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Protein

NFATC2-interacting protein

Gene

Nfatc2ip

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9.2 Publications

GO - Molecular functioni

GO - Biological processi

  • cytokine production Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein sumoylation Source: GO_Central
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NFATC2-interacting protein
Alternative name(s):
45 kDa NF-AT-interacting protein
Short name:
45 kDa NFAT-interacting protein
Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
Gene namesi
Name:Nfatc2ip
Synonyms:Nip45
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1329015. Nfatc2ip.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian ratio and appear healthy and viable. No alteration in thymic T-cell populations, T-cell proliferation, or peripheral lymphocyte development. Inefficient type-2 antiparasitic immune response to the intestinal nematode Trichinella spiralis due to impaired IL4 and IL13 cytokine production by Th2 cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412NFATC2-interacting proteinPRO_0000281009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei51 – 511PhosphoserineBy similarity
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei81 – 811PhosphoserineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei309 – 3091PhosphothreonineBy similarity
Modified residuei311 – 3111PhosphothreonineBy similarity
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei383 – 3831PhosphoserineBy similarity

Post-translational modificationi

Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiO09130.
MaxQBiO09130.
PaxDbiO09130.
PeptideAtlasiO09130.
PRIDEiO09130.

PTM databases

iPTMnetiO09130.
PhosphoSiteiO09130.

Expressioni

Tissue specificityi

Highest level detected in spleen, thymus and testis.1 Publication

Gene expression databases

BgeeiO09130.
GenevisibleiO09130. MM.

Interactioni

Subunit structurei

Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with UBE2I/UBC9.4 Publications

Protein-protein interaction databases

BioGridi201740. 2 interactions.
IntActiO09130. 1 interaction.
MINTiMINT-6476454.
STRINGi10090.ENSMUSP00000075094.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi341 – 3466Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi360 – 3623Combined sources
Helixi364 – 37512Combined sources
Beta strandi383 – 3864Combined sources
Helixi397 – 4004Combined sources
Beta strandi407 – 4115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A4RX-ray1.00A/B339-412[»]
3A4SX-ray2.70C/D339-412[»]
ProteinModelPortaliO09130.
SMRiO09130. Positions 237-331, 338-412.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09130.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini341 – 41272Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili168 – 22760Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000007119.
HOGENOMiHOG000285948.
HOVERGENiHBG082020.
InParanoidiO09130.
OMAiSHYEEAM.
OrthoDBiEOG73806D.
PhylomeDBiO09130.
TreeFamiTF328600.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O09130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPLRGRGP RSRGGRGARR ARGARGRCPR ARQSPARLIP DTVLVDLVSD
60 70 80 90 100
SDEEVLEVAD PVEVPVARLP APAKPEQDSD SDSEGAAEGP AGAPRTLVRR
110 120 130 140 150
RRRRLLDPGE APVVPVYSGK VQSSLNLIPD NSSLLKLCPS EPEDEADLTN
160 170 180 190 200
SGSSPSEDDA LPSGSPWRKK LRKKCEKEEK KMEEFPDQDI SPLPQPSSRN
210 220 230 240 250
KSRKHTEALQ KLREVNKRLQ DLRSCLSPKQ HQSPALQSTD DEVVLVEGPV
260 270 280 290 300
LPQSSRLFTL KIRCRADLVR LPVRMSEPLQ NVVDHMANHL GVSPNRILLL
310 320 330 340 350
FGESELSPTA TPSTLKLGVA DIIDCVVLAS SSEATETSQE LRLRVQGKEK
360 370 380 390 400
HQMLEISLSP DSPLKVLMSH YEEAMGLSGH KLSFFFDGTK LSGKELPADL
410
GLESGDLIEV WG
Length:412
Mass (Da):45,121
Last modified:July 1, 1997 - v1
Checksum:iDD58FE5C7055C186
GO

Sequence cautioni

The sequence BAB24331.1 differs from that shown. Reason: Frameshift at position 21. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → G in BAC26788 (PubMed:16141072).Curated
Sequence conflicti200 – 2001N → D in BAC26788 (PubMed:16141072).Curated
Sequence conflicti390 – 3912KL → NS in BAB24331 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76759 mRNA. Translation: AAC52963.1.
AK005947 mRNA. Translation: BAB24331.1. Frameshift.
AK030107 mRNA. Translation: BAC26788.1.
BC113761 mRNA. Translation: AAI13762.1.
CCDSiCCDS21827.1.
RefSeqiNP_035030.2. NM_010900.3.
UniGeneiMm.1389.

Genome annotation databases

EnsembliENSMUST00000075671; ENSMUSP00000075094; ENSMUSG00000030722.
GeneIDi18020.
KEGGimmu:18020.
UCSCiuc009jra.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76759 mRNA. Translation: AAC52963.1.
AK005947 mRNA. Translation: BAB24331.1. Frameshift.
AK030107 mRNA. Translation: BAC26788.1.
BC113761 mRNA. Translation: AAI13762.1.
CCDSiCCDS21827.1.
RefSeqiNP_035030.2. NM_010900.3.
UniGeneiMm.1389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A4RX-ray1.00A/B339-412[»]
3A4SX-ray2.70C/D339-412[»]
ProteinModelPortaliO09130.
SMRiO09130. Positions 237-331, 338-412.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201740. 2 interactions.
IntActiO09130. 1 interaction.
MINTiMINT-6476454.
STRINGi10090.ENSMUSP00000075094.

PTM databases

iPTMnetiO09130.
PhosphoSiteiO09130.

Proteomic databases

EPDiO09130.
MaxQBiO09130.
PaxDbiO09130.
PeptideAtlasiO09130.
PRIDEiO09130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075671; ENSMUSP00000075094; ENSMUSG00000030722.
GeneIDi18020.
KEGGimmu:18020.
UCSCiuc009jra.1. mouse.

Organism-specific databases

CTDi84901.
MGIiMGI:1329015. Nfatc2ip.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000007119.
HOGENOMiHOG000285948.
HOVERGENiHBG082020.
InParanoidiO09130.
OMAiSHYEEAM.
OrthoDBiEOG73806D.
PhylomeDBiO09130.
TreeFamiTF328600.

Miscellaneous databases

EvolutionaryTraceiO09130.
PROiO09130.
SOURCEiSearch...

Gene expression databases

BgeeiO09130.
GenevisibleiO09130. MM.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NF-AT-driven interleukin-4 transcription potentiated by NIP45."
    Hodge M.R., Chun H.J., Rengarajan J., Alt A., Lieberson R., Glimcher L.H.
    Science 274:1903-1905(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH NFATC2.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Tumor necrosis factor receptor-associated factor (TRAF)2 represses the T helper cell type 2 response through interaction with NFAT-interacting protein (NIP45)."
    Lieberson R., Mowen K.A., McBride K.D., Leautaud V., Zhang X., Suh W.-K., Wu L., Glimcher L.H.
    J. Exp. Med. 194:89-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2.
  5. "Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes."
    Mowen K.A., Schurter B.T., Fathman J.W., David M., Glimcher L.H.
    Mol. Cell 15:559-571(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, METHYLATION.
  6. "TRAF1 regulates Th2 differentiation, allergic inflammation and nuclear localization of the Th2 transcription factor, NIP45."
    Bryce P.J., Oyoshi M.K., Kawamoto S., Oettgen H.C., Tsitsikov E.N.
    Int. Immunol. 18:101-111(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF1, SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-81; SER-83; SER-191 AND SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Spleen and Testis.
  9. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45."
    Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.
    Proteins 78:1491-1502(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 338-412 IN COMPLEX WITH UBE2I/UBC9, FUNCTION.

Entry informationi

Entry nameiNF2IP_MOUSE
AccessioniPrimary (citable) accession number: O09130
Secondary accession number(s): Q8CDG2, Q9CVY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.