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O75122 (CLAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CLIP-associating protein 2
Alternative name(s):
Cytoplasmic linker-associated protein 2
Protein Orbit homolog 2
Short name=hOrbit2
Gene names
Name:CLASP2
Synonyms:KIAA0627
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.20

Subunit structure

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. Ref.3 Ref.7 Ref.8 Ref.10 Ref.13 Ref.18

Subcellular location

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. Ref.3 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.18 Ref.20

Tissue specificity

Brain-specific.

Domain

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. Ref.18

Post-translational modification

Phosphorylated by GSK3B. Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. Ref.8

Sequence similarities

Belongs to the CLASP family.

Contains 5 HEAT repeats.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCell membrane
Cell projection
Centromere
Chromosome
Cytoplasm
Cytoskeleton
Golgi apparatus
Kinetochore
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

establishment or maintenance of cell polarity

Traceable author statement PubMed 15928712. Source: UniProtKB

fucosylation

Non-traceable author statement Ref.3. Source: GOC

microtubule anchoring

Inferred from mutant phenotype Ref.13. Source: UniProtKB

microtubule nucleation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

microtubule organizing center organization

Inferred from mutant phenotype Ref.13. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of microtubule depolymerization

Non-traceable author statement Ref.3. Source: UniProtKB

regulation of microtubule polymerization or depolymerization

Inferred from mutant phenotype Ref.3. Source: UniProtKB

regulation of microtubule-based process

Inferred from mutant phenotype Ref.20. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.3. Source: UniProtKB

cell cortex

Inferred from direct assay PubMed 17113391. Source: MGI

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Non-traceable author statement Ref.3. Source: UniProtKB

cytoplasmic microtubule

Inferred from direct assay Ref.3. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

kinetochore microtubule

Traceable author statement PubMed 12837247. Source: UniProtKB

microtubule

Inferred from direct assay Ref.13Ref.20. Source: UniProtKB

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.20. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.20. Source: UniProtKB

trans-Golgi network

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functiongalactoside 2-alpha-L-fucosyltransferase activity

Non-traceable author statement Ref.3. Source: UniProtKB

microtubule plus-end binding

Inferred from direct assay Ref.3Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Clip2O551563EBI-913524,EBI-349416From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms exist.
Isoform 1 (identifier: O75122-1)

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.
Isoform 2 (identifier: O75122-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12941294CLIP-associating protein 2
PRO_0000089849

Regions

Repeat173 – 20836HEAT 1
Repeat209 – 24537HEAT 2
Repeat772 – 80938HEAT 3
Repeat1098 – 113538HEAT 4
Repeat1216 – 125338HEAT 5
Region444 – 580137Interaction with microtubules, MAPRE1 and MAPRE3
Region872 – 1294423Interaction with RSN and localization to the Golgi and kinetochores
Region1017 – 1294278Required for cortical localization
Coiled coil1055 – 108430 Potential
Motif494 – 4974Microtubule tip localization signal
Motif517 – 5204Microtubule tip localization signal
Compositional bias310 – 587278Ser-rich
Compositional bias1104 – 11085Poly-Leu

Amino acid modifications

Modified residue81Phosphoserine Ref.23
Modified residue3701Phosphoserine Ref.16 Ref.19 Ref.23
Modified residue4551Phosphoserine Ref.23
Modified residue5251Phosphoserine Ref.16
Modified residue5291Phosphoserine Ref.16
Modified residue5961Phosphoserine Ref.16 Ref.19 Ref.23
Modified residue10291Phosphoserine Ref.16 Ref.19 Ref.21

Natural variations

Alternative sequence1 – 66MAMGDD → MRRLICKRICDY in isoform 2.
VSP_015805
Alternative sequence410 – 42516DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2.
VSP_015806
Alternative sequence426 – 1294869Missing in isoform 2.
VSP_015807

Experimental info

Mutagenesis496 – 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. Ref.18
Mutagenesis519 – 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. Ref.18
Sequence conflict3921R → S in BAA31602. Ref.1
Sequence conflict3921R → S in AAH29035. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CLASP2 gamma) [UniParc].

Last modified October 11, 2005. Version 2.
Checksum: E4FF7E06049E65E5

FASTA1,294141,133
        10         20         30         40         50         60 
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG PKVGGASKEG 

        70         80         90        100        110        120 
GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS DDKHDWDQRA NALKKIRSLL 

       130        140        150        160        170        180 
VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS QVVREACITV AHLSTVLGNK FDHGAEAIVP 

       190        200        210        220        230        240 
TLFNLVPNSA KVMATSGCAA IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL 

       250        260        270        280        290        300 
QEWQTHSLER HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY 

       310        320        330        340        350        360 
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR VSAGSSKASS 

       370        380        390        400        410        420 
LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL NAGSYASLED TSDKLDGTAS 

       430        440        450        460        470        480 
EDGRVRAKLS APLAGMGNAK ADSRGRSRTK MVSQSQPGSR SGSPGRVLTT TALSTVSSGV 

       490        500        510        520        530        540 
QRVLVNSASA QKRSKIPRSQ GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT 

       550        560        570        580        590        600 
SPVRSFQPLA SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE 

       610        620        630        640        650        660 
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR QTEDVAEVLN 

       670        680        690        700        710        720 
RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT RMFADPHGKR VFSMFLETLV 

       730        740        750        760        770        780 
DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL GSVQAKVQKA LDVTRESFPN DLQFNILMRF 

       790        800        810        820        830        840 
TVDQTQTPSL KVKVAILKYI ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA 

       850        860        870        880        890        900 
AQSVLISLFE LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR 

       910        920        930        940        950        960 
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN FSFRSQEDMN 

       970        980        990       1000       1010       1020 
EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN KASLLHSMPT HSSPRSRDYN 

      1030       1040       1050       1060       1070       1080 
PYNYSDSISP FNKSALKEAM FDDDADQFPD DLSLDHSDLV AELLKELSNH NERVEERKIA 

      1090       1100       1110       1120       1130       1140 
LYELMKLTQE ESFSVWDEHF KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY 

      1150       1160       1170       1180       1190       1200 
AELTVMKTLE AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK 

      1210       1220       1230       1240       1250       1260 
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV IGDELKPHLS 

      1270       1280       1290 
QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS 

« Hide

Isoform 2 (CLASP2 beta) [UniParc].

Checksum: 5C5C731ECD32FFEB
Show »

FASTA43146,585

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"CLASPs attach microtubule plus ends to the cell cortex through a complex with LL5beta."
Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S., Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F., Akhmanova A.
Dev. Cell 11:21-32(2006) [PubMed] [Europe PMC] [Abstract]
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]"Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network."
Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M., Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X., Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.
Dev. Cell 12:917-930(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GCC2, SUBCELLULAR LOCATION.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT00386.
RefSeqNP_001193973.1. NM_001207044.1.
NP_055912.2. NM_015097.2.
UniGeneHs.108614.

3D structure databases

ProteinModelPortalO75122.
SMRO75122. Positions 64-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116743. 21 interactions.
DIPDIP-36804N.
IntActO75122. 12 interactions.
MINTMINT-4526878.
STRING9606.ENSP00000352581.

PTM databases

PhosphoSiteO75122.

Proteomic databases

MaxQBO75122.
PaxDbO75122.
PRIDEO75122.

Protocols and materials databases

DNASU23122.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313350; ENSP00000324364; ENSG00000163539.
GeneID23122.
KEGGhsa:23122.
UCSCuc021wvb.1. human. [O75122-1]

Organism-specific databases

CTD23122.
GeneCardsGC03M033537.
HGNCHGNC:17078. CLASP2.
MIM605853. gene.
neXtProtNX_O75122.
PharmGKBPA38435.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81443.
HOGENOMHOG000236347.
HOVERGENHBG079692.
InParanoidO75122.
KOK16578.
PhylomeDBO75122.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_227403. Developmental Biology.

Gene expression databases

ArrayExpressO75122.
BgeeO75122.
CleanExHS_CLASP2.
GenevestigatorO75122.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
[Graphical view]
PfamPF12348. CLASP_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSCLASP2. human.
GeneWikiCLASP2.
GenomeRNAi23122.
NextBio44351.
PROO75122.
SOURCESearch...

Entry information

Entry nameCLAP2_HUMAN
AccessionPrimary (citable) accession number: O75122
Secondary accession number(s): Q7L8F6 expand/collapse secondary AC list , Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM