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Q7Z460 (CLAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1538 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. Ref.4 Ref.7 Ref.9 Ref.11 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. Interacts with GCC2; recruits CLASP1 to Golgi membranes. Interacts with MACF1 By similarity. Ref.4 Ref.8 Ref.9 Ref.10 Ref.13

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Golgi apparatustrans-Golgi network Probable. 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.8 Ref.9 Ref.10 Ref.12 Ref.13

Sequence similarities

Belongs to the CLASP family.

Contains 7 HEAT repeats.

Sequence caution

The sequence AAH32563.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAX88872.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Golgi apparatus
Kinetochore
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cell division

Inferred from direct assay PubMed 21822276. Source: MGI

establishment of spindle orientation

Inferred from direct assay PubMed 21822276. Source: MGI

establishment or maintenance of cell polarity

Non-traceable author statement PubMed 15928712. Source: UniProtKB

exit from mitosis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

microtubule anchoring

Inferred from mutant phenotype Ref.13. Source: UniProtKB

microtubule bundle formation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from genetic interaction Ref.9. 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

negative regulation of microtubule depolymerization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of microtubule polymerization or depolymerization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.9. Source: UniProtKB

cell cortex

Inferred from direct assay PubMed 17113391. Source: MGI

centrosomal corona

Inferred from direct assay Ref.12. Source: UniProtKB

centrosome

Inferred from direct assay Ref.7Ref.9PubMed 21399614. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cortical microtubule cytoskeleton

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasmic microtubule

Inferred from direct assay Ref.4. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.7. Source: UniProtKB

kinetochore microtubule

Traceable author statement Ref.7. Source: UniProtKB

spindle microtubule

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionkinetochore binding

Inferred from mutant phenotype Ref.7. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.4. Source: UniProtKB

microtubule plus-end binding

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Clip1Q9JK252EBI-913476,EBI-908338From a different organism.
Clip2O551563EBI-913476,EBI-349416From a different organism.
KIF1BO603333EBI-913476,EBI-465633
SPAG5Q96R063EBI-913476,EBI-413317

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15381538CLIP-associating protein 1
PRO_0000089847

Regions

Repeat87 – 12438HEAT 1
Repeat163 – 20038HEAT 2
Repeat405 – 44036HEAT 3
Repeat441 – 47737HEAT 4
Repeat974 – 101138HEAT 5
Repeat1342 – 137938HEAT 6
Repeat1460 – 149738HEAT 7
Region662 – 785124Interaction with microtubules, MAPRE1 and MAPRE3
Region1254 – 1538285Interaction with CLIP2 By similarity
Region1254 – 1538285Interaction with PHLDB2 and RSN
Region1256 – 1538283Localization to kinetochores
Coiled coil1299 – 133032 Potential
Compositional bias530 – 765236Ser-rich
Compositional bias1526 – 15327Poly-Ser

Amino acid modifications

Modified residue6001Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue6461Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21
Modified residue6491Phosphoserine Ref.16
Modified residue6561Phosphothreonine Ref.16
Modified residue6841Phosphoserine Ref.21
Modified residue6881Phosphoserine Ref.16 Ref.18
Modified residue6951Phosphoserine Ref.16
Modified residue7111Phosphothreonine Ref.16
Modified residue7141Phosphoserine Ref.16
Modified residue7971Phosphoserine Ref.18
Modified residue10911Phosphoserine Ref.16 Ref.18
Modified residue10991Phosphothreonine Ref.16
Modified residue11961Phosphoserine Ref.15
Modified residue12231Phosphoserine Ref.19

Natural variations

Alternative sequence737 – 77236Missing in isoform 2 and isoform 3.
VSP_022386
Alternative sequence8081L → LLLGDSRSK in isoform 2 and isoform 3.
VSP_022387
Alternative sequence9111K → KIADSEAECEDKEGNLFPSE VSCT in isoform 3.
VSP_022388
Alternative sequence1123 – 116139Missing in isoform 2 and isoform 3.
VSP_022389
Natural variant2331I → T.
Corresponds to variant rs17761055 [ dbSNP | Ensembl ].
VAR_053818

Experimental info

Sequence conflict2511R → G in CAI46251. Ref.5
Sequence conflict5561S → F in CAI46251. Ref.5

Secondary structure

.................................... 1538
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2003. Version 1.
Checksum: 6E03BD948C227F8D

FASTA1,538169,451
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F027A39E35F82BA2
Show »

FASTA1,471162,110
Isoform 3 [UniParc].

Checksum: 0B69865E7CD5A48F
Show »

FASTA1,494164,566

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[9]"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.
[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: INTERACTION WITH ERC1 AND PHLDB2, 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.
[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]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[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-600; SER-646; SER-649; THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, 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]"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-600; SER-646; SER-688; SER-797 AND SER-1091, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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-646 AND SER-1223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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-600; SER-646 AND SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRT00387.
RefSeqNP_001135745.1. NM_001142273.1.
NP_001135746.1. NM_001142274.1.
NP_001193980.1. NM_001207051.1.
NP_056097.1. NM_015282.2.
UniGeneHs.469840.
Hs.708183.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4K92X-ray2.00A/B284-552[»]
ProteinModelPortalQ7Z460.
SMRQ7Z460. Positions 5-227, 296-538.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116919. 10 interactions.
IntActQ7Z460. 13 interactions.
MINTMINT-1683081.
STRING9606.ENSP00000263710.

PTM databases

PhosphoSiteQ7Z460.

Polymorphism databases

DMDM74723323.

Proteomic databases

PaxDbQ7Z460.
PRIDEQ7Z460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263710; ENSP00000263710; ENSG00000074054. [Q7Z460-1]
ENST00000409078; ENSP00000386442; ENSG00000074054. [Q7Z460-2]
GeneID23332.
KEGGhsa:23332.
UCSCuc002tnc.3. human. [Q7Z460-1]
uc010yza.2. human. [Q7Z460-2]

Organism-specific databases

CTD23332.
GeneCardsGC02M122095.
HGNCHGNC:17088. CLASP1.
MIM605852. gene.
neXtProtNX_Q7Z460.
PharmGKBPA38436.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81443.
HOGENOMHOG000236347.
HOVERGENHBG079692.
InParanoidQ7Z460.
KOK16578.
OMASGNMIQS.
PhylomeDBQ7Z460.
TreeFamTF101155.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ7Z460.
BgeeQ7Z460.
CleanExHS_CLASP1.
HS_MAST1.
GenevestigatorQ7Z460.

Family and domain databases

Gene3D1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028399. CLASP_metazoan.
IPR024395. CLASP_N_dom.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PANTHERPTHR21567:SF11. PTHR21567:SF11. 1 hit.
PfamPF12348. CLASP_N. 1 hit.
PF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
PROSITEPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLASP1. human.
GeneWikiCLASP1.
GenomeRNAi23332.
NextBio45259.
PMAP-CutDBQ7Z460.
PROQ7Z460.
SOURCESearch...

Entry information

Entry nameCLAP1_HUMAN
AccessionPrimary (citable) accession number: Q7Z460
Secondary accession number(s): O75118 expand/collapse secondary AC list , Q2KHQ9, Q5H9P0, Q8N5B8, Q9BQT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 114 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM