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Q5QJE6

- TDIF2_HUMAN

UniProt

Q5QJE6 - TDIF2_HUMAN

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Protein

Deoxynucleotidyltransferase terminal-interacting protein 2

Gene

DNTTIP2

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

Functioni

Regulates the transcriptional activity of DNTT and ESR1. May function as a chromatin remodeling protein.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxynucleotidyltransferase terminal-interacting protein 2
Alternative name(s):
Estrogen receptor-binding protein
LPTS-interacting protein 2
Short name:
LPTS-RP2
Terminal deoxynucleotidyltransferase-interacting factor 2
Short name:
TdIF2
Short name:
TdT-interacting factor 2
Gene namesi
Name:DNTTIP2
Synonyms:ERBP, TDIF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24013. DNTTIP2.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleolus Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671963.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756Deoxynucleotidyltransferase terminal-interacting protein 2PRO_0000318505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Phosphoserine2 Publications
Modified residuei117 – 1171Phosphoserine4 Publications
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei141 – 1411Phosphoserine5 Publications
Modified residuei145 – 1451Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei184 – 1841Phosphoserine2 Publications
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei232 – 2321Phosphothreonine4 Publications
Modified residuei251 – 2511Phosphoserine1 Publication
Modified residuei324 – 3241Phosphoserine1 Publication
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei381 – 3811Phosphoserine1 Publication
Modified residuei434 – 4341Phosphoserine2 Publications
Modified residuei512 – 5121Phosphoserine2 Publications
Modified residuei610 – 6101Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5QJE6.
PaxDbiQ5QJE6.
PRIDEiQ5QJE6.

PTM databases

PhosphoSiteiQ5QJE6.

Expressioni

Tissue specificityi

Widely expressed with higher levels in testis.2 Publications

Gene expression databases

BgeeiQ5QJE6.
CleanExiHS_DNTTIP2.
ExpressionAtlasiQ5QJE6. baseline and differential.
GenevestigatoriQ5QJE6.

Organism-specific databases

HPAiHPA044502.

Interactioni

Subunit structurei

Forms a ternary complex with DNTT and core histone; interaction with PCNA releases DNTT and H2A/H2B histones from this ternary complex. Interacts with ESR1, ESR2, PPARG and RXRA.2 Publications

Protein-protein interaction databases

BioGridi119052. 20 interactions.
IntActiQ5QJE6. 3 interactions.
MINTiMINT-3026940.
STRINGi9606.ENSP00000352137.

Structurei

3D structure databases

ProteinModelPortaliQ5QJE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni548 – 60558TdBR region; mediates interaction with DNTTAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili505 – 54238Sequence AnalysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG273245.
GeneTreeiENSGT00510000048142.
HOVERGENiHBG106308.
InParanoidiQ5QJE6.
OMAiEAESHVS.
OrthoDBiEOG76T9SJ.
PhylomeDBiQ5QJE6.
TreeFamiTF105964.

Family and domain databases

InterProiIPR014810. Fcf2.
[Graphical view]
PfamiPF08698. Fcf2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5QJE6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVVTRSARAK ASIQAASAES SGQKSFAANG IQAHPESSTG SDARTTAESQ
60 70 80 90 100
TTGKQSLIPR TPKARKRKSR TTGSLPKGTE PSTDGETSEA ESNYSVSEHH
110 120 130 140 150
DTILRVTRRR QILIACSPVS SVRKKPKVTP TKESYTEEIV SEAESHVSGI
160 170 180 190 200
SRIVLPTEKT TGARRSKAKS LTDPSQESHT EAISDAETSS SDISFSGIAT
210 220 230 240 250
RRTRSMQRKL KAQTEKKDSK IVPGNEKQIV GTPVNSEDSD TRQTSHLQAR
260 270 280 290 300
SLSEINKPNF YNNDFDDDFS HRSSENILTV HEQANVESLK ETKQNCKDLD
310 320 330 340 350
EDANGITDEG KEINEKSSQL KNLSELQDTS LQQLVSQRHS TPQNKNAVSV
360 370 380 390 400
HSNLNSEAVM KSLTQTFATV EVGRWNNNKK SPIKASDLTK FGDCGGSDDE
410 420 430 440 450
EESTVISVSE DMNSEGNVDF ECDTKLYTSA PNTSQGKDNS VLLVLSSDES
460 470 480 490 500
QQSENSENEE DTLCFVENSG QRESLSGDTG SLSCDNALFV IDTTPGMSAD
510 520 530 540 550
KNFYLEEEDK ASEVAIEEEK EEEEDEKSEE DSSDHDENED EFSDEEDFLN
560 570 580 590 600
STKAKLLKLT SSSIDPGLSI KQLGGLYINF NADKLQSNKR TLTQIKEKKK
610 620 630 640 650
NELLQKAVIT PDFEKNHCVP PYSESKYQLQ KKRRKERQKT AGDGWFGMKA
660 670 680 690 700
PEMTNELKND LKALKMRASM DPKRFYKKND RDGFPKYFQI GTIVDNPADF
710 720 730 740 750
YHSRIPKKQR KRTIVEELLA DSEFRRYNRR KYSEIMAEKA ANAAGKKFRK

KKKFRN
Length:756
Mass (Da):84,469
Last modified:February 5, 2008 - v2
Checksum:i5C58EFABA2B42E4B
GO

Sequence cautioni

The sequence AAH47688.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAA50601.1 differs from that shown. Reason: Frameshift at positions 717 and 726.
The sequence CAI21812.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471A → D in AAQ95169. (PubMed:15047147)Curated
Sequence conflicti47 – 471A → D in AAA50601. 1 PublicationCurated
Sequence conflicti67 – 671R → S in AAQ95169. (PubMed:15047147)Curated
Sequence conflicti67 – 671R → S in AAA50601. 1 PublicationCurated
Sequence conflicti648 – 6481M → I in BAD96442. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti309 – 3091E → D.4 Publications
Corresponds to variant rs3747965 [ dbSNP | Ensembl ].
VAR_038748
Natural varianti341 – 3411T → A.
Corresponds to variant rs3179879 [ dbSNP | Ensembl ].
VAR_038749
Natural varianti430 – 4301A → V.
Corresponds to variant rs35650636 [ dbSNP | Ensembl ].
VAR_038750
Natural varianti477 – 4771G → E.
Corresponds to variant rs41292661 [ dbSNP | Ensembl ].
VAR_061710
Natural varianti676 – 6761Y → F.
Corresponds to variant rs12748154 [ dbSNP | Ensembl ].
VAR_038751

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046574 mRNA. Translation: BAD08331.1.
AY394925 mRNA. Translation: AAQ95169.1.
U15552 mRNA. Translation: AAA50601.1. Frameshift.
AY336729 mRNA. Translation: AAR02407.1.
AK292379 mRNA. Translation: BAF85068.1.
AK222722 mRNA. Translation: BAD96442.1.
AL049796 Genomic DNA. Translation: CAI21812.1. Sequence problems.
CH471097 Genomic DNA. Translation: EAW73064.1.
BC047688 mRNA. Translation: AAH47688.1. Sequence problems.
BC130622 mRNA. Translation: AAI30623.1.
CCDSiCCDS44174.1.
PIRiG01522.
RefSeqiNP_055412.2. NM_014597.4.
UniGeneiHs.601998.
Hs.85769.

Genome annotation databases

EnsembliENST00000436063; ENSP00000411010; ENSG00000067334.
GeneIDi30836.
KEGGihsa:30836.
UCSCiuc001dqf.3. human.

Polymorphism databases

DMDMi166987398.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046574 mRNA. Translation: BAD08331.1 .
AY394925 mRNA. Translation: AAQ95169.1 .
U15552 mRNA. Translation: AAA50601.1 . Frameshift.
AY336729 mRNA. Translation: AAR02407.1 .
AK292379 mRNA. Translation: BAF85068.1 .
AK222722 mRNA. Translation: BAD96442.1 .
AL049796 Genomic DNA. Translation: CAI21812.1 . Sequence problems.
CH471097 Genomic DNA. Translation: EAW73064.1 .
BC047688 mRNA. Translation: AAH47688.1 . Sequence problems.
BC130622 mRNA. Translation: AAI30623.1 .
CCDSi CCDS44174.1.
PIRi G01522.
RefSeqi NP_055412.2. NM_014597.4.
UniGenei Hs.601998.
Hs.85769.

3D structure databases

ProteinModelPortali Q5QJE6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119052. 20 interactions.
IntActi Q5QJE6. 3 interactions.
MINTi MINT-3026940.
STRINGi 9606.ENSP00000352137.

PTM databases

PhosphoSitei Q5QJE6.

Polymorphism databases

DMDMi 166987398.

Proteomic databases

MaxQBi Q5QJE6.
PaxDbi Q5QJE6.
PRIDEi Q5QJE6.

Protocols and materials databases

DNASUi 30836.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000436063 ; ENSP00000411010 ; ENSG00000067334 .
GeneIDi 30836.
KEGGi hsa:30836.
UCSCi uc001dqf.3. human.

Organism-specific databases

CTDi 30836.
GeneCardsi GC01M094331.
H-InvDB HIX0023574.
HGNCi HGNC:24013. DNTTIP2.
HPAi HPA044502.
MIMi 611199. gene.
neXtProti NX_Q5QJE6.
PharmGKBi PA142671963.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG273245.
GeneTreei ENSGT00510000048142.
HOVERGENi HBG106308.
InParanoidi Q5QJE6.
OMAi EAESHVS.
OrthoDBi EOG76T9SJ.
PhylomeDBi Q5QJE6.
TreeFami TF105964.

Miscellaneous databases

ChiTaRSi DNTTIP2. human.
GeneWikii DNTTIP2.
GenomeRNAii 30836.
NextBioi 52954.
PROi Q5QJE6.
SOURCEi Search...

Gene expression databases

Bgeei Q5QJE6.
CleanExi HS_DNTTIP2.
ExpressionAtlasi Q5QJE6. baseline and differential.
Genevestigatori Q5QJE6.

Family and domain databases

InterProi IPR014810. Fcf2.
[Graphical view ]
Pfami PF08698. Fcf2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone."
    Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., Fujisaki S., Hayano T., Koiwai O.
    Genes Cells 8:559-571(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309, FUNCTION, IDENTIFICATION IN A COMPLEX WITH DNTT; PCNA AND CORE HISTONE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Thymus.
  2. "ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
    Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
    Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; ESR2; PPARG AND RXRA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "cDNA encoding an acidic 82 kDa protein."
    Carlsson P.
    Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "LPTS-RP2, one LPTS-interacting protein."
    Song H., Zhao M., Li T.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-309.
    Tissue: Liver.
  5. "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: Testis.
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-309.
  9. "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], VARIANT ASP-309.
    Tissue: Brain and Skin.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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 THR-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-117; THR-129; SER-141; SER-145; SER-148; SER-184; SER-194; THR-232; SER-324 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-141 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "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-21; SER-117; SER-141; THR-232; SER-251; SER-330; SER-434; SER-512 AND THR-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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-117; SER-141; THR-232; SER-434 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTDIF2_HUMAN
AccessioniPrimary (citable) accession number: Q5QJE6
Secondary accession number(s): Q12987
, Q53H59, Q5TFJ4, Q6TLI0, Q76MJ8, Q86WX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 80 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3