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UniProtKB - P24385 (CCND1_HUMAN)

Entry version 224 (07 Apr 2021)
Sequence version 1 (01 Mar 1992)
Previous versions | rss
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Protein

G1/S-specific cyclin-D1

Gene

CCND1

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

Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G1/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G1 phase. Hypophosphorylates RB1 in early G1 phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner.4 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 - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Molecular functionCyclin, Repressor
Biological processCell cycle, Cell division, DNA damage, Transcription, Transcription regulation

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P24385

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-1912408, Pre-NOTCH Transcription and Translation
R-HSA-3214858, RMTs methylate histone arginines
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-69231, Cyclin D associated events in G1
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8849470, PTK6 Regulates Cell Cycle
R-HSA-8853884, Transcriptional Regulation by VENTX
R-HSA-8878166, Transcriptional regulation by RUNX2
R-HSA-8934593, Regulation of RUNX1 Expression and Activity
R-HSA-8951430, RUNX3 regulates WNT signaling
R-HSA-8951936, RUNX3 regulates p14-ARF
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling
R-HSA-9661069, Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P24385

SIGNOR Signaling Network Open Resource

More...SIGNORi		P24385

<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%5Fand%5Ftaxonomy%5Fsection">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:
G1/S-specific cyclin-D1
Alternative name(s):
B-cell lymphoma 1 protein
Short name:
BCL-1
BCL-1 oncogene
PRAD1 oncogene
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:CCND1
Synonyms:BCL1, PRAD1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1582, CCND1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		168461, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P24385

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000110092.3

<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

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

A chromosomal aberration involving CCND1 may be a cause of B-lymphocytic malignancy, particularly mantle-cell lymphoma (MCL). Translocation t(11;14)(q13;q32) with immunoglobulin gene regions. Activation of CCND1 may be oncogenic by directly altering progression through the cell cycle.
A chromosomal aberration involving CCND1 may be a cause of parathyroid adenomas. Translocation t(11;11)(q13;p15) with the parathyroid hormone (PTH) enhancer.
Multiple myeloma (MM)1 Publication
The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration involving CCND1 is found in multiple myeloma. Translocation t(11;14)(q13;q32) with the IgH locus.
Disease descriptionA malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi286T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-288. Abolishes ubiquitination and subsequent degradation following DNA damage. 2 Publications1
Mutagenesisi288T → A: Reduces ubiquitination and subsequent degradation by the proteasome; when associated with A-286. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		595

MalaCards human disease database

More...MalaCardsi		CCND1
MIMi254500, phenotype

Open Targets

More...OpenTargetsi		ENSG00000110092

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		67038, B-cell chronic lymphocytic leukemia
52416, Mantle cell lymphoma
29073, Multiple myeloma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA75

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P24385, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3610

Drug and drug target database

More...DrugBanki		DB00945, Acetylsalicylic acid
DB01169, Arsenic trioxide
DB11752, Bryostatin 1
DB11718, Encorafenib

DrugCentral

More...DrugCentrali		P24385

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CCND1

Domain mapping of disease mutations (DMDM)

More...DMDMi		116152

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000804301 – 295G1/S-specific cyclin-D1Add BLAST295

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki269Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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 residuei286PhosphothreonineCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylation at Thr-286 by MAP kinases is required for ubiquitination and degradation following DNA damage. It probably plays an essential role for recognition by the FBXO31 component of SCF (SKP1-cullin-F-box) protein ligase complex.2 Publications
Ubiquitinated, primarily as 'Lys-48'-linked polyubiquitination. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex containing FBXO4 and CRYAB. Following DNA damage it is ubiquitinated by some SCF (SKP1-cullin-F-box) protein ligase complex containing FBXO31. SCF-type ubiquitination is dependent on Thr-286 phosphorylation (By similarity). Ubiquitinated also by UHRF2 apparently in a phosphorylation-independent manner. Ubiquitination leads to its degradation and G1 arrest. Deubiquitinated by USP2; leading to its stabilization.By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P24385

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P24385

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P24385

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

More...PaxDbi		P24385

PeptideAtlas

More...PeptideAtlasi		P24385

PRoteomics IDEntifications database

More...PRIDEi		P24385

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54198

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P24385

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

More...PhosphoSitePlusi		P24385

<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		ENSG00000110092, Expressed in endometrium epithelium and 229 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P24385, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P24385, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000110092, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with FBXO4 (By similarity).

Interacts with either CDK4 or CDK6 protein kinase to form a serine/threonine kinase holoenzyme complex. The cyclin subunit imparts substrate specificity to the complex.

Component of the ternary complex CCND1/CDK4/CDKN1B required for nuclear translocation and modulation of CDK4-mediated kinase activity.

Interacts directly with CDKN1B.

Interacts with UHRF2; the interaction ubiquitinates CCND1 and appears to occur independently of phosphorylation. Can form similar complexes with either CDKN1A or CDKN2A.

Interacts with USP2.

Interacts (via cyclin N-terminal domain) with INSM1 (via N-terminal region); the interaction competes with the binding of CCND1 to CDK4 during cell cycle progression and inhibits CDK4 activity.

Interacts with CDK4; the interaction is prevented with the binding of CCND1 to INSM1 during cell cycle progression.

By similarity9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107067, 227 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2010, Cyclin D1-CDK4 complex
CPX-2014, Cyclin D1-CDK6 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P24385

Database of interacting proteins

More...DIPi		DIP-123N

Protein interaction database and analysis system

More...IntActi		P24385, 69 interactors

Molecular INTeraction database

More...MINTi		P24385

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000227507

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P24385

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P24385, protein

<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

1295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P24385

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P24385

<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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini28 – 152Cyclin N-terminalAdd BLAST125

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi272 – 280Poly-Glu9

<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 cyclin family. Cyclin D subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0656, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157816

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_052190_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P24385

Identification of Orthologs from Complete Genome Data

More...OMAi		SCYRTTH

Database of Orthologous Groups

More...OrthoDBi		1234739at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P24385

TreeFam database of animal gene trees

More...TreeFami		TF101004

Family and domain databases

Conserved Domains Database

More...CDDi		cd00043, CYCLIN, 1 hit

Database of protein disorder

More...DisProti		DP02226

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR039361, Cyclin
IPR013763, Cyclin-like
IPR036915, Cyclin-like_sf
IPR004367, Cyclin_C-dom
IPR015451, Cyclin_D
IPR006671, Cyclin_N

The PANTHER Classification System

More...PANTHERi		PTHR10177, PTHR10177, 1 hit
PTHR10177:SF67, PTHR10177:SF67, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02984, Cyclin_C, 1 hit
PF00134, Cyclin_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00385, CYCLIN, 1 hit
SM01332, Cyclin_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47954, SSF47954, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00292, CYCLINS, 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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P24385-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEHQLLCCEV ETIRRAYPDA NLLNDRVLRA MLKAEETCAP SVSYFKCVQK 
        60         70         80         90        100
EVLPSMRKIV ATWMLEVCEE QKCEEEVFPL AMNYLDRFLS LEPVKKSRLQ 
       110        120        130        140        150
LLGATCMFVA SKMKETIPLT AEKLCIYTDN SIRPEELLQM ELLLVNKLKW 
       160        170        180        190        200
NLAAMTPHDF IEHFLSKMPE AEENKQIIRK HAQTFVALCA TDVKFISNPP 
       210        220        230        240        250
SMVAAGSVVA AVQGLNLRSP NNFLSYYRLT RFLSRVIKCD PDCLRACQEQ 
       260        270        280        290 
IEALLESSLR QAQQNMDPKA AEEEEEEEEE VDLACTPTDV RDVDI
Length:295
Mass (Da):33,729
Last modified:March 1, 1992 - 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:i3CC00C9905F58D3A
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
F5H437F5H437_HUMAN
G1/S-specific cyclin-D1
CCND1
67Annotation 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 conflicti130N → G in AAA52136 (PubMed:1827756).Curated1
Sequence conflicti168 – 169MP → IA in M74092 (PubMed:1833066).Curated2
Sequence conflicti188L → S in AAA52136 (PubMed:1827756).Curated1

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
X59798 mRNA Translation: CAA42470.1
M74092 mRNA No translation available.
M64349 mRNA Translation: AAA52136.1
M73554 mRNA Translation: AAA58392.1
Z23022 mRNA Translation: CAA80558.1
BT019845 mRNA Translation: AAV38648.1
AF511593 Genomic DNA Translation: AAM34300.2
BC000076 mRNA Translation: AAH00076.1
BC001501 mRNA Translation: AAH01501.1
BC014078 mRNA Translation: AAH14078.1
BC023620 mRNA Translation: AAH23620.1
BC025302 mRNA Translation: AAH25302.1
L09054 Genomic DNA Translation: AAA36481.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS8191.1

Protein sequence database of the Protein Information Resource

More...PIRi		A38977

NCBI Reference Sequences

More...RefSeqi		NP_444284.1, NM_053056.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000227507; ENSP00000227507; ENSG00000110092

Database of genes from NCBI RefSeq genomes

More...GeneIDi		595

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:595

Keywords - Coding sequence diversityi

Chromosomal rearrangement

<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%5Freferences%5Fsection">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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59798 mRNA Translation: CAA42470.1
M74092 mRNA No translation available.
M64349 mRNA Translation: AAA52136.1
M73554 mRNA Translation: AAA58392.1
Z23022 mRNA Translation: CAA80558.1
BT019845 mRNA Translation: AAV38648.1
AF511593 Genomic DNA Translation: AAM34300.2
BC000076 mRNA Translation: AAH00076.1
BC001501 mRNA Translation: AAH01501.1
BC014078 mRNA Translation: AAH14078.1
BC023620 mRNA Translation: AAH23620.1
BC025302 mRNA Translation: AAH25302.1
L09054 Genomic DNA Translation: AAA36481.1
CCDSiCCDS8191.1
PIRiA38977
RefSeqiNP_444284.1, NM_053056.2

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
2W96X-ray2.30A1-271[»]
2W99X-ray2.80A1-271[»]
2W9FX-ray2.85A1-271[»]
2W9ZX-ray2.45A16-271[»]
5VZUX-ray2.70E/F279-295[»]
6P8EX-ray2.30A19-267[»]
6P8FX-ray2.89A19-267[»]
6P8GX-ray2.80A19-267[»]
6P8HX-ray3.19A19-267[»]
SMRiP24385
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107067, 227 interactors
ComplexPortaliCPX-2010, Cyclin D1-CDK4 complex
CPX-2014, Cyclin D1-CDK6 complex
CORUMiP24385
DIPiDIP-123N
IntActiP24385, 69 interactors
MINTiP24385
STRINGi9606.ENSP00000227507

Chemistry databases

BindingDBiP24385
ChEMBLiCHEMBL3610
DrugBankiDB00945, Acetylsalicylic acid
DB01169, Arsenic trioxide
DB11752, Bryostatin 1
DB11718, Encorafenib
DrugCentraliP24385

PTM databases

iPTMnetiP24385
PhosphoSitePlusiP24385

Genetic variation databases

BioMutaiCCND1
DMDMi116152

Proteomic databases

EPDiP24385
jPOSTiP24385
MassIVEiP24385
PaxDbiP24385
PeptideAtlasiP24385
PRIDEiP24385
ProteomicsDBi54198

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3660, 2016 antibodies

The CPTC Antibody Portal

More...CPTCi		P24385, 7 antibodies

The DNASU plasmid repository

More...DNASUi		595

Genome annotation databases

EnsembliENST00000227507; ENSP00000227507; ENSG00000110092
GeneIDi595
KEGGihsa:595

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		595
DisGeNETi595

GeneCards: human genes, protein and diseases

More...GeneCardsi		CCND1
HGNCiHGNC:1582, CCND1
HPAiENSG00000110092, Low tissue specificity
MalaCardsiCCND1
MIMi168461, gene
254500, phenotype
neXtProtiNX_P24385
OpenTargetsiENSG00000110092
Orphaneti67038, B-cell chronic lymphocytic leukemia
52416, Mantle cell lymphoma
29073, Multiple myeloma
PharmGKBiPA75
VEuPathDBiHostDB:ENSG00000110092.3

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0656, Eukaryota
GeneTreeiENSGT00940000157816
HOGENOMiCLU_052190_0_0_1
InParanoidiP24385
OMAiSCYRTTH
OrthoDBi1234739at2759
PhylomeDBiP24385
TreeFamiTF101004

Enzyme and pathway databases

PathwayCommonsiP24385
ReactomeiR-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-1912408, Pre-NOTCH Transcription and Translation
R-HSA-3214858, RMTs methylate histone arginines
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-69231, Cyclin D associated events in G1
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8849470, PTK6 Regulates Cell Cycle
R-HSA-8853884, Transcriptional Regulation by VENTX
R-HSA-8878166, Transcriptional regulation by RUNX2
R-HSA-8934593, Regulation of RUNX1 Expression and Activity
R-HSA-8951430, RUNX3 regulates WNT signaling
R-HSA-8951936, RUNX3 regulates p14-ARF
R-HSA-9018519, Estrogen-dependent gene expression
R-HSA-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling
R-HSA-9661069, Defective binding of RB1 mutants to E2F1,(E2F2, E2F3)
SignaLinkiP24385
SIGNORiP24385

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		595, 524 hits in 998 CRISPR screens

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

More...ChiTaRSi		CCND1, human
EvolutionaryTraceiP24385

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Cyclin_D1

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

More...GenomeRNAii		595
PharosiP24385, Tchem

Protein Ontology

More...PROi		PR:P24385
RNActiP24385, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000110092, Expressed in endometrium epithelium and 229 other tissues
ExpressionAtlasiP24385, baseline and differential
GenevisibleiP24385, HS

Family and domain databases

CDDicd00043, CYCLIN, 1 hit
DisProtiDP02226
InterProiView protein in InterPro
IPR039361, Cyclin
IPR013763, Cyclin-like
IPR036915, Cyclin-like_sf
IPR004367, Cyclin_C-dom
IPR015451, Cyclin_D
IPR006671, Cyclin_N
PANTHERiPTHR10177, PTHR10177, 1 hit
PTHR10177:SF67, PTHR10177:SF67, 1 hit
PfamiView protein in Pfam
PF02984, Cyclin_C, 1 hit
PF00134, Cyclin_N, 1 hit
SMARTiView protein in SMART
SM00385, CYCLIN, 1 hit
SM01332, Cyclin_C, 1 hit
SUPFAMiSSF47954, SSF47954, 2 hits
PROSITEiView protein in PROSITE
PS00292, CYCLINS, 1 hit

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 nameiCCND1_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: P24385
Secondary accession number(s): Q6LEF0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 7, 2021
This is version 224 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
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, Reference proteome

Documents

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