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Protein

CLIP-associating protein 2

Gene

Clasp2

Organism
Mus musculus (Mouse)
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 similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Gene namesi
Name:Clasp2
Synonyms:Kiaa0627
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1923749. Clasp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61C → S: Impairs Golgi localization; when associated with S-10. 1 Publication
Mutagenesisi10 – 101C → S: Impairs Golgi localization; when associated with S-6. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12861286CLIP-associating protein 2PRO_0000089850Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei374 – 3741PhosphoserineCombined sources
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity
Modified residuei531 – 5311PhosphoserineBy similarity
Modified residuei535 – 5351PhosphoserineBy similarity
Modified residuei581 – 5811PhosphoserineBy similarity
Modified residuei620 – 6201PhosphoserineCombined sources
Modified residuei947 – 9471PhosphoserineCombined sources
Modified residuei1021 – 10211PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. Isoform 2 is phosphorylated on Ser-241.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BRT1.
MaxQBiQ8BRT1.
PaxDbiQ8BRT1.
PRIDEiQ8BRT1.

PTM databases

iPTMnetiQ8BRT1.
PhosphoSiteiQ8BRT1.

Expressioni

Tissue specificityi

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

Developmental stagei

Expressed in oocytes and early embryos.1 Publication

Gene expression databases

CleanExiMM_CLASP2.

Interactioni

Subunit structurei

Interacts with microtubules (PubMed:11290329). Interacts with MAPRE1; probably required for targeting to growing microtubule plus ends. Interacts with ERC1, MAPRE3 and PHLDB2. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP2 to Golgi membranes (By similarity). Interacts with CLIP2 and RSN (PubMed:11290329). Interacts with MACF1 (PubMed:18854161).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi218155. 7 interactions.
IntActiQ8BRT1. 5 interactions.
MINTiMINT-4112101.
STRINGi10090.ENSMUSP00000130201.

Structurei

Secondary structure

1
1286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi648 – 6558Combined sources
Helixi660 – 67516Combined sources
Helixi682 – 69514Combined sources
Helixi701 – 71818Combined sources
Helixi719 – 7213Combined sources
Turni723 – 7253Combined sources
Helixi726 – 73712Combined sources
Helixi743 – 75917Combined sources
Helixi762 – 77413Combined sources
Beta strandi776 – 7783Combined sources
Helixi782 – 79615Combined sources
Helixi801 – 8033Combined sources
Helixi808 – 82013Combined sources
Helixi827 – 84317Combined sources
Helixi845 – 8539Combined sources
Helixi857 – 86711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WOZX-ray2.20A/B/C/D642-873[»]
ProteinModelPortaliQ8BRT1.
SMRiQ8BRT1. Positions 69-314, 643-871.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati179 – 21436HEAT 1Sequence analysisAdd
BLAST
Repeati215 – 25137HEAT 2Sequence analysisAdd
BLAST
Repeati256 – 29338HEAT 3Sequence analysisAdd
BLAST
Repeati702 – 73938HEAT 4Sequence analysisAdd
BLAST
Repeati764 – 80138HEAT 5Sequence analysisAdd
BLAST
Repeati1046 – 108338HEAT 6Sequence analysisAdd
BLAST
Repeati1090 – 112738HEAT 7Sequence analysisAdd
BLAST
Repeati1208 – 124538HEAT 8Sequence analysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4040Golgi localizationAdd
BLAST
Regioni66 – 317252TOG 1By similarityAdd
BLAST
Regioni450 – 565116Interaction with microtubules, MAPRE1 and MAPRE3By similarityAdd
BLAST
Regioni642 – 873232TOG 2By similarityAdd
BLAST
Regioni864 – 1286423Interaction with RSN and localization to the Golgi and kinetochoresBy similarityAdd
BLAST
Regioni1009 – 1286278Required for cortical localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi500 – 5034SXIP motif 1; mediates interaction with MAPRE1 and targeting to microtubule plus endsBy similarity
Motifi523 – 5264SXIP motif 2; mediates interaction with MAPRE1 and targeting to microtubule plus endsBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi459 – 572114Ser-richAdd
BLAST

Domaini

The two SXIP sequence motifs mediate interaction with MAPRE1; this is necessary for targeting to growing microtubule plus ends.By similarity
Two TOG regions display structural characteristics similar to HEAT repeat domains and mediate interaction with microtubules.By similarity1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
HOGENOMiHOG000185856.
HOVERGENiHBG079692.
InParanoidiQ8BRT1.
KOiK16578.
PhylomeDBiQ8BRT1.

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. 4 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BRT1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK
60 70 80 90 100
PGSAGGPKVG GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS 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
STVAGRVSVG GSKANPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR
410 420 430 440 450
LGAGALNPGS YASLEDTSDK MDGTASDDGR VRAKLSTPLV AVGNAKTDSR
460 470 480 490 500
GRSRTKMVSQ SQPGSRSGSP GRVLTTTALS TVSSGAQRVL VNSASAQKRS
510 520 530 540 550
KIPRSQGCSR EASPSRLSVA RSSRIPRPSV SQGCSREASR ESSRDTSPVR
560 570 580 590 600
SFQPLGPGYG ISQSSRLSSS VSAMRVLNTG SDVEEAVADA LLLGDIRTKK
610 620 630 640 650
KPARRRYESY GMHSDDDANS DASSACSERS YSSRNGSIPT YMRQTEDVAE
660 670 680 690 700
VLNRCASSNW SERKEGLLGL QNLLKNQRTL SRIELKRLCE IFTRMFADPH
710 720 730 740 750
GKVFSMFLET LVDFIQVHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ
760 770 780 790 800
KALDITRESF PNDLQFNILM RFTVDQTQTP SLKVKVAILK YIETLAKQMD
810 820 830 840 850
PRDFTNSSET 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
MSEPVRRDPK KEDGDTICSG PGMSDPRAGG DAADGSQPAL DNKASLLHSM
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
VSKETLNMLL PEIMPGLIQG YDNSESSVRK ACVFCLVAVH AVIGDELKPH
1260 1270 1280
LSQLTGSKMK LLNLYIKRAQ TGSAGADPTA DVSGQS
Length:1,286
Mass (Da):140,739
Last modified:March 1, 2003 - v1
Checksum:i5B208D8F4E90CB93
GO
Isoform 2 (identifier: Q8BRT1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRRLICKRICDY → MEPRGAEYFC...GGMILSVCKD
     142-1054: Missing.

Show »
Length:600
Mass (Da):66,370
Checksum:iF7ADD06A38B893D3
GO
Isoform 3 (identifier: Q8BRT1-6) [UniParc]FASTAAdd to basket

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.

Show »
Length:167
Mass (Da):18,021
Checksum:i5512515D37A0CF08
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti657 – 6571S → T in BAC41436 (PubMed:12465718).Curated
Sequence conflicti683 – 6831I → V in BAC41436 (PubMed:12465718).Curated
Sequence conflicti699 – 6991P → L in BAC41436 (PubMed:12465718).Curated
Sequence conflicti702 – 7021K → KR in BAC41436 (PubMed:12465718).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212MRRLI…RICDY → MEPRGAEYFCAQVLQKDVSG RLQAGEELLLCLGTPGAIPD LEDDPSRLAKTVDALTRWVG SSNYRVSLLGLEILSAFVDR LSTRFKSYVTMVTTALIDRM GDVKDKVREEAQNLTLKLMD EVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGT QPLVISKLVPHLCVLFGDSN SQVRNAALSAVVEIYRHVGE KLRIDLCKRDIPPARLEMVL AKFDEVQNSGGMILSVCKD in isoform 2. 1 PublicationVSP_015808Add
BLAST
Alternative sequencei1 – 1212MRRLI…RICDY → MAMGDD in isoform 3. 2 PublicationsVSP_015809Add
BLAST
Alternative sequencei119 – 17355LKKIR…LSTVL → CMSCSLVASEVERALAWPLW SHLATYQHHCHCTLSHEDLP EKRLTSPVSSAFVQH in isoform 3. 2 PublicationsVSP_015810Add
BLAST
Alternative sequencei142 – 1054913Missing in isoform 2. 1 PublicationVSP_015811Add
BLAST
Alternative sequencei174 – 12861113Missing in isoform 3. 2 PublicationsVSP_015812Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52948.1. [Q8BRT1-1]
RefSeqiNP_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. [Q8BRT1-6]
UniGeneiMm.222272.

Genome annotation databases

GeneIDi76499.
KEGGimmu:76499.
UCSCiuc009rwt.2. mouse. [Q8BRT1-6]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52948.1. [Q8BRT1-1]
RefSeqiNP_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. [Q8BRT1-6]
UniGeneiMm.222272.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WOZX-ray2.20A/B/C/D642-873[»]
ProteinModelPortaliQ8BRT1.
SMRiQ8BRT1. Positions 69-314, 643-871.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218155. 7 interactions.
IntActiQ8BRT1. 5 interactions.
MINTiMINT-4112101.
STRINGi10090.ENSMUSP00000130201.

PTM databases

iPTMnetiQ8BRT1.
PhosphoSiteiQ8BRT1.

Proteomic databases

EPDiQ8BRT1.
MaxQBiQ8BRT1.
PaxDbiQ8BRT1.
PRIDEiQ8BRT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76499.
KEGGimmu:76499.
UCSCiuc009rwt.2. mouse. [Q8BRT1-6]

Organism-specific databases

CTDi23122.
MGIiMGI:1923749. Clasp2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2956. Eukaryota.
ENOG410ZMY0. LUCA.
HOGENOMiHOG000185856.
HOVERGENiHBG079692.
InParanoidiQ8BRT1.
KOiK16578.
PhylomeDBiQ8BRT1.

Miscellaneous databases

PROiQ8BRT1.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CLASP2.

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. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-374; SER-376; SER-620 AND SER-947, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "CLASP2 has two distinct TOG domains that contribute differently to microtubule dynamics."
    Maki T., Grimaldi A.D., Fuchigami S., Kaverina I., Hayashi I.
    J. Mol. Biol. 427:2379-2395(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 642-873, DOMAIN.

Entry informationi

Entry nameiCLAP2_MOUSE
AccessioniPrimary (citable) accession number: Q8BRT1
Secondary accession number(s): Q8CHE3, Q99JI3, Q9DB80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.