Q9NYB0 (TE2IP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TERF2IP
Synonyms:	DRIP5, RAP1
ORF Names:	PP8000

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.12 Ref.20
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.19
Subcellular location	Nucleus. Cytoplasm By similarity. Chromosome. Chromosome › telomere. 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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21
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.20). 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 process	Transcription Transcription regulation
Cellular component	Chromosome Cytoplasm Nucleus Telomere
Coding sequence diversity	Polymorphism
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of DNA recombination at telomere Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of telomere maintenance Inferred from direct assay. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade 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. Source: BHF-UCL protein localization to chromosome, telomeric region Inferred from mutant phenotype. Source: BHF-UCL regulation of double-strand break repair via homologous recombination Inferred from sequence or structural similarity. Source: UniProtKB telomere maintenance via telomerase Traceable author statement. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nuclear telomere cap complex Inferred from direct assay. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.19. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SLX4	Q8IY92	4	EBI-750109,EBI-2370740
TERF2	Q15554	5	EBI-750109,EBI-706637
TINF2	Q9BSI4-3	3	EBI-750109,EBI-717418

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 399

398

Telomeric repeat-binding factor 2-interacting protein 1

PRO_0000197126

Regions

Domain

78 – 101

24

BRCT

Domain

128 – 188

61

Myb-like

Motif

383 – 399

17

Nuclear localization signal Potential

Compositional bias

214 – 304

91

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.18

Modified residue

36

1

Phosphoserine Ref.17

Modified residue

154

1

Phosphoserine Ref.11 Ref.13 Ref.17 Ref.21

Modified residue

156

1

Phosphoserine Ref.13

Modified residue

203

1

Phosphoserine Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21

Modified residue

205

1

Phosphoserine Ref.18

Modified residue

206

1

Phosphoserine Ref.15

Natural variations

Natural variant

324

1

K → E.
Corresponds to variant rs4888444 [ dbSNP | Ensembl ].

VAR_050195

Experimental info

Sequence conflict

83

1

Y → H in BAA91317. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

399

Helix Strand Turn

Details...

Helix

138 – 150

13

Turn

155 – 159

5

Helix

162 – 169

8

Beta strand

172 – 174

3

Helix

178 – 187

10

Sequences

	Sequence		Length	Mass (Da)
	Q9NYB0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EAA615777F9D3D3D	FASTA	399	44,260
	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

References

	« Hide 'large scale' referencesShow '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: 10850490] [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: 15498874] [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: 14702039] [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: 15616553] [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. , 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: 15489334] [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: 14659874] [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: 15316005] [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: 15383534] [Abstract] Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Shelterin: the protein complex that shapes and safeguards human telomeres." de Lange T. Genes Dev. 19:2100-2110(2005) [PubMed: 16166375] [Abstract] Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
[13]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-156 AND SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-206, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-205, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"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: 19596235] [Abstract] Cited for: INTERACTION WITH SLX4.
[20]	"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: 19763083] [Abstract] Cited for: FUNCTION.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-203, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"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: 11545594] [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.

IPI

IPI00008961.

RefSeq

NP_061848.2. NM_018975.3.

UniGene

Hs.301419.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FEX	NMR	-	A	132-190	[»]
3K6G	X-ray	1.95	A/B/C	303-399	[»]

ProteinModelPortal

Q9NYB0.

SMR

Q9NYB0. Positions 17-101, 132-190, 306-398.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34868N.

IntAct

Q9NYB0. 14 interactions.

MINT

MINT-1454139.

STRING

Q9NYB0.

PTM databases

PhosphoSite

Q9NYB0.

Polymorphism databases

DMDM

21542267.

Proteomic databases

PeptideAtlas

Q9NYB0.

PRIDE

Q9NYB0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300086; ENSP00000300086; ENSG00000166848.

GeneID

54386.

KEGG

hsa:54386.

UCSC

uc002fet.1. human.

Organism-specific databases

CTD

54386.

GeneCards

GC16P075681.

H-InvDB

HIX0013251.

HGNC

HGNC:19246. TERF2IP.

HPA

CAB018660.
CAB018749.
HPA006719.

MIM

605061. gene.

neXtProt

NX_Q9NYB0.

PharmGKB

PA134976325.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000005351.

HOGENOM

HBG713232.

HOVERGEN

HBG054209.

InParanoid

Q9NYB0.

OMA

HGGGTVC.

OrthoDB

EOG4K6G59.

PhylomeDB

Q9NYB0.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111183. Meiosis.
REACT_22172. Chromosome Maintenance.

Gene expression databases

ArrayExpress

Q9NYB0.

Bgee

Q9NYB0.

CleanEx

HS_TERF2IP.

Genevestigator

Q9NYB0.

GermOnline

ENSG00000166848. Homo sapiens.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR015010. Myb_DNA-bd_2.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

KO

K11113.

Pfam

PF08914. Myb_DNA-bind_2. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.

PROSITE

PS50172. BRCT. False negative.
PS50090. MYB_LIKE. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

56609.

SOURCE

Search...

Entry information

Entry name

TE2IP_HUMAN

Accession

Primary (citable) accession number: Q9NYB0
Secondary accession number(s): B4DQN4 , Q4W4Y2, Q8WYZ3, Q9NWR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.