Full text data of CKAP5
CKAP5
(KIAA0097)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cytoskeleton-associated protein 5 (Colonic and hepatic tumor overexpressed gene protein; Ch-TOG)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytoskeleton-associated protein 5 (Colonic and hepatic tumor overexpressed gene protein; Ch-TOG)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14008
ID CKAP5_HUMAN Reviewed; 2032 AA.
AC Q14008; Q05D70; Q0VAX7; Q0VAX8; Q14668; Q2TA89; Q6NSH4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Cytoskeleton-associated protein 5;
DE AltName: Full=Colonic and hepatic tumor overexpressed gene protein;
DE Short=Ch-TOG;
GN Name=CKAP5; Synonyms=KIAA0097;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain tumor;
RX PubMed=8536682; DOI=10.1111/j.1432-1033.1995.406_b.x;
RA Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C.;
RT "Characterization of the cDNA and pattern of expression of a new gene
RT over-expressed in human hepatomas and colonic tumors.";
RL Eur. J. Biochem. 234:406-413(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH TACC1.
RX PubMed=11903063; DOI=10.1042/0264-6021:3630195;
RA Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
RT "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein
RT with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein
RT complexes in human cells.";
RL Biochem. J. 363:195-200(2002).
RN [6]
RP FUNCTION.
RX PubMed=12569123; DOI=10.1101/gad.245603;
RA Gergely F., Draviam V.M., Raff J.W.;
RT "The ch-TOG/XMAP215 protein is essential for spindle pole organization
RT in human somatic cells.";
RL Genes Dev. 17:336-341(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, INTERACTION WITH SLAIN2, AND SUBCELLULAR LOCATION.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
RA Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
RA Steinmetz M.O., Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Promotes
CC cytoplasmic microtubule nucleation and elongation. Plays a major
CC role in organizing spindle poles.
CC -!- SUBUNIT: Interacts with TACC1. Interacts with SLAIN2.
CC -!- INTERACTION:
CC P16333:NCK1; NbExp=3; IntAct=EBI-310585, EBI-389883;
CC O75410:TACC1; NbExp=3; IntAct=EBI-310585, EBI-624237;
CC O75410-1:TACC1; NbExp=3; IntAct=EBI-310585, EBI-624252;
CC O75410-6:TACC1; NbExp=2; IntAct=EBI-310585, EBI-624278;
CC Q9Y6A5:TACC3; NbExp=5; IntAct=EBI-310585, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle
CC pole. Note=Detected on centrosomes during interphase. Detected on
CC spindle poles and microtubules during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14008-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14008-2; Sequence=VSP_035668;
CC Name=3;
CC IsoId=Q14008-3; Sequence=VSP_036400;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Overexpressed in hepatomas and colonic tumors.
CC Also expressed in skeletal muscle, brain, heart, placenta, lung,
CC liver, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC -!- SIMILARITY: Contains 10 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17856.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH70136.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAI11044.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAI20871.1; Type=Frameshift; Positions=18;
CC Sequence=BAA07892.2; Type=Erroneous initiation;
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DR EMBL; X92474; CAA63212.1; -; mRNA.
DR EMBL; D43948; BAA07892.2; ALT_INIT; mRNA.
DR EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017856; AAH17856.1; ALT_SEQ; mRNA.
DR EMBL; BC070136; AAH70136.1; ALT_SEQ; mRNA.
DR EMBL; BC111043; AAI11044.1; ALT_SEQ; mRNA.
DR EMBL; BC120869; AAI20870.1; -; mRNA.
DR EMBL; BC120870; AAI20871.1; ALT_FRAME; mRNA.
DR PIR; S68176; S68176.
DR RefSeq; NP_001008938.1; NM_001008938.3.
DR RefSeq; NP_055571.2; NM_014756.3.
DR UniGene; Hs.201253; -.
DR UniGene; Hs.737795; -.
DR ProteinModelPortal; Q14008; -.
DR SMR; Q14008; 10-248, 269-499, 729-779, 1322-1348.
DR IntAct; Q14008; 22.
DR MINT; MINT-5002817; -.
DR STRING; 9606.ENSP00000346566; -.
DR PhosphoSite; Q14008; -.
DR DMDM; 212276513; -.
DR PaxDb; Q14008; -.
DR PRIDE; Q14008; -.
DR Ensembl; ENST00000312055; ENSP00000310227; ENSG00000175216.
DR Ensembl; ENST00000354558; ENSP00000346566; ENSG00000175216.
DR Ensembl; ENST00000415402; ENSP00000395302; ENSG00000175216.
DR Ensembl; ENST00000529230; ENSP00000432768; ENSG00000175216.
DR GeneID; 9793; -.
DR KEGG; hsa:9793; -.
DR UCSC; uc001ndi.2; human.
DR CTD; 9793; -.
DR GeneCards; GC11M048794; -.
DR H-InvDB; HIX0022364; -.
DR HGNC; HGNC:28959; CKAP5.
DR HPA; HPA039377; -.
DR HPA; HPA040375; -.
DR MIM; 611142; gene.
DR neXtProt; NX_Q14008; -.
DR PharmGKB; PA142672107; -.
DR eggNOG; NOG253097; -.
DR HOVERGEN; HBG050955; -.
DR InParanoid; Q14008; -.
DR KO; K16803; -.
DR OMA; TLQMAHV; -.
DR OrthoDB; EOG751NDM; -.
DR PhylomeDB; Q14008; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; CKAP5; human.
DR GeneWiki; CKAP5; -.
DR GenomeRNAi; 9793; -.
DR NextBio; 36878; -.
DR PRO; PR:Q14008; -.
DR ArrayExpress; Q14008; -.
DR Bgee; Q14008; -.
DR CleanEx; HS_CKAP5; -.
DR Genevestigator; Q14008; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051297; P:centrosome organization; IMP:HGNC.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:HGNC.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0050658; P:RNA transport; ISS:HGNC.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 6.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF12348; CLASP_N; 2.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 10.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 2032 Cytoskeleton-associated protein 5.
FT /FTId=PRO_0000089663.
FT REPEAT 159 197 HEAT 1.
FT REPEAT 356 394 HEAT 2.
FT REPEAT 434 472 HEAT 3.
FT REPEAT 750 788 HEAT 4.
FT REPEAT 855 893 HEAT 5.
FT REPEAT 936 974 HEAT 6.
FT REPEAT 1013 1051 HEAT 7.
FT REPEAT 1284 1322 HEAT 8.
FT REPEAT 1324 1357 HEAT 9.
FT REPEAT 1361 1399 HEAT 10.
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 816 816 Phosphoserine.
FT VAR_SEQ 1564 1623 Missing (in isoform 2).
FT /FTId=VSP_035668.
FT VAR_SEQ 1774 1774 K -> KSCMCLPQ (in isoform 3).
FT /FTId=VSP_036400.
FT VARIANT 785 785 Y -> C (in dbSNP:rs11038988).
FT /FTId=VAR_045627.
FT CONFLICT 476 476 N -> K (in Ref. 1; CAA63212 and 2;
FT BAA07892).
FT CONFLICT 1814 1814 E -> A (in Ref. 1; CAA63212).
FT CONFLICT 1822 1822 E -> A (in Ref. 1; CAA63212).
SQ SEQUENCE 2032 AA; 225495 MW; B2BBFB1CF2ED688B CRC64;
MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKFL GLIKKFVTDS
NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYIEIE
KGEAVQEELL KGLDNKNPKI IVACIETLRK ALSEFGSKII LLKPIIKVLP KLFESREKAV
RDEAKLIAVE IYRWIRDALR PPLQNINSVQ LKELEEEWVK LPTSAPRPTR FLRSQQELEA
KLEQQQSAGG DAEGGGDDGD EVPQIDAYEL LEAVEILSKL PKDFYDKIEA KKWQERKEAL
ESVEVLIKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG LRKKFGQYAG
HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED VLAVMDNKNP TIKQQTSLFI
ARSFRHCTAS TLPKSLLKPF CAALLKHIND SAPEVRDAAF EALGTALKVV GEKAVNPFLA
DVDKLKLDKI KECSEKVELI HGKKAGLAAD KKEFKPLPGR TAASGAAGDK DTKDISAPKP
GPLKKAPAAK AGGPPKKGKP AAPGGAGNTG TKNKKGLETK EIVEPELSIE VCEEKASAVL
PPTCIQLLDS SNWKERLACM EEFQKAVELM DRTEMPCQAL VRMLAKKPGW KETNFQVMQM
KLHIVALIAQ KGNFSKTSAQ VVLDGLVDKI GDVKCGNNAK EAMTAIAEAC MLPWTAEQVV
SMAFSQKNPK NQSETLNWLS NAIKEFGFSG LNVKAFISNV KTALAATNPA VRTAAITLLG
VMYLYVGPSL RMFFEDEKPA LLSQIDAEFE KMQGQSPPAP TRGISKHSTS GTDEGEDGDE
PDDGSNDVVD LLPRTEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIIND AKFIQPNIGE
LPTALKGRLN DSNKILVQQT LNILQQLAVA MGPNIKQHVK NLGIPIITVL GDSKNNVRAA
ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG WLAEKLPTLR STPTDLILCV
PHLYSCLEDR NGDVRKKAQD ALPFFMMHLG YEKMAKATGK LKPTSKDQVL AMLEKAKVNM
PAKPAPPTKA TSKPMGGSAP AKFQPASAPA EDCISSSTEP KPDPKKAKAP GLSSKAKSAQ
GKKMPSKTSL KEDEDKSGPI FIVVPNGKEQ RMKDEKGLKV LKWNFTTPRD EYIEQLKTQM
SSCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKEGVIG CLDLILKWLT LRFFDTNTSV
LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLVVKVGE PKDVIRKDVR AILNRMCLVY
PASKMFPFIM EGTKSKNSKQ RAECLEELGC LVESYGMNVC QPTPGKALKE IAVHIGDRDN
AVRNAALNTI VTVYNVHGDQ VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PIKQVEEKPQ
RAQNISSNAN MLRKGPAEDM SSKLNQARSM SGHPEAAQMV RREFQLDLDE IENDNGTVRC
EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA
LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYNTHM ADEKLEKDEI IKLYSCIIGN
MISLFQIESL AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD
QTNILSALLV LLQDSLLATA SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM
KVFPKEKLKQ CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL AELYEYKKKY
SDADIEPFLK NSSQFFQSYV ERGLRVIEME REGKGRISTS TGISPQMEVT CVPTPTSTVS
SIGNTNGEEV GPSVYLERLK ILRQRCGLDN TKQDDRPPLT SLLSKPAVPT VASSTDMLHS
KLSQLRESRE QHQHSDLDSN QTHSSGTVTS SSSTANIDDL KKRLERIKSS RK
//
ID CKAP5_HUMAN Reviewed; 2032 AA.
AC Q14008; Q05D70; Q0VAX7; Q0VAX8; Q14668; Q2TA89; Q6NSH4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-NOV-2008, sequence version 3.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Cytoskeleton-associated protein 5;
DE AltName: Full=Colonic and hepatic tumor overexpressed gene protein;
DE Short=Ch-TOG;
GN Name=CKAP5; Synonyms=KIAA0097;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain tumor;
RX PubMed=8536682; DOI=10.1111/j.1432-1033.1995.406_b.x;
RA Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C.;
RT "Characterization of the cDNA and pattern of expression of a new gene
RT over-expressed in human hepatomas and colonic tumors.";
RL Eur. J. Biochem. 234:406-413(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH TACC1.
RX PubMed=11903063; DOI=10.1042/0264-6021:3630195;
RA Lauffart B., Howell S.J., Tasch J.E., Cowell J.K., Still I.H.;
RT "Interaction of the transforming acidic coiled-coil 1 (TACC1) protein
RT with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing protein
RT complexes in human cells.";
RL Biochem. J. 363:195-200(2002).
RN [6]
RP FUNCTION.
RX PubMed=12569123; DOI=10.1101/gad.245603;
RA Gergely F., Draviam V.M., Raff J.W.;
RT "The ch-TOG/XMAP215 protein is essential for spindle pole organization
RT in human somatic cells.";
RL Genes Dev. 17:336-341(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, INTERACTION WITH SLAIN2, AND SUBCELLULAR LOCATION.
RX PubMed=21646404; DOI=10.1083/jcb.201012179;
RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V.,
RA Gouveia S.M., Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C.,
RA Steinmetz M.O., Akhmanova A.;
RT "SLAIN2 links microtubule plus end-tracking proteins and controls
RT microtubule growth in interphase.";
RL J. Cell Biol. 193:1083-1099(2011).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC microtubule dynamics and microtubule organization. Promotes
CC cytoplasmic microtubule nucleation and elongation. Plays a major
CC role in organizing spindle poles.
CC -!- SUBUNIT: Interacts with TACC1. Interacts with SLAIN2.
CC -!- INTERACTION:
CC P16333:NCK1; NbExp=3; IntAct=EBI-310585, EBI-389883;
CC O75410:TACC1; NbExp=3; IntAct=EBI-310585, EBI-624237;
CC O75410-1:TACC1; NbExp=3; IntAct=EBI-310585, EBI-624252;
CC O75410-6:TACC1; NbExp=2; IntAct=EBI-310585, EBI-624278;
CC Q9Y6A5:TACC3; NbExp=5; IntAct=EBI-310585, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle
CC pole. Note=Detected on centrosomes during interphase. Detected on
CC spindle poles and microtubules during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14008-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14008-2; Sequence=VSP_035668;
CC Name=3;
CC IsoId=Q14008-3; Sequence=VSP_036400;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Overexpressed in hepatomas and colonic tumors.
CC Also expressed in skeletal muscle, brain, heart, placenta, lung,
CC liver, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC -!- SIMILARITY: Contains 10 HEAT repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17856.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAH70136.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAI11044.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC Sequence=AAI20871.1; Type=Frameshift; Positions=18;
CC Sequence=BAA07892.2; Type=Erroneous initiation;
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DR EMBL; X92474; CAA63212.1; -; mRNA.
DR EMBL; D43948; BAA07892.2; ALT_INIT; mRNA.
DR EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017856; AAH17856.1; ALT_SEQ; mRNA.
DR EMBL; BC070136; AAH70136.1; ALT_SEQ; mRNA.
DR EMBL; BC111043; AAI11044.1; ALT_SEQ; mRNA.
DR EMBL; BC120869; AAI20870.1; -; mRNA.
DR EMBL; BC120870; AAI20871.1; ALT_FRAME; mRNA.
DR PIR; S68176; S68176.
DR RefSeq; NP_001008938.1; NM_001008938.3.
DR RefSeq; NP_055571.2; NM_014756.3.
DR UniGene; Hs.201253; -.
DR UniGene; Hs.737795; -.
DR ProteinModelPortal; Q14008; -.
DR SMR; Q14008; 10-248, 269-499, 729-779, 1322-1348.
DR IntAct; Q14008; 22.
DR MINT; MINT-5002817; -.
DR STRING; 9606.ENSP00000346566; -.
DR PhosphoSite; Q14008; -.
DR DMDM; 212276513; -.
DR PaxDb; Q14008; -.
DR PRIDE; Q14008; -.
DR Ensembl; ENST00000312055; ENSP00000310227; ENSG00000175216.
DR Ensembl; ENST00000354558; ENSP00000346566; ENSG00000175216.
DR Ensembl; ENST00000415402; ENSP00000395302; ENSG00000175216.
DR Ensembl; ENST00000529230; ENSP00000432768; ENSG00000175216.
DR GeneID; 9793; -.
DR KEGG; hsa:9793; -.
DR UCSC; uc001ndi.2; human.
DR CTD; 9793; -.
DR GeneCards; GC11M048794; -.
DR H-InvDB; HIX0022364; -.
DR HGNC; HGNC:28959; CKAP5.
DR HPA; HPA039377; -.
DR HPA; HPA040375; -.
DR MIM; 611142; gene.
DR neXtProt; NX_Q14008; -.
DR PharmGKB; PA142672107; -.
DR eggNOG; NOG253097; -.
DR HOVERGEN; HBG050955; -.
DR InParanoid; Q14008; -.
DR KO; K16803; -.
DR OMA; TLQMAHV; -.
DR OrthoDB; EOG751NDM; -.
DR PhylomeDB; Q14008; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; CKAP5; human.
DR GeneWiki; CKAP5; -.
DR GenomeRNAi; 9793; -.
DR NextBio; 36878; -.
DR PRO; PR:Q14008; -.
DR ArrayExpress; Q14008; -.
DR Bgee; Q14008; -.
DR CleanEx; HS_CKAP5; -.
DR Genevestigator; Q14008; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051297; P:centrosome organization; IMP:HGNC.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IMP:HGNC.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0050658; P:RNA transport; ISS:HGNC.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 6.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF12348; CLASP_N; 2.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 10.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Complete proteome; Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 2032 Cytoskeleton-associated protein 5.
FT /FTId=PRO_0000089663.
FT REPEAT 159 197 HEAT 1.
FT REPEAT 356 394 HEAT 2.
FT REPEAT 434 472 HEAT 3.
FT REPEAT 750 788 HEAT 4.
FT REPEAT 855 893 HEAT 5.
FT REPEAT 936 974 HEAT 6.
FT REPEAT 1013 1051 HEAT 7.
FT REPEAT 1284 1322 HEAT 8.
FT REPEAT 1324 1357 HEAT 9.
FT REPEAT 1361 1399 HEAT 10.
FT MOD_RES 48 48 N6-acetyllysine.
FT MOD_RES 816 816 Phosphoserine.
FT VAR_SEQ 1564 1623 Missing (in isoform 2).
FT /FTId=VSP_035668.
FT VAR_SEQ 1774 1774 K -> KSCMCLPQ (in isoform 3).
FT /FTId=VSP_036400.
FT VARIANT 785 785 Y -> C (in dbSNP:rs11038988).
FT /FTId=VAR_045627.
FT CONFLICT 476 476 N -> K (in Ref. 1; CAA63212 and 2;
FT BAA07892).
FT CONFLICT 1814 1814 E -> A (in Ref. 1; CAA63212).
FT CONFLICT 1822 1822 E -> A (in Ref. 1; CAA63212).
SQ SEQUENCE 2032 AA; 225495 MW; B2BBFB1CF2ED688B CRC64;
MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKFL GLIKKFVTDS
NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYIEIE
KGEAVQEELL KGLDNKNPKI IVACIETLRK ALSEFGSKII LLKPIIKVLP KLFESREKAV
RDEAKLIAVE IYRWIRDALR PPLQNINSVQ LKELEEEWVK LPTSAPRPTR FLRSQQELEA
KLEQQQSAGG DAEGGGDDGD EVPQIDAYEL LEAVEILSKL PKDFYDKIEA KKWQERKEAL
ESVEVLIKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG LRKKFGQYAG
HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED VLAVMDNKNP TIKQQTSLFI
ARSFRHCTAS TLPKSLLKPF CAALLKHIND SAPEVRDAAF EALGTALKVV GEKAVNPFLA
DVDKLKLDKI KECSEKVELI HGKKAGLAAD KKEFKPLPGR TAASGAAGDK DTKDISAPKP
GPLKKAPAAK AGGPPKKGKP AAPGGAGNTG TKNKKGLETK EIVEPELSIE VCEEKASAVL
PPTCIQLLDS SNWKERLACM EEFQKAVELM DRTEMPCQAL VRMLAKKPGW KETNFQVMQM
KLHIVALIAQ KGNFSKTSAQ VVLDGLVDKI GDVKCGNNAK EAMTAIAEAC MLPWTAEQVV
SMAFSQKNPK NQSETLNWLS NAIKEFGFSG LNVKAFISNV KTALAATNPA VRTAAITLLG
VMYLYVGPSL RMFFEDEKPA LLSQIDAEFE KMQGQSPPAP TRGISKHSTS GTDEGEDGDE
PDDGSNDVVD LLPRTEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIIND AKFIQPNIGE
LPTALKGRLN DSNKILVQQT LNILQQLAVA MGPNIKQHVK NLGIPIITVL GDSKNNVRAA
ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG WLAEKLPTLR STPTDLILCV
PHLYSCLEDR NGDVRKKAQD ALPFFMMHLG YEKMAKATGK LKPTSKDQVL AMLEKAKVNM
PAKPAPPTKA TSKPMGGSAP AKFQPASAPA EDCISSSTEP KPDPKKAKAP GLSSKAKSAQ
GKKMPSKTSL KEDEDKSGPI FIVVPNGKEQ RMKDEKGLKV LKWNFTTPRD EYIEQLKTQM
SSCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKEGVIG CLDLILKWLT LRFFDTNTSV
LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLVVKVGE PKDVIRKDVR AILNRMCLVY
PASKMFPFIM EGTKSKNSKQ RAECLEELGC LVESYGMNVC QPTPGKALKE IAVHIGDRDN
AVRNAALNTI VTVYNVHGDQ VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PIKQVEEKPQ
RAQNISSNAN MLRKGPAEDM SSKLNQARSM SGHPEAAQMV RREFQLDLDE IENDNGTVRC
EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA
LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYNTHM ADEKLEKDEI IKLYSCIIGN
MISLFQIESL AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD
QTNILSALLV LLQDSLLATA SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM
KVFPKEKLKQ CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL AELYEYKKKY
SDADIEPFLK NSSQFFQSYV ERGLRVIEME REGKGRISTS TGISPQMEVT CVPTPTSTVS
SIGNTNGEEV GPSVYLERLK ILRQRCGLDN TKQDDRPPLT SLLSKPAVPT VASSTDMLHS
KLSQLRESRE QHQHSDLDSN QTHSSGTVTS SSSTANIDDL KKRLERIKSS RK
//
MIM
611142
*RECORD*
*FIELD* NO
611142
*FIELD* TI
*611142 CYTOSKELETON-ASSOCIATED PROTEIN 5; CKAP5
;;COLONIC AND HEPATIC TUMOR OVEREXPRESSED GENE; CHTOG;;
read moreMINI SPINDLES, DROSOPHILA, HOMOLOG OF; MSPS;;
KIAA0097
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid
cell line cDNA library, Nagase et al. (1995) cloned CKAP5, which they
designated KIAA0097. The deduced protein contains 2,032 amino acids.
Northern blot analysis detected highest expression in skeletal muscle
and lower expression in all other tissues and cell lines examined,
except peripheral blood leukocytes.
Using TACC1 (605301) as bait in a yeast 2-hybrid screen of a mammary
epithelial cDNA library, Lauffart et al. (2002) cloned CKAP5, which they
called CHTOG. CHTOG contains a microtubule-binding domain in its
N-terminal half and a KXGS motif for binding tubulin (see 191110) dimers
in its C-terminal half.
GENE FUNCTION
Using RNA interference in HeLa cells, Gergely et al. (2003) found that
TACC3 (605303) depletion did not alter spindle organization, but partly
destabilized microtubules and redistributed CHTOG away from spindle
microtubules. In CHTOG-depleted cells, relatively robust spindles
formed, but they were highly disorganized. Gergely et al. (2003)
concluded that CHTOG plays a major role in organizing spindle poles,
whereas its role in stabilizing spindle microtubules is minor and, at
least in part, mediated via interaction with TACC3.
Brouhard et al. (2008) showed that the Xenopus CKAP5 ortholog, Xmap215,
functioned as a processive microtubule polymerase. Recombinant Xmap215
bound free porcine brain tubulin in a 1:1 complex that interacted with
the microtubule lattice and targeted the ends by a diffusion-facilitated
mechanism. Xmap215 persisted at the plus end and catalyzed the addition
of up to 25 tubulin dimers. Under some circumstances, Xmap215 catalyzed
the reverse reaction, microtubule shrinkage.
MAPPING
Using human-rodent hybrid cell lines, Nagase et al. (1995) mapped the
CKAP5 gene to chromosome 11.
*FIELD* RF
1. Brouhard, G. J.; Stear, J. H.; Noetzel, T. L.; Al-Bassam, J.; Kinoshita,
K.; Harrison, S. C.; Howard, J.; Hyman, A. A.: XMAP215 is a processive
microtubule polymerase. Cell 132: 79-88, 2008.
2. Gergely, F.; Draviam, V. M.; Raff, J. W.: The ch-TOG/XMAP215 protein
is essential for spindle pole organization in human somatic cells. Genes
Dev. 17: 336-341, 2003.
3. Lauffart, B.; Howell, S. J.; Tasch, J. E.; Cowell, J. K.; Still,
I. H.: Interaction of the transforming acidic coiled-coil 1 (TACC1)
protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing
protein complexes in human cells. Biochem. J. 363: 195-200, 2002.
4. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CN
Patricia A. Hartz - updated: 3/12/2008
*FIELD* CD
Patricia A. Hartz: 6/27/2007
*FIELD* ED
mgross: 03/13/2008
terry: 3/12/2008
mgross: 6/27/2007
*RECORD*
*FIELD* NO
611142
*FIELD* TI
*611142 CYTOSKELETON-ASSOCIATED PROTEIN 5; CKAP5
;;COLONIC AND HEPATIC TUMOR OVEREXPRESSED GENE; CHTOG;;
read moreMINI SPINDLES, DROSOPHILA, HOMOLOG OF; MSPS;;
KIAA0097
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated immature myeloid
cell line cDNA library, Nagase et al. (1995) cloned CKAP5, which they
designated KIAA0097. The deduced protein contains 2,032 amino acids.
Northern blot analysis detected highest expression in skeletal muscle
and lower expression in all other tissues and cell lines examined,
except peripheral blood leukocytes.
Using TACC1 (605301) as bait in a yeast 2-hybrid screen of a mammary
epithelial cDNA library, Lauffart et al. (2002) cloned CKAP5, which they
called CHTOG. CHTOG contains a microtubule-binding domain in its
N-terminal half and a KXGS motif for binding tubulin (see 191110) dimers
in its C-terminal half.
GENE FUNCTION
Using RNA interference in HeLa cells, Gergely et al. (2003) found that
TACC3 (605303) depletion did not alter spindle organization, but partly
destabilized microtubules and redistributed CHTOG away from spindle
microtubules. In CHTOG-depleted cells, relatively robust spindles
formed, but they were highly disorganized. Gergely et al. (2003)
concluded that CHTOG plays a major role in organizing spindle poles,
whereas its role in stabilizing spindle microtubules is minor and, at
least in part, mediated via interaction with TACC3.
Brouhard et al. (2008) showed that the Xenopus CKAP5 ortholog, Xmap215,
functioned as a processive microtubule polymerase. Recombinant Xmap215
bound free porcine brain tubulin in a 1:1 complex that interacted with
the microtubule lattice and targeted the ends by a diffusion-facilitated
mechanism. Xmap215 persisted at the plus end and catalyzed the addition
of up to 25 tubulin dimers. Under some circumstances, Xmap215 catalyzed
the reverse reaction, microtubule shrinkage.
MAPPING
Using human-rodent hybrid cell lines, Nagase et al. (1995) mapped the
CKAP5 gene to chromosome 11.
*FIELD* RF
1. Brouhard, G. J.; Stear, J. H.; Noetzel, T. L.; Al-Bassam, J.; Kinoshita,
K.; Harrison, S. C.; Howard, J.; Hyman, A. A.: XMAP215 is a processive
microtubule polymerase. Cell 132: 79-88, 2008.
2. Gergely, F.; Draviam, V. M.; Raff, J. W.: The ch-TOG/XMAP215 protein
is essential for spindle pole organization in human somatic cells. Genes
Dev. 17: 336-341, 2003.
3. Lauffart, B.; Howell, S. J.; Tasch, J. E.; Cowell, J. K.; Still,
I. H.: Interaction of the transforming acidic coiled-coil 1 (TACC1)
protein with ch-TOG and GAS41/NuBI1 suggests multiple TACC1-containing
protein complexes in human cells. Biochem. J. 363: 195-200, 2002.
4. Nagase, T; Miyajima, N; Tanaka, A.; Sazuka, T.; Seki, N.; Sato,
S.; Tabata, S.; Ishikawa, K.; Kawarabayashi, Y.; Kotani, H.; Nomura,
N.: Prediction of the coding sequences of unidentified human genes.
III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced
by analysis of cDNA clones from human cell line KG-1. DNA Res. 2:
37-43, 1995.
*FIELD* CN
Patricia A. Hartz - updated: 3/12/2008
*FIELD* CD
Patricia A. Hartz: 6/27/2007
*FIELD* ED
mgross: 03/13/2008
terry: 3/12/2008
mgross: 6/27/2007