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Protein

TERF1-interacting nuclear factor 2

Gene

TINF2

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

Functioni

Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix.2 Publications

GO - Molecular functioni

  1. telomeric DNA binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of epithelial cell proliferation Source: BHF-UCL
  2. negative regulation of protein ADP-ribosylation Source: BHF-UCL
  3. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
  4. positive regulation of telomere maintenance Source: BHF-UCL
  5. protein localization to chromosome Source: BHF-UCL
  6. protein localization to chromosome, telomeric region Source: BHF-UCL
  7. telomere assembly Source: BHF-UCL
  8. telomere maintenance Source: Reactome
  9. telomere maintenance via telomere lengthening Source: BHF-UCL
Complete GO annotation...

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:
TERF1-interacting nuclear factor 2
Alternative name(s):
TRF1-interacting nuclear protein 2
Gene namesi
Name:TINF2
Synonyms:TIN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:11824. TINF2.

Subcellular locationi

Nucleus 1 Publication. Chromosometelomere 1 Publication
Note: Associated with telomeres.
Isoform 1 : Nucleus matrix 1 Publication

GO - Cellular componenti

  1. chromosome, telomeric region Source: BHF-UCL
  2. nuclear matrix Source: UniProtKB-SubCell
  3. nuclear telomere cap complex Source: BHF-UCL
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. perinucleolar chromocenter Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Dyskeratosis congenita, autosomal dominant, 3 (DKCA3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.

See also OMIM:613990
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801K → E in DKCA3. 1 Publication
VAR_043914
Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
VAR_043915
Natural varianti282 – 2821R → S in DKCA3. 1 Publication
VAR_043916
Dyskeratosis congenita, autosomal dominant, 5 (DKCA5)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by bone marrow hypoplasia, nail dystrophy, fine sparse hair, fine reticulate skin pigmentation, oral leukoplakia, bilateral exudative retinopathy, cerebellar hypoplasia, and growth retardation.

See also OMIM:268130
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
VAR_043915

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi258 – 2581F → A: Abolishes interaction with TERF1. 1 Publication
Mutagenesisi262 – 2621P → A: Does not effect interaction with TERF1. 1 Publication

Keywords - Diseasei

Disease mutation, Dyskeratosis congenita

Organism-specific databases

MIMi268130. phenotype.
613990. phenotype.
Orphaneti1775. Dyskeratosis congenita.
3322. Hoyeraal-Hreidarsson syndrome.
3088. Revesz syndrome.
PharmGKBiPA36530.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 451450TERF1-interacting nuclear factor 2PRO_0000072541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei295 – 2951Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BSI4.
PaxDbiQ9BSI4.
PRIDEiQ9BSI4.

PTM databases

PhosphoSiteiQ9BSI4.

Expressioni

Tissue specificityi

Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiQ9BSI4.
CleanExiHS_TINF2.
ExpressionAtlasiQ9BSI4. baseline and differential.
GenevestigatoriQ9BSI4.

Interactioni

Subunit structurei

Monomer. Found in a complex with POT1; TERF1 and TNKS1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF1, TERF2 and ACD.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACDQ96AP05EBI-717418,EBI-717666
TERF2Q155544EBI-717418,EBI-706637
TERF2IPQ9NYB03EBI-717418,EBI-750109

Protein-protein interaction databases

BioGridi117660. 94 interactions.
DIPiDIP-29413N.
IntActiQ9BSI4. 10 interactions.
MINTiMINT-221357.
STRINGi9606.ENSP00000267415.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi263 – 2653Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BQOX-ray2.00B257-276[»]
3BU8X-ray2.15C/D258-275[»]
ProteinModelPortaliQ9BSI4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BSI4.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi256 – 27823TBMAdd
BLAST
Motifi262 – 2687Nuclear localization signalSequence Analysis

Domaini

The TBM domain mediates interaction with TERF1.1 Publication

Phylogenomic databases

eggNOGiNOG43106.
GeneTreeiENSGT00400000022326.
HOGENOMiHOG000247003.
HOVERGENiHBG057120.
InParanoidiQ9BSI4.
KOiK11112.
OMAiYGVDMGW.
PhylomeDBiQ9BSI4.
TreeFamiTF334731.

Family and domain databases

InterProiIPR029400. TINF2_N.
[Graphical view]
PfamiPF14973. TINF2_N. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9BSI4-1) [UniParc]FASTAAdd to basket

Also known as: TIN2L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATPLVAGPA ALRFAAAASW QVVRGRCVEH FPRVLEFLRS LRAVAPGLVR
60 70 80 90 100
YRHHERLCMG LKAKVVVELI LQGRPWAQVL KALNHHFPES GPIVRDPKAT
110 120 130 140 150
KQDLRKILEA QETFYQQVKQ LSEAPVDLAS KLQELEQEYG EPFLAAMEKL
160 170 180 190 200
LFEYLCQLEK ALPTPQAQQL QDVLSWMQPG VSITSSLAWR QYGVDMGWLL
210 220 230 240 250
PECSVTDSVN LAEPMEQNPP QQQRLALHNP LPKAKPGTHL PQGPSSRTHP
260 270 280 290 300
EPLAGRHFNL APLGRRRVQS QWASTRGGHK ERPTVMLFPF RNLGSPTQVI
310 320 330 340 350
SKPESKEEHA IYTADLAMGT RAASTGKSKS PCQTLGGRAL KENPVDLPAT
360 370 380 390 400
EQKENCLDCY MDPLRLSLLP PRARKPVCPP SLCSSVITIG DLVLDSDEEE
410 420 430 440 450
NGQGEGKESL ENYQKTKFDT LIPTLCEYLP PSGHGAIPVS SCDCRDSSRP

L
Length:451
Mass (Da):50,023
Last modified:May 31, 2001 - v1
Checksum:iE5A7FD11CE523979
GO
Isoform 2 (identifier: Q9BSI4-2) [UniParc]FASTAAdd to basket

Also known as: TIN2S

The sequence of this isoform differs from the canonical sequence as follows:
     355-451: Missing.

Show »
Length:354
Mass (Da):39,444
Checksum:i903B69D7B6A15C01
GO
Isoform 3 (identifier: Q9BSI4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-137: ELEQ → VRLV
     138-451: Missing.

Show »
Length:137
Mass (Da):15,434
Checksum:i3BA7286B15EAC870
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441V → I in BAB14440 (PubMed:14702039).Curated
Sequence conflicti67 – 671Missing in BAB14440 (PubMed:14702039).Curated
Sequence conflicti302 – 3021K → N in AAF18439 (PubMed:10581025).Curated
Sequence conflicti323 – 33210ASTGKSKSPC → PSNGKYKGPY in AAF18439 (PubMed:10581025).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431A → T.
Corresponds to variant rs35653076 [ dbSNP | Ensembl ].
VAR_051423
Natural varianti237 – 2371G → D.
Corresponds to variant rs17102313 [ dbSNP | Ensembl ].
VAR_051424
Natural varianti241 – 2411P → S.
Corresponds to variant rs17102311 [ dbSNP | Ensembl ].
VAR_051425
Natural varianti280 – 2801K → E in DKCA3. 1 Publication
VAR_043914
Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
VAR_043915
Natural varianti282 – 2821R → S in DKCA3. 1 Publication
VAR_043916

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 1374ELEQ → VRLV in isoform 3. 1 PublicationVSP_003987
Alternative sequencei138 – 451314Missing in isoform 3. 1 PublicationVSP_003988Add
BLAST
Alternative sequencei355 – 45197Missing in isoform 2. 1 PublicationVSP_003989Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195512 mRNA. Translation: AAF18439.1.
AK023166 mRNA. Translation: BAB14440.1.
BC005030 mRNA. Translation: AAH05030.1.
BC019343 mRNA. Translation: AAH19343.1.
EU851975 mRNA. Translation: ACF17559.1.
CCDSiCCDS41936.1. [Q9BSI4-1]
CCDS41937.1. [Q9BSI4-2]
RefSeqiNP_001092744.1. NM_001099274.1. [Q9BSI4-1]
NP_036593.2. NM_012461.2. [Q9BSI4-2]
UniGeneiHs.496191.

Genome annotation databases

EnsembliENST00000267415; ENSP00000267415; ENSG00000092330. [Q9BSI4-1]
ENST00000399423; ENSP00000382350; ENSG00000092330. [Q9BSI4-2]
GeneIDi26277.
KEGGihsa:26277.
UCSCiuc001woa.4. human. [Q9BSI4-1]

Polymorphism databases

DMDMi21542262.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195512 mRNA. Translation: AAF18439.1.
AK023166 mRNA. Translation: BAB14440.1.
BC005030 mRNA. Translation: AAH05030.1.
BC019343 mRNA. Translation: AAH19343.1.
EU851975 mRNA. Translation: ACF17559.1.
CCDSiCCDS41936.1. [Q9BSI4-1]
CCDS41937.1. [Q9BSI4-2]
RefSeqiNP_001092744.1. NM_001099274.1. [Q9BSI4-1]
NP_036593.2. NM_012461.2. [Q9BSI4-2]
UniGeneiHs.496191.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BQOX-ray2.00B257-276[»]
3BU8X-ray2.15C/D258-275[»]
ProteinModelPortaliQ9BSI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117660. 94 interactions.
DIPiDIP-29413N.
IntActiQ9BSI4. 10 interactions.
MINTiMINT-221357.
STRINGi9606.ENSP00000267415.

PTM databases

PhosphoSiteiQ9BSI4.

Polymorphism databases

DMDMi21542262.

Proteomic databases

MaxQBiQ9BSI4.
PaxDbiQ9BSI4.
PRIDEiQ9BSI4.

Protocols and materials databases

DNASUi26277.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267415; ENSP00000267415; ENSG00000092330. [Q9BSI4-1]
ENST00000399423; ENSP00000382350; ENSG00000092330. [Q9BSI4-2]
GeneIDi26277.
KEGGihsa:26277.
UCSCiuc001woa.4. human. [Q9BSI4-1]

Organism-specific databases

CTDi26277.
GeneCardsiGC14M024708.
GeneReviewsiTINF2.
HGNCiHGNC:11824. TINF2.
MIMi268130. phenotype.
604319. gene.
613990. phenotype.
neXtProtiNX_Q9BSI4.
Orphaneti1775. Dyskeratosis congenita.
3322. Hoyeraal-Hreidarsson syndrome.
3088. Revesz syndrome.
PharmGKBiPA36530.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG43106.
GeneTreeiENSGT00400000022326.
HOGENOMiHOG000247003.
HOVERGENiHBG057120.
InParanoidiQ9BSI4.
KOiK11112.
OMAiYGVDMGW.
PhylomeDBiQ9BSI4.
TreeFamiTF334731.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9BSI4.
GeneWikiiTINF2.
GenomeRNAii26277.
NextBioi35470863.
PROiQ9BSI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BSI4.
CleanExiHS_TINF2.
ExpressionAtlasiQ9BSI4. baseline and differential.
GenevestigatoriQ9BSI4.

Family and domain databases

InterProiIPR029400. TINF2_N.
[Graphical view]
PfamiPF14973. TINF2_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TIN2, a new regulator of telomere length in human cells."
    Kim S.-H., Kaminker P., Campisi J.
    Nat. Genet. 23:405-412(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fibroblast.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Teratocarcinoma.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta and Uterus.
  4. "A novel form of telomere-associated TIN2 localizes to the nuclear matrix."
    Kaminker P.G., Kim S.-H., Desprez P.Y., Campisi J.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-451 (ISOFORM 1).
  5. "POT1 as a terminal transducer of TRF1 telomere length control."
    Loayza D., De Lange T.
    Nature 423:1013-1018(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH POT1; TERF1 AND TNKS1.
  6. "POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex."
    Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M., Chait B.T., de Lange T.
    Genes Dev. 18:1649-1654(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACD.
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
  9. "Shelterin: the protein complex that shapes and safeguards human telomeres."
    de Lange T.
    Genes Dev. 19:2100-2110(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
  10. "A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly."
    O'Connor M.S., Safari A., Xin H., Liu D., Songyang Z.
    Proc. Natl. Acad. Sci. U.S.A. 103:11874-11879(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SHELTERIN COMPLEX ASSEMBLY.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "The long and short of it: a new isoform of TIN2 in the nuclear matrix."
    Smith S.
    Cell Cycle 8:797-798(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION.
  13. "A novel form of the telomere-associated protein TIN2 localizes to the nuclear matrix."
    Kaminker P.G., Kim S.H., Desprez P.Y., Campisi J.
    Cell Cycle 8:931-939(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1).
  14. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins."
    Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M.
    Science 319:1092-1096(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 258-275 IN COMPLEX WITH TERF1 OR TERF2, DOMAIN TBM, MUTAGENESIS OF PHE-258 AND PRO-262.
  18. "TINF2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita."
    Savage S.A., Giri N., Baerlocher G.M., Orr N., Lansdorp P.M., Alter B.P.
    Am. J. Hum. Genet. 82:501-509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DKCA3 GLU-280; HIS-282 AND SER-282, VARIANT DKCA5 HIS-282.

Entry informationi

Entry nameiTINF2_HUMAN
AccessioniPrimary (citable) accession number: Q9BSI4
Secondary accession number(s): B3W5Q7, Q9H904, Q9UHC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2002
Last sequence update: May 31, 2001
Last modified: March 3, 2015
This is version 128 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.