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Q9NYB0

- TE2IP_HUMAN

UniProt

Q9NYB0 - TE2IP_HUMAN

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Protein

Telomeric repeat-binding factor 2-interacting protein 1

Gene

TERF2IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Molecular functioni

  1. DNA binding Source: InterPro

GO - Biological processi

  1. negative regulation of DNA recombination at telomere Source: UniProtKB
  2. negative regulation of telomere maintenance Source: UniProtKB
  3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  4. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  5. protection from non-homologous end joining at telomere Source: BHF-UCL
  6. protein localization to chromosome, telomeric region Source: BHF-UCL
  7. regulation of double-strand break repair via homologous recombination Source: UniProtKB
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. telomere maintenance Source: BHF-UCL
  10. telomere maintenance via telomerase Source: ProtInc
  11. telomere maintenance via telomere lengthening Source: UniProtKB
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

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
Gene namesi
Name:TERF2IP
Synonyms:DRIP5, RAP1
ORF Names:PP8000
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:19246. TERF2IP.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nuclear chromosome Source: ProtInc
  4. nuclear chromosome, telomeric region Source: BHF-UCL
  5. nuclear telomere cap complex Source: BHF-UCL
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134976325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 399398Telomeric repeat-binding factor 2-interacting protein 1PRO_0000197126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei36 – 361Phosphoserine2 Publications
Modified residuei154 – 1541Phosphoserine3 Publications
Modified residuei156 – 1561Phosphoserine1 Publication
Modified residuei203 – 2031Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NYB0.
PaxDbiQ9NYB0.
PeptideAtlasiQ9NYB0.
PRIDEiQ9NYB0.

PTM databases

PhosphoSiteiQ9NYB0.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed.

Gene expression databases

BgeeiQ9NYB0.
CleanExiHS_TERF2IP.
ExpressionAtlasiQ9NYB0. baseline and differential.
GenevestigatoriQ9NYB0.

Organism-specific databases

HPAiCAB018660.
CAB018749.
HPA006719.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SLX4Q8IY924EBI-750109,EBI-2370740
TERF2Q155547EBI-750109,EBI-706637
TINF2Q9BSI4-33EBI-750109,EBI-717418

Protein-protein interaction databases

BioGridi119942. 147 interactions.
DIPiDIP-34868N.
IntActiQ9NYB0. 17 interactions.
MINTiMINT-1454139.
STRINGi9606.ENSP00000300086.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 15013
Turni155 – 1595
Helixi162 – 1698
Beta strandi172 – 1743
Helixi178 – 18710
Helixi308 – 32417
Helixi329 – 33810
Turni339 – 3413
Helixi343 – 35210
Helixi364 – 3707
Helixi375 – 38511
Helixi387 – 39711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FEXNMR-A132-190[»]
3K6GX-ray1.95A/B/C303-399[»]
ProteinModelPortaliQ9NYB0.
SMRiQ9NYB0. Positions 132-190, 306-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NYB0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 10124BRCTAdd
BLAST
Domaini128 – 18861Myb-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi383 – 39917Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi214 – 30491Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the RAP1 family.Curated
Contains 1 BRCT domain.Curated
Contains 1 Myb-like domain.Curated

Phylogenomic databases

eggNOGiNOG39788.
GeneTreeiENSGT00390000005351.
HOGENOMiHOG000120115.
HOVERGENiHBG054209.
InParanoidiQ9NYB0.
KOiK11113.
OMAiSISFYVR.
OrthoDBiEOG7KDFBG.
PhylomeDBiQ9NYB0.
TreeFamiTF332348.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view]
PfamiPF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:iEAA615777F9D3D3D
GO

Sequence cautioni

The sequence AAL55783.1 differs from that shown. Reason: Frameshift at position 151.
The sequence BAG60996.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA91317.1 differs from that shown. Reason: Erroneous termination at position 299. Translated as Glu.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831Y → H in BAA91317. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241K → E.
Corresponds to variant rs4888444 [ dbSNP | Ensembl ].
VAR_050195

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

EnsembliENST00000300086; ENSP00000300086; ENSG00000166848.
GeneIDi54386.
KEGGihsa:54386.
UCSCiuc002fet.2. human.

Polymorphism databases

DMDMi21542267.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS32491.1.
RefSeqi NP_061848.2. NM_018975.3.
UniGenei Hs.301419.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FEX NMR - A 132-190 [» ]
3K6G X-ray 1.95 A/B/C 303-399 [» ]
ProteinModelPortali Q9NYB0.
SMRi Q9NYB0. Positions 132-190, 306-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119942. 147 interactions.
DIPi DIP-34868N.
IntActi Q9NYB0. 17 interactions.
MINTi MINT-1454139.
STRINGi 9606.ENSP00000300086.

PTM databases

PhosphoSitei Q9NYB0.

Polymorphism databases

DMDMi 21542267.

Proteomic databases

MaxQBi Q9NYB0.
PaxDbi Q9NYB0.
PeptideAtlasi Q9NYB0.
PRIDEi Q9NYB0.

Protocols and materials databases

DNASUi 54386.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300086 ; ENSP00000300086 ; ENSG00000166848 .
GeneIDi 54386.
KEGGi hsa:54386.
UCSCi uc002fet.2. human.

Organism-specific databases

CTDi 54386.
GeneCardsi GC16P075681.
HGNCi HGNC:19246. TERF2IP.
HPAi CAB018660.
CAB018749.
HPA006719.
MIMi 605061. gene.
neXtProti NX_Q9NYB0.
PharmGKBi PA134976325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39788.
GeneTreei ENSGT00390000005351.
HOGENOMi HOG000120115.
HOVERGENi HBG054209.
InParanoidi Q9NYB0.
KOi K11113.
OMAi SISFYVR.
OrthoDBi EOG7KDFBG.
PhylomeDBi Q9NYB0.
TreeFami TF332348.

Enzyme and pathway databases

Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_75792. Meiotic synapsis.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

ChiTaRSi TERF2IP. human.
EvolutionaryTracei Q9NYB0.
GeneWikii TERF2IP.
GenomeRNAii 54386.
NextBioi 56609.
PROi Q9NYB0.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYB0.
CleanExi HS_TERF2IP.
ExpressionAtlasi Q9NYB0. baseline and differential.
Genevestigatori Q9NYB0.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR009057. Homeodomain-like.
IPR021661. Rap1_C.
IPR015010. Rap1_Myb_dom.
[Graphical view ]
Pfami PF08914. Myb_DNA-bind_2. 1 hit.
PF11626. Rap1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. 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. 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.

Entry informationi

Entry nameiTE2IP_HUMAN
AccessioniPrimary (citable) accession number: Q9NYB0
Secondary accession number(s): B4DQN4
, Q4W4Y2, Q8WYZ3, Q9NWR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3