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Protein

Fidgetin-like protein 1

Gene

FIGNL1

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

Functioni

Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei404 – 4041ATP; via amide nitrogen and carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi444 – 4496ATP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fidgetin-like protein 1 (EC:3.6.4.-)
Gene namesi
Name:FIGNL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:13286. FIGNL1.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) treatment.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi295 – 2951F → E: Reduces interaction with RAD51 and inhibits HR-mediated DNA repair. Strongly reduce, but does abolish, interaction with RAD51; when associated with E-340. 1 Publication
Mutagenesisi340 – 3401F → E: Reduces weakly interaction with RAD51. Strongly reduce, but does abolish, interaction with RAD51; when associated with E-295. 1 Publication
Mutagenesisi447 – 4471K → A: Inhibits HR-mediated DNA repair. 1 Publication
Mutagenesisi500 – 5001D → A: Inhibits HR-mediated DNA repair. 1 Publication

Organism-specific databases

PharmGKBiPA28148.

Polymorphism and mutation databases

BioMutaiFIGNL1.
DMDMi158563967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Fidgetin-like protein 1PRO_0000302723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei339 – 3391N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6PIW4.
MaxQBiQ6PIW4.
PaxDbiQ6PIW4.
PeptideAtlasiQ6PIW4.
PRIDEiQ6PIW4.

PTM databases

iPTMnetiQ6PIW4.
PhosphoSiteiQ6PIW4.

Expressioni

Gene expression databases

BgeeiQ6PIW4.
CleanExiHS_FIGNL1.
ExpressionAtlasiQ6PIW4. baseline and differential.
GenevisibleiQ6PIW4. HS.

Organism-specific databases

HPAiHPA055542.

Interactioni

Subunit structurei

Hexamer (By similarity). Interacts (via N-terminal one-half region) with RAD51; the interaction is direct. Interacts (via N-terminal one-half region) with SPIDR (via the C-terminal region); the interaction is direct.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1BP1O147133EBI-8468390,EBI-2127319

Protein-protein interaction databases

BioGridi122026. 30 interactions.
IntActiQ6PIW4. 10 interactions.
MINTiMINT-4908266.
STRINGi9606.ENSP00000349356.

Structurei

Secondary structure

1
674
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi381 – 39010Combined sources
Helixi400 – 4023Combined sources
Helixi407 – 41610Combined sources
Helixi418 – 4225Combined sources
Turni424 – 4263Combined sources
Helixi429 – 4313Combined sources
Beta strandi435 – 4428Combined sources
Helixi447 – 45711Combined sources
Beta strandi461 – 4666Combined sources
Helixi467 – 4704Combined sources
Helixi477 – 49115Combined sources
Beta strandi494 – 5007Combined sources
Helixi502 – 5054Combined sources
Helixi516 – 52914Combined sources
Beta strandi539 – 5468Combined sources
Helixi548 – 5503Combined sources
Helixi553 – 5564Combined sources
Beta strandi561 – 5644Combined sources
Helixi570 – 58213Combined sources
Helixi590 – 59910Combined sources
Turni600 – 6023Combined sources
Helixi605 – 61612Combined sources
Helixi618 – 6225Combined sources
Helixi633 – 6353Combined sources
Helixi641 – 65111Combined sources
Helixi652 – 6543Combined sources
Helixi660 – 67011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D8BX-ray2.00A/B341-674[»]
ProteinModelPortaliQ6PIW4.
SMRiQ6PIW4. Positions 343-674.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6PIW4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni295 – 34450Necessary and sufficient for interaction with RAD511 PublicationAdd
BLAST

Domaini

The N-terminus is necessary for its recruitment to DNA damage sites.

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225145.
HOVERGENiHBG061204.
InParanoidiQ6PIW4.
OMAiQILRIQY.
OrthoDBiEOG7GXPCR.
PhylomeDBiQ6PIW4.
TreeFamiTF105013.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PIW4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQTSSSRSVH LSEWQKNYFA ITSGICTGPK ADAYRAQILR IQYAWANSEI
60 70 80 90 100
SQVCATKLFK KYAEKYSAII DSDNVESGLN NYAENILTLA GSQQTDSDKW
110 120 130 140 150
QSGLSINNVF KMSSVQKMMQ AGKKFKDSLL EPALASVVIH KEATVFDLPK
160 170 180 190 200
FSVCGSSQES DSLPNSAHDR DRTQDFPESN RLKLLQNAQP PMVTNTARTC
210 220 230 240 250
PTFSAPVGES ATAKFHVTPL FGNVKKENHS SAKENIGLNV FLSNQSCFPA
260 270 280 290 300
ACENPQRKSF YGSGTIDALS NPILNKACSK TEDNGPKEDS SLPTFKTAKE
310 320 330 340 350
QLWVDQQKKY HQPQRASGSS YGGVKKSLGA SRSRGILGKF VPPIPKQDGG
360 370 380 390 400
EQNGGMQCKP YGAGPTEPAH PVDERLKNLE PKMIELIMNE IMDHGPPVNW
410 420 430 440 450
EDIAGVEFAK ATIKEIVVWP MLRPDIFTGL RGPPKGILLF GPPGTGKTLI
460 470 480 490 500
GKCIASQSGA TFFSISASSL TSKWVGEGEK MVRALFAVAR CQQPAVIFID
510 520 530 540 550
EIDSLLSQRG DGEHESSRRI KTEFLVQLDG ATTSSEDRIL VVGATNRPQE
560 570 580 590 600
IDEAARRRLV KRLYIPLPEA SARKQIVINL MSKEQCCLSE EEIEQIVQQS
610 620 630 640 650
DAFSGADMTQ LCREASLGPI RSLQTADIAT ITPDQVRPIA YIDFENAFRT
660 670
VRPSVSPKDL ELYENWNKTF GCGK
Length:674
Mass (Da):74,077
Last modified:September 11, 2007 - v2
Checksum:i2EB812B407495BF2
GO
Isoform 2 (identifier: Q6PIW4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.

Show »
Length:563
Mass (Da):61,686
Checksum:iDD30D9C1EEC2DEA3
GO

Sequence cautioni

The sequence BAB14567.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti614 – 6141E → G in BAB14426 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371V → M.1 Publication
Corresponds to variant rs10235371 [ dbSNP | Ensembl ].
VAR_034941
Natural varianti216 – 2161H → Y.
Corresponds to variant rs35929700 [ dbSNP | Ensembl ].
VAR_034942

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111Missing in isoform 2. 1 PublicationVSP_027937Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023142 mRNA. Translation: BAB14426.1.
AK023411 mRNA. Translation: BAB14567.1. Different initiation.
AL834387 mRNA. Translation: CAD39050.1.
AC018705 Genomic DNA. Translation: AAS01996.1.
CH236955 Genomic DNA. Translation: EAL23899.1.
CH471128 Genomic DNA. Translation: EAW60975.1.
CH471128 Genomic DNA. Translation: EAW60976.1.
BC051867 mRNA. Translation: AAH51867.1.
CCDSiCCDS5510.1. [Q6PIW4-1]
RefSeqiNP_001036227.1. NM_001042762.2. [Q6PIW4-1]
NP_001274421.1. NM_001287492.1. [Q6PIW4-1]
NP_001274422.1. NM_001287493.1. [Q6PIW4-1]
NP_001274423.1. NM_001287494.1. [Q6PIW4-1]
NP_001274424.1. NM_001287495.1. [Q6PIW4-1]
NP_001274425.1. NM_001287496.1. [Q6PIW4-2]
NP_071399.2. NM_022116.4. [Q6PIW4-1]
XP_005271840.1. XM_005271783.1. [Q6PIW4-2]
XP_011513771.1. XM_011515469.1. [Q6PIW4-1]
XP_011513772.1. XM_011515470.1. [Q6PIW4-1]
XP_011513773.1. XM_011515471.1. [Q6PIW4-1]
XP_011513774.1. XM_011515472.1. [Q6PIW4-2]
UniGeneiHs.137516.

Genome annotation databases

EnsembliENST00000356889; ENSP00000349356; ENSG00000132436. [Q6PIW4-1]
ENST00000395556; ENSP00000378924; ENSG00000132436. [Q6PIW4-1]
ENST00000419119; ENSP00000410811; ENSG00000132436. [Q6PIW4-1]
ENST00000433017; ENSP00000399997; ENSG00000132436. [Q6PIW4-1]
ENST00000611938; ENSP00000484551; ENSG00000132436. [Q6PIW4-1]
ENST00000613602; ENSP00000481751; ENSG00000132436. [Q6PIW4-1]
ENST00000615084; ENSP00000483543; ENSG00000132436. [Q6PIW4-1]
ENST00000617389; ENSP00000483126; ENSG00000132436. [Q6PIW4-1]
GeneIDi63979.
KEGGihsa:63979.
UCSCiuc003tpc.5. human. [Q6PIW4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023142 mRNA. Translation: BAB14426.1.
AK023411 mRNA. Translation: BAB14567.1. Different initiation.
AL834387 mRNA. Translation: CAD39050.1.
AC018705 Genomic DNA. Translation: AAS01996.1.
CH236955 Genomic DNA. Translation: EAL23899.1.
CH471128 Genomic DNA. Translation: EAW60975.1.
CH471128 Genomic DNA. Translation: EAW60976.1.
BC051867 mRNA. Translation: AAH51867.1.
CCDSiCCDS5510.1. [Q6PIW4-1]
RefSeqiNP_001036227.1. NM_001042762.2. [Q6PIW4-1]
NP_001274421.1. NM_001287492.1. [Q6PIW4-1]
NP_001274422.1. NM_001287493.1. [Q6PIW4-1]
NP_001274423.1. NM_001287494.1. [Q6PIW4-1]
NP_001274424.1. NM_001287495.1. [Q6PIW4-1]
NP_001274425.1. NM_001287496.1. [Q6PIW4-2]
NP_071399.2. NM_022116.4. [Q6PIW4-1]
XP_005271840.1. XM_005271783.1. [Q6PIW4-2]
XP_011513771.1. XM_011515469.1. [Q6PIW4-1]
XP_011513772.1. XM_011515470.1. [Q6PIW4-1]
XP_011513773.1. XM_011515471.1. [Q6PIW4-1]
XP_011513774.1. XM_011515472.1. [Q6PIW4-2]
UniGeneiHs.137516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D8BX-ray2.00A/B341-674[»]
ProteinModelPortaliQ6PIW4.
SMRiQ6PIW4. Positions 343-674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122026. 30 interactions.
IntActiQ6PIW4. 10 interactions.
MINTiMINT-4908266.
STRINGi9606.ENSP00000349356.

PTM databases

iPTMnetiQ6PIW4.
PhosphoSiteiQ6PIW4.

Polymorphism and mutation databases

BioMutaiFIGNL1.
DMDMi158563967.

Proteomic databases

EPDiQ6PIW4.
MaxQBiQ6PIW4.
PaxDbiQ6PIW4.
PeptideAtlasiQ6PIW4.
PRIDEiQ6PIW4.

Protocols and materials databases

DNASUi63979.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356889; ENSP00000349356; ENSG00000132436. [Q6PIW4-1]
ENST00000395556; ENSP00000378924; ENSG00000132436. [Q6PIW4-1]
ENST00000419119; ENSP00000410811; ENSG00000132436. [Q6PIW4-1]
ENST00000433017; ENSP00000399997; ENSG00000132436. [Q6PIW4-1]
ENST00000611938; ENSP00000484551; ENSG00000132436. [Q6PIW4-1]
ENST00000613602; ENSP00000481751; ENSG00000132436. [Q6PIW4-1]
ENST00000615084; ENSP00000483543; ENSG00000132436. [Q6PIW4-1]
ENST00000617389; ENSP00000483126; ENSG00000132436. [Q6PIW4-1]
GeneIDi63979.
KEGGihsa:63979.
UCSCiuc003tpc.5. human. [Q6PIW4-1]

Organism-specific databases

CTDi63979.
GeneCardsiFIGNL1.
HGNCiHGNC:13286. FIGNL1.
HPAiHPA055542.
MIMi615383. gene.
neXtProtiNX_Q6PIW4.
PharmGKBiPA28148.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0740. Eukaryota.
COG0464. LUCA.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225145.
HOVERGENiHBG061204.
InParanoidiQ6PIW4.
OMAiQILRIQY.
OrthoDBiEOG7GXPCR.
PhylomeDBiQ6PIW4.
TreeFamiTF105013.

Miscellaneous databases

EvolutionaryTraceiQ6PIW4.
GenomeRNAii63979.
PROiQ6PIW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PIW4.
CleanExiHS_FIGNL1.
ExpressionAtlasiQ6PIW4. baseline and differential.
GenevisibleiQ6PIW4. 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] (ISOFORM 1).
    Tissue: Ovary.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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), VARIANT MET-137.
    Tissue: Pancreas and Skin.
  8. "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-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  12. "FIGNL1-containing protein complex is required for efficient homologous recombination repair."
    Yuan J., Chen J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10640-10645(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD51 AND SPIDR, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-295; PHE-340; LYS-447 AND ASP-500, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Human fidgetin-like protein 1."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 341-674 IN COMPLEX WITH ADP.

Entry informationi

Entry nameiFIGL1_HUMAN
AccessioniPrimary (citable) accession number: Q6PIW4
Secondary accession number(s): D3DVM6
, Q86V18, Q8ND59, Q9H8P1, Q9H917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: July 6, 2016
This is version 123 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.