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Protein

Filaggrin-2

Gene

Flg2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi62 – 7312PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Filaggrin-2
Short name:
FLG-2
Alternative name(s):
Intermediate filament-associated protein
Gene namesi
Name:Flg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:3645678. Flg2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmic granule By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23622362Filaggrin-2PRO_0000331455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1198 – 11981PhosphoserineCombined sources
Modified residuei1204 – 12041PhosphoserineCombined sources
Modified residuei1205 – 12051PhosphoserineCombined sources
Modified residuei1278 – 12781PhosphoserineCombined sources
Modified residuei1284 – 12841PhosphoserineCombined sources
Modified residuei1285 – 12851PhosphoserineCombined sources
Modified residuei1356 – 13561PhosphoserineCombined sources
Modified residuei1362 – 13621PhosphoserineCombined sources
Modified residuei1363 – 13631PhosphoserineCombined sources
Modified residuei1438 – 14381PhosphoserineCombined sources
Modified residuei1439 – 14391PhosphoserineCombined sources
Modified residuei1510 – 15101PhosphoserineCombined sources
Modified residuei1516 – 15161PhosphoserineCombined sources
Modified residuei1517 – 15171PhosphoserineCombined sources
Modified residuei1590 – 15901PhosphoserineCombined sources
Modified residuei1596 – 15961PhosphoserineCombined sources
Modified residuei1597 – 15971PhosphoserineCombined sources
Modified residuei1744 – 17441PhosphoserineCombined sources
Modified residuei1750 – 17501PhosphoserineCombined sources
Modified residuei1751 – 17511PhosphoserineCombined sources
Modified residuei1824 – 18241PhosphoserineCombined sources
Modified residuei1830 – 18301PhosphoserineCombined sources
Modified residuei1831 – 18311PhosphoserineCombined sources
Modified residuei1902 – 19021PhosphoserineCombined sources
Modified residuei1908 – 19081PhosphoserineCombined sources
Modified residuei1909 – 19091PhosphoserineCombined sources
Modified residuei1980 – 19801PhosphoserineCombined sources
Modified residuei1986 – 19861PhosphoserineCombined sources
Modified residuei1987 – 19871PhosphoserineCombined sources
Modified residuei2104 – 21041PhosphoserineCombined sources

Post-translational modificationi

Deiminated by PADI1, PADI2 or PADI3 in vitro. The deiminated form is degraded by calpain-1/CAPN1 more quickly and into shorter peptides than the intact protein.By similarity
May be processed by calpain-1/CAPN1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2VIS4.
PRIDEiQ2VIS4.

PTM databases

iPTMnetiQ2VIS4.
PhosphoSiteiQ2VIS4.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096482.

Structurei

3D structure databases

ProteinModelPortaliQ2VIS4.
SMRiQ2VIS4. Positions 4-84.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini49 – 8436EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Repeati261 – 30848Filaggrin 1Add
BLAST
Repeati373 – 41442Filaggrin 2Add
BLAST
Repeati555 – 60753Filaggrin 3Add
BLAST
Repeati672 – 72352Filaggrin 4Add
BLAST
Repeati880 – 92748Filaggrin 5Add
BLAST
Repeati984 – 103552Filaggrin 6Add
BLAST
Repeati1165 – 121046Filaggrin 7Add
BLAST
Repeati1280 – 133455Filaggrin 8Add
BLAST
Repeati1474 – 152249Filaggrin 9Add
BLAST
Repeati1723 – 175634Filaggrin 10Add
BLAST
Repeati2016 – 207055Filaggrin 11Add
BLAST
Repeati2218 – 225942Filaggrin 12Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8181S-100-likeBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi110 – 12011Poly-GluAdd
BLAST
Compositional biasi265 – 911647Ser-richAdd
BLAST
Compositional biasi994 – 1970977Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the S100-fused protein family.Curated
In the N-terminal section; belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 12 filaggrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IX7U. Eukaryota.
ENOG410ZH9F. LUCA.
HOGENOMiHOG000112590.
InParanoidiQ2VIS4.
KOiK10384.
PhylomeDBiQ2VIS4.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2VIS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYLLRSVVT IIDVFYKYTK QDEECGTLSK DELKELLEKE FRPILKNPDD
60 70 80 90 100
PDTVDVIMHM LDRDHDRRLD FTEFILMIFK LALACNKVLG KEYCKASGSK
110 120 130 140 150
KHRRGHQHQE EESETEEEEE TPRQKSGFRF SSWSEGEEHG HSSGGSRGPA
160 170 180 190 200
KHRRGSNSKR LERQDELSSS EESRKKHHGS IFGHSWSSNK EKDGSRSEEL
210 220 230 240 250
GEKGDKSYDS PSRESEEEYE SGYRLNHQGR EGHSGLSCGL EKNKYELNYI
260 270 280 290 300
QLRKGGEQKL GYNTSSSGNS KIQSHVYGFS NSSGCCRPKN ASSSCQASRS
310 320 330 340 350
QGQGNQSCRT QSNCQSGTSG GQGYGCVSEG QSSRCCQPKP RSCSQSSSQR
360 370 380 390 400
GYGSKQCGQP QNCGRQQRMG SSHSSCCGPY GSGATQSSGC GQQRMSSCGH
410 420 430 440 450
SSSSHQKGCS SNGFSKGDQR ASGSGHSSCC EQHGTNSSQS SGFKQHGHES
460 470 480 490 500
GQSCCGQHGT ASSQSSGYSQ HRVGSGQSCH YGQHGSSSGQ SSSSGRHGSG
510 520 530 540 550
SGQSSSSRHN RSGSSQSSGL EEHGSSSHQS HSSGHHGSGS RQSSGSEQHG
560 570 580 590 600
AVSGQSSGSG KHETGPSQSS SSGHHGSGSQ QHGGGSGQST GFGEHESSSG
610 620 630 640 650
HSSSSGQHRS GSRHSSGSGK HESGRSQSSG SGHHGSGSQQ HGGGSGNSTG
660 670 680 690 700
FGEHGSSSHP LPSSGQNESS SGQSSRSERH GTGSGQSSGF GQHGSGSHQS
710 720 730 740 750
SSSGHNEYGS GQTSSSWPHG KGSGQESGYG EQESGHGQSS SSWQHGTGPG
760 770 780 790 800
QSSSSEEEES RPGQSSSSWQ HGKGSGQESG YGEQEAGHGQ SSSSWQHGTG
810 820 830 840 850
AGNQSSGYGE HKSGPSHSSR SWHHGTGSGQ SLGFGQHGKG SHQSESSGHY
860 870 880 890 900
ESVSEPSSSS WQHGNGSGES YGYGEHESGH GQSSSAWNHG NESGQSNGYG
910 920 930 940 950
EHESGHGQSS SAWNHGNESG QSNGFGENES GRDQEGYQQR ESFHGQHRHP
960 970 980 990 1000
LSQHEQHSQF GYGRSPRSPV HPESSEGEEH SVVPRRYSGY GHGQGQAGHQ
1010 1020 1030 1040 1050
QRESGYGQRG RPQGPSQDSS RQPQAGHGQP SQSGYGRSPR RSQVHPEYSE
1060 1070 1080 1090 1100
GEAHSEVSQR HSGSSHCHCH CHGQARHQQR ESVHGQRGRP QGPSQDSSRH
1110 1120 1130 1140 1150
PQAGPGQPSQ SGSRRSPRSQ PVHPESSEGE EHSVVPQRHS GSGHGHGQGQ
1160 1170 1180 1190 1200
GQAGHQQRES VHGQQGRPQG PSQDSSRQPQ AGQGQPSQSG SGRSPRRSPV
1210 1220 1230 1240 1250
HPESSEGEEH SVVPQRHSGS GHGHGQGQGQ GQAGHQQRES VHGQRSRPQG
1260 1270 1280 1290 1300
PFQDSSRQPQ AGQGQPSQSG SGRSPRRSPV HPESSEGEEH SVVPQRHSGS
1310 1320 1330 1340 1350
GHGHGQGQGQ AGHQQRESVH GQPVRPEVPT QDSSRQPQAG QGQPSQSGSG
1360 1370 1380 1390 1400
RSPRRSPVHP ESSEGEEHSV VPQRNSESCH CHCHDQAGHQ QRESVHGQRG
1410 1420 1430 1440 1450
RPQGPSQDSS RHPQAGPGQP SQSGSRRSPR SSPVHPESSE GEEHSVVPQR
1460 1470 1480 1490 1500
HSGSGHGHGQ GQGQAGHQQR ESVHGQRGRP QGPTQDSSRQ PQAGQGQPSQ
1510 1520 1530 1540 1550
SGSGRSPRRS PVHPESSEGE EHSVVPQRHS GSGHGHGHGQ GQGQAGHQQR
1560 1570 1580 1590 1600
ESVHGQRGRP QGPSQDSSRQ PQAGQGQPSQ SGSGRSPRRS PVHPESSEGE
1610 1620 1630 1640 1650
EHSVVPQRYS GSGHGHGQGQ AGHQQRESVH GQRGRPQGPS QDSSRQPQAG
1660 1670 1680 1690 1700
QGQPSQSGSG RSPRRSPVHP ESSEGEEHSV IPQRHSGSGH SHGQGQVHAE
1710 1720 1730 1740 1750
HQQRESVHGQ RGRPQGPSQD SSRQPQAGQG QPSLSGSGRS PRRSPVHPES
1760 1770 1780 1790 1800
SEGEEHSVVP QRHSHSESGH GHGQGQGQAG HQQRESVHGQ RGRPQGPSQD
1810 1820 1830 1840 1850
SSRQPQAGQG QPSQSGSGRS PGRSPVHPES SEGEEHSVVP QRHSESGHGH
1860 1870 1880 1890 1900
GQGQGQAGHQ QRESVHGQRG RPQGPSQDSS RQPQAGQGQP SQSGSGRSPR
1910 1920 1930 1940 1950
RSPVHPESSE GEEHSVVPQR HSGSGHGHGQ GQGQAGHQQR ESVHGQPVRP
1960 1970 1980 1990 2000
QGPSQDSSSQ PQASQGQPSQ SGSGRSPRRS PVHPESSEGE EHSVVPQRHS
2010 2020 2030 2040 2050
GSGHGHGQGQ GQAGHQQRES LHGQRGRSQS PFHPSHSIHW QSKCTISKKS
2060 2070 2080 2090 2100
SRLSGHYGRN HFQSTISGNQ YDSSQSSRHG SYGPQDYDYG QSGYGPSGRL
2110 2120 2130 2140 2150
RSNSQSSIPF SSAHRATNME VLPCGQSFSP SDHVGTKANE QIGELVFKYR
2160 2170 2180 2190 2200
ESETGPDQSV DYYNLTESNS TTRGHECSHG HSVVVPEHSD DSDFNYGHSY
2210 2220 2230 2240 2250
NGKQQICQSQ PTVQSCFDDS QYILFQKHLE SPSFGNQSGF SPNERQLYTC
2260 2270 2280 2290 2300
NESIDSYHLS SDSNNRNQIY SSNNSFPNLY CIGTEQCIYL PSATILGEGT
2310 2320 2330 2340 2350
EGQEPGYTQP GTICKYNQFL DGRKSRTRGN HETGKMKSGS AYLDSNTPLY
2360
TYVQEQKSYY FE
Length:2,362
Mass (Da):251,372
Last modified:April 29, 2008 - v2
Checksum:iF3FB473737052808
GO

Sequence cautioni

The sequence BAC29615.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2118 – 21181N → H in AAZ99028 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ118292 Genomic DNA. Translation: AAZ99028.1.
AK036878 mRNA. Translation: BAC29615.1. Different initiation.
RefSeqiNP_001013826.1. NM_001013804.1.
UniGeneiMm.10755.

Genome annotation databases

GeneIDi229574.
KEGGimmu:229574.
UCSCiuc029unl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ118292 Genomic DNA. Translation: AAZ99028.1.
AK036878 mRNA. Translation: BAC29615.1. Different initiation.
RefSeqiNP_001013826.1. NM_001013804.1.
UniGeneiMm.10755.

3D structure databases

ProteinModelPortaliQ2VIS4.
SMRiQ2VIS4. Positions 4-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096482.

PTM databases

iPTMnetiQ2VIS4.
PhosphoSiteiQ2VIS4.

Proteomic databases

PaxDbiQ2VIS4.
PRIDEiQ2VIS4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi229574.
KEGGimmu:229574.
UCSCiuc029unl.1. mouse.

Organism-specific databases

CTDi388698.
MGIiMGI:3645678. Flg2.

Phylogenomic databases

eggNOGiENOG410IX7U. Eukaryota.
ENOG410ZH9F. LUCA.
HOGENOMiHOG000112590.
InParanoidiQ2VIS4.
KOiK10384.
PhylomeDBiQ2VIS4.

Miscellaneous databases

NextBioi379521.
PROiQ2VIS4.
SOURCEiSearch...

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FLG-2, a novel repetitive protein that is abundantly expressed in mammalian epidermis and functionally related to filaggrin."
    Listwan P., Rothnagel J.A.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  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] OF 2047-2362.
    Strain: C57BL/6J.
    Tissue: Vagina.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198; SER-1204; SER-1205; SER-1278; SER-1284; SER-1285; SER-1356; SER-1362; SER-1363; SER-1438; SER-1439; SER-1510; SER-1516; SER-1517; SER-1590; SER-1596; SER-1597; SER-1744; SER-1750; SER-1751; SER-1824; SER-1830; SER-1831; SER-1902; SER-1908; SER-1909; SER-1980; SER-1986; SER-1987 AND SER-2104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue.

Entry informationi

Entry nameiFILA2_MOUSE
AccessioniPrimary (citable) accession number: Q2VIS4
Secondary accession number(s): Q8CB36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 11, 2016
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.