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Q99576

- T22D3_HUMAN

UniProt

Q99576 - T22D3_HUMAN

Protein

TSC22 domain family protein 3

Gene

TSC22D3

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

    Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities By similarity. Isoform 1 inhibits myogenic differentiation and mediates anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG By similarity.By similarity

    GO - Molecular functioni

    1. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. body fluid secretion Source: Ensembl
    2. ion transmembrane transport Source: Reactome
    3. negative regulation of activation-induced cell death of T cells Source: Ensembl
    4. negative regulation of skeletal muscle tissue development Source: Ensembl
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of transcription, DNA-templated Source: ProtInc
    7. response to osmotic stress Source: Ensembl
    8. transmembrane transport Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TSC22 domain family protein 3
    Alternative name(s):
    DSIP-immunoreactive peptide
    Short name:
    Protein DIP
    Short name:
    hDIP
    Delta sleep-inducing peptide immunoreactor
    Glucocorticoid-induced leucine zipper protein
    Short name:
    GILZ
    TSC-22-like protein
    TSC-22-related protein
    Short name:
    TSC-22R
    Gene namesi
    Name:TSC22D3
    Synonyms:DSIPI, GILZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3051. TSC22D3.

    Subcellular locationi

    Isoform 1 : Cytoplasm By similarity. Nucleus By similarity
    Note: Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the cytoplasm, but in differentiating myoblasts, isoform 1 is localized to the nucleus By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27504.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 134134TSC22 domain family protein 3PRO_0000219370Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99576.
    PaxDbiQ99576.
    PRIDEiQ99576.

    PTM databases

    PhosphoSiteiQ99576.

    Expressioni

    Tissue specificityi

    Expressed in brain, lung, spleen and skeletal muscle. Lower levels detected in heart and kidney. Not detected in the pancreas. In non-lymphoid tissues, in the absence of inflammation, the major source of constitutive expression is the macrophage lineage. Also expressed in cells from different hemopoietic cell lineages, including bone marrow cells, CD34+ stem cells, mature B- and T-cells, monocytes and granulocytes. Down-regulated in activated macrophages from inflammatory lesions of delayed-type hypersensitivity (DTH) reactions, such as in tuberculosis and in Crohn disease, whereas in Burkitt lymphoma, persists in macrophages involved in the phagocytosis of apoptotic malignant cells.2 Publications

    Inductioni

    By glucocorticoids in lymphoid cells and upon IL4, IL10, IL13 or glucocorticoid treatment in monocyte/macrophage cells. Transiently induced by IL2 deprivation in T-cells. Isoform 1 expression is up-regulated by synthetic glucocorticoid dexamethasone in differentiating myoblasts By similarity.By similarity

    Gene expression databases

    ArrayExpressiQ99576.
    BgeeiQ99576.
    CleanExiHS_TSC22D3.
    GenevestigatoriQ99576.

    Organism-specific databases

    HPAiHPA001916.

    Interactioni

    Subunit structurei

    Can form homodimers, however it is likely to function as a monomer. Interacts with AP1 By similarity. Interacts with NFKB1. Isoform 1 interacts with MYOD1 By similarity. Isoform 1 interacts with HDAC1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108165. 22 interactions.
    IntActiQ99576. 5 interactions.
    MINTiMINT-4715756.
    STRINGi9606.ENSP00000361458.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99576.
    SMRiQ99576. Positions 58-134.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6060AP1-bindingBy similarityAdd
    BLAST
    Regioni76 – 9722Leucine-zipperAdd
    BLAST

    Domaini

    The leucine-zipper is involved in homodimerization.By similarity

    Sequence similaritiesi

    Belongs to the TSC-22/Dip/Bun family.Curated

    Phylogenomic databases

    eggNOGiNOG329226.
    HOVERGENiHBG056226.
    OMAiGRTFIVY.
    PhylomeDBiQ99576.
    TreeFamiTF329224.

    Family and domain databases

    InterProiIPR000580. TSC-22_Dip_Bun.
    [Graphical view]
    PANTHERiPTHR12348. PTHR12348. 1 hit.
    PfamiPF01166. TSC22. 1 hit.
    [Graphical view]
    ProDomiPD007152. TSC-22_Dip_Bun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    PROSITEiPS01289. TSC22. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99576-1) [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

    MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI    50
    DNKIEQAMDL VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL 100
    ASPEQLEKFQ SCLSPEEPAP ESPQVPEAPG GSAV 134
    Length:134
    Mass (Da):14,810
    Last modified:June 1, 2001 - v2
    Checksum:i77B1024969FA8687
    GO
    Isoform 2 (identifier: Q99576-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: MNTEMYQTPM...GDVVSVKLDN → MAQSKLDCRS...TMLSILLFFH

    Note: Contains a phosphoserine at position 42. Contains a phosphoserine at position 73.

    Show »
    Length:200
    Mass (Da):22,213
    Checksum:i5CBFE801E1700C8C
    GO
    Isoform 3 (identifier: Q99576-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDNS → GGWPSAVRAWEKAGSLPAEKEFLASFRAG

    Note: Incomplete sequence. No experimental confirmation available.

    Show »
    Length:122
    Mass (Da):13,286
    Checksum:i3FA577D9052EDB7C
    GO

    Sequence cautioni

    The sequence CAB53669.1 differs from that shown. Reason: Frameshift at position 4.
    The sequence AAH18148.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA90644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541I → F in CAA90644. (PubMed:8982256)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141MNTEM…KLDNS → GGWPSAVRAWEKAGSLPAEK EFLASFRAG in isoform 3. 2 PublicationsVSP_020732Add
    BLAST
    Alternative sequencei1 – 4040MNTEM…VKLDN → MAQSKLDCRSPVGLDCCNCC LDLAHRSGLQRGSSGENNNP GSPTVSNFRQLQEKLVFENL NTDKLNSIMRQDSLEPVLRD PCYLINEGICNRNIDQTMLS ILLFFH in isoform 2. 1 PublicationVSP_012689Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50781 mRNA. Translation: CAA90644.1. Different initiation.
    AF228339 mRNA. Translation: AAG12456.1.
    AF183393 mRNA. Translation: AAD56234.1.
    AB025432 mRNA. Translation: BAB18680.1.
    AF153603 mRNA. Translation: AAD41085.1.
    AL110191 mRNA. Translation: CAB53669.1. Frameshift.
    AK092645 mRNA. Translation: BAC03934.1.
    AK092669 mRNA. Translation: BAG52587.1.
    AL590423 Genomic DNA. Translation: CAI41544.1.
    CH471120 Genomic DNA. Translation: EAX02704.1.
    CH471120 Genomic DNA. Translation: EAX02705.1.
    CH471120 Genomic DNA. Translation: EAX02706.1.
    CR933650 mRNA. Translation: CAI45951.1.
    BC018148 mRNA. Translation: AAH18148.3. Different initiation.
    BC072446 mRNA. Translation: AAH72446.1.
    CR533450 mRNA. Translation: CAG38481.1.
    CCDSiCCDS14530.1. [Q99576-3]
    CCDS14531.1. [Q99576-1]
    PIRiT14749.
    RefSeqiNP_001015881.1. NM_001015881.1.
    NP_004080.2. NM_004089.3. [Q99576-1]
    NP_932174.1. NM_198057.2. [Q99576-3]
    XP_005262155.1. XM_005262098.1. [Q99576-3]
    XP_005262156.1. XM_005262099.1. [Q99576-3]
    XP_005262157.1. XM_005262100.1. [Q99576-3]
    XP_005262158.1. XM_005262101.1. [Q99576-3]
    XP_005262159.1. XM_005262102.1. [Q99576-3]
    XP_005262160.1. XM_005262103.1. [Q99576-3]
    XP_006724692.1. XM_006724629.1. [Q99576-3]
    UniGeneiHs.522074.

    Genome annotation databases

    EnsembliENST00000315660; ENSP00000314655; ENSG00000157514. [Q99576-3]
    ENST00000372383; ENSP00000361458; ENSG00000157514. [Q99576-3]
    ENST00000372384; ENSP00000361459; ENSG00000157514. [Q99576-3]
    ENST00000372397; ENSP00000361474; ENSG00000157514. [Q99576-1]
    ENST00000506081; ENSP00000427427; ENSG00000157514. [Q99576-3]
    GeneIDi1831.
    KEGGihsa:1831.
    UCSCiuc004enf.3. human. [Q99576-1]
    uc004enh.3. human. [Q99576-3]

    Polymorphism databases

    DMDMi14195584.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50781 mRNA. Translation: CAA90644.1 . Different initiation.
    AF228339 mRNA. Translation: AAG12456.1 .
    AF183393 mRNA. Translation: AAD56234.1 .
    AB025432 mRNA. Translation: BAB18680.1 .
    AF153603 mRNA. Translation: AAD41085.1 .
    AL110191 mRNA. Translation: CAB53669.1 . Frameshift.
    AK092645 mRNA. Translation: BAC03934.1 .
    AK092669 mRNA. Translation: BAG52587.1 .
    AL590423 Genomic DNA. Translation: CAI41544.1 .
    CH471120 Genomic DNA. Translation: EAX02704.1 .
    CH471120 Genomic DNA. Translation: EAX02705.1 .
    CH471120 Genomic DNA. Translation: EAX02706.1 .
    CR933650 mRNA. Translation: CAI45951.1 .
    BC018148 mRNA. Translation: AAH18148.3 . Different initiation.
    BC072446 mRNA. Translation: AAH72446.1 .
    CR533450 mRNA. Translation: CAG38481.1 .
    CCDSi CCDS14530.1. [Q99576-3 ]
    CCDS14531.1. [Q99576-1 ]
    PIRi T14749.
    RefSeqi NP_001015881.1. NM_001015881.1.
    NP_004080.2. NM_004089.3. [Q99576-1 ]
    NP_932174.1. NM_198057.2. [Q99576-3 ]
    XP_005262155.1. XM_005262098.1. [Q99576-3 ]
    XP_005262156.1. XM_005262099.1. [Q99576-3 ]
    XP_005262157.1. XM_005262100.1. [Q99576-3 ]
    XP_005262158.1. XM_005262101.1. [Q99576-3 ]
    XP_005262159.1. XM_005262102.1. [Q99576-3 ]
    XP_005262160.1. XM_005262103.1. [Q99576-3 ]
    XP_006724692.1. XM_006724629.1. [Q99576-3 ]
    UniGenei Hs.522074.

    3D structure databases

    ProteinModelPortali Q99576.
    SMRi Q99576. Positions 58-134.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108165. 22 interactions.
    IntActi Q99576. 5 interactions.
    MINTi MINT-4715756.
    STRINGi 9606.ENSP00000361458.

    PTM databases

    PhosphoSitei Q99576.

    Polymorphism databases

    DMDMi 14195584.

    Proteomic databases

    MaxQBi Q99576.
    PaxDbi Q99576.
    PRIDEi Q99576.

    Protocols and materials databases

    DNASUi 1831.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315660 ; ENSP00000314655 ; ENSG00000157514 . [Q99576-3 ]
    ENST00000372383 ; ENSP00000361458 ; ENSG00000157514 . [Q99576-3 ]
    ENST00000372384 ; ENSP00000361459 ; ENSG00000157514 . [Q99576-3 ]
    ENST00000372397 ; ENSP00000361474 ; ENSG00000157514 . [Q99576-1 ]
    ENST00000506081 ; ENSP00000427427 ; ENSG00000157514 . [Q99576-3 ]
    GeneIDi 1831.
    KEGGi hsa:1831.
    UCSCi uc004enf.3. human. [Q99576-1 ]
    uc004enh.3. human. [Q99576-3 ]

    Organism-specific databases

    CTDi 1831.
    GeneCardsi GC0XM106956.
    HGNCi HGNC:3051. TSC22D3.
    HPAi HPA001916.
    MIMi 300506. gene.
    neXtProti NX_Q99576.
    PharmGKBi PA27504.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329226.
    HOVERGENi HBG056226.
    OMAi GRTFIVY.
    PhylomeDBi Q99576.
    TreeFami TF329224.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.

    Miscellaneous databases

    ChiTaRSi TSC22D3. human.
    GeneWikii TSC22D3.
    GenomeRNAii 1831.
    NextBioi 7473.
    PROi Q99576.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99576.
    Bgeei Q99576.
    CleanExi HS_TSC22D3.
    Genevestigatori Q99576.

    Family and domain databases

    InterProi IPR000580. TSC-22_Dip_Bun.
    [Graphical view ]
    PANTHERi PTHR12348. PTHR12348. 1 hit.
    Pfami PF01166. TSC22. 1 hit.
    [Graphical view ]
    ProDomi PD007152. TSC-22_Dip_Bun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS01289. TSC22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "hDIP -- a potential transcriptional regulator related to murine TSC-22 and Drosophila shortsighted (shs) -- is expressed in a large number of human tissues."
      Vogel P., Maegert H.-J., Cieslak A., Adermann K., Forssmann W.-G.
      Biochim. Biophys. Acta 1309:200-204(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Fetal brain.
    2. "Cloning, chromosomal assignment and tissue distribution of human GILZ, a glucocorticoid hormone-induced gene."
      Cannarile L., Zollo O., D'Adamio F., Ayroldi E., Marchetti C., Tabilio A., Bruscoli S., Riccardi C.
      Cell Death Differ. 8:201-203(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: T-cell.
    3. "Full-length sequence of ocular cDNA clones."
      Wistow G.J.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Iris.
    4. "Human GILZ."
      Okada T.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
      Kim M.K., Kim Y.H., Suh J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Kim J.C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hair follicle dermal papilla.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal kidney.
    7. "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] (ISOFORM 2).
      Tissue: Prostate and Pulmonary artery.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adipose tissue.
    9. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-122 (ISOFORM 3).
      Tissue: Colon and Melanoma.
    12. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-134.
    13. "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappa B."
      Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O., Cannarile L., D'Adamio F., Riccardi C.
      Blood 98:743-753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFKB1.
    14. "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10."
      Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G., Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P., Peuchmaur M., Riccardi C., Emilie D.
      Blood 101:729-738(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH NFKB1.
    15. "GILZ, a new target for the transcription factor FoxO3, protects T lymphocytes from interleukin-2 withdrawal-induced apoptosis."
      Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D., Zennaro M.-C., Bertoglio J., Pallardy M.
      Blood 104:215-223(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-73 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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].
    18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiT22D3_HUMAN
    AccessioniPrimary (citable) accession number: Q99576
    Secondary accession number(s): Q5H9S3
    , Q5JRI9, Q6FIH6, Q8NAI1, Q8WVB9, Q9UBN5, Q9UG13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 134 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3