Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 75 (18 Sep 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Cytoskeleton-associated protein 5-A

Gene

ckap5-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:12176362, PubMed:18191222, PubMed:21282620). Plays a major role in organizing spindle poles (PubMed:23974040). 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. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments (By similarity).By similarity4 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell cycle, Cell division, Mitosis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytoskeleton-associated protein 5-A
Alternative name(s):
Microtubule-associated protein 215 kDa
XMAP215
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ckap5-a
Synonyms:xmap215
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-6253126 ckap5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi21W → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-102; A-292; A-373; A-610; A-691; A-870; A-950; A-1250 and A-1335. Greatly impairs microtubule polymerase activity; when associated with A-102; A-292 and A-373. 1 Publication1
Mutagenesisi102K → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-292; A-373; A-610; A-691; A-870; A-950; A-1250 and A-1335. Greatly impairs microtubule polymerase activity; when associated with A-21; A-292 and A-373. 1 Publication1
Mutagenesisi292W → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-373; A-610; A-691; A-870; A-950; A-1250 and A-1335. Greatly impairs microtubule polymerase activity; when associated with A-21; A-102 and A-373. 1 Publication1
Mutagenesisi373K → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-610; A-691; A-870; A-950; A-1250 and A-1335. Greatly impairs microtubule polymerase activity; when associated with A-21; A-102 and A-292. 1 Publication1
Mutagenesisi610W → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-691; A-870; A-950; A-1250 and A-1335. Slightly impairs microtubule polymerase activity; when associated with A-691; A-870; A-950; A-1250 and A-1335. 1 Publication1
Mutagenesisi691K → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-610; A-870; A-950; A-1250 and A-1335. Slightly impairs microtubule polymerase activity; when associated with A-610; A-870; A-950; A-1250 and A-1335. 1 Publication1
Mutagenesisi870W → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-610; A-691; A-950; A-1250 and A-1335. Slightly impairs microtubule polymerase activity; when associated with A-610; A-691; A-950; A-1250 and A-1335. 1 Publication1
Mutagenesisi950K → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-610; A-691; A-870; A-1250 and A-1335. Slightly impairs microtubule polymerase activity; when associated with A-610; A-691; A-870; A-1250 and A-1335. 1 Publication1
Mutagenesisi1250F → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-610; A-691; A-870; A-950 and A-1335. Slightly impairs microtubule polymerase activity; when associated with A-1335. 1 Publication1
Mutagenesisi1335K → A: Abolishes binding to tubulin and microtubule polymerase activity; when associated with A-21; A-102; A-292; A-373; A-610; A-691; A-870; A-950 and A-1250. Slightly impairs microtubule polymerase activity; when associated with A-1250. 1 Publication1
Mutagenesisi2053L → S: Disrupts interaction with tacc3; when associated with S-2060. 1 Publication1
Mutagenesisi2054K → D: Disrupts interaction with tacc3; when associated with D-2061. 1 Publication1
Mutagenesisi2060I → S: Disrupts interaction with tacc3; when associated with S-2053. 1 Publication1
Mutagenesisi2061K → D: Disrupts interaction with tacc3; when associated with D-2054. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004375731 – 2065Cytoskeleton-associated protein 5-AAdd BLAST2065

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with tacc3; two molecules of ckap5 interact with 1 molecule of tacc3 probably mediated by coiled coil domains forming a four-helix bundle.

Interacts with tacc3 and clathrin forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges.

Interacts with ndc80; indicative for an association with the NDC80 comnplex (By similarity).

By similarity1 Publication

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9PT63, 4 interactors

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati120 – 157HEAT 1Sequence analysisAdd BLAST38
Repeati160 – 197HEAT 2Sequence analysisAdd BLAST38
Repeati270 – 311HEAT 3Sequence analysisAdd BLAST42
Repeati314 – 352HEAT 4Sequence analysisAdd BLAST39
Repeati356 – 393HEAT 5Sequence analysisAdd BLAST38
Repeati395 – 432HEAT 6Sequence analysisAdd BLAST38
Repeati436 – 477HEAT 7PROSITE-ProRule annotationAdd BLAST42
Repeati652 – 689HEAT 8Sequence analysisAdd BLAST38
Repeati748 – 785HEAT 9Sequence analysisAdd BLAST38
Repeati852 – 889HEAT 10Sequence analysisAdd BLAST38
Repeati892 – 929HEAT 11Sequence analysisAdd BLAST38
Repeati933 – 970HEAT 12Sequence analysisAdd BLAST38
Repeati1015 – 1052HEAT 13PROSITE-ProRule annotationAdd BLAST38
Repeati1251 – 1288HEAT 14Sequence analysisAdd BLAST38
Repeati1295 – 1318HEAT 15Sequence analysisAdd BLAST24
Repeati1319 – 1355HEAT 16Sequence analysisAdd BLAST37
Repeati1357 – 1390HEAT 17Sequence analysisAdd BLAST34
Repeati1395 – 1432HEAT 18Sequence analysisAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 240TOG 1CuratedAdd BLAST240
Regioni264 – 515TOG 2CuratedAdd BLAST252
Regioni644 – 808TOG 3CuratedAdd BLAST165
Regioni846 – 1090TOG 4CuratedAdd BLAST245
Regioni1150 – 1235Interaction with microtubule lattice1 PublicationAdd BLAST86
Regioni1191 – 1460TOG 5CuratedAdd BLAST270
Regioni2002 – 2065Interaction with tacc31 PublicationAdd BLAST64

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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. TOG 1 and TOG 2 are critical for microtubule polymerase activity.By similarity1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the TOG/XMAP215 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K16803

Database of Orthologous Groups

More...
OrthoDBi
33681at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.10.10, 5 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR024395 CLASP_N_dom
IPR021133 HEAT_type_2
IPR034085 TOG

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12348 CLASP_N, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01349 TOG, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48371 SSF48371, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50077 HEAT_REPEAT, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9PT63-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDDSEWMKL PIDQKCEHKV WKARLNGYEE AVKLFQKIVD EKSPEWSKYL
60 70 80 90 100
GLIKRFVTES NAVAQLKGLE AALVYVENAH VAGKTTGEVV NGVVNKVFNQ
110 120 130 140 150
PKARAKELGA DICLMYVEIE KAEVVQEELL KGLDNKNPKI VVACVETVRK
160 170 180 190 200
ALSEFGSKIM TLKPIIKVLP KLFESREKAI RDEAKLLAVE IYRWIRDALR
210 220 230 240 250
PPLQNINPVQ LKELEEEWVK LPQSAPKQTR FLRSQQDLKA KFEQQQAAGD
260 270 280 290 300
DGGDDGEEEI VPQVDAYELL EAVEILSKLP KDFYDKIEAK KWQERKEALE
310 320 330 340 350
AVEALVKNPK IEAGDFADLV KALKTVVGKD TNVMLVALAA KCIAGLAAGL
360 370 380 390 400
RKKFGSYAGH IVPTILEKFK EKKPQVVQAL QEAIDAVFLT TTLQNISEDV
410 420 430 440 450
LAVMDNKNPA IKQQTSLFLA RSFRHCTPST LPKSLLKPFC VALLKQINDS
460 470 480 490 500
APEVRDAAFE ALGTAQKVVG EKAVNPFLAE VDKLKLDRIK ECADKAELAN
510 520 530 540 550
GKKGGAAAGE KKETKAPAAA PGKPVPNQGA AAEKDAGKAA AAPKKAPAAK
560 570 580 590 600
PGGPVKKAKA PASSGATAKG KKAVENKEII EQELSPEACE ERAAAVLPAS
610 620 630 640 650
CMQQLDSSNW KERLASMEEF QKTVESMERN DIPCQALVKM LAKKPGFKET
660 670 680 690 700
NFQVMQMKLH IVALIAQKGN FSKTSACAVL DGLVDKVGDV KCGGNAKEAL
710 720 730 740 750
SGIAEACTLP WTAEQVVSLA FAQKNPKNQS ETLNWLSNAI KEFGFTGINV
760 770 780 790 800
KAFISNVKTA LAATNPAIRT SAITLLGVMY LYMGAPLRMF FEEEKPALLS
810 820 830 840 850
QIDAEFEKMK GQTPPVSIRG SKHGSGRDEG EEGEEQDEDA PADVTDLLPR
860 870 880 890 900
TDISDKISSD LVSKIEDKNW KIRKEGLDEV TAIINEAKFI QPSIGELPSA
910 920 930 940 950
LKGRLNDSNK ILVQQTLTIL QQLSTAMGHN IKQHVKNLGM PIITVLGDSK
960 970 980 990 1000
ANVRAAALGT LKSWVDQTGM KDWLEGEDLS EELKKENPFL RQELLGWLAE
1010 1020 1030 1040 1050
KLPSMRTVPS DLQLCVPYLY NCLEDRNGDV RKKAQEALPI FMMHIGFEKM
1060 1070 1080 1090 1100
SKATSKLKPA SKDQVVALLE KAKASMPAKP AGPPGKASSK QPPAVAQASA
1110 1120 1130 1140 1150
SPPPAASSDS GSSTSDYKPD PKKTKPGTQA SKAKTQSVSS EGNTSLNPSN
1160 1170 1180 1190 1200
TSLTPSKANT SLSKAKPAKQ TLPGKKAPSK PNAKDEEDKS GPIYIIVPNG
1210 1220 1230 1240 1250
KEQRVKDEKA LKVLKWNFTT PRDEYIEQLK TQMSPCIARW LQDELFHADF
1260 1270 1280 1290 1300
QRQIKGLAVM TEHLESEKEG VISCLDLVLK WFTLRFFDTN TSVLMKCLEY
1310 1320 1330 1340 1350
LKLLFIMLSQ EEYHLTEMEG TSFLPYLMLK VGEPKDIVRK DVRAILTKMC
1360 1370 1380 1390 1400
QVYPASKMFN FVMEGTKSKN SKQRAECLEE LGCLVESYGM NVCQPTPAKA
1410 1420 1430 1440 1450
LKEIAIHIGD RDTTVRNAAL NTIVTVYNVH GEQVFKLIGN LSEKDMSMLE
1460 1470 1480 1490 1500
ERIKRAGKKQ AAAAPAKQVE EKPQRVQSAN ASILRKAPPE DMSSKLNQAR
1510 1520 1530 1540 1550
NMGGHTEPSH SVPREFQLDL DEIENDNGTV RCEMPALVQH KLDEIFEPVL
1560 1570 1580 1590 1600
IPEPKIRAVS PHFDDMHSNT ASTINFVISQ VASVDINASI QALAQIDEVL
1610 1620 1630 1640 1650
RQEDKAEAMS GHIDQFLIAT FMQLRLAYNT HMADERLDKD DIVRLYSCII
1660 1670 1680 1690 1700
GNMISLFQME SLAREASTGV LKDLMHGLIS LMLDARIEDL EEGQQVVRSV
1710 1720 1730 1740 1750
NLLVVKVLEK SDQTNIISAL LMLLQDSLLA TASSPNFSEL VMKCLWRMIR
1760 1770 1780 1790 1800
LLPEAINNLN LDRILLDIHN FMRVLPKEKL KQHKSEMPMR TLKTLLHTLC
1810 1820 1830 1840 1850
KLKGPKIMDH LSMIENKHES ELEAHLLRVM KHSIDRTGSK GDKETEKGAS
1860 1870 1880 1890 1900
CIEDKVGKAN VSDFLAEMFK KIGSKENTKE GLAELYEYKK KYSDADIKPF
1910 1920 1930 1940 1950
LKNSSQFFQS YVERGLRLIE MEREGKARIA PNTGMSTHVT EMTPLPTVTN
1960 1970 1980 1990 2000
TAAPVSNTNG EEVGPSVYLE RLKILRQRCG LDNAKQDERP PLTSLLSKSS
2010 2020 2030 2040 2050
APAVVSSTDM LHSKLSQLRE SREQFQHVEL DSNQTYPSTT TSSSASSTNI
2060
DDLKKRLERI KSSRK
Length:2,065
Mass (Da):228,390
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C879F481E86D5CB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ251130 mRNA Translation: CAB61894.1

NCBI Reference Sequences

More...
RefSeqi
NP_001090169.1, NM_001096700.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
779014

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:779014

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ251130 mRNA Translation: CAB61894.1
RefSeqiNP_001090169.1, NM_001096700.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

IntActiQ9PT63, 4 interactors

Genome annotation databases

GeneIDi779014
KEGGixla:779014

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
779014
XenbaseiXB-GENE-6253126 ckap5

Phylogenomic databases

KOiK16803
OrthoDBi33681at2759

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, 2 hits
PROSITEiView protein in PROSITE
PS50077 HEAT_REPEAT, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCKAP5_XENLA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9PT63
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
Last sequence update: May 1, 2000
Last modified: September 18, 2019
This is version 75 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again