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Protein

CLIP-associating protein 2

Gene

CLASP2

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. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.7 Publications

GO - Molecular functioni

  • dystroglycan binding Source: UniProtKB
  • galactoside 2-alpha-L-fucosyltransferase activity Source: UniProtKB
  • microtubule plus-end binding Source: UniProtKB

GO - Biological processi

  • axon guidance Source: Reactome
  • cell division Source: UniProtKB-KW
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • establishment or maintenance of cell polarity Source: UniProtKB
  • fucosylation Source: GOC
  • Golgi organization Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • microtubule cytoskeleton organization Source: UniProtKB
  • microtubule nucleation Source: UniProtKB
  • microtubule organizing center organization Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of microtubule depolymerization Source: UniProtKB
  • negative regulation of stress fiber assembly Source: UniProtKB
  • negative regulation of wound healing, spreading of epidermal cells Source: UniProtKB
  • 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 gastrulation Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
  • regulation of microtubule polymerization or depolymerization 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_19230. Role of Abl in Robo-Slit signaling.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Protein Orbit homolog 2
Short name:
hOrbit2
Gene namesi
Name:CLASP2
Synonyms:KIAA0627
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17078. CLASP2.

Subcellular locationi

GO - Cellular componenti

  • basal cortex Source: UniProtKB
  • cell cortex Source: MGI
  • cell leading edge Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic microtubule Source: UniProtKB
  • cytosol Source: Reactome
  • Golgi apparatus Source: UniProtKB
  • kinetochore microtubule Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi496 – 4972IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 519-S-S-520. 1 Publication
Mutagenesisi519 – 5202IP → SS: Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 496-S-S-497. 1 Publication

Organism-specific databases

PharmGKBiPA38435.

Polymorphism and mutation databases

BioMutaiCLASP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12941294CLIP-associating protein 2PRO_0000089849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei370 – 3701Phosphoserine3 Publications
Modified residuei455 – 4551Phosphoserine1 Publication
Modified residuei525 – 5251Phosphoserine1 Publication
Modified residuei529 – 5291Phosphoserine1 Publication
Modified residuei596 – 5961Phosphoserine3 Publications
Modified residuei1029 – 10291Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75122.
PaxDbiO75122.
PRIDEiO75122.

PTM databases

PhosphoSiteiO75122.

Expressioni

Tissue specificityi

Brain-specific.

Gene expression databases

BgeeiO75122.
CleanExiHS_CLASP2.
ExpressionAtlasiO75122. baseline and differential.
GenevisibleiO75122. HS.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Clip2O551563EBI-913524,EBI-349416From a different organism.

Protein-protein interaction databases

BioGridi116743. 25 interactions.
DIPiDIP-36804N.
IntActiO75122. 14 interactions.
MINTiMINT-4526878.
STRINGi9606.ENSP00000419974.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WOYX-ray2.10A60-310[»]
ProteinModelPortaliO75122.
SMRiO75122. Positions 64-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati173 – 20836HEAT 1Add
BLAST
Repeati209 – 24537HEAT 2Add
BLAST
Repeati772 – 80938HEAT 3Add
BLAST
Repeati1098 – 113538HEAT 4Add
BLAST
Repeati1216 – 125338HEAT 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni444 – 580137Interaction with microtubules, MAPRE1 and MAPRE3Add
BLAST
Regioni872 – 1294423Interaction with RSN and localization to the Golgi and kinetochoresAdd
BLAST
Regioni1017 – 1294278Required for cortical localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1055 – 108430Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi494 – 4974Microtubule tip localization signal
Motifi517 – 5204Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi310 – 587278Ser-richAdd
BLAST
Compositional biasi1104 – 11085Poly-Leu

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.1 Publication

Sequence similaritiesi

Belongs to the CLASP family.Curated
Contains 5 HEAT repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG81443.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiO75122.
KOiK16578.
PhylomeDBiO75122.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequences (3)i

Sequence statusi: Complete.

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

Note: Additional isoforms exist.

Isoform 1 (identifier: O75122-1) [UniParc]FASTAAdd to basket

Also known as: CLASP2 gamma

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
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG
60 70 80 90 100
PKVGGASKEG GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS
110 120 130 140 150
DDKHDWDQRA NALKKIRSLL VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS
160 170 180 190 200
QVVREACITV AHLSTVLGNK FDHGAEAIVP TLFNLVPNSA KVMATSGCAA
210 220 230 240 250
IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL QEWQTHSLER
260 270 280 290 300
HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY
310 320 330 340 350
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR
360 370 380 390 400
VSAGSSKASS LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL
410 420 430 440 450
NAGSYASLED TSDKLDGTAS EDGRVRAKLS APLAGMGNAK ADSRGRSRTK
460 470 480 490 500
MVSQSQPGSR SGSPGRVLTT TALSTVSSGV QRVLVNSASA QKRSKIPRSQ
510 520 530 540 550
GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT SPVRSFQPLA
560 570 580 590 600
SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE
610 620 630 640 650
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR
660 670 680 690 700
QTEDVAEVLN RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT
710 720 730 740 750
RMFADPHGKR VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL
760 770 780 790 800
GSVQAKVQKA LDVTRESFPN DLQFNILMRF TVDQTQTPSL KVKVAILKYI
810 820 830 840 850
ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA AQSVLISLFE
860 870 880 890 900
LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR
910 920 930 940 950
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN
960 970 980 990 1000
FSFRSQEDMN EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN
1010 1020 1030 1040 1050
KASLLHSMPT HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD
1060 1070 1080 1090 1100
DLSLDHSDLV AELLKELSNH NERVEERKIA LYELMKLTQE ESFSVWDEHF
1110 1120 1130 1140 1150
KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY AELTVMKTLE
1160 1170 1180 1190 1200
AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK
1210 1220 1230 1240 1250
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV
1260 1270 1280 1290
IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS
Length:1,294
Mass (Da):141,133
Last modified:October 11, 2005 - v2
Checksum:iE4FF7E06049E65E5
GO
Isoform 2 (identifier: O75122-2) [UniParc]FASTAAdd to basket

Also known as: CLASP2 beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAMGDD → MRRLICKRICDY
     410-425: DTSDKLDGTASEDGRV → CEAFWRSGRTAKLYSV
     426-1294: Missing.

Show »
Length:431
Mass (Da):46,585
Checksum:i5C5C731ECD32FFEB
GO
Isoform 3 (identifier: O75122-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAMGD → MEPRSMEYFC...SGGMILSVCK
     54-54: G → GA
     550-570: Missing.
     606-606: L → LLLGDIRTK

Note: No experimental confirmation available.
Show »
Length:1,515
Mass (Da):165,924
Checksum:iDEA3BC38A9E35DF5
GO

Sequence cautioni

The sequence BAA31602.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14995.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921R → S in BAA31602 (PubMed:9734811).Curated
Sequence conflicti392 – 3921R → S in AAH29035 (PubMed:15489334).Curated
Sequence conflicti392 – 3921R → S in AAI40779 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MAMGDD → MRRLICKRICDY in isoform 2. 2 PublicationsVSP_015805
Alternative sequencei1 – 55MAMGD → MEPRSMEYFCAQVQQKDVGG RLQVGQELLLYLGAPGAISD LEEDLGRLGKTVDALTGWVG SSNYRVSLMGLEILSAFVDR LSTRFKSYVAMVIVALIDRM GDAKDKVRDEAQTLILKLMD QVAPPMYIWEQLASGFKHKN FRSREGVCLCLIETLNIFGA QPLVISKLIPHLCILFGDSN SQVRDAAILAIVEIYRHVGE KVRMDLYKRGIPPARLEMIF AKFDEVQSSGGMILSVCK in isoform 3. 1 PublicationVSP_057273
Alternative sequencei54 – 541G → GA in isoform 3. 1 PublicationVSP_057274
Alternative sequencei410 – 42516DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2. 2 PublicationsVSP_015806Add
BLAST
Alternative sequencei426 – 1294869Missing in isoform 2. 2 PublicationsVSP_015807Add
BLAST
Alternative sequencei550 – 57021Missing in isoform 3. 1 PublicationVSP_057275Add
BLAST
Alternative sequencei606 – 6061L → LLLGDIRTK in isoform 3. 1 PublicationVSP_057276

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014527 mRNA. Translation: BAA31602.2. Different initiation.
AC093114 Genomic DNA. No translation available.
AC113170 Genomic DNA. No translation available.
AC132515 Genomic DNA. No translation available.
BC029035 mRNA. Translation: AAH29035.1.
BC140778 mRNA. Translation: AAI40779.1.
AJ288058 mRNA. Translation: CAC35157.1.
AJ288059 mRNA. Translation: CAC35158.1.
AL137636 mRNA. Translation: CAB70852.1.
AK024770 mRNA. Translation: BAB14995.1. Different initiation.
PIRiT00386.
RefSeqiNP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGeneiHs.108614.

Genome annotation databases

EnsembliENST00000313350; ENSP00000324364; ENSG00000163539.
ENST00000359576; ENSP00000352581; ENSG00000163539.
GeneIDi23122.
KEGGihsa:23122.
UCSCiuc021wvb.1. human. [O75122-1]
uc021wvc.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014527 mRNA. Translation: BAA31602.2. Different initiation.
AC093114 Genomic DNA. No translation available.
AC113170 Genomic DNA. No translation available.
AC132515 Genomic DNA. No translation available.
BC029035 mRNA. Translation: AAH29035.1.
BC140778 mRNA. Translation: AAI40779.1.
AJ288058 mRNA. Translation: CAC35157.1.
AJ288059 mRNA. Translation: CAC35158.1.
AL137636 mRNA. Translation: CAB70852.1.
AK024770 mRNA. Translation: BAB14995.1. Different initiation.
PIRiT00386.
RefSeqiNP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGeneiHs.108614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WOYX-ray2.10A60-310[»]
ProteinModelPortaliO75122.
SMRiO75122. Positions 64-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116743. 25 interactions.
DIPiDIP-36804N.
IntActiO75122. 14 interactions.
MINTiMINT-4526878.
STRINGi9606.ENSP00000419974.

PTM databases

PhosphoSiteiO75122.

Polymorphism and mutation databases

BioMutaiCLASP2.

Proteomic databases

MaxQBiO75122.
PaxDbiO75122.
PRIDEiO75122.

Protocols and materials databases

DNASUi23122.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313350; ENSP00000324364; ENSG00000163539.
ENST00000359576; ENSP00000352581; ENSG00000163539.
GeneIDi23122.
KEGGihsa:23122.
UCSCiuc021wvb.1. human. [O75122-1]
uc021wvc.1. human.

Organism-specific databases

CTDi23122.
GeneCardsiGC03M033537.
HGNCiHGNC:17078. CLASP2.
MIMi605853. gene.
neXtProtiNX_O75122.
PharmGKBiPA38435.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81443.
HOGENOMiHOG000236347.
HOVERGENiHBG079692.
InParanoidiO75122.
KOiK16578.
PhylomeDBiO75122.

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_355252. RHO GTPases Activate Formins.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiCLASP2. human.
GeneWikiiCLASP2.
GenomeRNAii23122.
NextBioi35509099.
PROiO75122.
SOURCEiSearch...

Gene expression databases

BgeeiO75122.
CleanExiHS_CLASP2.
ExpressionAtlasiO75122. baseline and differential.
GenevisibleiO75122. HS.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamiPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Brain.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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 3).
    Tissue: Brain.
  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 1-9 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 939-1294 (ISOFORM 1).
    Tissue: Testis.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1294 (ISOFORM 1).
  7. "The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream of the tyrosine kinase Abl in mediating axon guidance."
    Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.
    Neuron 42:913-926(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "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.
  9. "Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta in migrating epithelial cells."
    Wittmann T., Waterman-Storer C.M.
    J. Cell Biol. 169:929-939(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION BY GSK3B.
  10. Erratum
    Wittmann T., Waterman-Storer C.M.
    J. Cell Biol. 171:393-393(2005)
  11. Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERC1; PHLDB2 AND RSN, 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. Cited for: FUNCTION, INTERACTION WITH GCC2, SUBCELLULAR LOCATION.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-525; SER-529; SER-596 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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].
  19. Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF 496-ILE-PRO-497 AND 519-ILE-PRO-520.
  20. "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-370; SER-596 AND SER-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
    Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
    Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  22. "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-1029, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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-8; SER-370; SER-455 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCLAP2_HUMAN
AccessioniPrimary (citable) accession number: O75122
Secondary accession number(s): B2RTR1
, F5H604, Q7L8F6, Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: July 22, 2015
This is version 132 of the entry and version 2 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 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.