O75122 (CLAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1294 AA.
Sequence status	Complete.
Protein existence	Evidence 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.19
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.17
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle. Golgi apparatus. Golgi apparatus › trans-Golgi network. Cell membrane. Cell projection › ruffle 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.17 Ref.19
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.17
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 process	Cell cycle Cell division Mitosis
Cellular component	Cell membrane Cell projection Centromere Chromosome Cytoplasm Cytoskeleton Golgi apparatus Kinetochore Membrane Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW establishment or maintenance of cell polarity Traceable author statement PubMed 15928712. Source: UniProtKB 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 prometaphase Traceable author statement. Source: Reactome negative regulation of microtubule depolymerization Non-traceable author statement Ref.3. Source: UniProtKB
Cellular_component	Golgi 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 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 organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from direct assay Ref.19. Source: UniProtKB trans-Golgi network Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	galactoside 2-alpha-L-fucosyltransferase activity Non-traceable author statement Ref.3. Source: UniProtKB microtubule plus-end binding Inferred from direct assay Ref.3Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Clip2	O55156	3	EBI-913524,EBI-349416	From 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1294	1294	CLIP-associating protein 2		PRO_0000089849
Regions
	Repeat	173 – 208	36	HEAT 1
	Repeat	209 – 245	37	HEAT 2
	Repeat	772 – 809	38	HEAT 3
	Repeat	1098 – 1135	38	HEAT 4
	Repeat	1216 – 1253	38	HEAT 5
	Region	444 – 580	137	Interaction with microtubules, MAPRE1 and MAPRE3
	Region	872 – 1294	423	Interaction with RSN and localization to the Golgi and kinetochores
	Region	1017 – 1294	278	Required for cortical localization
	Coiled coil	1055 – 1084	30	Potential
	Motif	494 – 497	4	Microtubule tip localization signal
	Motif	517 – 520	4	Microtubule tip localization signal
	Compositional bias	310 – 587	278	Ser-rich
	Compositional bias	1104 – 1108	5	Poly-Leu
Amino acid modifications
	Modified residue	8	1	Phosphoserine Ref.22
	Modified residue	370	1	Phosphoserine Ref.16 Ref.18 Ref.22
	Modified residue	455	1	Phosphoserine Ref.22
	Modified residue	507	1	Phosphoserine By similarity
	Modified residue	525	1	Phosphoserine Ref.16
	Modified residue	529	1	Phosphoserine Ref.16
	Modified residue	596	1	Phosphoserine Ref.16 Ref.18 Ref.22
	Modified residue	1029	1	Phosphoserine Ref.16 Ref.18 Ref.20
Natural variations
	Alternative sequence	1 – 6	6	MAMGDD → MRRLICKRICDY in isoform 2.		VSP_015805
	Alternative sequence	410 – 425	16	DTSDK…EDGRV → CEAFWRSGRTAKLYSV in isoform 2.		VSP_015806
	Alternative sequence	426 – 1294	869	Missing in isoform 2.		VSP_015807
Experimental info
	Mutagenesis	496 – 497	2	IP → 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.17
	Mutagenesis	519 – 520	2	IP → 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.17
	Sequence conflict	392	1	R → S in BAA31602. Ref.1
	Sequence conflict	392	1	R → S in AAH29035. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CLASP2 gamma) [UniParc]. Last modified October 11, 2005. Version 2. Checksum: E4FF7E06049E65E5	FASTA	1,294	141,133
	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
	Isoform 2 (CLASP2 beta) [UniParc]. Checksum: 5C5C731ECD32FFEB	FASTA	431	46,585
	10 20 30 40 50 60 MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT SGNPANSARK PGSAGGPKVG 70 80 90 100 110 120 GASKEGGAGA VDEDDFIKAF TDVPSIQIYS SRELEETLNK IREILSDDKH DWDQRANALK 130 140 150 160 170 180 KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG 190 200 210 220 230 240 AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE 250 260 270 280 290 300 FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN 310 320 330 340 350 360 SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP STVAGRVSAG 370 380 390 400 410 420 SSKASSLPGS LQRSRSDIDV NAAAGAKAHH AAGQSVRRGR LGAGALNAGS YASLECEAFW 430 RSGRTAKLYS V

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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.
[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-370; SER-596 AND SER-1029, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00167067. IPI00945554.
PIR	T00386.
RefSeq	NP_001193973.1. NM_001207044.1. NP_055912.2. NM_015097.2.
UniGene	Hs.108614.
3D structure databases
ProteinModelPortal	O75122.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36804N.
IntAct	O75122. 9 interactions.
STRING	9606.ENSP00000352581.
PTM databases
PhosphoSite	O75122.
Proteomic databases
PaxDb	O75122.
PRIDE	O75122.
Protocols and materials databases
DNASU	23122.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000313350; ENSP00000324364; ENSG00000163539.
GeneID	23122.
KEGG	hsa:23122.
UCSC	uc021wvb.1. human.
Organism-specific databases
CTD	23122.
GeneCards	GC03M033512.
HGNC	HGNC:17078. CLASP2.
MIM	605853. gene.
neXtProt	NX_O75122.
PharmGKB	PA38435.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG81443.
HOGENOM	HOG000236347.
HOVERGEN	HBG079692.
InParanoid	O75122.
KO	K16578.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_113552. Developmental Biology. REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	O75122.
Bgee	O75122.
CleanEx	HS_CLASP2.
Genevestigator	O75122.
GermOnline	ENSG00000163539. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 3 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR024395. CLASP_N_dom. [Graphical view]
Pfam	PF12348. CLASP_N. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CLASP2. human.
GenomeRNAi	23122.
NextBio	44351.
SOURCE	Search...

Entry information

Entry name

CLAP2_HUMAN

Accession

Primary (citable) accession number: O75122
Secondary accession number(s): Q7L8F6 , Q8N6R6, Q9BQT3, Q9BQT4, Q9H7A3, Q9NSZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.