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O75122

- CLAP2_HUMAN

UniProt

O75122 - CLAP2_HUMAN

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Protein
CLIP-associating protein 2
Gene
CLASP2, KIAA0627
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. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.7 Publications

GO - Molecular functioni

  1. galactoside 2-alpha-L-fucosyltransferase activity Source: UniProtKB
  2. microtubule plus-end binding Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. establishment or maintenance of cell polarity Source: UniProtKB
  3. fucosylation Source: GOC
  4. microtubule anchoring Source: UniProtKB
  5. microtubule nucleation Source: UniProtKB
  6. microtubule organizing center organization Source: UniProtKB
  7. mitotic cell cycle Source: Reactome
  8. mitotic nuclear division Source: UniProtKB-KW
  9. negative regulation of microtubule depolymerization Source: UniProtKB
  10. regulation of microtubule polymerization or depolymerization Source: UniProtKB
  11. regulation of microtubule-based process 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_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: Chromosome 3

Organism-specific databases

HGNCiHGNC:17078. CLASP2.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Golgi apparatus. Golgi apparatustrans-Golgi network. Cell membrane. Cell projectionruffle membrane
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. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosophorylated form to the cell membrane.10 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cell cortex Source: MGI
  3. condensed chromosome kinetochore Source: UniProtKB-SubCell
  4. cytoplasm Source: UniProtKB
  5. cytoplasmic microtubule Source: UniProtKB
  6. cytosol Source: Reactome
  7. kinetochore microtubule Source: UniProtKB
  8. microtubule Source: UniProtKB
  9. microtubule organizing center Source: UniProtKB-SubCell
  10. plasma membrane Source: UniProtKB
  11. ruffle membrane Source: UniProtKB
  12. 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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine1 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

ArrayExpressiO75122.
BgeeiO75122.
CleanExiHS_CLASP2.
GenevestigatoriO75122.

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.6 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi116743. 21 interactions.
DIPiDIP-36804N.
IntActiO75122. 12 interactions.
MINTiMINT-4526878.
STRINGi9606.ENSP00000352581.

Structurei

3D structure databases

ProteinModelPortaliO75122.
SMRiO75122. Positions 64-306.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni444 – 580137Interaction with microtubules, MAPRE1 and MAPRE3
Add
BLAST
Regioni872 – 1294423Interaction with RSN and localization to the Golgi and kinetochores
Add
BLAST
Regioni1017 – 1294278Required for cortical localization
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1055 – 108430 Reviewed prediction
Add
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-rich
Add
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.
Contains 5 HEAT repeats.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG     50
PKVGGASKEG GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS 100
DDKHDWDQRA NALKKIRSLL VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS 150
QVVREACITV AHLSTVLGNK FDHGAEAIVP TLFNLVPNSA KVMATSGCAA 200
IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL QEWQTHSLER 250
HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY 300
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR 350
VSAGSSKASS LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL 400
NAGSYASLED TSDKLDGTAS EDGRVRAKLS APLAGMGNAK ADSRGRSRTK 450
MVSQSQPGSR SGSPGRVLTT TALSTVSSGV QRVLVNSASA QKRSKIPRSQ 500
GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT SPVRSFQPLA 550
SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE 600
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR 650
QTEDVAEVLN RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT 700
RMFADPHGKR VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL 750
GSVQAKVQKA LDVTRESFPN DLQFNILMRF TVDQTQTPSL KVKVAILKYI 800
ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA AQSVLISLFE 850
LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR 900
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN 950
FSFRSQEDMN EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN 1000
KASLLHSMPT HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD 1050
DLSLDHSDLV AELLKELSNH NERVEERKIA LYELMKLTQE ESFSVWDEHF 1100
KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY AELTVMKTLE 1150
AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK 1200
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV 1250
IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS 1294
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

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MAMGDD → MRRLICKRICDY in isoform 2.
VSP_015805
Alternative sequencei410 – 42516DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2.
VSP_015806Add
BLAST
Alternative sequencei426 – 1294869Missing in isoform 2.
VSP_015807Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti392 – 3921R → S in BAA31602. 1 Publication
Sequence conflicti392 – 3921R → S in AAH29035. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014527 mRNA. Translation: BAA31602.2. Different initiation.
BC029035 mRNA. Translation: AAH29035.1.
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.
GeneIDi23122.
KEGGihsa:23122.
UCSCiuc021wvb.1. human. [O75122-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB014527 mRNA. Translation: BAA31602.2 . Different initiation.
BC029035 mRNA. Translation: AAH29035.1 .
AJ288058 mRNA. Translation: CAC35157.1 .
AJ288059 mRNA. Translation: CAC35158.1 .
AL137636 mRNA. Translation: CAB70852.1 .
AK024770 mRNA. Translation: BAB14995.1 . Different initiation.
PIRi T00386.
RefSeqi NP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGenei Hs.108614.

3D structure databases

ProteinModelPortali O75122.
SMRi O75122. Positions 64-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116743. 21 interactions.
DIPi DIP-36804N.
IntActi O75122. 12 interactions.
MINTi MINT-4526878.
STRINGi 9606.ENSP00000352581.

PTM databases

PhosphoSitei O75122.

Proteomic databases

MaxQBi O75122.
PaxDbi O75122.
PRIDEi O75122.

Protocols and materials databases

DNASUi 23122.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313350 ; ENSP00000324364 ; ENSG00000163539 .
GeneIDi 23122.
KEGGi hsa:23122.
UCSCi uc021wvb.1. human. [O75122-1 ]

Organism-specific databases

CTDi 23122.
GeneCardsi GC03M033537.
HGNCi HGNC:17078. CLASP2.
MIMi 605853. gene.
neXtProti NX_O75122.
PharmGKBi PA38435.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG81443.
HOGENOMi HOG000236347.
HOVERGENi HBG079692.
InParanoidi O75122.
KOi K16578.
PhylomeDBi O75122.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi CLASP2. human.
GeneWikii CLASP2.
GenomeRNAii 23122.
NextBioi 44351.
PROi O75122.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75122.
Bgeei O75122.
CleanExi HS_CLASP2.
Genevestigatori O75122.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view ]
Pfami PF12348. CLASP_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
ProtoNeti Search...

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 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] (ISOFORM 2).
    Tissue: Brain.
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 939-1294 (ISOFORM 1).
    Tissue: Testis.
  5. "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).
  6. "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.
  7. "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.
  8. "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.
  9. Erratum
    Wittmann T., Waterman-Storer C.M.
    J. Cell Biol. 171:393-393(2005)
  10. Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERC1; PHLDB2 AND RSN, 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, SUBCELLULAR LOCATION.
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "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.
  16. 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.
  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. Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF 496-ILE-PRO-497 AND 519-ILE-PRO-520.
  19. "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.
  20. "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.
  21. "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.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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].

Entry informationi

Entry nameiCLAP2_HUMAN
AccessioniPrimary (citable) accession number: O75122
Secondary accession number(s): Q7L8F6
, Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: September 3, 2014
This is version 122 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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