Reviewed, UniProtKB/Swiss-Prot Q7Z460 (CLAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    CLIP-associating protein 1
Alternative name(s):
    Cytoplasmic linker-associated protein 1
    Multiple asters homolog 1
    Protein Orbit homolog 1
      Short name=hOrbit1

Gene names

Name:	CLASP1
Synonyms:	KIAA0622, MAST1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1538 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. 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. Ref.4 Ref.7 Ref.10 Ref.12 Ref.13
Subunit structure	Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules, PHLDB2 and RSN. The interaction with ERC1 may be mediated by PHLDB2. Ref.4 Ref.10 Ref.9 Ref.11
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cytoskeleton › centrosome. Kinetochore. Cytoplasm › cytoskeleton › spindle. 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. Ref.4 Ref.7 Ref.10 Ref.13 Ref.9 Ref.11
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21
Sequence similarities	Belongs to the CLASP family. Contains 7 HEAT repeats.
Sequence caution	The sequence AAX88872.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Kinetochore Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW establishment or maintenance of cell polarity Non-traceable author statement. Source: UniProtKB exit from mitosis Ref.12 Inferred from mutant phenotype. Source: UniProtKB microtubule bundle formation Ref.7 Inferred from mutant phenotype. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of microtubule depolymerization Ref.10 Ref.12 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	Golgi apparatus Ref.10 Inferred from direct assay. Source: UniProtKB centrosomal corona Ref.13 Inferred from direct assay. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cortical microtubule cytoskeleton Ref.7 Inferred from direct assay. Source: UniProtKB cytoplasmic microtubule Ref.4 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome kinetochore microtubule Ref.7 Traceable author statement. Source: UniProtKB
Molecular function	kinetochore binding Ref.7 Inferred from mutant phenotype. Source: UniProtKB microtubule plus-end binding Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Clip2	O55156	3	EBI-913476,EBI-349416	From a different organism.
Rsn	Q9JK25	2	EBI-913476,EBI-908338	From a different organism.
YWHAG	P61981	1	EBI-913476,EBI-359832

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7Z460-1)

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: Q7Z460-2)

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

Isoform 3 (identifier: Q7Z460-3)

The sequence of this isoform differs from the canonical sequence as follows:
     737-772: Missing.
     808-808: L → LLLGDSRSK
     911-911: K → KIADSEAECEDKEGNLFPSEVSCT
     1123-1161: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1538	1538	CLIP-associating protein 1		PRO_0000089847
Regions
	Repeat	87 – 124	38	HEAT 1
	Repeat	163 – 200	38	HEAT 2
	Repeat	405 – 440	36	HEAT 3
	Repeat	441 – 477	37	HEAT 4
	Repeat	974 – 1011	38	HEAT 5
	Repeat	1342 – 1379	38	HEAT 6
	Repeat	1460 – 1497	38	HEAT 7
	Region	662 – 785	124	Interaction with microtubules, MAPRE1 and MAPRE3
	Region	1254 – 1538	285	Interaction with CLIP2 By similarity
	Region	1254 – 1538	285	Interaction with PHLDB2 and RSN
	Region	1256 – 1538	283	Localization to kinetochores
	Coiled coil	1299 – 1330	32	Potential
	Compositional bias	530 – 765	236	Ser-rich
	Compositional bias	1526 – 1532	7	Poly-Ser
Amino acid modifications
	Modified residue	545	1	Phosphoserine By similarity
	Modified residue	559	1	Phosphoserine Ref.14
	Modified residue	568	1	Phosphoserine Ref.14
	Modified residue	594	1	Phosphoserine Ref.19
	Modified residue	598	1	Phosphoserine By similarity
	Modified residue	600	1	Phosphoserine Ref.17 Ref.19 Ref.21
	Modified residue	609	1	Phosphoserine Ref.8
	Modified residue	636	1	Phosphoserine Ref.21
	Modified residue	646	1	Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21
	Modified residue	647	1	Phosphoserine Ref.17 Ref.19
	Modified residue	649	1	Phosphoserine Ref.17 Ref.19
	Modified residue	651	1	Phosphothreonine Ref.19
	Modified residue	656	1	Phosphothreonine Ref.17
	Modified residue	688	1	Phosphoserine Ref.17 Ref.21
	Modified residue	695	1	Phosphoserine Ref.17
	Modified residue	711	1	Phosphothreonine Ref.17
	Modified residue	714	1	Phosphoserine Ref.17
	Modified residue	797	1	Phosphoserine Ref.19 Ref.21
	Modified residue	1091	1	Phosphoserine Ref.16 Ref.17 Ref.19 Ref.21
	Modified residue	1099	1	Phosphothreonine Ref.16 Ref.17
	Modified residue	1196	1	Phosphoserine Ref.15
	Modified residue	1223	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	737 – 772	36	Missing in isoform 2 and isoform 3.		VSP_022386
	Alternative sequence	808	1	L → LLLGDSRSK in isoform 2 and isoform 3.		VSP_022387
	Alternative sequence	911	1	K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3.		VSP_022388
	Alternative sequence	1123 – 1161	39	Missing in isoform 2 and isoform 3.		VSP_022389
	Natural variant	233	1	I → T: dbSNP rs17761055.		VAR_053818
Experimental info
	Sequence conflict	251	1	R → G in CAI46251. Ref.5
	Sequence conflict	556	1	S → F in CAI46251. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 6E03BD948C227F8D	FASTA	1,538	169,451
	10 20 30 40 50 60 MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN 70 80 90 100 110 120 SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD 130 140 150 160 170 180 QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN 190 200 210 220 230 240 SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN 250 260 270 280 290 300 FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 310 320 330 340 350 360 DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD 370 380 390 400 410 420 NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN 430 440 450 460 470 480 SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL 490 500 510 520 530 540 ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL 550 560 570 580 590 600 KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 610 620 630 640 650 660 DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR 670 680 690 700 710 720 GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI 730 740 750 760 770 780 PRSQGCSRET SPNRIGLARS SRIPRPSMSQ GCSRDTSRES SRDTSPARGF PPLDRFGLGQ 790 800 810 820 830 840 PGRIPGSVNA MRVLSTSTDL EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY 850 860 870 880 890 900 GSRNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI 910 920 930 940 950 960 FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ 970 980 990 1000 1010 1020 KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK YIESLARQMD PTDFVNSSET 1030 1040 1050 1060 1070 1080 RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM LLGALPKTFQ DGATKLLHNH 1090 1100 1110 1120 1130 1140 LKNSSNTSVG SPSNTIGRTP SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP 1150 1160 1170 1180 1190 1200 PFSQPNSIPT APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL 1210 1220 1230 1240 1250 1260 NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT QPPRAFPGPR 1270 1280 1290 1300 1310 1320 ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH SDLVADLLKE LSNHNERVEE 1330 1340 1350 1360 1370 1380 RKGALLELLK ITREDSLGVW EEHFKTILLL LLETLGDKDH SIRALALRVL REILRNQPAR 1390 1400 1410 1420 1430 1440 FKNYAELTIM KTLEAHKDSH KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL 1450 1460 1470 1480 1490 1500 AAIKMQTKVV ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK 1510 1520 1530 PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS
	Isoform 2. Checksum: F027A39E35F82BA2	FASTA	1,471	162,110
	10 20 30 40 50 60 MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN 70 80 90 100 110 120 SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD 130 140 150 160 170 180 QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN 190 200 210 220 230 240 SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN 250 260 270 280 290 300 FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 310 320 330 340 350 360 DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD 370 380 390 400 410 420 NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN 430 440 450 460 470 480 SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL 490 500 510 520 530 540 ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL 550 560 570 580 590 600 KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 610 620 630 640 650 660 DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR 670 680 690 700 710 720 GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI 730 740 750 760 770 780 PRSQGCSRET SPNRIGLDRF GLGQPGRIPG SVNAMRVLST STDLEAAVAD ALLLGDSRSK 790 800 810 820 830 840 KKPVRRRYEP YGMYSDDDAN SDASSVCSER SYGSRNGGIP HYLRQTEDVA EVLNHCASSN 850 860 870 880 890 900 WSERKEGLLG LQNLLKSQRT LSRVELKRLC EIFTRMFADP HSKRVFSMFL ETLVDFIIIH 910 920 930 940 950 960 KDDLQDWLFV LLTQLLKKMG ADLLGSVQAK VQKALDVTRD SFPFDQQFNI LMRFIVDQTQ 970 980 990 1000 1010 1020 TPNLKVKVAI LKYIESLARQ MDPTDFVNSS ETRLAVSRII TWTTEPKSSD VRKAAQIVLI 1030 1040 1050 1060 1070 1080 SLFELNTPEF TMLLGALPKT FQDGATKLLH NHLKNSSNTS VGSPSNTIGR TPSRHTSSRT 1090 1100 1110 1120 1130 1140 SPLTSPTNCS HGGLSPSMLD YDTENLNSEE IYSSLRGVTE AIEKFSFRSQ EDLNEPIKRD 1150 1160 1170 1180 1190 1200 GKKECDIVSR DGGAASPATE GRGGSEVEGG RTALDNKTSL LNTQPPRAFP GPRARDYNPY 1210 1220 1230 1240 1250 1260 PYSDAINTYD KTALKEAVFD DDMEQLRDVP IDHSDLVADL LKELSNHNER VEERKGALLE 1270 1280 1290 1300 1310 1320 LLKITREDSL GVWEEHFKTI LLLLLETLGD KDHSIRALAL RVLREILRNQ PARFKNYAEL 1330 1340 1350 1360 1370 1380 TIMKTLEAHK DSHKEVVRAA EEAASTLASS IHPEQCIKVL CPIIQTADYP INLAAIKMQT 1390 1400 1410 1420 1430 1440 KVVERIAKES LLQLLVDIIP GLLQGYDNTE SSVRKASVFC LVAIYSVIGE DLKPHLAQLT 1450 1460 1470 GSKMKLLNLY IKRAQTTNSN SSSSSDVSTH S
	Isoform 3. Checksum: 0B69865E7CD5A48F	FASTA	1,494	164,566
	10 20 30 40 50 60 MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN 70 80 90 100 110 120 SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD 130 140 150 160 170 180 QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN 190 200 210 220 230 240 SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN 250 260 270 280 290 300 FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE 310 320 330 340 350 360 DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD 370 380 390 400 410 420 NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN 430 440 450 460 470 480 SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL 490 500 510 520 530 540 ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL 550 560 570 580 590 600 KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS 610 620 630 640 650 660 DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR 670 680 690 700 710 720 GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI 730 740 750 760 770 780 PRSQGCSRET SPNRIGLDRF GLGQPGRIPG SVNAMRVLST STDLEAAVAD ALLLGDSRSK 790 800 810 820 830 840 KKPVRRRYEP YGMYSDDDAN SDASSVCSER SYGSRNGGIP HYLRQTEDVA EVLNHCASSN 850 860 870 880 890 900 WSERKEGLLG LQNLLKSQRT LSRVELKRLC EIFTRMFADP HSKIADSEAE CEDKEGNLFP 910 920 930 940 950 960 SEVSCTRVFS MFLETLVDFI IIHKDDLQDW LFVLLTQLLK KMGADLLGSV QAKVQKALDV 970 980 990 1000 1010 1020 TRDSFPFDQQ FNILMRFIVD QTQTPNLKVK VAILKYIESL ARQMDPTDFV NSSETRLAVS 1030 1040 1050 1060 1070 1080 RIITWTTEPK SSDVRKAAQI VLISLFELNT PEFTMLLGAL PKTFQDGATK LLHNHLKNSS 1090 1100 1110 1120 1130 1140 NTSVGSPSNT IGRTPSRHTS SRTSPLTSPT NCSHGGLSPS MLDYDTENLN SEEIYSSLRG 1150 1160 1170 1180 1190 1200 VTEAIEKFSF RSQEDLNEPI KRDGKKECDI VSRDGGAASP ATEGRGGSEV EGGRTALDNK 1210 1220 1230 1240 1250 1260 TSLLNTQPPR AFPGPRARDY NPYPYSDAIN TYDKTALKEA VFDDDMEQLR DVPIDHSDLV 1270 1280 1290 1300 1310 1320 ADLLKELSNH NERVEERKGA LLELLKITRE DSLGVWEEHF KTILLLLLET LGDKDHSIRA 1330 1340 1350 1360 1370 1380 LALRVLREIL RNQPARFKNY AELTIMKTLE AHKDSHKEVV RAAEEAASTL ASSIHPEQCI 1390 1400 1410 1420 1430 1440 KVLCPIIQTA DYPINLAAIK MQTKVVERIA KESLLQLLVD IIPGLLQGYD NTESSVRKAS 1450 1460 1470 1480 1490 VFCLVAIYSV IGEDLKPHLA QLTGSKMKLL NLYIKRAQTT NSNSSSSSDV STHS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Full length cDNA of a human homologue of Drosophila melanogaster multiple asters (MAST) gene." Maiato H., Sunkel C.E., Earnshaw W.C. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2). Tissue: Eye.
[4]	"Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts." Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F., Galjart N. Cell 104:923-935(2001) [PubMed: 11290329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-266, FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, INTERACTION WITH CLIP2; MICROTUBULES AND RSN. Tissue: Brain.
[5]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3). Tissue: Testis.
[6]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-1538. Tissue: Brain.
[7]	"Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics." Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E., Earnshaw W.C. Cell 113:891-904(2003) [PubMed: 12837247] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609 AND SER-1223, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Microtubule bundle formation and cell death induced by the human CLASP/Orbit N-terminal fragment." Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N., Matsukage A. Cell Struct. Funct. 30:7-13(2005) [PubMed: 16145243] [Abstract] Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[10]	"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: 15631994] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, SUBCELLULAR LOCATION.
[11]	"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: 16824950] [Abstract] Cited for: INTERACTION WITH ERC1 AND PHLDB2, 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: 16866869] [Abstract] Cited for: FUNCTION.
[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: 16914514] [Abstract] Cited for: FUNCTION, 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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-568, MASS SPECTROMETRY.
[15]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646; SER-1091 AND THR-1099, MASS SPECTROMETRY.
[17]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-647; SER-649; THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; SER-600; SER-646; SER-647; SER-649; THR-651; SER-797 AND SER-1091, MASS SPECTROMETRY.
[20]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, MASS SPECTROMETRY.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-636; SER-646; SER-688; SER-797 AND SER-1091, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF347693 mRNA. Translation: AAQ15051.1. AC013399 Genomic DNA. Translation: AAX88872.1. Sequence problems. AC012447 Genomic DNA. No translation available. AC079449 Genomic DNA. No translation available. BC032563 mRNA. Translation: AAH32563.1. Different initiation. BC112940 mRNA. Translation: AAI12941.1. AJ288057 mRNA. Translation: CAC35156.1. CR933722 mRNA. Translation: CAI46251.1. AB014522 mRNA. Translation: BAA31597.1.
IPI	IPI00396279. IPI00744551. IPI00828013.
PIR	T00387.
RefSeq	NP_001135745.1. NP_001135746.1. NP_056097.1.
UniGene	Hs.469840 Hs.708183
3D structure databases
SMR	Q7Z460. Positions 15-223, 20-498, 1306-1524.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q7Z460. 4 interactions.
STRING	Q7Z460.
PTM databases
PhosphoSite	Q7Z460.
Proteomic databases
PRIDE	Q7Z460.
Genome annotation databases
Ensembl	ENST00000263710; ENSP00000263710; ENSG00000074054; Homo sapiens. [Genome view]
GeneID	23332.
KEGG	hsa:23332.
Organism-specific databases
CTD	23332.
GeneCards	GC02M121811.
H-InvDB	HIX0002422.
HGNC	HGNC:17088. CLASP1.
MIM	605852. gene.
PharmGKB	PA38436.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG714912.
HOVERGEN	Q7Z460.
InParanoid	Q7Z460.
OMA	IHKDDLQ.
PhylomeDB	Q7Z460.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_18266. Axon guidance.
Gene expression databases
ArrayExpress	Q7Z460.
Bgee	Q7Z460.
CleanEx	HS_CLASP1. HS_MAST1.
Genevestigator	Q7Z460.
GermOnline	ENSG00000074054. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000357. HEAT. IPR021133. HEAT_type_2. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
Pfam	PF02985. HEAT. 2 hits. [Graphical view]
PROSITE	PS50077. HEAT_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	45259.
PMAP-CutDB	Q7Z460.
SOURCE	Search...

Entry information

Entry name

CLAP1_HUMAN

Accession

Primary (citable) accession number: Q7Z460
Secondary accession number(s): O75118 , Q2KHQ9, Q5H9P0, Q8N5B8, Q9BQT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.