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Q13045 (FLII_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein flightless-1 homolog
Gene names
Name:FLII
Synonyms:FLIL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1269 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development By similarity. May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation. Ref.10

Subunit structure

Interacts with actin, ACTL6A, NCOA2, CARM1 and MYD88. Interacts with LRRFIP1 and LRRFIP2. Upon LPS stimulation, LRRFIP2 competes for MYD88-binding. LRRFIP1 constitutively blocks the interaction with MyD88, even in the absence of LPS. Interacts with the nuclear receptors ESR1 and THRB. Interacts with SGK3. Ref.7 Ref.8 Ref.9 Ref.10 Ref.16 Ref.17

Subcellular location

Nucleus By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cell junctionfocal adhesion By similarity. Note: Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes By similarity.

Tissue specificity

Strongest expression in skeletal muscle with high expression also in the heart and lung. Ref.7

Sequence similarities

Contains 5 gelsolin-like repeats.

Contains 15 LRR (leucine-rich) repeats.

Sequence caution

The sequence BAG58522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRRFIP1Q32MZ42EBI-351549,EBI-1369100

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13045-1)

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: Q13045-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-191: Missing.
     416-416: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q13045-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEATGVLPFVRGVDLSGNDFK → MDLRGLRPVP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12691269Protein flightless-1 homolog
PRO_0000218750

Regions

Repeat7 – 3226LRR 1
Repeat33 – 5523LRR 2
Repeat56 – 7823LRR 3
Repeat80 – 10324LRR 4
Repeat104 – 12623LRR 5
Repeat127 – 14923LRR 6
Repeat150 – 17324LRR 7
Repeat175 – 19622LRR 8
Repeat197 – 22226LRR 9
Repeat223 – 24523LRR 10
Repeat247 – 26822LRR 11
Repeat269 – 29123LRR 12
Repeat293 – 31624LRR 13
Repeat318 – 33922LRR 14
Repeat340 – 36324LRR 15
Repeat501 – 55959Gelsolin-like 1
Repeat640 – 67031Gelsolin-like 2
Repeat755 – 79844Gelsolin-like 3
Repeat1068 – 111548Gelsolin-like 4
Repeat1176 – 121843Gelsolin-like 5
Region1 – 427427Interaction with LRRFIP1 and LRRFIP2
Region495 – 827333Interaction with ACTL6A
Compositional bias411 – 4155Poly-Ala
Compositional bias892 – 97887Glu-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.23 Ref.24
Modified residue211N6-acetyllysine Ref.19
Modified residue4061Phosphoserine Ref.12 Ref.20
Modified residue4361Phosphoserine; by SGK3 Ref.16 Ref.20 Ref.22
Modified residue8181Phosphothreonine; by SGK3 Ref.16
Modified residue8561Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.20 Ref.22

Natural variations

Alternative sequence1 – 2121MEATG…GNDFK → MDLRGLRPVP in isoform 3.
VSP_046887
Alternative sequence138 – 19154Missing in isoform 2.
VSP_044686
Alternative sequence4161Missing in isoform 2.
VSP_044687
Natural variant12431R → H.
Corresponds to variant rs8821 [ dbSNP | Ensembl ].
VAR_029258

Experimental info

Mutagenesis5861E → K: No change in ESR1 binding but reduced binding to ACTL6A and reduced coactivator function. Ref.10
Mutagenesis6031G → S: No change in binding to ACTL6A or in coactivator function. Ref.10
Sequence conflict11M → V in BAG58522. Ref.2
Sequence conflict2981Y → N in BAG58522. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 29AC7C07738B7B47

FASTA1,269144,751
        10         20         30         40         50         60 
MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE ELAALQKLEH 

        70         80         90        100        110        120 
LSVSHNNLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI FKLDDLSVLD LSHNQLTECP 

       130        140        150        160        170        180 
RELENAKNML VLNLSHNSID TIPNQLFINL TDLLYLDLSE NRLESLPPQM RRLVHLQTLV 

       190        200        210        220        230        240 
LNGNPLLHAQ LRQLPAMTAL QTLHLRSTQR TQSNLPTSLE GLSNLADVDL SCNDLTRVPE 

       250        260        270        280        290        300 
CLYTLPSLRR LNLSSNQITE LSLCIDQWVH VETLNLSRNQ LTSLPSAICK LSKLKKLYLN 

       310        320        330        340        350        360 
SNKLDFDGLP SGIGKLTNLE EFMAANNNLE LVPESLCRCP KLRKLVLNKN HLVTLPEAIH 

       370        380        390        400        410        420 
FLTEIEVLDV RENPNLVMPP KPADRAAEWY NIDFSLQNQL RLAGASPATV AAAAAAGSGP 

       430        440        450        460        470        480 
KDPMARKMRL RRRKDSAQDD QAKQVLKGMS DVAQEKNKKQ EESADARAPS GKVRRWDQGL 

       490        500        510        520        530        540 
EKPRLDYSEF FTEDVGQLPG LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS 

       550        560        570        580        590        600 
LNWEIYYWIG GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY 

       610        620        630        640        650        660 
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGT SLDPRFVFLL DRGLDIYVWR 

       670        680        690        700        710        720 
GAQATLSSTT KARLFAEKIN KNERKGKAEI TLLVQGQELP EFWEALGGEP SEIKKHVPED 

       730        740        750        760        770        780 
FWPPQPKLYK VGLGLGYLEL PQINYKLSVE HKQRPKVELM PRMRLLQSLL DTRCVYILDC 

       790        800        810        820        830        840 
WSDVFIWLGR KSPRLVRAAA LKLGQELCGM LHRPRHATVS RSLEGTEAQV FKAKFKNWDD 

       850        860        870        880        890        900 
VLTVDYTRNA EAVLQSPGLS GKVKRDAEKK DQMKADLTAL FLPRQPPMSL AEAEQLMEEW 

       910        920        930        940        950        960 
NEDLDGMEGF VLEGKKFARL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE KKEDKEEKAE 

       970        980        990       1000       1010       1020 
GKEGEEATAE AEEKQPEEDF QCIVYFWQGR EASNMGWLTF TFSLQKKFES LFPGKLEVVR 

      1030       1040       1050       1060       1070       1080 
MTQQQENPKF LSHFKRKFII HRGKRKAVQG AQQPSLYQIR TNGSALCTRC IQINTDSSLL 

      1090       1100       1110       1120       1130       1140 
NSEFCFILKV PFESEDNQGI VYAWVGRASD PDEAKLAEDI LNTMFDTSYS KQVINEGEEP 

      1150       1160       1170       1180       1190       1200 
ENFFWVGIGA QKPYDDDAEY MKHTRLFRCS NEKGYFAVTE KCSDFCQDDL ADDDIMLLDN 

      1210       1220       1230       1240       1250       1260 
GQEVYMWVGT QTSQVEIKLS LKACQVYIQH MRSKEHERPR RLRLVRKGNE QHAFTRCFHA 


WSAFCKALA 

« Hide

Isoform 2 [UniParc].

Checksum: C0ACCF1BB28C366C
Show »

FASTA1,214138,493
Isoform 3 [UniParc].

Checksum: 8D087C091CFAD08B
Show »

FASTA1,258143,652

References

« Hide 'large scale' references
[1]"Genomic structure, evolution, and expression of human FLII, a gelsolin and leucine-rich-repeat family member: overlap with LLGL."
Campbell H.D., Fountain S., Young I.G., Claudianos C., Hoheisel J.D., Chen K.-S., Lupski J.R.
Genomics 42:46-54(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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: Hippocampus.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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).
Tissue: Kidney.
[5]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11, ACETYLATION AT MET-1.
Tissue: Platelet.
[6]"The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans."
Campbell H.D., Schimansky T., Claudianos C., Ozsarac N., Kasprzak A.B., Cotsell J.N., Young I.G., de Couet H.G., Miklos G.L.G.
Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-1269 (ISOFORM 1).
Tissue: Hippocampus.
[7]"Identification of the binding partners for flightless I, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies."
Liu Y.-T., Yin H.L.
J. Biol. Chem. 273:7920-7927(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTIN AND LRRFIP1, TISSUE SPECIFICITY.
[8]"TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I."
Wilson S.A., Brown E.C., Kingsman A.J., Kingsman S.M.
Nucleic Acids Res. 26:3460-3467(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRRFIP1.
[9]"Novel proteins interacting with the leucine-rich repeat domain of human flightless-I identified by the yeast two-hybrid system."
Fong K.S.K., de Couet H.G.
Genomics 58:146-157(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRRFIP1 AND LRRFIP2.
Tissue: Skeletal muscle.
[10]"Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity."
Lee Y.-H., Campbell H.D., Stallcup M.R.
Mol. Cell. Biol. 24:2103-2117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CARM1; ESR1; THRB; NCOA2 AND ACTL6A, MUTAGENESIS OF GLU-586 AND GLY-603.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"Identification of Flightless-I as a substrate of the cytokine-independent survival kinase CISK."
Xu J., Liao L., Qin J., Xu J., Liu D., Songyang Z.
J. Biol. Chem. 284:14377-14385(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-436 AND THR-818, INTERACTION WITH SGK3.
[17]"Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins."
Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.
J. Immunol. 182:3450-3460(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRRFIP1; LRRFIP2 AND MYD88.
[18]"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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-406; SER-436 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80184 Genomic DNA. Translation: AAC02796.1.
AK295655 mRNA. Translation: BAG58522.1. Different initiation.
AC127537 Genomic DNA. No translation available.
BC025300 mRNA. Translation: AAH25300.1.
U01184 mRNA. Translation: AAC03568.1.
CCDSCCDS11192.1. [Q13045-1]
CCDS58521.1. [Q13045-3]
CCDS58522.1. [Q13045-2]
PIRA49674.
RefSeqNP_001243193.1. NM_001256264.1. [Q13045-3]
NP_001243194.1. NM_001256265.1. [Q13045-2]
NP_002009.1. NM_002018.3. [Q13045-1]
UniGeneHs.513984.

3D structure databases

ProteinModelPortalQ13045.
SMRQ13045. Positions 2-415, 485-1264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108603. 30 interactions.
IntActQ13045. 7 interactions.
MINTMINT-1399971.
STRING9606.ENSP00000324573.

PTM databases

PhosphoSiteQ13045.

Polymorphism databases

DMDM18202493.

Proteomic databases

MaxQBQ13045.
PaxDbQ13045.
PeptideAtlasQ13045.
PRIDEQ13045.

Protocols and materials databases

DNASU2314.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327031; ENSP00000324573; ENSG00000177731. [Q13045-1]
ENST00000545457; ENSP00000438536; ENSG00000177731. [Q13045-2]
ENST00000579294; ENSP00000463534; ENSG00000177731. [Q13045-3]
GeneID2314.
KEGGhsa:2314.
UCSCuc002gsq.2. human. [Q13045-1]

Organism-specific databases

CTD2314.
GeneCardsGC17M018148.
HGNCHGNC:3750. FLII.
HPACAB016132.
HPA007084.
HPA008903.
MIM600362. gene.
neXtProtNX_Q13045.
Orphanet819. Smith-Magenis syndrome.
PharmGKBPA28171.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000016110.
HOVERGENHBG051627.
InParanoidQ13045.
OMAMEEWNED.
PhylomeDBQ13045.
TreeFamTF313468.

Gene expression databases

ArrayExpressQ13045.
BgeeQ13045.
CleanExHS_FLII.
GenevestigatorQ13045.

Family and domain databases

Gene3D3.40.20.10. 7 hits.
InterProIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERPTHR11977. PTHR11977. 1 hit.
PfamPF00626. Gelsolin. 4 hits.
PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 2 hits.
PF13855. LRR_8. 2 hits.
[Graphical view]
PRINTSPR00597. GELSOLIN.
SMARTSM00262. GEL. 6 hits.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFLII. human.
GeneWikiFLII.
GenomeRNAi2314.
NextBio35508702.
PROQ13045.
SOURCESearch...

Entry information

Entry nameFLII_HUMAN
AccessionPrimary (citable) accession number: Q13045
Secondary accession number(s): B4DIL0, F5H407, J3QLG3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM