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 - Q9NYB0 (TE2IP_HUMAN)

Protein

Telomeric repeat-binding factor 2-interacting protein 1

Gene

TERF2IP

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

Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.2 Publications

Miscellaneous

Shares a bidirectional promoter with KARS.1 Publication

Caution

Was reported to participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair in the absence of TERF2 (PubMed:19763083). However, this probably does not corresponds to its primary function and experiments in mouse showed that it is dispensible for such process and is required for repressiion of homology-directed repair (HDR).1 Publication

<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

  • G-rich strand telomeric DNA binding Source: BHF-UCL
  • phosphatase binding Source: CAFA
  • telomeric DNA binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

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

Molecular functionActivator
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence

<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:
Telomeric repeat-binding factor 2-interacting protein 1
Short name:
TERF2-interacting telomeric protein 1
Short name:
TRF2-interacting telomeric protein 1
Alternative name(s):
Dopamine receptor-interacting protein 5
Repressor/activator protein 1 homolog
Short name:
RAP1 homolog
Short name:
hRap1
<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:TERF2IP
Synonyms:DRIP5, RAP1
ORF Names:PP8000
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000166848.5

Human Gene Nomenclature Database

More...HGNCi		HGNC:19246 TERF2IP

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605061 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NYB0

<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

Chromosome, Cytoplasm, Nucleus, Telomere

<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		54386

MalaCards human disease database

More...MalaCardsi		TERF2IP

Open Targets

More...OpenTargetsi		ENSG00000166848

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

More...Orphaneti		618 Familial melanoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134976325

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3751647

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TERF2IP

Domain mapping of disease mutations (DMDM)

More...DMDMi		21542267

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001971262 – 399Telomeric repeat-binding factor 2-interacting protein 1Add BLAST398

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 residuei2N-acetylalanineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Modified residuei43PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei154PhosphoserineCombined sources1
Modified residuei156PhosphoserineCombined sources1
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei203PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NYB0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9NYB0

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9NYB0

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

More...PaxDbi		Q9NYB0

PeptideAtlas

More...PeptideAtlasi		Q9NYB0

PRoteomics IDEntifications database

More...PRIDEi		Q9NYB0

ProteomicsDB human proteome resource

More...ProteomicsDBi		83206

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NYB0

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

More...PhosphoSitePlusi		Q9NYB0

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous. Highly expressed.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000166848 Expressed in 238 organ(s), highest expression level in pituitary gland

CleanEx database of gene expression profiles

More...CleanExi		HS_TERF2IP

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9NYB0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NYB0 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB018660
CAB018749
HPA006719

<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

Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG (By similarity). Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Interacts with SLX4/BTBD12.By similarity3 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
AIMP2Q131552EBI-750109,EBI-745226
AKR1A1P145502EBI-750109,EBI-372388
AKR1B10O602182EBI-750109,EBI-1572139
AKR7A3O951542EBI-750109,EBI-748869
AKT1P317492EBI-750109,EBI-296087
BABAM1Q9NWV82EBI-750109,EBI-745725
BCL7BQ9BQE92EBI-750109,EBI-2560588
C1orf174Q8IYL32EBI-750109,EBI-715898
C9orf78Q9NZ632EBI-750109,EBI-2557577
CALML3P274822EBI-750109,EBI-747537
CHMP2BQ9UQN32EBI-750109,EBI-718324
COTL1Q140192EBI-750109,EBI-79926
CPNE2Q96FN42EBI-750109,EBI-7097057
CRKP461082EBI-750109,EBI-886
CTBP1Q133632EBI-750109,EBI-908846
DHX38Q926202EBI-750109,EBI-1043041
ENAHQ8N8S72EBI-750109,EBI-2834410
EPS8L1Q8TE682EBI-750109,EBI-7487998
FABP2P121042EBI-750109,EBI-3905109
FAM122AQ96E092EBI-750109,EBI-9355758
GAGE5Q130692EBI-750109,EBI-745702
GPKOWQ929172EBI-750109,EBI-746309
HAGHQ167752EBI-750109,EBI-3905342
HMGB3O153472EBI-750109,EBI-2214136
HMGN4O004792EBI-750109,EBI-2867693
HNRNPKP619782EBI-750109,EBI-304185
IL1RNP185102EBI-750109,EBI-1026330
LANCL2Q9NS862EBI-750109,EBI-2510837
MAGOHBQ96A722EBI-750109,EBI-746778
MCM2P497362EBI-750109,EBI-374819
MRTO4Q9UKD22EBI-750109,EBI-1046493
MT1XP802972EBI-750109,EBI-11308402
MT3P257132EBI-750109,EBI-8084264
NASPP493212EBI-750109,EBI-716205
NUDT14O958482EBI-750109,EBI-536866
NUDT18Q6ZVK82EBI-750109,EBI-740486
NUMA1Q149802EBI-750109,EBI-521611
OGFRQ9NZT22EBI-750109,EBI-1044212
PCNPQ8WW122EBI-750109,EBI-10972020
PCP4P485392EBI-750109,EBI-4287270
PEA15Q151212EBI-750109,EBI-714410
PGLSO953362EBI-750109,EBI-11307753
POLD1P283402EBI-750109,EBI-716569
PPP6R3Q5H9R72EBI-750109,EBI-355498
PRXQ9BXM02EBI-750109,EBI-1753064
PTMAP064542EBI-750109,EBI-2682091
RABIFP472242EBI-750109,EBI-713992
RBBP9O758842EBI-750109,EBI-11310604
RGMAQ96B862EBI-750109,EBI-722102
RPP25Q9BUL92EBI-750109,EBI-366570
S100PP258152EBI-750109,EBI-743700
SCLYQ96I152EBI-750109,EBI-2823066
SLX4Q8IY924EBI-750109,EBI-2370740
SMARCC2Q8TAQ22EBI-750109,EBI-357418
TALDO1P378372EBI-750109,EBI-1056712
TBCAO753472EBI-750109,EBI-2686341
TERF2Q1555436EBI-750109,EBI-706637
TINF2Q9BSI4-33EBI-750109,EBI-717418
TMSB4YO146042EBI-750109,EBI-751196
TOR1AIP1Q5JTV82EBI-750109,EBI-2559665
TSSC4Q9Y5U22EBI-750109,EBI-717229
TWF2Q6IBS02EBI-750109,EBI-722204
UCHL1P099362EBI-750109,EBI-714860
VGLL4Q141352EBI-750109,EBI-5278589
WDR5P619642EBI-750109,EBI-540834
XAGE2Q96GT92EBI-750109,EBI-750167
XRCC6P129563EBI-750109,EBI-353208
ZNF414Q96IQ92EBI-750109,EBI-744257

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		119942, 160 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-152 Shelterin complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9NYB0

Database of interacting proteins

More...DIPi		DIP-34868N

Protein interaction database and analysis system

More...IntActi		Q9NYB0, 150 interactors

Molecular INTeraction database

More...MINTi		Q9NYB0

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000300086

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9NYB0

<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

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
4RQIX-ray2.44E/F/G/H89-106[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		Q9NYB0

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

More...SMRi		Q9NYB0

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		Q9NYB0

<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_and_domains_section">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>Domaini78 – 101BRCTAdd BLAST24
Domaini128 – 188Myb-likeAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi383 – 399Nuclear localization signalSequence analysisAdd BLAST17

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 biasi214 – 304Asp/Glu-rich (acidic)Add BLAST91

<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 RAP1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IJNC Eukaryota
ENOG4111QPC LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005351

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000120115

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG054209

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NYB0

KEGG Orthology (KO)

More...KOi		K11113

Identification of Orthologs from Complete Genome Data

More...OMAi		TQHSWQA

Database of Orthologous Groups

More...OrthoDBi		602157at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NYB0

TreeFam database of animal gene trees

More...TreeFami		TF332348

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.2170, 1 hit
3.40.50.10190, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR009057 Homeobox-like_sf
IPR021661 Rap1_C
IPR038104 Rap1_C_sf
IPR015010 Rap1_Myb_dom
IPR039595 TE2IP/Rap1

The PANTHER Classification System

More...PANTHERi		PTHR16466 PTHR16466, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16589 BRCT_2, 1 hit
PF08914 Myb_DNA-bind_2, 1 hit
PF11626 Rap1_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF46689 SSF46689, 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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9NYB0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG 
        60         70         80         90        100
GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR 
       110        120        130        140        150
LGPASAADTG SEAKPGALAE GAAEPEPQRH AGRIAFTDAD DVAILTYVKE 
       160        170        180        190        200
NARSPSSVTG NALWKAMEKS SLTQHSWQSL KDRYLKHLRG QEHKYLLGDA 
       210        220        230        240        250
PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK EEIQENEEAV 
       260        270        280        290        300
KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE 
       310        320        330        340        350
EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL 
       360        370        380        390 
ASGQRADGYP IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK
Length:399
Mass (Da):44,260
Last modified:October 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:iEAA615777F9D3D3D
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BMI8H3BMI8_HUMAN
Telomeric repeat-binding factor 2-i...
TERF2IP
99Annotation 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>
H3BR63H3BR63_HUMAN
Telomeric repeat-binding factor 2-i...
TERF2IP
122Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL55783 differs from that shown. Reason: Frameshift at position 151.Curated
The sequence BAA91317 differs from that shown. Reason: Erroneous termination at position 299. Translated as Glu.Curated
The sequence BAG60996 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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 conflicti83Y → H in BAA91317 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_050195324K → E. Corresponds to variant dbSNP:rs4888444Ensembl.1

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
AF262988 mRNA Translation: AAF72711.1
AF250393 mRNA Translation: AAQ14259.1
AF289599 mRNA Translation: AAL55783.1 Frameshift.
AK000669 mRNA Translation: BAA91317.1 Sequence problems.
AK298880 mRNA Translation: BAG60996.1 Different initiation.
AC025287 Genomic DNA No translation available.
CH471114 Genomic DNA Translation: EAW95616.1
CH471114 Genomic DNA Translation: EAW95618.1
BC004465 mRNA Translation: AAH04465.1
BC005841 mRNA Translation: AAH05841.1
BC022428 mRNA Translation: AAH22428.1
BC078171 mRNA Translation: AAH78171.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS32491.1

NCBI Reference Sequences

More...RefSeqi		NP_061848.2, NM_018975.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.301419

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000300086; ENSP00000300086; ENSG00000166848

Database of genes from NCBI RefSeq genomes

More...GeneIDi		54386

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:54386

UCSC genome browser

More...UCSCi		uc002fet.3 human

Keywords - Coding sequence diversityi

Polymorphism

<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
AF262988 mRNA Translation: AAF72711.1
AF250393 mRNA Translation: AAQ14259.1
AF289599 mRNA Translation: AAL55783.1 Frameshift.
AK000669 mRNA Translation: BAA91317.1 Sequence problems.
AK298880 mRNA Translation: BAG60996.1 Different initiation.
AC025287 Genomic DNA No translation available.
CH471114 Genomic DNA Translation: EAW95616.1
CH471114 Genomic DNA Translation: EAW95618.1
BC004465 mRNA Translation: AAH04465.1
BC005841 mRNA Translation: AAH05841.1
BC022428 mRNA Translation: AAH22428.1
BC078171 mRNA Translation: AAH78171.1
CCDSiCCDS32491.1
RefSeqiNP_061848.2, NM_018975.3
UniGeneiHs.301419

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
4RQIX-ray2.44E/F/G/H89-106[»]
ProteinModelPortaliQ9NYB0
SMRiQ9NYB0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119942, 160 interactors
ComplexPortaliCPX-152 Shelterin complex
CORUMiQ9NYB0
DIPiDIP-34868N
IntActiQ9NYB0, 150 interactors
MINTiQ9NYB0
STRINGi9606.ENSP00000300086

Chemistry databases

BindingDBiQ9NYB0
ChEMBLiCHEMBL3751647

PTM databases

iPTMnetiQ9NYB0
PhosphoSitePlusiQ9NYB0

Polymorphism and mutation databases

BioMutaiTERF2IP
DMDMi21542267

Proteomic databases

EPDiQ9NYB0
jPOSTiQ9NYB0
MaxQBiQ9NYB0
PaxDbiQ9NYB0
PeptideAtlasiQ9NYB0
PRIDEiQ9NYB0
ProteomicsDBi83206

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		54386
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300086; ENSP00000300086; ENSG00000166848
GeneIDi54386
KEGGihsa:54386
UCSCiuc002fet.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		54386
DisGeNETi54386
EuPathDBiHostDB:ENSG00000166848.5

GeneCards: human genes, protein and diseases

More...GeneCardsi		TERF2IP
HGNCiHGNC:19246 TERF2IP
HPAiCAB018660
CAB018749
HPA006719
MalaCardsiTERF2IP
MIMi605061 gene
neXtProtiNX_Q9NYB0
OpenTargetsiENSG00000166848
Orphaneti618 Familial melanoma
PharmGKBiPA134976325

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IJNC Eukaryota
ENOG4111QPC LUCA
GeneTreeiENSGT00390000005351
HOGENOMiHOG000120115
HOVERGENiHBG054209
InParanoidiQ9NYB0
KOiK11113
OMAiTQHSWQA
OrthoDBi602157at2759
PhylomeDBiQ9NYB0
TreeFamiTF332348

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence

Miscellaneous databases

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

More...ChiTaRSi		TERF2IP human
EvolutionaryTraceiQ9NYB0

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TERF2IP

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

More...GenomeRNAii		54386

Protein Ontology

More...PROi		PR:Q9NYB0

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000166848 Expressed in 238 organ(s), highest expression level in pituitary gland
CleanExiHS_TERF2IP
ExpressionAtlasiQ9NYB0 baseline and differential
GenevisibleiQ9NYB0 HS

Family and domain databases

Gene3Di1.10.10.2170, 1 hit
3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR009057 Homeobox-like_sf
IPR021661 Rap1_C
IPR038104 Rap1_C_sf
IPR015010 Rap1_Myb_dom
IPR039595 TE2IP/Rap1
PANTHERiPTHR16466 PTHR16466, 2 hits
PfamiView protein in Pfam
PF16589 BRCT_2, 1 hit
PF08914 Myb_DNA-bind_2, 1 hit
PF11626 Rap1_C, 1 hit
SUPFAMiSSF46689 SSF46689, 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 nameiTE2IP_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: Q9NYB0
Secondary accession number(s): B4DQN4
, Q4W4Y2, Q8WYZ3, Q9NWR2
<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: June 20, 2002
Last sequence update: October 1, 2000
Last modified: January 16, 2019
This is version 182 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
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