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Protein

Cytoskeleton-associated protein 5

Gene

CKAP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (PubMed:27156448).7 Publications

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • centrosome duplication Source: GO_Central
  • centrosome organization Source: HGNC
  • establishment or maintenance of microtubule cytoskeleton polarity Source: HGNC
  • G2/M transition of mitotic cell cycle Source: Reactome
  • microtubule polymerization Source: GO_Central
  • mitotic nuclear division Source: UniProtKB-KW
  • RNA transport Source: HGNC
  • sister chromatid cohesion Source: Reactome
  • spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175216-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoskeleton-associated protein 5
Alternative name(s):
Colonic and hepatic tumor overexpressed gene protein
Short name:
Ch-TOG
Gene namesi
Name:CKAP5
Synonyms:KIAA0097
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28959. CKAP5.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • centrosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • membrane Source: UniProtKB
  • protein complex Source: MGI
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1939L → A or R: Disrupts interaction with TACC3. 1 Publication1
Mutagenesisi1939L → A: Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1942. 1 Publication1
Mutagenesisi1942L → A or R: Disrupts interaction with TACC3. 1 Publication1
Mutagenesisi1942L → A: Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1939. 1 Publication1

Organism-specific databases

DisGeNETi9793.
OpenTargetsiENSG00000175216.
PharmGKBiPA142672107.

Polymorphism and mutation databases

BioMutaiCKAP5.
DMDMi212276513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000896631 – 2032Cytoskeleton-associated protein 5Add BLAST2032

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysineCombined sources1
Modified residuei816PhosphoserineCombined sources1
Modified residuei845PhosphoserineCombined sources1
Modified residuei1469PhosphoserineCombined sources1
Modified residuei1861PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14008.
MaxQBiQ14008.
PaxDbiQ14008.
PeptideAtlasiQ14008.
PRIDEiQ14008.

PTM databases

iPTMnetiQ14008.
PhosphoSitePlusiQ14008.
SwissPalmiQ14008.

Expressioni

Tissue specificityi

Overexpressed in hepatomas and colonic tumors. Also expressed in skeletal muscle, brain, heart, placenta, lung, liver, kidney and pancreas. Expression is elevated in the brain; highly expressed in the Purkinje cell bodies of the cerebellum.2 Publications

Gene expression databases

BgeeiENSG00000175216.
CleanExiHS_CKAP5.
ExpressionAtlasiQ14008. baseline and differential.
GenevisibleiQ14008. HS.

Organism-specific databases

HPAiHPA039377.
HPA040375.

Interactioni

Subunit structurei

Interacts with TACC1 (PubMed:11903063). Interacts with SLAIN2 (PubMed:21646404). Interacts with HNRNPA2B1 (PubMed:15703215). Interacts with TACC3 independently of clathrin. Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges (PubMed:21297582). Interacts with NDC80; indicative for an association with the NDC80 comnplex (PubMed:27156448).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-310585,EBI-389883
SLAIN2Q9P2704EBI-310585,EBI-3959887
TACC1O754104EBI-310585,EBI-624237
TACC1O75410-13EBI-310585,EBI-624252
TACC1O75410-62EBI-310585,EBI-624278
TACC3Q9Y6A57EBI-310585,EBI-2554984

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115137. 97 interactors.
IntActiQ14008. 65 interactors.
MINTiMINT-5002817.
STRINGi9606.ENSP00000432768.

Structurei

Secondary structure

12032
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi858 – 860Combined sources3
Helixi863 – 869Combined sources7
Helixi874 – 891Combined sources18
Beta strandi892 – 894Combined sources3
Helixi901 – 906Combined sources6
Turni907 – 910Combined sources4
Helixi914 – 931Combined sources18
Helixi932 – 938Combined sources7
Turni939 – 942Combined sources4
Helixi943 – 948Combined sources6
Helixi949 – 951Combined sources3
Helixi955 – 972Combined sources18
Helixi975 – 978Combined sources4
Beta strandi979 – 981Combined sources3
Helixi982 – 987Combined sources6
Helixi992 – 1005Combined sources14
Helixi1006 – 1008Combined sources3
Helixi1016 – 1019Combined sources4
Helixi1020 – 1027Combined sources8
Helixi1032 – 1049Combined sources18
Helixi1051 – 1056Combined sources6
Helixi1057 – 1060Combined sources4
Helixi1063 – 1076Combined sources14
Helixi1077 – 1079Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QMIX-ray1.90A/B846-1081[»]
4QMJX-ray2.50A846-1081[»]
ProteinModelPortaliQ14008.
SMRiQ14008.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati159 – 197HEAT 1Add BLAST39
Repeati356 – 394HEAT 2Add BLAST39
Repeati434 – 472HEAT 3Add BLAST39
Repeati750 – 788HEAT 4Add BLAST39
Repeati855 – 893HEAT 5Add BLAST39
Repeati936 – 974HEAT 6Add BLAST39
Repeati1013 – 1051HEAT 7Add BLAST39
Repeati1284 – 1322HEAT 8Add BLAST39
Repeati1324 – 1357HEAT 9Add BLAST34
Repeati1361 – 1399HEAT 10Add BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 223TOG 11 PublicationAdd BLAST223
Regioni268 – 502TOG 21 PublicationAdd BLAST235
Regioni588 – 817TOG 31 PublicationAdd BLAST230
Regioni853 – 1081TOG 41 PublicationAdd BLAST229
Regioni1193 – 1428TOG 51 PublicationAdd BLAST236
Regioni1932 – 1957Interaction with TACC31 PublicationAdd BLAST26

Domaini

The TOG (tumor overexpressed gene) domains are arranged in a N-terminal pentameric array with each domain composed of six (for the most part non-canonical) HEAT repeats forming a oblong paddle-like structure. Intra-HEAT loops are positioned along a face of the TOG domain and bind to a single alpha/beta-tubulin heterodimer. The TOG domains in the array seem to be structurally and functionally polarized. Differential functions may range from mictotubule (MT) lattice binding and/or free tubulin heterodimer binding to potentiating stable incorporation of tubulin into the MT lattice.1 Publication

Sequence similaritiesi

Belongs to the TOG/XMAP215 family.Curated
Contains 10 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1820. Eukaryota.
ENOG410XPTW. LUCA.
GeneTreeiENSGT00390000014757.
HOVERGENiHBG050955.
InParanoidiQ14008.
KOiK16803.
OMAiIFLPCLM.
OrthoDBiEOG091G00YR.
PhylomeDBiQ14008.
TreeFamiTF105639.

Family and domain databases

Gene3Di1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF12348. CLASP_N. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 10 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14008-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKFL
60 70 80 90 100
GLIKKFVTDS NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ
110 120 130 140 150
PKAKAKELGI EICLMYIEIE KGEAVQEELL KGLDNKNPKI IVACIETLRK
160 170 180 190 200
ALSEFGSKII LLKPIIKVLP KLFESREKAV RDEAKLIAVE IYRWIRDALR
210 220 230 240 250
PPLQNINSVQ LKELEEEWVK LPTSAPRPTR FLRSQQELEA KLEQQQSAGG
260 270 280 290 300
DAEGGGDDGD EVPQIDAYEL LEAVEILSKL PKDFYDKIEA KKWQERKEAL
310 320 330 340 350
ESVEVLIKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG
360 370 380 390 400
LRKKFGQYAG HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED
410 420 430 440 450
VLAVMDNKNP TIKQQTSLFI ARSFRHCTAS TLPKSLLKPF CAALLKHIND
460 470 480 490 500
SAPEVRDAAF EALGTALKVV GEKAVNPFLA DVDKLKLDKI KECSEKVELI
510 520 530 540 550
HGKKAGLAAD KKEFKPLPGR TAASGAAGDK DTKDISAPKP GPLKKAPAAK
560 570 580 590 600
AGGPPKKGKP AAPGGAGNTG TKNKKGLETK EIVEPELSIE VCEEKASAVL
610 620 630 640 650
PPTCIQLLDS SNWKERLACM EEFQKAVELM DRTEMPCQAL VRMLAKKPGW
660 670 680 690 700
KETNFQVMQM KLHIVALIAQ KGNFSKTSAQ VVLDGLVDKI GDVKCGNNAK
710 720 730 740 750
EAMTAIAEAC MLPWTAEQVV SMAFSQKNPK NQSETLNWLS NAIKEFGFSG
760 770 780 790 800
LNVKAFISNV KTALAATNPA VRTAAITLLG VMYLYVGPSL RMFFEDEKPA
810 820 830 840 850
LLSQIDAEFE KMQGQSPPAP TRGISKHSTS GTDEGEDGDE PDDGSNDVVD
860 870 880 890 900
LLPRTEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIIND AKFIQPNIGE
910 920 930 940 950
LPTALKGRLN DSNKILVQQT LNILQQLAVA MGPNIKQHVK NLGIPIITVL
960 970 980 990 1000
GDSKNNVRAA ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG
1010 1020 1030 1040 1050
WLAEKLPTLR STPTDLILCV PHLYSCLEDR NGDVRKKAQD ALPFFMMHLG
1060 1070 1080 1090 1100
YEKMAKATGK LKPTSKDQVL AMLEKAKVNM PAKPAPPTKA TSKPMGGSAP
1110 1120 1130 1140 1150
AKFQPASAPA EDCISSSTEP KPDPKKAKAP GLSSKAKSAQ GKKMPSKTSL
1160 1170 1180 1190 1200
KEDEDKSGPI FIVVPNGKEQ RMKDEKGLKV LKWNFTTPRD EYIEQLKTQM
1210 1220 1230 1240 1250
SSCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKEGVIG CLDLILKWLT
1260 1270 1280 1290 1300
LRFFDTNTSV LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLVVKVGE
1310 1320 1330 1340 1350
PKDVIRKDVR AILNRMCLVY PASKMFPFIM EGTKSKNSKQ RAECLEELGC
1360 1370 1380 1390 1400
LVESYGMNVC QPTPGKALKE IAVHIGDRDN AVRNAALNTI VTVYNVHGDQ
1410 1420 1430 1440 1450
VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PIKQVEEKPQ RAQNISSNAN
1460 1470 1480 1490 1500
MLRKGPAEDM SSKLNQARSM SGHPEAAQMV RREFQLDLDE IENDNGTVRC
1510 1520 1530 1540 1550
EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA
1560 1570 1580 1590 1600
SGDINTSIQA LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYNTHM
1610 1620 1630 1640 1650
ADEKLEKDEI IKLYSCIIGN MISLFQIESL AREASTGVLK DLMHGLITLM
1660 1670 1680 1690 1700
LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD QTNILSALLV LLQDSLLATA
1710 1720 1730 1740 1750
SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM KVFPKEKLKQ
1760 1770 1780 1790 1800
CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
1810 1820 1830 1840 1850
SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL
1860 1870 1880 1890 1900
AELYEYKKKY SDADIEPFLK NSSQFFQSYV ERGLRVIEME REGKGRISTS
1910 1920 1930 1940 1950
TGISPQMEVT CVPTPTSTVS SIGNTNGEEV GPSVYLERLK ILRQRCGLDN
1960 1970 1980 1990 2000
TKQDDRPPLT SLLSKPAVPT VASSTDMLHS KLSQLRESRE QHQHSDLDSN
2010 2020 2030
QTHSSGTVTS SSSTANIDDL KKRLERIKSS RK
Length:2,032
Mass (Da):225,495
Last modified:November 4, 2008 - v3
Checksum:iB2BBFB1CF2ED688B
GO
Isoform 2 (identifier: Q14008-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1564-1623: Missing.

Show »
Length:1,972
Mass (Da):218,525
Checksum:i17596E610D1B7FC9
GO
Isoform 3 (identifier: Q14008-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1774-1774: K → KSCMCLPQ

Note: No experimental confirmation available.
Show »
Length:2,039
Mass (Da):226,258
Checksum:i94281848BC2A3952
GO

Sequence cautioni

The sequence AAH17856 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH70136 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI11044 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI20871 differs from that shown. Reason: Frameshift at position 18.Curated
The sequence BAA07892 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti476N → K in CAA63212 (PubMed:8536682).Curated1
Sequence conflicti476N → K in BAA07892 (PubMed:7788527).Curated1
Sequence conflicti1814E → A in CAA63212 (PubMed:8536682).Curated1
Sequence conflicti1822E → A in CAA63212 (PubMed:8536682).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045627785Y → C.Corresponds to variant rs11038988dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0356681564 – 1623Missing in isoform 2. 1 PublicationAdd BLAST60
Alternative sequenceiVSP_0364001774K → KSCMCLPQ in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92474 mRNA. Translation: CAA63212.1.
D43948 mRNA. Translation: BAA07892.2. Different initiation.
AC115088 Genomic DNA. No translation available.
BC017856 mRNA. Translation: AAH17856.1. Sequence problems.
BC070136 mRNA. Translation: AAH70136.1. Sequence problems.
BC111043 mRNA. Translation: AAI11044.1. Sequence problems.
BC120869 mRNA. Translation: AAI20870.1.
BC120870 mRNA. Translation: AAI20871.1. Frameshift.
CCDSiCCDS31477.1. [Q14008-1]
CCDS7924.1. [Q14008-2]
PIRiS68176.
RefSeqiNP_001008938.1. NM_001008938.3. [Q14008-1]
NP_055571.2. NM_014756.3. [Q14008-2]
UniGeneiHs.201253.
Hs.737795.

Genome annotation databases

EnsembliENST00000312055; ENSP00000310227; ENSG00000175216. [Q14008-2]
ENST00000354558; ENSP00000346566; ENSG00000175216. [Q14008-2]
ENST00000529230; ENSP00000432768; ENSG00000175216. [Q14008-1]
GeneIDi9793.
KEGGihsa:9793.
UCSCiuc001ndi.3. human. [Q14008-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92474 mRNA. Translation: CAA63212.1.
D43948 mRNA. Translation: BAA07892.2. Different initiation.
AC115088 Genomic DNA. No translation available.
BC017856 mRNA. Translation: AAH17856.1. Sequence problems.
BC070136 mRNA. Translation: AAH70136.1. Sequence problems.
BC111043 mRNA. Translation: AAI11044.1. Sequence problems.
BC120869 mRNA. Translation: AAI20870.1.
BC120870 mRNA. Translation: AAI20871.1. Frameshift.
CCDSiCCDS31477.1. [Q14008-1]
CCDS7924.1. [Q14008-2]
PIRiS68176.
RefSeqiNP_001008938.1. NM_001008938.3. [Q14008-1]
NP_055571.2. NM_014756.3. [Q14008-2]
UniGeneiHs.201253.
Hs.737795.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QMIX-ray1.90A/B846-1081[»]
4QMJX-ray2.50A846-1081[»]
ProteinModelPortaliQ14008.
SMRiQ14008.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115137. 97 interactors.
IntActiQ14008. 65 interactors.
MINTiMINT-5002817.
STRINGi9606.ENSP00000432768.

PTM databases

iPTMnetiQ14008.
PhosphoSitePlusiQ14008.
SwissPalmiQ14008.

Polymorphism and mutation databases

BioMutaiCKAP5.
DMDMi212276513.

Proteomic databases

EPDiQ14008.
MaxQBiQ14008.
PaxDbiQ14008.
PeptideAtlasiQ14008.
PRIDEiQ14008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312055; ENSP00000310227; ENSG00000175216. [Q14008-2]
ENST00000354558; ENSP00000346566; ENSG00000175216. [Q14008-2]
ENST00000529230; ENSP00000432768; ENSG00000175216. [Q14008-1]
GeneIDi9793.
KEGGihsa:9793.
UCSCiuc001ndi.3. human. [Q14008-1]

Organism-specific databases

CTDi9793.
DisGeNETi9793.
GeneCardsiCKAP5.
H-InvDBHIX0022364.
HGNCiHGNC:28959. CKAP5.
HPAiHPA039377.
HPA040375.
MIMi611142. gene.
neXtProtiNX_Q14008.
OpenTargetsiENSG00000175216.
PharmGKBiPA142672107.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1820. Eukaryota.
ENOG410XPTW. LUCA.
GeneTreeiENSGT00390000014757.
HOVERGENiHBG050955.
InParanoidiQ14008.
KOiK16803.
OMAiIFLPCLM.
OrthoDBiEOG091G00YR.
PhylomeDBiQ14008.
TreeFamiTF105639.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175216-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiCKAP5. human.
GeneWikiiCKAP5.
GenomeRNAii9793.
PROiQ14008.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175216.
CleanExiHS_CKAP5.
ExpressionAtlasiQ14008. baseline and differential.
GenevisibleiQ14008. HS.

Family and domain databases

Gene3Di1.25.10.10. 6 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024395. CLASP_N_dom.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF12348. CLASP_N. 3 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 10 hits.
PROSITEiPS50077. HEAT_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCKAP5_HUMAN
AccessioniPrimary (citable) accession number: Q14008
Secondary accession number(s): Q05D70
, Q0VAX7, Q0VAX8, Q14668, Q2TA89, Q6NSH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 4, 2008
Last modified: November 30, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.