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Q80TV8 (CLAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CLIP-associating protein 1
Alternative name(s):
Cytoplasmic linker-associated protein 1
Gene names
Name:Clasp1
Synonyms:Kiaa0622
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1535 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 By similarity.

Subunit structure

Interacts with ERC1, MAPRE1, MAPRE3, microtubules, and PHLDB2. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP1 to Golgi membranes By similarity. Interacts with CLIP2 and RSN. Interacts with MACF1. Ref.2 Ref.8

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle By similarity. Golgi apparatustrans-Golgi network By similarity. Note: Localizes to microtubule plus ends By similarity. Localizes to centrosomes, kinetochores and the mitotic spindle from prometaphase By similarity. Subsequently localizes to the spindle midzone from anaphase and to the midbody from telophase By similarity. In migrating cells localizes to the plus ends of microtubules within the cell body and to the entire microtubule lattice within the lamella By similarity. Localizes to the cell cortex and this requires ERC1 and PHLDB2 By similarity.

Tissue specificity

Highly expressed in brain and heart and at lower levels in kidney, lung, skeletal muscle and testis. Ref.2

Sequence similarities

Belongs to the CLASP family.

Contains 7 HEAT repeats.

Sequence caution

The sequence BAB24639.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC38020.1 differs from that shown. Reason: Intron retention.

Ontologies

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

Inferred from sequence orthology PubMed 21822276. Source: MGI

establishment of spindle orientation

Inferred from sequence orthology PubMed 21822276. Source: MGI

exit from mitosis

Inferred from electronic annotation. Source: Ensembl

microtubule anchoring

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from electronic annotation. Source: Ensembl

microtubule nucleation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule organizing center organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of microtubule depolymerization

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosomal corona

Inferred from electronic annotation. Source: Ensembl

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cortical microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasmic microtubule

Inferred from direct assay Ref.2. Source: MGI

kinetochore microtubule

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmicrotubule binding

Inferred from direct assay Ref.2. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Clip2O551563EBI-908322,EBI-349416From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80TV8-1)

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: Q80TV8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     770-770: L → LASRRHSRSTSALSTAESVGQS
     805-805: L → LLLGDARSK
     1120-1158: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15351535CLIP-associating protein 1
PRO_0000272274

Regions

Repeat87 – 12438HEAT 1
Repeat163 – 20038HEAT 2
Repeat405 – 44036HEAT 3
Repeat441 – 47737HEAT 4
Repeat971 – 100838HEAT 5
Repeat1339 – 137638HEAT 6
Repeat1457 – 149438HEAT 7
Region662 – 782121Interaction with microtubules, MAPRE1 and MAPRE3 By similarity
Region1251 – 1535285Interaction with CLIP2 and RSN
Region1251 – 1535285Interaction with PHLDB2 By similarity
Region1253 – 1535283Localization to kinetochores By similarity
Coiled coil1296 – 132732 Potential
Compositional bias530 – 762233Ser-rich

Amino acid modifications

Modified residue6001Phosphoserine By similarity
Modified residue6461Phosphoserine By similarity
Modified residue6491Phosphoserine By similarity
Modified residue6561Phosphothreonine By similarity
Modified residue6841Phosphoserine By similarity
Modified residue6881Phosphoserine By similarity
Modified residue6951Phosphoserine By similarity
Modified residue7081Phosphothreonine By similarity
Modified residue7111Phosphoserine By similarity
Modified residue7941Phosphoserine By similarity
Modified residue10881Phosphoserine By similarity
Modified residue10961Phosphothreonine By similarity
Modified residue11931Phosphoserine By similarity
Modified residue12201Phosphoserine Ref.7

Natural variations

Alternative sequence7701L → LASRRHSRSTSALSTAESVG QS in isoform 2.
VSP_022390
Alternative sequence8051L → LLLGDARSK in isoform 2.
VSP_022391
Alternative sequence1120 – 115839Missing in isoform 2.
VSP_022392

Experimental info

Sequence conflict12311I → K in BAB24639. Ref.3
Sequence conflict14171P → S in AAH75708. Ref.5

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: 5EE40CCE493C64D2

FASTA1,535169,227
        10         20         30         40         50         60 
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDRQKSADL EHDQTLLDKL VDGLATSWVN 

        70         80         90        100        110        120 
SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD 

       130        140        150        160        170        180 
QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN 

       190        200        210        220        230        240 
SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANEKN 

       250        260        270        280        290        300 
FDDEDSVDGN RPSSASSSSS KAPSSSRRNV NLGTTRRLMS SSLGSKSSAA KEGAGAVDEE 

       310        320        330        340        350        360 
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD 

       370        380        390        400        410        420 
NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN 

       430        440        450        460        470        480 
SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL 

       490        500        510        520        530        540 
ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL 

       550        560        570        580        590        600 
KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTASR GSTVSTKSVS TTGSLQRSRS 

       610        620        630        640        650        660 
DIDVNAAASA KSKVSSSSGS PAFSSAAALP PGSYASLGRI RTRRQSSGST TNVASTPDSR 

       670        680        690        700        710        720 
GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGLAGG SSRGPPVTPS SEKRSKIPRS 

       730        740        750        760        770        780 
QGCSRETSPN RIGLARSSRI PRPSMSQGCS RDTSRESSRD TSPARGFTPL DRFGLGQSGR 

       790        800        810        820        830        840 
IPGSVNAMRV LSTSTDLEAA VADALKKPVR RRYEPYGMYS DDDANSDASS VCSERSYGSR 

       850        860        870        880        890        900 
NGGIPHYLRQ TEDVAEVLNH CASSNWSERK EGLLGLQNLL KSQRTLSRVE LKRLCEIFTR 

       910        920        930        940        950        960 
MFADPHSKRV FSMFLETLVD FIIIHKDDLQ DWLFVLLTQL LKKMGADLLG SVQAKVQKAL 

       970        980        990       1000       1010       1020 
DVTRDSFPFD QQFNILMRFI VDQTQTPNLK VKVAILKYIE SLARQMDPTD FVNSSETRLA 

      1030       1040       1050       1060       1070       1080 
VSRIITWTTE PKSSDVRKAA QIVLISLFEL NTPEFTMLLG ALPKTFQDGA TKLLHNHLKN 

      1090       1100       1110       1120       1130       1140 
SSNTGVGSPS NTIGRTPSRH PSSRTSPLTS PTNCSHGGLS PSRLWGWSAD GLSKPPPPFS 

      1150       1160       1170       1180       1190       1200 
QPNSIPTAPS HKTLRRSYSP SMLDYDTENL NSEEIYSSLR GVTEAIEKFS FRSQEDLNEP 

      1210       1220       1230       1240       1250       1260 
IKRDGKKDCD IVSRDGGAAS PATEGRGGSE IEGGRMALDN KTSLLNTQPP RAFPGPRARE 

      1270       1280       1290       1300       1310       1320 
YNPYPYSDTI NTYDKTALKE AVFDDDMEQL RDVPIDHSDL VADLLKELSN HNERVEERKG 

      1330       1340       1350       1360       1370       1380 
ALLELLKITR EDSLGVWEEH FKTILLLLLE TLGDKDHSIR ALALRVLREI LRNQPARFKN 

      1390       1400       1410       1420       1430       1440 
YAELTIMKTL EAHKDSHKEV VRAAEEAAST LASSIHPEQC IKVLCPIIQT ADYPINLAAI 

      1450       1460       1470       1480       1490       1500 
KMQTKVVERI TKESLLQLLV DIIPGLLQGY DNTESSVRKA SVFCLVAIYS VIGEDLKPHL 

      1510       1520       1530 
AQLTGSKMKL LNLYIKRAQT TNSNSSSSSD VSTHS 

« Hide

Isoform 2 [UniParc].

Checksum: CA1BA686C4C8CB03
Show »

FASTA1,525167,939

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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] OF 1-306 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1535 (ISOFORMS 1/2), INTERACTION WITH CLIP2 AND RSN, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"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] OF 1-393 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1535 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Embryo and Testis.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 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., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1535 (ISOFORM 2).
Tissue: Brain.
[5]"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] OF 985-1535 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 997-1535 (ISOFORM 2).
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Salivary gland.
[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]"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-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"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
AC109294 Genomic DNA. No translation available.
AC131804 Genomic DNA. No translation available.
AC136636 Genomic DNA. No translation available.
AJ276962 mRNA. Translation: CAC35162.1.
AJ288061 mRNA. Translation: CAC35163.1.
AK006534 mRNA. Translation: BAB24639.2. Different initiation.
AK080782 mRNA. Translation: BAC38020.1. Sequence problems.
AK122330 mRNA. Translation: BAC65612.1.
BC057312 mRNA. Translation: AAH57312.1.
BC075708 mRNA. Translation: AAH75708.1.
BC094554 mRNA. Translation: AAH94554.1.
RefSeqNP_083985.2. NM_029709.2.
NP_808216.2. NM_177548.2.
UniGeneMm.138740.

3D structure databases

ProteinModelPortalQ80TV8.
SMRQ80TV8. Positions 5-227, 296-538, 1318-1394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80TV8. 6 interactions.
MINTMINT-4123448.
STRING10090.ENSMUSP00000042266.

PTM databases

PhosphoSiteQ80TV8.

Proteomic databases

PaxDbQ80TV8.
PRIDEQ80TV8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID76707.
KEGGmmu:76707.

Organism-specific databases

CTD23332.
MGIMGI:1923957. Clasp1.
RougeSearch...

Phylogenomic databases

eggNOGNOG81443.
HOVERGENHBG079692.
InParanoidQ80TV8.
KOK16578.
PhylomeDBQ80TV8.

Gene expression databases

ArrayExpressQ80TV8.
BgeeQ80TV8.
CleanExMM_CLASP1.
GenevestigatorQ80TV8.

Family and domain databases

Gene3D1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028399. CLASP_metazoan.
IPR024395. CLASP_N_dom.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERPTHR21567:SF11. PTHR21567:SF11. 1 hit.
PfamPF12348. CLASP_N. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
PROSITEPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio345659.
PROQ80TV8.
SOURCESearch...

Entry information

Entry nameCLAP1_MOUSE
AccessionPrimary (citable) accession number: Q80TV8
Secondary accession number(s): Q505G6 expand/collapse secondary AC list , Q6DI75, Q6PG14, Q8BNS4, Q99JH5, Q99JI2, Q9CVU1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 82 of the entry and version 2 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