases
CleanEx	MM_CLASP2.
Genevestigator	Q8BRT1.
GermOnline	ENSMUSG00000033392. Mus musculus.
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
SOURCE	Search...

Entry information

Entry name

CLAP2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program