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Protein

TSC22 domain family protein 3

Gene

TSC22D3

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

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
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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

BgeeiQ99576.
CleanExiHS_TSC22D3.
ExpressionAtlasiQ99576. baseline and differential.
GenevestigatoriQ99576.

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. 30 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.
GeneTreeiENSGT00530000063062.
HOVERGENiHBG056226.
InParanoidiQ99576.
OMAiSTEMFAK.
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. AlignAdd to basket

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

        10         20         30         40         50
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI
60 70 80 90 100
DNKIEQAMDL VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL
110 120 130
ASPEQLEKFQ SCLSPEEPAP ESPQVPEAPG GSAV
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 73.1 Publication

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi108165. 30 interactions.
IntActiQ99576. 5 interactions.
MINTiMINT-4715756.
STRINGi9606.ENSP00000361458.

PTM databases

PhosphoSiteiQ99576.

Polymorphism databases

DMDMi14195584.

Proteomic databases

MaxQBiQ99576.
PaxDbiQ99576.
PRIDEiQ99576.

Protocols and materials databases

DNASUi1831.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi1831.
GeneCardsiGC0XM106956.
HGNCiHGNC:3051. TSC22D3.
MIMi300506. gene.
neXtProtiNX_Q99576.
PharmGKBiPA27504.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG329226.
GeneTreeiENSGT00530000063062.
HOVERGENiHBG056226.
InParanoidiQ99576.
OMAiSTEMFAK.
PhylomeDBiQ99576.
TreeFamiTF329224.

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Miscellaneous databases

ChiTaRSiTSC22D3. human.
GeneWikiiTSC22D3.
GenomeRNAii1831.
NextBioi7473.
PROiQ99576.
SOURCEiSearch...

Gene expression databases

BgeeiQ99576.
CleanExiHS_TSC22D3.
ExpressionAtlasiQ99576. baseline and differential.
GenevestigatoriQ99576.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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(2000) [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 (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Iris.
  4. "Human GILZ."
    Okada T.
    Submitted (FEB-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 (APR-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(2003) [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(2004) [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(2003) [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 (MAY-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(2000) [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(2002) [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(2003) [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(2008) [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(2009) [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: March 4, 2015
This is version 138 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

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.