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Protein

CLIP-associating protein 1

Gene

CLASP1

Organism
Homo sapiens (Human)
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.6 Publications

GO - Molecular functioni

  • dystroglycan binding Source: UniProtKB
  • kinetochore binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB

GO - Biological processi

  • axon guidance Source: Reactome
  • cell division Source: MGI
  • establishment of epithelial cell polarity Source: UniProtKB
  • establishment of spindle orientation Source: MGI
  • establishment or maintenance of cell polarity Source: UniProtKB
  • exit from mitosis Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: Reactome
  • Golgi organization Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • microtubule bundle formation Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • microtubule organizing center organization Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • negative regulation of microtubule depolymerization Source: UniProtKB
  • negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • negative regulation of wound healing, spreading of epidermal cells Source: UniProtKB
  • organelle organization Source: Reactome
  • positive regulation of basement membrane assembly involved in embryonic body morphogenesis Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of exocytosis Source: UniProtKB
  • positive regulation of extracellular matrix disassembly Source: UniProtKB
  • regulation of epithelial to mesenchymal transition Source: UniProtKB
  • regulation of focal adhesion assembly Source: UniProtKB
  • regulation of gastrulation Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
  • vesicle targeting 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_267965. Anchoring of the basal body to the plasma membrane.
REACT_355252. RHO GTPases Activate Formins.
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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:17088. CLASP1.

Subcellular locationi

GO - Cellular componenti

  • basal cortex Source: UniProtKB
  • cell cortex Source: MGI
  • centrosomal corona Source: UniProtKB
  • centrosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cortical microtubule cytoskeleton Source: UniProtKB
  • cytoplasmic microtubule Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • kinetochore Source: UniProtKB
  • kinetochore microtubule Source: UniProtKB
  • membrane Source: UniProtKB
  • spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38436.

Polymorphism and mutation databases

BioMutaiCLASP1.
DMDMi74723323.

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

BgeeiQ7Z460.
CleanExiHS_CLASP1.
HS_MAST1.
ExpressionAtlasiQ7Z460. baseline and differential.
GenevisibleiQ7Z460. HS.

Organism-specific databases

HPAiHPA062664.
HPA065219.

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Clip1Q9JK252EBI-913476,EBI-908338From a different organism.
Clip2O551563EBI-913476,EBI-349416From a different organism.
JAKMIP2Q96AA83EBI-10257534,EBI-752007
KIF1BO603333EBI-913476,EBI-465633
SPAG5Q96R063EBI-913476,EBI-413317

Protein-protein interaction databases

BioGridi116919. 11 interactions.
IntActiQ7Z460. 14 interactions.
MINTiMINT-1683081.
STRINGi9606.ENSP00000263710.

Structurei

Secondary structure

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

3D structure databases

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

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 CLIP2By similarityAdd
BLAST
Regioni1254 – 1538285Interaction with PHLDB2 and RSNAdd
BLAST
Regioni1256 – 1538283Localization to kinetochoresAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1299 – 133032Sequence AnalysisAdd
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.Curated
Contains 7 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG81443.
GeneTreeiENSGT00390000001762.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiQ7Z460.
KOiK16578.
OMAiRDYNPYP.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL
60 70 80 90 100
VDGLATSWVN SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL
110 120 130 140 150
GDAKDSVREQ DQTLLLKIMD QAANPQYVWD RMLGGFKHKN FRTREGICLC
160 170 180 190 200
LIATLNASGA QTLTLSKIVP HICNLLGDPN SQVRDAAINS LVEIYRHVGE
210 220 230 240 250
RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN FDDEDSVDGN
260 270 280 290 300
RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE
310 320 330 340 350
DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS
360 370 380 390 400
LLLAGAAEYD NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG
410 420 430 440 450
NKFDHGAEAI MPTIFNLIPN SAKIMATSGV VAVRLIIRHT HIPRLIPVIT
460 470 480 490 500
SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL ERHISVLAET IKKGIHDADS
510 520 530 540 550
EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL KNSDSIVSLP
560 570 580 590 600
QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS
610 620 630 640 650
DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA
660 670 680 690 700
TNVASTPDNR GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL
710 720 730 740 750
TGGSSRGPPV TPSSEKRSKI PRSQGCSRET SPNRIGLARS SRIPRPSMSQ
760 770 780 790 800
GCSRDTSRES SRDTSPARGF PPLDRFGLGQ PGRIPGSVNA MRVLSTSTDL
810 820 830 840 850
EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY GSRNGGIPHY
860 870 880 890 900
LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI
910 920 930 940 950
FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD
960 970 980 990 1000
LLGSVQAKVQ KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK
1010 1020 1030 1040 1050
YIESLARQMD PTDFVNSSET RLAVSRIITW TTEPKSSDVR KAAQIVLISL
1060 1070 1080 1090 1100
FELNTPEFTM LLGALPKTFQ DGATKLLHNH LKNSSNTSVG SPSNTIGRTP
1110 1120 1130 1140 1150
SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP PFSQPNSIPT
1160 1170 1180 1190 1200
APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL
1210 1220 1230 1240 1250
NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT
1260 1270 1280 1290 1300
QPPRAFPGPR ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH
1310 1320 1330 1340 1350
SDLVADLLKE LSNHNERVEE RKGALLELLK ITREDSLGVW EEHFKTILLL
1360 1370 1380 1390 1400
LLETLGDKDH SIRALALRVL REILRNQPAR FKNYAELTIM KTLEAHKDSH
1410 1420 1430 1440 1450
KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL AAIKMQTKVV
1460 1470 1480 1490 1500
ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK
1510 1520 1530
PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS
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
Isoform 5 (identifier: Q7Z460-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     637-637: L → LDGTTTKAE
     737-772: Missing.
     808-808: L → LLLGDSRSK
     1123-1161: Missing.

Note: No experimental confirmation available.
Show »
Length:1,479
Mass (Da):162,914
Checksum:iEC0A6357FB967AC4
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511R → G in CAI46251 (PubMed:17974005).Curated
Sequence conflicti556 – 5561S → F in CAI46251 (PubMed:17974005).Curated

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. 1 PublicationVSP_054412
Alternative sequencei637 – 6371L → LDGTTTKAE in isoform 5. 1 PublicationVSP_057272
Alternative sequencei673 – 68210RSRSANPAGA → P in isoform 4. 1 PublicationVSP_054413
Alternative sequencei737 – 77236Missing in isoform 2, isoform 3 and isoform 4, isoform 5. 2 PublicationsVSP_022386Add
BLAST
Alternative sequencei808 – 8081L → LLLGDSRSK in isoform 2, isoform 3 and isoform 5. 2 PublicationsVSP_022387
Alternative sequencei808 – 8081L → LLLGDSRS in isoform 4. 1 PublicationVSP_054414
Alternative sequencei911 – 9111K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3. 1 PublicationVSP_022388
Alternative sequencei1123 – 116139Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_022389Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
BC132723 mRNA. Translation: AAI32724.1.
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. [Q7Z460-5]
NP_001135746.1. NM_001142274.1. [Q7Z460-2]
NP_001193980.1. NM_001207051.1. [Q7Z460-4]
NP_056097.1. NM_015282.2. [Q7Z460-1]
XP_011509150.1. XM_011510848.1. [Q7Z460-3]
UniGeneiHs.469840.
Hs.708183.

Genome annotation databases

EnsembliENST00000263710; ENSP00000263710; ENSG00000074054.
ENST00000397587; ENSP00000380717; ENSG00000074054. [Q7Z460-5]
ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
ENST00000541377; ENSP00000441625; ENSG00000074054. [Q7Z460-4]
GeneIDi23332.
KEGGihsa:23332.
UCSCiuc002tnc.3. human. [Q7Z460-1]
uc002tng.1. human.
uc010yyz.2. human.
uc010yza.2. human. [Q7Z460-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
BC132723 mRNA. Translation: AAI32724.1.
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. [Q7Z460-5]
NP_001135746.1. NM_001142274.1. [Q7Z460-2]
NP_001193980.1. NM_001207051.1. [Q7Z460-4]
NP_056097.1. NM_015282.2. [Q7Z460-1]
XP_011509150.1. XM_011510848.1. [Q7Z460-3]
UniGeneiHs.469840.
Hs.708183.

3D structure databases

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

Protein-protein interaction databases

BioGridi116919. 11 interactions.
IntActiQ7Z460. 14 interactions.
MINTiMINT-1683081.
STRINGi9606.ENSP00000263710.

PTM databases

PhosphoSiteiQ7Z460.

Polymorphism and mutation databases

BioMutaiCLASP1.
DMDMi74723323.

Proteomic databases

MaxQBiQ7Z460.
PaxDbiQ7Z460.
PRIDEiQ7Z460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263710; ENSP00000263710; ENSG00000074054.
ENST00000397587; ENSP00000380717; ENSG00000074054. [Q7Z460-5]
ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
ENST00000541377; ENSP00000441625; ENSG00000074054. [Q7Z460-4]
GeneIDi23332.
KEGGihsa:23332.
UCSCiuc002tnc.3. human. [Q7Z460-1]
uc002tng.1. human.
uc010yyz.2. human.
uc010yza.2. human. [Q7Z460-2]

Organism-specific databases

CTDi23332.
GeneCardsiGC02M122095.
HGNCiHGNC:17088. CLASP1.
HPAiHPA062664.
HPA065219.
MIMi605852. gene.
neXtProtiNX_Q7Z460.
PharmGKBiPA38436.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81443.
GeneTreeiENSGT00390000001762.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiQ7Z460.
KOiK16578.
OMAiRDYNPYP.
PhylomeDBiQ7Z460.
TreeFamiTF101155.

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_267965. Anchoring of the basal body to the plasma membrane.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiCLASP1. human.
GeneWikiiCLASP1.
GenomeRNAii23332.
NextBioi35507246.
PMAP-CutDBQ7Z460.
PROiQ7Z460.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z460.
CleanExiHS_CLASP1.
HS_MAST1.
ExpressionAtlasiQ7Z460. baseline and differential.
GenevisibleiQ7Z460. HS.

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]
ProtoNetiSearch...

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; 4 AND 5), 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].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCLAP1_HUMAN
AccessioniPrimary (citable) accession number: Q7Z460
Secondary accession number(s): A2RU21
, B7ZLX3, F5GWS0, O75118, Q2KHQ9, Q5H9P0, Q8N5B8, Q9BQT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 129 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

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 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.