Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q13042 (CDC16_HUMAN)

Protein

Cell division cycle protein 16 homolog

Gene

CDC16

Organism
Homo sapiens (Human)
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

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

<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

View the complete GO annotation on QuickGO ...

<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, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-HSA-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-HSA-176412 Phosphorylation of the APC/C
R-HSA-179409 APC-Cdc20 mediated degradation of Nek2A
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q13042

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00143

<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:
Cell division cycle protein 16 homolog
Alternative name(s):
Anaphase-promoting complex subunit 6
Short name:
APC6
CDC16 homolog
Short name:
CDC16Hs
Cyclosome subunit 6
<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:CDC16
Synonyms:ANAPC6
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000130177.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:1720 CDC16

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603461 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q13042

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<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

Organism-specific databases

DisGeNET

More...DisGeNETi		8881

Open Targets

More...OpenTargetsi		ENSG00000130177

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26256

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CDC16

Domain mapping of disease mutations (DMDM)

More...DMDMi		37537763

<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_00001062671 – 620Cell division cycle protein 16 homologAdd BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei112Phosphoserine1 Publication1
Modified residuei490Phosphoserine1 Publication1
Modified residuei560PhosphoserineCombined sources1 Publication1
Modified residuei581PhosphothreonineCombined sources1 Publication1
Modified residuei595Phosphoserine1 Publication1
Modified residuei599Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation on Ser-560 occurs specifically during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q13042

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q13042

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q13042

PeptideAtlas

More...PeptideAtlasi		Q13042

PRoteomics IDEntifications database

More...PRIDEi		Q13042

ProteomicsDB human proteome resource

More...ProteomicsDBi		59116
59117 [Q13042-2]
59118 [Q13042-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q13042

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q13042

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000130177 Expressed in 230 organ(s), highest expression level in right uterine tube

CleanEx database of gene expression profiles

More...CleanExi		HS_CDC16

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q13042 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q13042 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA042826

<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

V-shaped homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (PubMed:26083744, PubMed:25043029). Interacts with PPP5C and CDC20 (PubMed:9628895, PubMed:9405394). Interacts with CDC26 (PubMed:19668213).5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
CDC26Q8NHZ811EBI-994830,EBI-2555941

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		114400, 183 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q13042

Database of interacting proteins

More...DIPi		DIP-36423N

Protein interaction database and analysis system

More...IntActi		Q13042, 60 interactors

Molecular INTeraction database

More...MINTi		Q13042

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000348554

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1620
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q13042

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q13042

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q13042

<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>Repeati4 – 33TPR 1Add BLAST30
Repeati37 – 62TPR 2Add BLAST26
Repeati70 – 93TPR 3Add BLAST24
Repeati128 – 159TPR 4Add BLAST32
Repeati164 – 187TPR 5Add BLAST24
Repeati198 – 222TPR 6Add BLAST25
Repeati232 – 260TPR 7Add BLAST29
Repeati267 – 294TPR 8Add BLAST28
Repeati299 – 329TPR 9Add BLAST31
Repeati334 – 362TPR 10Add BLAST29
Repeati369 – 397TPR 11Add BLAST29
Repeati402 – 434TPR 12Add BLAST33
Repeati442 – 474TPR 13Add BLAST33
Repeati479 – 508TPR 14Add BLAST30

<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

TPR repeats 1-7 mediate homodimerization, while the C-terminal TPR repeats bind to CDC26, burying its hydrophobic N-terminus.1 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 APC6/CDC16 family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1173 Eukaryota
ENOG410XNY1 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153625

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000230908

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG050857

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q13042

KEGG Orthology (KO)

More...KOi		K03353

Identification of Orthologs from Complete Genome Data

More...OMAi		YIDQQQY

Database of Orthologous Groups

More...OrthoDBi		EOG091G0HW1

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q13042

TreeFam database of animal gene trees

More...TreeFami		TF101054

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00028 TPR, 6 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48452 SSF48452, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 1 hit

<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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<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.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q13042-1) [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
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT 
        60         70         80         90        100
AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DVLDMEEPIN 
       110        120        130        140        150
KRLFEKYLKD ESGFKDPSSD WEMSQSSIKS SICLLRGKIY DALDNRTLAT 
       160        170        180        190        200
YSYKEALKLD VYCFEAFDLL TSHHMLTAQE EKELLESLPL SKLCNEEQEL 
       210        220        230        240        250
LRFLFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER HYYNCDFKMC 
       260        270        280        290        300
YKLTSVVMEK DPFHASCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV 
       310        320        330        340        350
SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH 
       360        370        380        390        400
DQAMAAYFTA AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FSQALSIAPE 
       410        420        430        440        450
DPFVMHEVGV VAFQNGEWKT AEKWFLDALE KIKAIGNEVT VDKWEPLLNN 
       460        470        480        490        500
LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS TYSAIGYIHS LMGNFENAVD 
       510        520        530        540        550
YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD KLKCYDFDVH 
       560        570        580        590        600
TMKTLKNIIS PPWDFREFEV EKQTAEETGL TPLETSRKTP DSRPSLEETF 
       610        620
EIEMNESDMM LETSMSDHST
Length:620
Mass (Da):71,656
Last modified:October 3, 2003 - v2
<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:iA9C4F24615DF17EB
GO
Isoform 2 (identifier: Q13042-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Missing.

Note: No experimental confirmation available.
Show »
Length:619
Mass (Da):71,527
Checksum:i87D5542D21C14CD6
GO
Isoform 3 (identifier: Q13042-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Missing.
     367-417: Missing.

Show »
Length:568
Mass (Da):65,860
Checksum:i0B5B3A3B468B3109
GO
Isoform 4 (identifier: Q13042-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.

Note: No experimental confirmation available.
Show »
Length:526
Mass (Da):60,371
Checksum:i0F077329FB0AA56B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T8C6Q5T8C6_HUMAN
Cell division cycle protein 16 homo...
CDC16
475Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti138K → Q in AAC50200 (PubMed:7736578).Curated1
Sequence conflicti299P → L in AAD45156 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0572701 – 94Missing in isoform 4. 1 PublicationAdd BLAST94
Alternative sequenceiVSP_00842736Missing in isoform 2 and isoform 3. 1 Publication1
Alternative sequenceiVSP_008428367 – 417Missing in isoform 3. CuratedAdd BLAST51

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
U18291 mRNA Translation: AAC50200.1
AF164598 mRNA Translation: AAD45156.1
AY599074 Genomic DNA Translation: AAS94323.1
AL160396 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09237.1
CH471085 Genomic DNA Translation: EAX09244.1
CH471085 Genomic DNA Translation: EAX09245.1
BC010875 mRNA Translation: AAH10875.1
BC017244 mRNA Translation: AAH17244.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS81786.1 [Q13042-2]
CCDS81787.1 [Q13042-4]
CCDS9542.2 [Q13042-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A56519

NCBI Reference Sequences

More...RefSeqi		NP_001072113.1, NM_001078645.2 [Q13042-1]
NP_001305446.1, NM_001318517.2 [Q13042-2]
NP_001305447.1, NM_001318518.2 [Q13042-3]
NP_001317030.1, NM_001330101.1 [Q13042-2]
NP_001317033.1, NM_001330104.1 [Q13042-4]
NP_001317034.1, NM_001330105.1 [Q13042-4]
NP_003894.3, NM_003903.4 [Q13042-1]
XP_016876322.1, XM_017020833.1 [Q13042-4]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.374127

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000252457; ENSP00000252457; ENSG00000130177 [Q13042-2]
ENST00000356221; ENSP00000348554; ENSG00000130177 [Q13042-1]
ENST00000360383; ENSP00000353549; ENSG00000130177 [Q13042-1]
ENST00000375308; ENSP00000364457; ENSG00000130177 [Q13042-4]
ENST00000375310; ENSP00000364459; ENSG00000130177 [Q13042-4]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8881

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8881

UCSC genome browser

More...UCSCi		uc001vuk.1 human [Q13042-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18291 mRNA Translation: AAC50200.1
AF164598 mRNA Translation: AAD45156.1
AY599074 Genomic DNA Translation: AAS94323.1
AL160396 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09237.1
CH471085 Genomic DNA Translation: EAX09244.1
CH471085 Genomic DNA Translation: EAX09245.1
BC010875 mRNA Translation: AAH10875.1
BC017244 mRNA Translation: AAH17244.1
CCDSiCCDS81786.1 [Q13042-2]
CCDS81787.1 [Q13042-4]
CCDS9542.2 [Q13042-1]
PIRiA56519
RefSeqiNP_001072113.1, NM_001078645.2 [Q13042-1]
NP_001305446.1, NM_001318517.2 [Q13042-2]
NP_001305447.1, NM_001318518.2 [Q13042-3]
NP_001317030.1, NM_001330101.1 [Q13042-2]
NP_001317033.1, NM_001330104.1 [Q13042-4]
NP_001317034.1, NM_001330105.1 [Q13042-4]
NP_003894.3, NM_003903.4 [Q13042-1]
XP_016876322.1, XM_017020833.1 [Q13042-4]
UniGeneiHs.374127

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HYMX-ray2.80B/D/F/H/J/L212-539[»]
4UI9electron microscopy3.60J/K1-620[»]
5A31electron microscopy4.30J/K1-620[»]
5G04electron microscopy4.00J/K1-620[»]
5G05electron microscopy3.40J/K1-620[»]
5KHRelectron microscopy6.10J/K1-620[»]
5KHUelectron microscopy4.80J/K1-620[»]
5L9Telectron microscopy6.40J/K1-620[»]
5L9Uelectron microscopy6.40J/K1-620[»]
5LCWelectron microscopy4.00J/K1-620[»]
ProteinModelPortaliQ13042
SMRiQ13042
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114400, 183 interactors
CORUMiQ13042
DIPiDIP-36423N
IntActiQ13042, 60 interactors
MINTiQ13042
STRINGi9606.ENSP00000348554

PTM databases

iPTMnetiQ13042
PhosphoSitePlusiQ13042

Polymorphism and mutation databases

BioMutaiCDC16
DMDMi37537763

Proteomic databases

EPDiQ13042
MaxQBiQ13042
PaxDbiQ13042
PeptideAtlasiQ13042
PRIDEiQ13042
ProteomicsDBi59116
59117 [Q13042-2]
59118 [Q13042-3]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		8881
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252457; ENSP00000252457; ENSG00000130177 [Q13042-2]
ENST00000356221; ENSP00000348554; ENSG00000130177 [Q13042-1]
ENST00000360383; ENSP00000353549; ENSG00000130177 [Q13042-1]
ENST00000375308; ENSP00000364457; ENSG00000130177 [Q13042-4]
ENST00000375310; ENSP00000364459; ENSG00000130177 [Q13042-4]
GeneIDi8881
KEGGihsa:8881
UCSCiuc001vuk.1 human [Q13042-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8881
DisGeNETi8881
EuPathDBiHostDB:ENSG00000130177.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		CDC16
HGNCiHGNC:1720 CDC16
HPAiHPA042826
MIMi603461 gene
neXtProtiNX_Q13042
OpenTargetsiENSG00000130177
PharmGKBiPA26256

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1173 Eukaryota
ENOG410XNY1 LUCA
GeneTreeiENSGT00940000153625
HOGENOMiHOG000230908
HOVERGENiHBG050857
InParanoidiQ13042
KOiK03353
OMAiYIDQQQY
OrthoDBiEOG091G0HW1
PhylomeDBiQ13042
TreeFamiTF101054

Enzyme and pathway databases

UniPathwayi
UPA00143

ReactomeiR-HSA-141430 Inactivation of APC/C via direct inhibition of the APC/C complex
R-HSA-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176407 Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase
R-HSA-176408 Regulation of APC/C activators between G1/S and early anaphase
R-HSA-176409 APC/C:Cdc20 mediated degradation of mitotic proteins
R-HSA-176412 Phosphorylation of the APC/C
R-HSA-179409 APC-Cdc20 mediated degradation of Nek2A
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiQ13042

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CDC16 human
EvolutionaryTraceiQ13042

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CDC16

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8881

Protein Ontology

More...PROi		PR:Q13042

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000130177 Expressed in 230 organ(s), highest expression level in right uterine tube
CleanExiHS_CDC16
ExpressionAtlasiQ13042 baseline and differential
GenevisibleiQ13042 HS

Family and domain databases

InterProiView protein in InterPro
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
SMARTiView protein in SMART
SM00028 TPR, 6 hits
SUPFAMiSSF48452 SSF48452, 2 hits
PROSITEiView protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiCDC16_HUMAN
<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: Q13042
Secondary accession number(s): A2A365
, Q5T8C8, Q7Z651, Q96AE6, Q9Y564
<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: October 3, 2003
Last sequence update: October 3, 2003
Last modified: December 5, 2018
This is version 178 of the entry and version 2 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
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.

<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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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