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Protein

Fidgetin

Gene

FIGN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, that may lead to the suppression of microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei489 – 4891ATP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi529 – 5346ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fidgetin
Gene namesi
Name:FIGN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:13285. FIGN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi532 – 5321K → A: Inhibits the ability to sever and depolymerize microtubules. 1 Publication

Organism-specific databases

PharmGKBiPA28147.

Polymorphism and mutation databases

BioMutaiFIGN.
DMDMi115502199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759FidgetinPRO_0000250748Add
BLAST

Proteomic databases

PaxDbiQ5HY92.
PRIDEiQ5HY92.

PTM databases

iPTMnetiQ5HY92.
PhosphoSiteiQ5HY92.

Expressioni

Gene expression databases

BgeeiQ5HY92.
CleanExiHS_FIGN.
ExpressionAtlasiQ5HY92. baseline and differential.
GenevisibleiQ5HY92. HS.

Organism-specific databases

HPAiHPA034987.
HPA057919.

Interactioni

Subunit structurei

Interacts with AKAP8 (via C-terminus).By similarity

Protein-protein interaction databases

BioGridi120441. 3 interactions.
STRINGi9606.ENSP00000333836.

Structurei

3D structure databases

ProteinModelPortaliQ5HY92.
SMRiQ5HY92. Positions 404-757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi202 – 29190Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225145.
HOVERGENiHBG061204.
InParanoidiQ5HY92.
OMAiIVHASFL.
OrthoDBiEOG7R2BJ3.
PhylomeDBiQ5HY92.
TreeFamiTF105015.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5HY92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISSTSVYGL KMQWTPEHAQ WPEQHFDITS TTRSPAHKVE AYRGHLQRTY
60 70 80 90 100
QYAWANDDIS ALTASNLLKK YAEKYSGILE GPVDRPVLSN YSDTPSGLVN
110 120 130 140 150
GRKNESEPWQ PSLNSEAVYP MNCVPDVITA SKAGVSSALP PADVSASIGS
160 170 180 190 200
SPGVASNLTE PSYSSSTCGS HTVPSLHAGL PSQEYAPGYN GSYLHSTYSS
210 220 230 240 250
QPAPALPSPH PSPLHSSGLL QPPPPPPPPP ALVPGYNGTS NLSSYSYPSA
260 270 280 290 300
SYPPQTAVGS GYSPGGAPPP PSAYLPSGIP APTPLPPTTV PGYTYQGHGL
310 320 330 340 350
TPIAPSALTN SSASSLKRKA FYMAGQGDMD SSYGNYSYGQ QRSTQSPMYR
360 370 380 390 400
MPDNSISNTN RGNGFDRSAE TSSLAFKPTK QLMSSEQQRK FSSQSSRALT
410 420 430 440 450
PPSYSTAKNS LGSRSSESFG KYTSPVMSEH GDEHRQLLSH PMQGPGLRAA
460 470 480 490 500
TSSNHSVDEQ LKNTDTHLID LVTNEIITQG PPVDWNDIAG LDLVKAVIKE
510 520 530 540 550
EVLWPVLRSD AFSGLTALPR SILLFGPRGT GKTLLGRCIA SQLGATFFKI
560 570 580 590 600
AGSGLVAKWL GEAEKIIHAS FLVARCRQPS VIFVSDIDML LSSQVNEEHS
610 620 630 640 650
PVSRMRTEFL MQLDTVLTSA EDQIVVICAT SKPEEIDESL RRYFMKRLLI
660 670 680 690 700
PLPDSTARHQ IIVQLLSQHN YCLNDKEFAL LVQRTEGFSG LDVAHLCQEA
710 720 730 740 750
VVGPLHAMPA TDLSAIMPSQ LRPVTYQDFE NAFCKIQPSI SQKELDMYVE

WNKMFGCSQ
Length:759
Mass (Da):82,146
Last modified:October 3, 2006 - v2
Checksum:i68E1C4C8CA66AE2A
GO

Sequence cautioni

The sequence AAX81992.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA91590.1 differs from that shown. Reason: Frameshift at position 71. Curated
The sequence BAA91590.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15231.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti713 – 7131L → I in CAI45980 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961S → L.
Corresponds to variant rs2231902 [ dbSNP | Ensembl ].
VAR_027613
Natural varianti448 – 4481R → C.
Corresponds to variant rs2231904 [ dbSNP | Ensembl ].
VAR_027614
Natural varianti565 – 5651K → R.
Corresponds to variant rs2231905 [ dbSNP | Ensembl ].
VAR_027615

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001267 mRNA. Translation: BAA91590.1. Sequence problems.
AK025747 mRNA. Translation: BAB15231.1. Different initiation.
AK125324 mRNA. Translation: BAG54182.1.
BX649105 mRNA. Translation: CAI45980.1.
AC093727 Genomic DNA. Translation: AAX81992.1. Sequence problems.
CCDSiCCDS2221.2.
RefSeqiNP_060556.2. NM_018086.2.
UniGeneiHs.593650.

Genome annotation databases

EnsembliENST00000333129; ENSP00000333836; ENSG00000182263.
GeneIDi55137.
KEGGihsa:55137.
UCSCiuc002uck.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001267 mRNA. Translation: BAA91590.1. Sequence problems.
AK025747 mRNA. Translation: BAB15231.1. Different initiation.
AK125324 mRNA. Translation: BAG54182.1.
BX649105 mRNA. Translation: CAI45980.1.
AC093727 Genomic DNA. Translation: AAX81992.1. Sequence problems.
CCDSiCCDS2221.2.
RefSeqiNP_060556.2. NM_018086.2.
UniGeneiHs.593650.

3D structure databases

ProteinModelPortaliQ5HY92.
SMRiQ5HY92. Positions 404-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120441. 3 interactions.
STRINGi9606.ENSP00000333836.

PTM databases

iPTMnetiQ5HY92.
PhosphoSiteiQ5HY92.

Polymorphism and mutation databases

BioMutaiFIGN.
DMDMi115502199.

Proteomic databases

PaxDbiQ5HY92.
PRIDEiQ5HY92.

Protocols and materials databases

DNASUi55137.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333129; ENSP00000333836; ENSG00000182263.
GeneIDi55137.
KEGGihsa:55137.
UCSCiuc002uck.2. human.

Organism-specific databases

CTDi55137.
GeneCardsiFIGN.
HGNCiHGNC:13285. FIGN.
HPAiHPA034987.
HPA057919.
MIMi605295. gene.
neXtProtiNX_Q5HY92.
PharmGKBiPA28147.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225145.
HOVERGENiHBG061204.
InParanoidiQ5HY92.
OMAiIVHASFL.
OrthoDBiEOG7R2BJ3.
PhylomeDBiQ5HY92.
TreeFamiTF105015.

Miscellaneous databases

GenomeRNAii55137.
NextBioi58822.
PROiQ5HY92.
SOURCEiSearch...

Gene expression databases

BgeeiQ5HY92.
CleanExiHS_FIGN.
ExpressionAtlasiQ5HY92. baseline and differential.
GenevisibleiQ5HY92. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Salivary gland.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human Fidgetin is a microtubule severing the enzyme and minus-end depolymerase that regulates mitosis."
    Mukherjee S., Diaz Valencia J.D., Stewman S., Metz J., Monnier S., Rath U., Asenjo A.B., Charafeddine R.A., Sosa H.J., Ross J.L., Ma A., Sharp D.J.
    Cell Cycle 11:2359-2366(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-532.

Entry informationi

Entry nameiFIGN_HUMAN
AccessioniPrimary (citable) accession number: Q5HY92
Secondary accession number(s): B3KWM0, Q9H6M5, Q9NVZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: March 16, 2016
This is version 96 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.