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Q8NHU6

- TDRD7_HUMAN

UniProt

Q8NHU6 - TDRD7_HUMAN

Protein

Tudor domain-containing protein 7

Gene

TDRD7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Component of specific cytoplasmic RNA granules involved in post-transcriptional regulation of specific genes: probably acts by binding to specific mRNAs and regulating their translation. Required for lens transparency during lens development, by regulating translation of genes such as CRYBB3 and HSPB1 in the developing lens. Also required during spermatogenesis.1 Publication

    GO - Molecular functioni

    1. mRNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. germ cell development Source: Ensembl
    2. lens fiber cell differentiation Source: UniProtKB
    3. lens morphogenesis in camera-type eye Source: UniProtKB
    4. posttranscriptional regulation of gene expression Source: UniProtKB
    5. spermatogenesis Source: UniProtKB

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tudor domain-containing protein 7
    Alternative name(s):
    PCTAIRE2-binding protein
    Tudor repeat associator with PCTAIRE-2
    Short name:
    Trap
    Gene namesi
    Name:TDRD7
    Synonyms:PCTAIRE2BP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:30831. TDRD7.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Localizes to cytoplasmic RNA granules. Present in chromatoid body (CB) of spermatids (mammalian counterpart of germplasm, pole plasm or polar granules in Drosophila germ cells), also named processing bodies (P-bodies) in somatic cells. Detected in the multilobular cytoplasmic CBs (also called intermitochondrial cementin) in pachytene spermatocytes and as a single perinuclear CB in haploid round spermatids By similarity.By similarity

    GO - Cellular componenti

    1. chromatoid body Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. mitochondrial matrix Source: Ensembl
    4. P granule Source: Ensembl
    5. ribonucleoprotein granule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 36 (CTRCT36) [MIM:613887]: An opacification of the crystalline lens of the eye becoming evident at birth. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti618 – 6181Missing in CTRCT36. 1 Publication
    VAR_065247

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi613887. phenotype.
    PharmGKBiPA134937960.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10981098Tudor domain-containing protein 7PRO_0000183169Add
    BLAST

    Proteomic databases

    MaxQBiQ8NHU6.
    PaxDbiQ8NHU6.
    PRIDEiQ8NHU6.

    PTM databases

    PhosphoSiteiQ8NHU6.

    Expressioni

    Gene expression databases

    BgeeiQ8NHU6.
    CleanExiHS_TDRD7.
    GenevestigatoriQ8NHU6.

    Organism-specific databases

    HPAiCAB020800.
    HPA024529.

    Interactioni

    Subunit structurei

    Found in a mRNP complex, at least composed of TDRD1, TDRD6, TDRD7 and DDX4. Found in a complex containing CABLES1, CDK16 and CDK17. Interacts with CABLES1, CDK17 and PIWIL1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDKN2AP427712EBI-624505,EBI-375053
    TACC1O754104EBI-624505,EBI-624237
    TACC1O75410-13EBI-624505,EBI-624252

    Protein-protein interaction databases

    BioGridi116994. 8 interactions.
    IntActiQ8NHU6. 6 interactions.
    MINTiMINT-2871006.
    STRINGi9606.ENSP00000347444.

    Structurei

    Secondary structure

    1
    1098
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi24 – 3512
    Turni41 – 455
    Helixi49 – 546
    Turni57 – 593
    Beta strandi60 – 645
    Beta strandi70 – 745

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RCOX-ray1.80A/B1-82[»]
    ProteinModelPortaliQ8NHU6.
    SMRiQ8NHU6. Positions 1-77, 234-412, 663-787, 970-1077.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7674HTH OST-type 1PROSITE-ProRule annotationsAdd
    BLAST
    Domaini233 – 30270HTH OST-type 2PROSITE-ProRule annotationsAdd
    BLAST
    Domaini337 – 40670HTH OST-type 3PROSITE-ProRule annotationsAdd
    BLAST
    Domaini513 – 57058Tudor 1PROSITE-ProRule annotationsAdd
    BLAST
    Domaini703 – 76058Tudor 2PROSITE-ProRule annotationsAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni861 – 1098238Interacts with CDK17By similarityAdd
    BLAST
    Regioni893 – 1098206Interacts with CABLES1By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TDRD7 family.Curated
    Contains 3 HTH OST-type domains.PROSITE-ProRule annotations
    Contains 2 Tudor domains.PROSITE-ProRule annotations

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG256635.
    HOVERGENiHBG103662.
    InParanoidiQ8NHU6.
    OMAiYDTSGED.
    OrthoDBiEOG7BW0HQ.
    PhylomeDBiQ8NHU6.

    Family and domain databases

    InterProiIPR025605. OST-HTH/LOTUS_dom.
    IPR002999. Tudor.
    [Graphical view]
    PfamiPF12872. OST-HTH. 1 hit.
    PF00567. TUDOR. 3 hits.
    [Graphical view]
    SMARTiSM00333. TUDOR. 2 hits.
    [Graphical view]
    PROSITEiPS51644. HTH_OST. 3 hits.
    PS50304. TUDOR. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NHU6-1) [UniParc]FASTAAdd to Basket

    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

    MLEGDLVSKM LRAVLQSHKN GVALPRLQGE YRSLTGDWIP FKQLGFPTLE     50
    AYLRSVPAVV RIETSRSGEI TCYAMACTET ARIAQLVARQ RSSKRKTGRQ 100
    VNCQMRVKKT MPFFLEGKPK ATLRQPGFAS NFSVGKKPNP APLRDKGNSV 150
    GVKPDAEMSP YMLHTTLGNE AFKDIPVQRH VTMSTNNRFS PKASLQPPLQ 200
    MHLSRTSTKE MSDNLNQTVE KPNVKPPASY TYKMDEVQNR IKEILNKHNN 250
    GIWISKLPHF YKELYKEDLN QGILQQFEHW PHICTVEKPC SGGQDLLLYP 300
    AKRKQLLRSE LDTEKVPLSP LPGPKQTPPL KGCPTVMAGD FKEKVADLLV 350
    KYTSGLWASA LPKAFEEMYK VKFPEDALKN LASLSDVCSI DYISGNPQKA 400
    ILYAKLPLPT DKIQKDAGQA HGDNDIKAMV EQEYLQVEES IAESANTFME 450
    DITVPPLMIP TEASPSVLVV ELSNTNEVVI RYVGKDYSAA QELMEDEMKE 500
    YYSKNPKITP VQAVNVGQLL AVNAEEDAWL RAQVISTEEN KIKVCYVDYG 550
    FSENVEKSKA YKLNPKFCSL SFQATKCKLA GLEVLSDDPD LVKVVESLTC 600
    GKIFAVEILD KADIPLVVLY DTSGEDDINI NATCLKAICD KSLEVHLQVD 650
    AMYTNVKVTN ICSDGTLYCQ VPCKGLNKLS DLLRKIEDYF HCKHMTSECF 700
    VSLPFCGKIC LFHCKGKWLR VEITNVHSSR ALDVQFLDSG TVTSVKVSEL 750
    REIPPRFLQE MIAIPPQAIK CCLADLPQSI GMWTPDAVLW LRDSVLNCSD 800
    CSIKVTKVDE TRGIAHVYLF TPKNFPDPHR SINRQITNAD LWKHQKDVFL 850
    SAISSGADSP NSKNGNMPMS GNTGENFRKN LTDVIKKSMV DHTSAFSTEE 900
    LPPPVHLSKP GEHMDVYVPV ACHPGYFVIQ PWQEIHKLEV LMEEMILYYS 950
    VSEERHIAVE KDQVYAAKVE NKWHRVLLKG ILTNGLVSVY ELDYGKHELV 1000
    NIRKVQPLVD MFRKLPFQAV TAQLAGVKCN QWSEEASMVF RNHVEKKPLV 1050
    ALVQTVIENA NPWDRKVVVY LVDTSLPDTD TWIHDFMSEY LIELSKVN 1098
    Length:1,098
    Mass (Da):123,586
    Last modified:July 10, 2007 - v2
    Checksum:iF27E383E5B18C428
    GO
    Isoform 2 (identifier: Q8NHU6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,024
    Mass (Da):115,338
    Checksum:i37280FAC875C7EE5
    GO
    Isoform 3 (identifier: Q8NHU6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-651: Missing.
         694-722: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:418
    Mass (Da):47,539
    Checksum:iADDFA5052CF8D146
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501V → A.2 Publications
    Corresponds to variant rs2045732 [ dbSNP | Ensembl ].
    VAR_019070
    Natural varianti456 – 4561P → L.1 Publication
    Corresponds to variant rs17852595 [ dbSNP | Ensembl ].
    VAR_033044
    Natural varianti618 – 6181Missing in CTRCT36. 1 Publication
    VAR_065247

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 651651Missing in isoform 3. 1 PublicationVSP_041314Add
    BLAST
    Alternative sequencei1 – 7474Missing in isoform 2. 1 PublicationVSP_041315Add
    BLAST
    Alternative sequencei694 – 72229Missing in isoform 3. 1 PublicationVSP_041316Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti659 – 6591T → A in BAG63369. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK294488 mRNA. Translation: BAG57710.1.
    AK301954 mRNA. Translation: BAG63369.1.
    AK314853 mRNA. Translation: BAG37370.1.
    AL512590, AL449464 Genomic DNA. Translation: CAH71605.1.
    AL449464, AL512590 Genomic DNA. Translation: CAI14933.1.
    CH471105 Genomic DNA. Translation: EAW58844.1.
    BC028694 mRNA. Translation: AAH28694.1.
    AB025254 mRNA. Translation: BAA76379.1.
    AL122110 mRNA. Translation: CAB59271.1.
    CCDSiCCDS6725.1. [Q8NHU6-1]
    PIRiT34547.
    RefSeqiNP_055105.2. NM_014290.2. [Q8NHU6-1]
    XP_006717088.1. XM_006717025.1. [Q8NHU6-2]
    UniGeneiHs.193842.

    Genome annotation databases

    EnsembliENST00000355295; ENSP00000347444; ENSG00000196116. [Q8NHU6-1]
    GeneIDi23424.
    KEGGihsa:23424.
    UCSCiuc004axj.3. human. [Q8NHU6-1]
    uc011luy.2. human. [Q8NHU6-3]

    Polymorphism databases

    DMDMi152031705.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK294488 mRNA. Translation: BAG57710.1 .
    AK301954 mRNA. Translation: BAG63369.1 .
    AK314853 mRNA. Translation: BAG37370.1 .
    AL512590 , AL449464 Genomic DNA. Translation: CAH71605.1 .
    AL449464 , AL512590 Genomic DNA. Translation: CAI14933.1 .
    CH471105 Genomic DNA. Translation: EAW58844.1 .
    BC028694 mRNA. Translation: AAH28694.1 .
    AB025254 mRNA. Translation: BAA76379.1 .
    AL122110 mRNA. Translation: CAB59271.1 .
    CCDSi CCDS6725.1. [Q8NHU6-1 ]
    PIRi T34547.
    RefSeqi NP_055105.2. NM_014290.2. [Q8NHU6-1 ]
    XP_006717088.1. XM_006717025.1. [Q8NHU6-2 ]
    UniGenei Hs.193842.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RCO X-ray 1.80 A/B 1-82 [» ]
    ProteinModelPortali Q8NHU6.
    SMRi Q8NHU6. Positions 1-77, 234-412, 663-787, 970-1077.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116994. 8 interactions.
    IntActi Q8NHU6. 6 interactions.
    MINTi MINT-2871006.
    STRINGi 9606.ENSP00000347444.

    PTM databases

    PhosphoSitei Q8NHU6.

    Polymorphism databases

    DMDMi 152031705.

    Proteomic databases

    MaxQBi Q8NHU6.
    PaxDbi Q8NHU6.
    PRIDEi Q8NHU6.

    Protocols and materials databases

    DNASUi 23424.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355295 ; ENSP00000347444 ; ENSG00000196116 . [Q8NHU6-1 ]
    GeneIDi 23424.
    KEGGi hsa:23424.
    UCSCi uc004axj.3. human. [Q8NHU6-1 ]
    uc011luy.2. human. [Q8NHU6-3 ]

    Organism-specific databases

    CTDi 23424.
    GeneCardsi GC09P100174.
    H-InvDB HIX0008211.
    HGNCi HGNC:30831. TDRD7.
    HPAi CAB020800.
    HPA024529.
    MIMi 611258. gene.
    613887. phenotype.
    neXtProti NX_Q8NHU6.
    PharmGKBi PA134937960.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256635.
    HOVERGENi HBG103662.
    InParanoidi Q8NHU6.
    OMAi YDTSGED.
    OrthoDBi EOG7BW0HQ.
    PhylomeDBi Q8NHU6.

    Miscellaneous databases

    GeneWikii TDRD7.
    GenomeRNAii 23424.
    NextBioi 45647.
    PROi Q8NHU6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NHU6.
    CleanExi HS_TDRD7.
    Genevestigatori Q8NHU6.

    Family and domain databases

    InterProi IPR025605. OST-HTH/LOTUS_dom.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF12872. OST-HTH. 1 hit.
    PF00567. TUDOR. 3 hits.
    [Graphical view ]
    SMARTi SM00333. TUDOR. 2 hits.
    [Graphical view ]
    PROSITEi PS51644. HTH_OST. 3 hits.
    PS50304. TUDOR. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1; 2 AND 3), VARIANT ALA-150.
      Tissue: Amygdala and Testis.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-150.
    4. "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] (ISOFORM 1), VARIANT LEU-456.
      Tissue: Testis.
    5. "Identification of tudor repeat associator with PCTAIRE 2 (Trap). A novel protein that interacts with the N-terminal domain of PCTAIRE 2 in rat brain."
      Hirose T., Kawabuchi M., Tamaru T., Okumura N., Nagai K., Okada M.
      Eur. J. Biochem. 267:2113-2121(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 631-1098.
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 837-1098.
      Tissue: Testis.
    7. "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].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "LOTUS, a new domain associated with small RNA pathways in the germline."
      Callebaut I., Mornon J.P.
      Bioinformatics 26:1140-1144(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
    10. "OST-HTH: a novel predicted RNA-binding domain."
      Anantharaman V., Zhang D., Aravind L.
      Biol. Direct 5:13-13(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
    11. Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, VARIANT CTRCT36 VAL-618 DEL.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTDRD7_HUMAN
    AccessioniPrimary (citable) accession number: Q8NHU6
    Secondary accession number(s): A6NCI6
    , B2RBX3, B4DG99, B4DXF7, E7EQD4, Q5VV27, Q96JT1, Q9UFF0, Q9Y2M3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 104 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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

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