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Q9NYB0 (TE2IP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:TERF2IP
Synonyms:DRIP5, RAP1
ORF Names:PP8000
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.17

Subunit structure

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. Ref.9 Ref.10 Ref.16

Subcellular location

Nucleus. Cytoplasm By similarity. Chromosome. Chromosometelomere. Note: Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex By similarity.

Tissue specificity

Ubiquitous. Highly expressed.

Miscellaneous

Shares a bidirectional promoter with KARS (Ref.8).

Sequence similarities

Belongs to the RAP1 family.

Contains 1 BRCT domain.

Contains 1 Myb-like domain.

Caution

Was reported to participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair in the absence of TERF2 (Ref.17). 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).

Sequence caution

The sequence AAL55783.1 differs from that shown. Reason: Frameshift at position 151.

The sequence BAA91317.1 differs from that shown. Reason: Erroneous termination at position 299. Translated as Glu.

The sequence BAG60996.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Cytoplasm
Nucleus
Telomere
   Coding sequence diversityPolymorphism
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of DNA recombination at telomere

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of telomere maintenance

Inferred from direct assay PubMed 17055345. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protection from non-homologous end joining at telomere

Inferred from mutant phenotype PubMed 17499040. Source: BHF-UCL

protein localization to chromosome, telomeric region

Inferred from mutant phenotype PubMed 17499040. Source: BHF-UCL

regulation of double-strand break repair via homologous recombination

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

telomere maintenance

Inferred from direct assay PubMed 14565979. Source: BHF-UCL

telomere maintenance via telomerase

Traceable author statement Ref.1. Source: ProtInc

telomere maintenance via telomere lengthening

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome, telomeric region

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromosome

Traceable author statement Ref.1. Source: ProtInc

nuclear chromosome, telomeric region

Inferred from direct assay PubMed 14565979. Source: BHF-UCL

nuclear telomere cap complex

Inferred from direct assay PubMed 15181449PubMed 16880378. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17055345. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 14690602Ref.16. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 399398Telomeric repeat-binding factor 2-interacting protein 1
PRO_0000197126

Regions

Domain78 – 10124BRCT
Domain128 – 18861Myb-like
Motif383 – 39917Nuclear localization signal Potential
Compositional bias214 – 30491Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine Ref.15
Modified residue361Phosphoserine Ref.14 Ref.19
Modified residue1541Phosphoserine Ref.14 Ref.18 Ref.19
Modified residue1561Phosphoserine Ref.12
Modified residue2031Phosphoserine Ref.12 Ref.14 Ref.18 Ref.19 Ref.21

Natural variations

Natural variant3241K → E.
Corresponds to variant rs4888444 [ dbSNP | Ensembl ].
VAR_050195

Experimental info

Sequence conflict831Y → H in BAA91317. Ref.4

Secondary structure

........................ 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NYB0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EAA615777F9D3D3D

FASTA39944,260
        10         20         30         40         50         60 
MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG GTVCRVQEPG 

        70         80         90        100        110        120 
AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR LGPASAADTG SEAKPGALAE 

       130        140        150        160        170        180 
GAAEPEPQRH AGRIAFTDAD DVAILTYVKE NARSPSSVTG NALWKAMEKS SLTQHSWQSL 

       190        200        210        220        230        240 
KDRYLKHLRG QEHKYLLGDA PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK 

       250        260        270        280        290        300 
EEIQENEEAV KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE 

       310        320        330        340        350        360 
EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL ASGQRADGYP 

       370        380        390 
IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of human RAP1: implications for telomere evolution."
Li B., Oestreich S., de Lange T.
Cell 101:471-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[2]"Cloning and characterization of DRIP5, a new protein that specifically interacts with the D1 dopamine receptor."
Lafuente M.J., Nasir J.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ileal mucosa and Teratocarcinoma.
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon, Lung and Skin.
[8]"The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes."
Tan M., Wei C., Price C.M.
Gene 323:1-10(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIDIRECTIONAL PROMOTER WITH KARS.
[9]"TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres."
Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., Krutchinsky A.N., Chait B.T., de Lange T.
J. Biol. Chem. 279:47264-47271(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[10]"Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins."
Liu D., O'Connor M.S., Qin J., Songyang Z.
J. Biol. Chem. 279:51338-51342(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[11]"Shelterin: the protein complex that shapes and safeguards human telomeres."
de Lange T.
Genes Dev. 19:2100-2110(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[16]"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLX4.
[17]"Human RAP1 inhibits non-homologous end joining at telomeres."
Sarthy J., Bae N.S., Scrafford J., Baumann P.
EMBO J. 28:3390-3399(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains."
Hanaoka S., Nagadoi A., Yoshimura S., Aimoto S., Li B., de Lange T., Nishimura Y.
J. Mol. Biol. 312:167-175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 132-190.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32491.1.
RefSeqNP_061848.2. NM_018975.3.
UniGeneHs.301419.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
ProteinModelPortalQ9NYB0.
SMRQ9NYB0. Positions 132-190, 306-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119942. 143 interactions.
DIPDIP-34868N.
IntActQ9NYB0. 17 interactions.
MINTMINT-1454139.
STRING9606.ENSP00000300086.

PTM databases

PhosphoSiteQ9NYB0.

Polymorphism databases

DMDM21542267.

Proteomic databases

MaxQBQ9NYB0.
PaxDbQ9NYB0.
PeptideAtlasQ9NYB0.
PRIDEQ9NYB0.

Protocols and materials databases

DNASU54386.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300086; ENSP00000300086; ENSG00000166848.
GeneID54386.
KEGGhsa:54386.
UCSCuc002fet.2. human.

Organism-specific databases

CTD54386.
GeneCardsGC16P075681.
HGNCHGNC:19246. TERF2IP.
HPACAB018660.
CAB018749.
HPA006719.
MIM605061. gene.
neXtProtNX_Q9NYB0.
PharmGKBPA134976325.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39788.
HOGENOMHOG000120115.
HOVERGENHBG054209.
InParanoidQ9NYB0.
KOK11113.
OMASISFYVR.
OrthoDBEOG7KDFBG.
PhylomeDBQ9NYB0.
TreeFamTF332348.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9NYB0.
BgeeQ9NYB0.
CleanExHS_TERF2IP.
GenevestigatorQ9NYB0.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view]
PfamPF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTERF2IP. human.
EvolutionaryTraceQ9NYB0.
GeneWikiTERF2IP.
GenomeRNAi54386.
NextBio56609.
PROQ9NYB0.
SOURCESearch...

Entry information

Entry nameTE2IP_HUMAN
AccessionPrimary (citable) accession number: Q9NYB0
Secondary accession number(s): B4DQN4 expand/collapse secondary AC list , Q4W4Y2, Q8WYZ3, Q9NWR2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM