Reviewed,
UniProtKB/Swiss-Prot Q7Z460 (CLAP1_HUMAN)
Last modified
February 9, 2010.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: CLIP-associating protein 1 Alternative name(s): Cytoplasmic linker-associated protein 1 Multiple asters homolog 1 Protein Orbit homolog 1 Short name=hOrbit1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1538 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. 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. Ref.4 Ref.7 Ref.10 Ref.12 Ref.13 |
| Subunit structure | Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules, PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2. Ref.4 Ref.10 Ref.9 Ref.11 |
| Subcellular location | Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Kinetochore. Cytoplasm › cytoskeleton › spindle. 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. Ref.4 Ref.7 Ref.10 Ref.13 Ref.9 Ref.11 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 |
| Sequence similarities | Belongs to the CLASP family. Contains 7 HEAT repeats. |
| Sequence caution | The sequence AAX88872.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Clip2 | O55156 | 3 | EBI-913476,EBI-349416 | From a different organism. |
| Rsn | Q9JK25 | 2 | EBI-913476,EBI-908338 | From a different organism. |
| YWHAG | P61981 | 1 | EBI-913476,EBI-359832 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q7Z460-1) 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: Q7Z460-2) The sequence of this isoform differs from the canonical sequence as follows: 737-772: Missing. 808-808: L → LLLGDSRSK 1123-1161: Missing. | ||||||
| Isoform 3 (identifier: Q7Z460-3) The sequence of this isoform differs from the canonical sequence as follows: 737-772: Missing. 808-808: L → LLLGDSRSK 911-911: K → KIADSEAECEDKEGNLFPSEVSCT 1123-1161: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1538 | 1538 | CLIP-associating protein 1 | PRO_0000089847 | |||||
Regions | |||||||||
| Repeat | 87 – 124 | 38 | HEAT 1 | ||||||
| Repeat | 163 – 200 | 38 | HEAT 2 | ||||||
| Repeat | 405 – 440 | 36 | HEAT 3 | ||||||
| Repeat | 441 – 477 | 37 | HEAT 4 | ||||||
| Repeat | 974 – 1011 | 38 | HEAT 5 | ||||||
| Repeat | 1342 – 1379 | 38 | HEAT 6 | ||||||
| Repeat | 1460 – 1497 | 38 | HEAT 7 | ||||||
| Region | 662 – 785 | 124 | Interaction with microtubules, MAPRE1 and MAPRE3 | ||||||
| Region | 1254 – 1538 | 285 | Interaction with CLIP2 By similarity | ||||||
| Region | 1254 – 1538 | 285 | Interaction with PHLDB2 and RSN | ||||||
| Region | 1256 – 1538 | 283 | Localization to kinetochores | ||||||
| Coiled coil | 1299 – 1330 | 32 | Potential | ||||||
| Compositional bias | 530 – 765 | 236 | Ser-rich | ||||||
| Compositional bias | 1526 – 1532 | 7 | Poly-Ser | ||||||
Amino acid modifications | |||||||||
| Modified residue | 545 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 559 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 568 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 594 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 598 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 600 | 1 | Phosphoserine Ref.17 Ref.19 Ref.21 | ||||||
| Modified residue | 609 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 636 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 646 | 1 | Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21 | ||||||
| Modified residue | 647 | 1 | Phosphoserine Ref.17 Ref.19 | ||||||
| Modified residue | 649 | 1 | Phosphoserine Ref.17 Ref.19 | ||||||
| Modified residue | 651 | 1 | Phosphothreonine Ref.19 | ||||||
| Modified residue | 656 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 688 | 1 | Phosphoserine Ref.17 Ref.21 | ||||||
| Modified residue | 695 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 711 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 714 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 797 | 1 | Phosphoserine Ref.19 Ref.21 | ||||||
| Modified residue | 1091 | 1 | Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21 | ||||||
| Modified residue | 1099 | 1 | Phosphothreonine Ref.16 Ref.17 | ||||||
| Modified residue | 1196 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1223 | 1 | Phosphoserine Ref.8 | ||||||
Natural variations | |||||||||
| Alternative sequence | 737 – 772 | 36 | Missing in isoform 2 and isoform 3. | VSP_022386 | |||||
| Alternative sequence | 808 | 1 | L → LLLGDSRSK in isoform 2 and isoform 3. | VSP_022387 | |||||
| Alternative sequence | 911 | 1 | K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3. | VSP_022388 | |||||
| Alternative sequence | 1123 – 1161 | 39 | Missing in isoform 2 and isoform 3. | VSP_022389 | |||||
| Natural variant | 233 | 1 | I → T: dbSNP rs17761055. | VAR_053818 | |||||
Experimental info | |||||||||
| Sequence conflict | 251 | 1 | R → G in CAI46251. Ref.5 | ||||||
| Sequence conflict | 556 | 1 | S → F in CAI46251. Ref.5 | ||||||
Sequences
| ||||||||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Full length cDNA of a human homologue of Drosophila melanogaster multiple asters (MAST) gene." Maiato H., Sunkel C.E., Earnshaw W.C. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). |
| [2] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2). Tissue: Eye. |
| [4] | "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: 11290329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-266, FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, INTERACTION WITH CLIP2; MICROTUBULES AND RSN. Tissue: Brain. |
| [5] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3). Tissue: Testis. |
| [6] | "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-1538. Tissue: Brain. |
| [7] | "Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics." Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E., Earnshaw W.C. Cell 113:891-904(2003) [PubMed: 12837247] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [8] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609 AND SER-1223, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "Microtubule bundle formation and cell death induced by the human CLASP/Orbit N-terminal fragment." Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N., Matsukage A. Cell Struct. Funct. 30:7-13(2005) [PubMed: 16145243] [Abstract] Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION. |
| [10] | "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex." Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C., Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A. J. Cell Biol. 168:141-153(2005) [PubMed: 15631994] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, SUBCELLULAR LOCATION. |
| [11] | "CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta." Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S., Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F., Akhmanova A. Dev. Cell 11:21-32(2006) [PubMed: 16824950] [Abstract] Cited for: INTERACTION WITH ERC1 AND PHLDB2, SUBCELLULAR LOCATION. |
| [12] | "Mammalian CLASPs are required for mitotic spindle organization and kinetochore alignment." Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A., Tsukita S., Vorobjev I. Genes Cells 11:845-857(2006) [PubMed: 16866869] [Abstract] Cited for: FUNCTION. |
| [13] | "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: 16914514] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [14] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-568, MASS SPECTROMETRY. |
| [15] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, MASS SPECTROMETRY. Tissue: Platelet. |
| [16] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-1091 AND THR-1099, MASS SPECTROMETRY. |
| [17] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-647; SER-649; THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [19] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; SER-600; SER-646; SER-647; SER-649; THR-651; SER-797 AND SER-1091, MASS SPECTROMETRY. |
| [20] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, MASS SPECTROMETRY. |
| [21] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-636; SER-646; SER-688; SER-797 AND SER-1091, MASS SPECTROMETRY. Tissue: T-cell. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF347693 mRNA. Translation: AAQ15051.1. AC013399 Genomic DNA. Translation: AAX88872.1. Sequence problems. AC012447 Genomic DNA. No translation available. AC079449 Genomic DNA. No translation available. BC032563 mRNA. Translation: AAH32563.1. Different initiation. BC112940 mRNA. Translation: AAI12941.1. AJ288057 mRNA. Translation: CAC35156.1. CR933722 mRNA. Translation: CAI46251.1. AB014522 mRNA. Translation: BAA31597.1. |
| IPI | IPI00396279. IPI00744551. IPI00828013. |
| PIR | T00387. |
| RefSeq | NP_001135745.1. NP_001135746.1. NP_056097.1. |
| UniGene | Hs.469840 Hs.708183 |
3D structure databases | |
| SMR | Q7Z460. Positions 15-223, 20-498, 1306-1524. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q7Z460. 4 interactions. |
| STRING | Q7Z460. |
PTM databases | |
| PhosphoSite | Q7Z460. |
Proteomic databases | |
| PRIDE | Q7Z460. |
Genome annotation databases | |
| Ensembl | ENST00000263710; ENSP00000263710; ENSG00000074054; Homo sapiens. [Genome view] |
| GeneID | 23332. |
| KEGG | hsa:23332. |
Organism-specific databases | |
| CTD | 23332. |
| GeneCards | GC02M121811. |
| H-InvDB | HIX0002422. |
| HGNC | HGNC:17088. CLASP1. |
| MIM | 605852. gene. |
| PharmGKB | PA38436. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | HBG714912. |
| HOVERGEN | Q7Z460. |
| InParanoid | Q7Z460. |
| OMA | IHKDDLQ. |
| PhylomeDB | Q7Z460. |
Enzyme and pathway databases | |
| Reactome | REACT_152. Cell Cycle, Mitotic. REACT_18266. Axon guidance. |
Gene expression databases | |
| ArrayExpress | Q7Z460. |
| Bgee | Q7Z460. |
| CleanEx | HS_CLASP1. HS_MAST1. |
| Genevestigator | Q7Z460. |
| GermOnline | ENSG00000074054. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000357. HEAT. IPR021133. HEAT_type_2. [Graphical view] |
| Gene3D | G3DSA:1.25.10.10. ARM-like. 1 hit. |
| Pfam | PF02985. HEAT. 2 hits. [Graphical view] |
| PROSITE | PS50077. HEAT_REPEAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 45259. |
| PMAP-CutDB | Q7Z460. |
| SOURCE | Search... |
Entry information
| Entry name | CLAP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q7Z460 Secondary accession number(s): O75118 Q9BQT5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


