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Q7Z460

- CLAP1_HUMAN

UniProt

Q7Z460 - CLAP1_HUMAN

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Protein

CLIP-associating protein 1

Gene
CLASP1, KIAA0622, MAST1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.6 Publications

GO - Molecular functioni

  1. kinetochore binding Source: UniProtKB
  2. microtubule binding Source: UniProtKB
  3. microtubule plus-end binding Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell division Source: MGI
  3. establishment of spindle orientation Source: MGI
  4. establishment or maintenance of cell polarity Source: UniProtKB
  5. exit from mitosis Source: UniProtKB
  6. G2/M transition of mitotic cell cycle Source: Reactome
  7. microtubule anchoring Source: UniProtKB
  8. microtubule bundle formation Source: UniProtKB
  9. microtubule cytoskeleton organization Source: UniProtKB
  10. microtubule nucleation Source: UniProtKB
  11. microtubule organizing center organization Source: UniProtKB
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of microtubule depolymerization Source: UniProtKB
  14. negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CLASP1
Synonyms:KIAA0622, MAST1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17088. CLASP1.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Golgi apparatustrans-Golgi network Inferred
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 PHLDB2.7 Publications

GO - Cellular componenti

  1. cell cortex Source: MGI
  2. centrosomal corona Source: UniProtKB
  3. centrosome Source: UniProtKB
  4. condensed chromosome kinetochore Source: UniProtKB-SubCell
  5. cortical microtubule cytoskeleton Source: UniProtKB
  6. cytoplasmic microtubule Source: UniProtKB
  7. cytosol Source: Reactome
  8. extracellular vesicular exosome Source: UniProt
  9. Golgi apparatus Source: UniProtKB
  10. kinetochore Source: UniProtKB
  11. kinetochore microtubule Source: UniProtKB
  12. spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Kinetochore, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15381538CLIP-associating protein 1PRO_0000089847Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei600 – 6001Phosphoserine3 Publications
Modified residuei646 – 6461Phosphoserine4 Publications
Modified residuei649 – 6491Phosphoserine1 Publication
Modified residuei656 – 6561Phosphothreonine1 Publication
Modified residuei684 – 6841Phosphoserine1 Publication
Modified residuei688 – 6881Phosphoserine2 Publications
Modified residuei695 – 6951Phosphoserine1 Publication
Modified residuei711 – 7111Phosphothreonine1 Publication
Modified residuei714 – 7141Phosphoserine1 Publication
Modified residuei797 – 7971Phosphoserine1 Publication
Modified residuei1091 – 10911Phosphoserine2 Publications
Modified residuei1099 – 10991Phosphothreonine1 Publication
Modified residuei1196 – 11961Phosphoserine1 Publication
Modified residuei1223 – 12231Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7Z460.
PaxDbiQ7Z460.
PRIDEiQ7Z460.

PTM databases

PhosphoSiteiQ7Z460.

Miscellaneous databases

PMAP-CutDBQ7Z460.

Expressioni

Gene expression databases

ArrayExpressiQ7Z460.
BgeeiQ7Z460.
CleanExiHS_CLASP1.
HS_MAST1.
GenevestigatoriQ7Z460.

Interactioni

Subunit structurei

Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules, PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2. Interacts with GCC2; recruits CLASP1 to Golgi membranes. Interacts with MACF1 By similarity.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Clip1Q9JK252EBI-913476,EBI-908338From a different organism.
Clip2O551563EBI-913476,EBI-349416From a different organism.
KIF1BO603333EBI-913476,EBI-465633
SPAG5Q96R063EBI-913476,EBI-413317

Protein-protein interaction databases

BioGridi116919. 10 interactions.
IntActiQ7Z460. 13 interactions.
MINTiMINT-1683081.
STRINGi9606.ENSP00000263710.

Structurei

Secondary structure

1
1538
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi297 – 30610
Helixi317 – 33115
Helixi338 – 35316
Helixi356 – 3583
Helixi362 – 3676
Helixi370 – 3778
Helixi382 – 39918
Helixi400 – 4034
Helixi404 – 41512
Turni416 – 4194
Helixi423 – 43917
Helixi445 – 4517
Helixi452 – 4543
Helixi458 – 47417
Helixi477 – 4793
Turni480 – 4823
Helixi484 – 49512
Helixi500 – 51617
Helixi518 – 52710
Helixi530 – 5378

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4K92X-ray2.00A/B284-552[»]
ProteinModelPortaliQ7Z460.
SMRiQ7Z460. Positions 5-227, 296-538.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati87 – 12438HEAT 1Add
BLAST
Repeati163 – 20038HEAT 2Add
BLAST
Repeati405 – 44036HEAT 3Add
BLAST
Repeati441 – 47737HEAT 4Add
BLAST
Repeati974 – 101138HEAT 5Add
BLAST
Repeati1342 – 137938HEAT 6Add
BLAST
Repeati1460 – 149738HEAT 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni662 – 785124Interaction with microtubules, MAPRE1 and MAPRE3Add
BLAST
Regioni1254 – 1538285Interaction with CLIP2 By similarityAdd
BLAST
Regioni1254 – 1538285Interaction with PHLDB2 and RSNAdd
BLAST
Regioni1256 – 1538283Localization to kinetochoresAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1299 – 133032 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi530 – 765236Ser-richAdd
BLAST
Compositional biasi1526 – 15327Poly-Ser

Sequence similaritiesi

Belongs to the CLASP family.
Contains 7 HEAT repeats.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG81443.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiQ7Z460.
KOiK16578.
OMAiSGNMIQS.
PhylomeDBiQ7Z460.
TreeFamiTF101155.

Family and domain databases

Gene3Di1.25.10.10. 4 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028399. CLASP_metazoan.
IPR024395. CLASP_N_dom.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERiPTHR21567:SF28. PTHR21567:SF28. 1 hit.
PfamiPF12348. CLASP_N. 1 hit.
PF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q7Z460-1) [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

MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL     50
VDGLATSWVN SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL 100
GDAKDSVREQ DQTLLLKIMD QAANPQYVWD RMLGGFKHKN FRTREGICLC 150
LIATLNASGA QTLTLSKIVP HICNLLGDPN SQVRDAAINS LVEIYRHVGE 200
RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN FDDEDSVDGN 250
RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 300
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS 350
LLLAGAAEYD NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG 400
NKFDHGAEAI MPTIFNLIPN SAKIMATSGV VAVRLIIRHT HIPRLIPVIT 450
SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL ERHISVLAET IKKGIHDADS 500
EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL KNSDSIVSLP 550
QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 600
DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA 650
TNVASTPDNR GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL 700
TGGSSRGPPV TPSSEKRSKI PRSQGCSRET SPNRIGLARS SRIPRPSMSQ 750
GCSRDTSRES SRDTSPARGF PPLDRFGLGQ PGRIPGSVNA MRVLSTSTDL 800
EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY GSRNGGIPHY 850
LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI 900
FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD 950
LLGSVQAKVQ KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK 1000
YIESLARQMD PTDFVNSSET RLAVSRIITW TTEPKSSDVR KAAQIVLISL 1050
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LKNSSNTSVG SPSNTIGRTP 1100
SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP PFSQPNSIPT 1150
APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL 1200
NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT 1250
QPPRAFPGPR ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH 1300
SDLVADLLKE LSNHNERVEE RKGALLELLK ITREDSLGVW EEHFKTILLL 1350
LLETLGDKDH SIRALALRVL REILRNQPAR FKNYAELTIM KTLEAHKDSH 1400
KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL AAIKMQTKVV 1450
ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK 1500
PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS 1538
Length:1,538
Mass (Da):169,451
Last modified:October 1, 2003 - v1
Checksum:i6E03BD948C227F8D
GO
Isoform 2 (identifier: Q7Z460-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     737-772: Missing.
     808-808: L → LLLGDSRSK
     1123-1161: Missing.

Show »
Length:1,471
Mass (Da):162,110
Checksum:iF027A39E35F82BA2
GO
Isoform 3 (identifier: Q7Z460-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,494
Mass (Da):164,566
Checksum:i0B69865E7CD5A48F
GO
Isoform 4 (identifier: Q7Z460-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     637-637: L → LESRHMREDMEYIGLDS
     673-682: RSRSANPAGA → P
     737-772: Missing.
     808-808: L → LLLGDSRS
     1123-1161: Missing.

Note: No experimental confirmation available.

Show »
Length:1,477
Mass (Da):163,061
Checksum:i7C56388FDF06760C
GO

Sequence cautioni

The sequence AAH32563.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAX88872.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331I → T.
Corresponds to variant rs17761055 [ dbSNP | Ensembl ].
VAR_053818

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei637 – 6371L → LESRHMREDMEYIGLDS in isoform 4. VSP_054412
Alternative sequencei673 – 68210RSRSANPAGA → P in isoform 4. VSP_054413
Alternative sequencei737 – 77236Missing in isoform 2, isoform 3 and isoform 4. VSP_022386Add
BLAST
Alternative sequencei808 – 8081L → LLLGDSRSK in isoform 2 and isoform 3. VSP_022387
Alternative sequencei808 – 8081L → LLLGDSRS in isoform 4. VSP_054414
Alternative sequencei911 – 9111K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3. VSP_022388
Alternative sequencei1123 – 116139Missing in isoform 2, isoform 3 and isoform 4. VSP_022389Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511R → G in CAI46251. 1 Publication
Sequence conflicti556 – 5561S → F in CAI46251. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF347693 mRNA. Translation: AAQ15051.1.
AC012447 Genomic DNA. No translation available.
AC013399 Genomic DNA. Translation: AAX88872.1. Sequence problems.
AC018737 Genomic DNA. No translation available.
AC079449 Genomic DNA. No translation available.
BC032563 mRNA. Translation: AAH32563.1. Different initiation.
BC112940 mRNA. Translation: AAI12941.1.
BC144107 mRNA. Translation: AAI44108.1.
AJ288057 mRNA. Translation: CAC35156.1.
CR933722 mRNA. Translation: CAI46251.1.
AB014522 mRNA. Translation: BAA31597.1.
PIRiT00387.
RefSeqiNP_001135745.1. NM_001142273.1.
NP_001135746.1. NM_001142274.1. [Q7Z460-2]
NP_001193980.1. NM_001207051.1. [Q7Z460-4]
NP_056097.1. NM_015282.2. [Q7Z460-1]
UniGeneiHs.469840.
Hs.708183.

Genome annotation databases

EnsembliENST00000263710; ENSP00000263710; ENSG00000074054. [Q7Z460-1]
ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
ENST00000541377; ENSP00000441625; ENSG00000074054.
GeneIDi23332.
KEGGihsa:23332.
UCSCiuc002tnc.3. human. [Q7Z460-1]
uc010yza.2. human. [Q7Z460-2]

Polymorphism databases

DMDMi74723323.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF347693 mRNA. Translation: AAQ15051.1 .
AC012447 Genomic DNA. No translation available.
AC013399 Genomic DNA. Translation: AAX88872.1 . Sequence problems.
AC018737 Genomic DNA. No translation available.
AC079449 Genomic DNA. No translation available.
BC032563 mRNA. Translation: AAH32563.1 . Different initiation.
BC112940 mRNA. Translation: AAI12941.1 .
BC144107 mRNA. Translation: AAI44108.1 .
AJ288057 mRNA. Translation: CAC35156.1 .
CR933722 mRNA. Translation: CAI46251.1 .
AB014522 mRNA. Translation: BAA31597.1 .
PIRi T00387.
RefSeqi NP_001135745.1. NM_001142273.1.
NP_001135746.1. NM_001142274.1. [Q7Z460-2 ]
NP_001193980.1. NM_001207051.1. [Q7Z460-4 ]
NP_056097.1. NM_015282.2. [Q7Z460-1 ]
UniGenei Hs.469840.
Hs.708183.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4K92 X-ray 2.00 A/B 284-552 [» ]
ProteinModelPortali Q7Z460.
SMRi Q7Z460. Positions 5-227, 296-538.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116919. 10 interactions.
IntActi Q7Z460. 13 interactions.
MINTi MINT-1683081.
STRINGi 9606.ENSP00000263710.

PTM databases

PhosphoSitei Q7Z460.

Polymorphism databases

DMDMi 74723323.

Proteomic databases

MaxQBi Q7Z460.
PaxDbi Q7Z460.
PRIDEi Q7Z460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263710 ; ENSP00000263710 ; ENSG00000074054 . [Q7Z460-1 ]
ENST00000409078 ; ENSP00000386442 ; ENSG00000074054 . [Q7Z460-2 ]
ENST00000541377 ; ENSP00000441625 ; ENSG00000074054 .
GeneIDi 23332.
KEGGi hsa:23332.
UCSCi uc002tnc.3. human. [Q7Z460-1 ]
uc010yza.2. human. [Q7Z460-2 ]

Organism-specific databases

CTDi 23332.
GeneCardsi GC02M122095.
HGNCi HGNC:17088. CLASP1.
MIMi 605852. gene.
neXtProti NX_Q7Z460.
PharmGKBi PA38436.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG81443.
HOGENOMi HOG000236347.
HOVERGENi HBG079692.
InParanoidi Q7Z460.
KOi K16578.
OMAi SGNMIQS.
PhylomeDBi Q7Z460.
TreeFami TF101155.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi CLASP1. human.
GeneWikii CLASP1.
GenomeRNAii 23332.
NextBioi 45259.
PMAP-CutDB Q7Z460.
PROi Q7Z460.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q7Z460.
Bgeei Q7Z460.
CleanExi HS_CLASP1.
HS_MAST1.
Genevestigatori Q7Z460.

Family and domain databases

Gene3Di 1.25.10.10. 4 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028399. CLASP_metazoan.
IPR024395. CLASP_N_dom.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view ]
PANTHERi PTHR21567:SF28. PTHR21567:SF28. 1 hit.
Pfami PF12348. CLASP_N. 1 hit.
PF02985. HEAT. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 5 hits.
PROSITEi PS50077. HEAT_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-266, FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
    Tissue: Brain.
  5. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, SUBCELLULAR LOCATION.
  10. Cited for: INTERACTION WITH ERC1 AND PHLDB2, SUBCELLULAR LOCATION.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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.
  13. Cited for: FUNCTION, INTERACTION WITH GCC2, SUBCELLULAR LOCATION.
  14. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-649; THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-688; SER-797 AND SER-1091, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646 AND SER-1223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646 AND SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLAP1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z460
Secondary accession number(s): B7ZLX3
, O75118, Q2KHQ9, Q5H9P0, Q8N5B8, Q9BQT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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