Q13469 (NFAC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear factor of activated T-cells, cytoplasmic 2
Short name=NF-ATc2
Short name=NFATc2

Alternative name(s):
NFAT pre-existing subunit
Short name=NF-ATp
T-cell transcription factor NFAT1

Gene names

Name:	NFATC2
Synonyms:	NFAT1, NFATP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	925 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway. Ref.11
Subunit structure	Member of the multicomponent NFATC transcription complex that consists of at least two components, a pre-existing cytoplasmic component NFATC2 and an inducible nuclear component NFATC1. Other members such as NFATC4, NFATC3 or members of the activating protein-1 family, MAF, GATA4 and Cbp/p300 can also bind the complex. The phosphorylated form specifically interacts with XPO1; which mediates nuclear export. NFATC proteins bind to DNA as monomers. Interacts with NFATC2IP By similarity.
Subcellular location	Cytoplasm. Nucleus. Note: Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription.
Tissue specificity	Expressed in thymus, spleen, heart, testis, brain, placenta, muscle and pancreas. Isoform 1 is highly expressed in the small intestine, heart, testis, prostate, thymus, placenta and thyroid. Isoform 3 is highly expressed in stomach, uterus, placenta, trachea and thyroid. Ref.1
Induction	Inducibly expressed in T-lymphocytes upon activation of the T-cell receptor (TCR) complex. Induced after co-addition of phorbol 12-myristate 13-acetate (PMA) and ionomycin.
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.8 Rel Similarity Domain (RSD) allows DNA-binding and cooperative interactions with AP1 factors By similarity. Ref.8
Post-translational modification	In resting cells, phosphorylated by NFATC-kinase on at least 18 sites in the 99-363 region. Upon cell stimulation, all these sites except Ser-243 are dephosphorylated by calcineurin. Dephosphorylation induces a conformational change that simultaneously exposes an NLS and masks an NES, which results in nuclear localization. Simultaneously, Ser-53 or Ser-56 is phosphorylated; which is required for full transcriptional activity.
Sequence similarities	Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB cell migration Inferred from direct assay Ref.11. Source: UniProtKB cytokine production Inferred from electronic annotation. Source: Compara positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15790681. Source: MGI response to DNA damage stimulus Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB response to drug Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 12656674. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA ribonucleoprotein complex Inferred from electronic annotation. Source: Compara transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Traceable author statement Ref.1. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: UniProtKB transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LRRK2	Q5S007	3	EBI-716258,EBI-5323863
VRK2	Q86Y07-1	3	EBI-716258,EBI-1207633
VRK2	Q86Y07-2	4	EBI-716258,EBI-1207636

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q13469-1)

Also known as: C; NFATc2_IB_IIL;

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.

Isoform 2 (identifier: Q13469-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL

Isoform 3 (identifier: Q13469-3)

Also known as: NFATc2_IA_IIL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNE → MQREAAFRLGHCHPLRIMGSVDQ
     908-925: VNEIIRKEFSGPPARNQT → ELIDTHLSWIQNIL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 925

925

Nuclear factor of activated T-cells, cytoplasmic 2

PRO_0000205178

Regions

Repeat

184 – 200

17

1

Repeat

213 – 229

17

2

Repeat

272 – 286

15

3; approximate

Domain

392 – 574

183

RHD

DNA binding

421 – 428

8

Region

111 – 116

6

Calcineurin-binding

Region

119 – 199

81

Trans-activation domain A (TAD-A)

Region

161 – 175

15

Required for cytoplasmic retention of the phosphorylated form By similarity

Region

184 – 286

103

3 X approximate SP repeats

Motif

26 – 34

9

9aaTAD

Motif

251 – 253

3

Nuclear localization signal

Motif

664 – 666

3

Nuclear localization signal

Motif

904 – 913

10

Nuclear export signal

Amino acid modifications

Modified residue

99

1

Phosphoserine By similarity

Modified residue

148

1

Phosphoserine Ref.9

Modified residue

213

1

Phosphoserine By similarity

Modified residue

217

1

Phosphoserine By similarity

Modified residue

221

1

Phosphoserine By similarity

Modified residue

236

1

Phosphoserine By similarity

Modified residue

243

1

Phosphoserine By similarity

Modified residue

268

1

Phosphoserine By similarity

Modified residue

274

1

Phosphoserine By similarity

Modified residue

276

1

Phosphoserine By similarity

Modified residue

280

1

Phosphoserine By similarity

Modified residue

326

1

Phosphoserine By similarity

Modified residue

330

1

Phosphoserine Ref.7 Ref.9

Modified residue

363

1

Phosphoserine By similarity

Modified residue

755

1

Phosphoserine Ref.9

Modified residue

757

1

Phosphoserine Ref.10

Modified residue

759

1

Phosphoserine Ref.9 Ref.10

Modified residue

859

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1 – 43

43

MNAPE…LNPNE → MQREAAFRLGHCHPLRIMGS VDQ in isoform 3.

VSP_042757

Alternative sequence

908 – 925

18

VNEII…ARNQT → ELIDTHLSWIQNIL in isoform 2 and isoform 3.

VSP_005595

Natural variant

446

1

H → R.
Corresponds to variant rs12479626 [ dbSNP | Ensembl ].

VAR_051783

Experimental info

Sequence conflict

65

1

L → M in AAC50886. Ref.1

Sequence conflict

65

1

L → M in AAC50887. Ref.1

Secondary structure

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925

Helix Strand Turn

Details...

Beta strand

397 – 399

3

Beta strand

402 – 405

4

Beta strand

408 – 414

7

Beta strand

436 – 439

4

Beta strand

442 – 445

4

Beta strand

450 – 452

3

Beta strand

454 – 461

8

Beta strand

464 – 466

3

Beta strand

474 – 478

5

Beta strand

481 – 483

3

Beta strand

490 – 492

3

Beta strand

494 – 496

3

Beta strand

498 – 503

6

Helix

505 – 507

3

Beta strand

510 – 512

3

Beta strand

515 – 520

6

Helix

523 – 526

4

Beta strand

529 – 531

3

Beta strand

541 – 552

12

Turn

553 – 555

3

Beta strand

556 – 563

8

Helix

571 – 576

6

Beta strand

579 – 584

6

Beta strand

586 – 589

4

Beta strand

595 – 602

8

Beta strand

608 – 614

7

Beta strand

616 – 618

3

Beta strand

620 – 626

7

Turn

630 – 632

3

Beta strand

637 – 641

5

Beta strand

646 – 648

3

Beta strand

654 – 662

9

Turn

663 – 665

3

Beta strand

671 – 676

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (C) (NFATc2_IB_IIL) [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 8DAE86855CCB58D3	FASTA	925	100,146
	10 20 30 40 50 60 MNAPERQPQP DGGDAPGHEP GGSPQDELDF SILFDYEYLN PNEEEPNAHK VASPPSGPAY 70 80 90 100 110 120 PDDVLDYGLK PYSPLASLSG EPPGRFGEPD RVGPQKFLSA AKPAGASGLS PRIEITPSHE 130 140 150 160 170 180 LIQAVGPLRM RDAGLLVEQP PLAGVAASPR FTLPVPGFEG YREPLCLSPA SSGSSASFIS 190 200 210 220 230 240 DTFSPYTSPC VSPNNGGPDD LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR 250 260 270 280 290 300 PASRSSSPGA KRRHSCAEAL VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS 310 320 330 340 350 360 AVIMDALNSL ATDSPCGIPP KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE FLGPCEQGER 370 380 390 400 410 420 RNSAPESILL VPPTWPKPLV PAIPICSIPV TASLPPLEWP LSSQSGSYEL RIEVQPKPHH 430 440 450 460 470 480 RAHYETEGSR GAVKAPTGGH PVVQLHGYME NKPLGLQIFI GTADERILKP HAFYQVHRIT 490 500 510 520 530 540 GKTVTTTSYE KIVGNTKVLE IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT 550 560 570 580 590 600 RVRLVFRVHI PESSGRIVSL QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG 610 620 630 640 650 660 QNFTSESKVV FTEKTTDGQQ IWEMEATVDK DKSQPNMLFV EIPEYRNKHI RTPVKVNFYV 670 680 690 700 710 720 INGKRKRSQP QHFTYHPVPA IKTEPTDEYD PTLICSPTHG GLGSQPYYPQ HPMVAESPSC 730 740 750 760 770 780 LVATMAPCQQ FRTGLSSPDA RYQQQNPAAV LYQRSKSLSP SLLGYQQPAL MAAPLSLADA 790 800 810 820 830 840 HRSVLVHAGS QGQSSALLHP SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG 850 860 870 880 890 900 TTRPGPPPVS QGQRLSPGSY PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL 910 920 DQTYLDDVNE IIRKEFSGPP ARNQT
	Isoform 2 (B) [UniParc]. Checksum: 71C45C9B348AE9C8	FASTA	921	99,784
	10 20 30 40 50 60 MNAPERQPQP DGGDAPGHEP GGSPQDELDF SILFDYEYLN PNEEEPNAHK VASPPSGPAY 70 80 90 100 110 120 PDDVLDYGLK PYSPLASLSG EPPGRFGEPD RVGPQKFLSA AKPAGASGLS PRIEITPSHE 130 140 150 160 170 180 LIQAVGPLRM RDAGLLVEQP PLAGVAASPR FTLPVPGFEG YREPLCLSPA SSGSSASFIS 190 200 210 220 230 240 DTFSPYTSPC VSPNNGGPDD LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR 250 260 270 280 290 300 PASRSSSPGA KRRHSCAEAL VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS 310 320 330 340 350 360 AVIMDALNSL ATDSPCGIPP KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE FLGPCEQGER 370 380 390 400 410 420 RNSAPESILL VPPTWPKPLV PAIPICSIPV TASLPPLEWP LSSQSGSYEL RIEVQPKPHH 430 440 450 460 470 480 RAHYETEGSR GAVKAPTGGH PVVQLHGYME NKPLGLQIFI GTADERILKP HAFYQVHRIT 490 500 510 520 530 540 GKTVTTTSYE KIVGNTKVLE IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT 550 560 570 580 590 600 RVRLVFRVHI PESSGRIVSL QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG 610 620 630 640 650 660 QNFTSESKVV FTEKTTDGQQ IWEMEATVDK DKSQPNMLFV EIPEYRNKHI RTPVKVNFYV 670 680 690 700 710 720 INGKRKRSQP QHFTYHPVPA IKTEPTDEYD PTLICSPTHG GLGSQPYYPQ HPMVAESPSC 730 740 750 760 770 780 LVATMAPCQQ FRTGLSSPDA RYQQQNPAAV LYQRSKSLSP SLLGYQQPAL MAAPLSLADA 790 800 810 820 830 840 HRSVLVHAGS QGQSSALLHP SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG 850 860 870 880 890 900 TTRPGPPPVS QGQRLSPGSY PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL 910 920 DQTYLDDELI DTHLSWIQNI L
	Isoform 3 (NFATc2_IA_IIL) [UniParc]. Checksum: 158B2F7F9966CCBA	FASTA	901	97,693
	10 20 30 40 50 60 MQREAAFRLG HCHPLRIMGS VDQEEPNAHK VASPPSGPAY PDDVLDYGLK PYSPLASLSG 70 80 90 100 110 120 EPPGRFGEPD RVGPQKFLSA AKPAGASGLS PRIEITPSHE LIQAVGPLRM RDAGLLVEQP 130 140 150 160 170 180 PLAGVAASPR FTLPVPGFEG YREPLCLSPA SSGSSASFIS DTFSPYTSPC VSPNNGGPDD 190 200 210 220 230 240 LCPQFQNIPA HYSPRTSPIM SPRTSLAEDS CLGRHSPVPR PASRSSSPGA KRRHSCAEAL 250 260 270 280 290 300 VALPPGASPQ RSRSPSPQPS SHVAPQDHGS PAGYPPVAGS AVIMDALNSL ATDSPCGIPP 310 320 330 340 350 360 KMWKTSPDPS PVSAAPSKAG LPRHIYPAVE FLGPCEQGER RNSAPESILL VPPTWPKPLV 370 380 390 400 410 420 PAIPICSIPV TASLPPLEWP LSSQSGSYEL RIEVQPKPHH RAHYETEGSR GAVKAPTGGH 430 440 450 460 470 480 PVVQLHGYME NKPLGLQIFI GTADERILKP HAFYQVHRIT GKTVTTTSYE KIVGNTKVLE 490 500 510 520 530 540 IPLEPKNNMR ATIDCAGILK LRNADIELRK GETDIGRKNT RVRLVFRVHI PESSGRIVSL 550 560 570 580 590 600 QTASNPIECS QRSAHELPMV ERQDTDSCLV YGGQQMILTG QNFTSESKVV FTEKTTDGQQ 610 620 630 640 650 660 IWEMEATVDK DKSQPNMLFV EIPEYRNKHI RTPVKVNFYV INGKRKRSQP QHFTYHPVPA 670 680 690 700 710 720 IKTEPTDEYD PTLICSPTHG GLGSQPYYPQ HPMVAESPSC LVATMAPCQQ FRTGLSSPDA 730 740 750 760 770 780 RYQQQNPAAV LYQRSKSLSP SLLGYQQPAL MAAPLSLADA HRSVLVHAGS QGQSSALLHP 790 800 810 820 830 840 SPTNQQASPV IHYSPTNQQL RCGSHQEFQH IMYCENFAPG TTRPGPPPVS QGQRLSPGSY 850 860 870 880 890 900 PTVIQQQNAT SQRAAKNGPP VSDQKEVLPA GVTIKQEQNL DQTYLDDELI DTHLSWIQNI L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Recombinant NFAT1 (NFATp) is regulated by calcineurin in T cells and mediates transcription of several cytokine genes." Luo C., Burgeon E., Carew J.A., McCaffrey P.G., Badalian T.M., Lane W.S., Hogan P.G., Rao A. Mol. Cell. Biol. 16:3955-3966(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[2]	"Alternative splicing and expression of human and mouse NFAT genes." Vihma H., Pruunsild P., Timmusk T. Genomics 92:279-291(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 2).
[6]	"Generic signals and specific outcomes: signaling through Ca2+, calcineurin, and NF-AT." Crabtree G.R. Cell 96:611-614(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[7]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[9]	"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-148; SER-330; SER-755; SER-759 AND SER-859, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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-757 AND SER-759, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"NFAT promotes carcinoma invasive migration through glypican-6." Yiu G.K., Kaunisto A., Chin Y.R., Toker A. Biochem. J. 440:157-166(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U43341 mRNA. Translation: AAC50886.1.
U43342 mRNA. Translation: AAC50887.1.
EU887573 mRNA. Translation: ACG55593.1.
EU887574 mRNA. Translation: ACG55594.1.
AL132866 Genomic DNA. Translation: CAC00528.2.
AL035682, AL035684, AL132866 Genomic DNA. Translation: CAI18852.1.
AL035682, AL035684, AL132866 Genomic DNA. Translation: CAI18853.1.
AL035684, AL035682, AL132866 Genomic DNA. Translation: CAI19205.1.
AL035684, AL035682, AL132866 Genomic DNA. Translation: CAI19206.1.
AL132866, AL035682, AL035684 Genomic DNA. Translation: CAI23549.1.
CH471077 Genomic DNA. Translation: EAW75602.1.
BC144074 mRNA. Translation: AAI44075.1.

IPI

IPI00247309.
IPI00297845.

PIR

G02326.

RefSeq

NP_001129493.1. NM_001136021.2.
NP_036472.2. NM_012340.4.
NP_775114.1. NM_173091.3.

UniGene

Hs.599855.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A02	X-ray	2.70	N	396-678	[»]
1OWR	X-ray	3.00	M/N/P/Q	396-678	[»]
1P7H	X-ray	2.60	L/M/N/O	396-678	[»]
1PZU	X-ray	3.10	B/D/H/I/L/M	396-678	[»]
1S9K	X-ray	3.10	C	399-678	[»]
2AS5	X-ray	2.70	M/N	392-678	[»]
2O93	X-ray	3.05	L/M/O	396-678	[»]
3QRF	X-ray	2.80	M/N	396-678	[»]

ProteinModelPortal

Q13469.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27630N.

IntAct

Q13469. 10 interactions.

MINT

MINT-1398456.

STRING

9606.ENSP00000379330.

PTM databases

PhosphoSite

Q13469.

Polymorphism databases

DMDM

68846905.

Proteomic databases

PaxDb

Q13469.

PRIDE

Q13469.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000371564; ENSP00000360619; ENSG00000101096.
ENST00000396009; ENSP00000379330; ENSG00000101096.
ENST00000414705; ENSP00000396471; ENSG00000101096.

GeneID

4773.

KEGG

hsa:4773.

UCSC

uc002xwd.3. human.

Organism-specific databases

CTD

4773.

GeneCards

GC20M050003.

HGNC

HGNC:7776. NFATC2.

HPA

CAB018567.
HPA008789.
HPA024369.

MIM

600490. gene.

neXtProt

NX_Q13469.

PharmGKB

PA31583.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG84065.

HOGENOM

HOG000231780.

HOVERGEN

HBG069754.

InParanoid

Q13469.

KO

K04446.

OMA

FEGYREP.

PhylomeDB

Q13469.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_118664. Calcineurin Dephosphorylates NFATC1/2/3.

Gene expression databases

ArrayExpress

Q13469.

Bgee

Q13469.

CleanEx

HS_NFATC2.

Genevestigator

Q13469.

GermOnline

ENSG00000101096. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
2.60.40.340. 1 hit.

InterPro

IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
IPR008366. NFAT.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]

PANTHER

PTHR12533. PTHR12533. 1 hit.

Pfam

PF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]

PRINTS

PR01789. NUCFACTORATC.

SMART

SM00429. IPT. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.

PROSITE

PS01204. REL_1. False negative.
PS50254. REL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13469.

ChEMBL

CHEMBL4120.

EvolutionaryTrace

Q13469.

GenomeRNAi

4773.

NextBio

18400.

SOURCE

Search...

Entry information

Entry name

NFAC2_HUMAN

Accession

Primary (citable) accession number: Q13469
Secondary accession number(s): B5B2N8 , B5B2N9, Q13468, Q5TFW7, Q5TFW8, Q9NPX6, Q9NQH3, Q9UJR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.