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UniProtKB - Q14008 (CKAP5_HUMAN)

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Protein

Cytoskeleton-associated protein 5

Gene

CKAP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • centrosome cycle Source: HGNC
  • centrosome duplication Source: GO_Central
  • ciliary basal body-plasma membrane docking Source: Reactome
  • establishment or maintenance of microtubule cytoskeleton polarity Source: HGNC
  • G2/M transition of mitotic cell cycle Source: Reactome
  • microtubule depolymerization Source: ARUK-UCL
  • microtubule polymerization Source: GO_Central
  • regulation of G2/M transition of mitotic cell cycle Source: Reactome
  • RNA transport Source: HGNC
  • spindle organization Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000175216.14
HGNCiHGNC:28959 CKAP5
MIMi611142 gene
neXtProtiNX_Q14008

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi59791
59792 [Q14008-2]
59793 [Q14008-3]

PTM databases

CarbonylDBiQ14008
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 and SLAIN1 (PubMed:21646404). Interacts with HNRNPA2B1 (PubMed:15703215). Interacts with TACC3 independently of clathrin (PubMed:25596274). Interacts with TACC3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges (PubMed:21297582, PubMed:23532825). Interacts with NDC80; indicative for an association with the NDC80 complex (PubMed:27156448).7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi115137, 106 interactors
CORUMiQ14008
IntActiQ14008, 66 interactors
MINTiQ14008
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

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 microtubule (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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1820 Eukaryota
ENOG410XPTW LUCA
GeneTreeiENSGT00390000014757
HOVERGENiHBG050955
InParanoidiQ14008
KOiK16803
OMAiTEMPCQA
OrthoDBiEOG091G00YR
PhylomeDBiQ14008
TreeFamiTF105639

Family and domain databases

Gene3Di1.25.10.10, 5 hits
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024395 CLASP_N_dom
IPR021133 HEAT_type_2
IPR034085 TOG
PfamiView protein in Pfam
PF12348 CLASP_N, 3 hits
SMARTiView protein in SMART
SM01349 TOG, 5 hits
SUPFAMiSSF48371 SSF48371, 10 hits
PROSITEiView protein in PROSITE
PS50077 HEAT_REPEAT, 1 hit

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 dbSNP:rs11038988Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiCKAP5_HUMAN
AccessioniPrimary (citable) accession number: Q14008
Secondary accession number(s): Q05D70
, Q0VAX7, Q0VAX8, Q14668, Q2TA89, Q6NSH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 4, 2008
Last modified: June 20, 2018
This is version 177 of the entry and version 3 of the sequence. See 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

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