Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NZ56

- FMN2_HUMAN

UniProt

Q9NZ56 - FMN2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Formin-2

Gene

FMN2

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

Functioni

Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.By similarity2 Publications

GO - Molecular functioni

  1. actin binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. cellular response to hypoxia Source: UniProtKB
  3. establishment of meiotic spindle localization Source: BHF-UCL
  4. formin-nucleated actin cable assembly Source: UniProtKB
  5. homologous chromosome movement towards spindle pole involved in homologous chromosome segregation Source: BHF-UCL
  6. intracellular signal transduction Source: InterPro
  7. intracellular transport Source: UniProtKB
  8. multicellular organismal development Source: UniProtKB-KW
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of protein catabolic process Source: UniProtKB
  11. oogenesis Source: BHF-UCL
  12. polar body extrusion after meiotic divisions Source: BHF-UCL
  13. protein transport Source: UniProtKB-KW
  14. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

DNA damage, Protein transport, Stress response, Transport

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ9NZ56.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-2
Gene namesi
Name:FMN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14074. FMN2.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cytoplasmcytosol. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmcell cortex By similarity. Nucleusnucleolus
Note: Recruited to the membranes via its interaction with SPIRE1. Colocalizes with the actin cytoskeleton. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion (By similarity).By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum membrane Source: Ensembl
  5. microvillus Source: Ensembl
  6. nucleolus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
  8. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1715 – 17151K → A or E: Abolishes interaction with SPIRE1. 1 Publication
Mutagenesisi1717 – 17171K → A: Strongly reduces interaction with SPIRE1. 1 Publication
Mutagenesisi1721 – 17211K → A or E: Strongly reduces interaction with SPIRE1. 1 Publication

Organism-specific databases

PharmGKBiPA28185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17221722Formin-2PRO_0000194888Add
BLAST

Proteomic databases

MaxQBiQ9NZ56.
PaxDbiQ9NZ56.
PRIDEiQ9NZ56.

PTM databases

PhosphoSiteiQ9NZ56.

Expressioni

Tissue specificityi

Expressed almost exclusively in the developing and mature central nervous system.1 Publication

Inductioni

Up-regulated in response to cellular stress, hypoxia and DNA damage via NF-kappa-B.1 Publication

Gene expression databases

BgeeiQ9NZ56.
CleanExiHS_FMN2.
ExpressionAtlasiQ9NZ56. baseline and differential.
GenevestigatoriQ9NZ56.

Organism-specific databases

HPAiHPA004937.

Interactioni

Subunit structurei

Interacts with SPIRE1. Binds actin. Interacts with CDKN1A.4 Publications

Protein-protein interaction databases

BioGridi121199. 6 interactions.
STRINGi9606.ENSP00000318884.

Structurei

Secondary structure

1
1722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1706 – 17083Combined sources
Helixi1714 – 17196Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YLEX-ray1.80B1694-1722[»]
3R7GX-ray2.20B1701-1722[»]
ProteinModelPortaliQ9NZ56.
SMRiQ9NZ56. Positions 1308-1699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini758 – 1268511FH1Add
BLAST
Domaini1283 – 1698416FH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1715 – 17228Important for interaction with SPIRE1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili193 – 23139Sequence AnalysisAdd
BLAST
Coiled coili670 – 70637Sequence AnalysisAdd
BLAST
Coiled coili1567 – 159731Sequence AnalysisAdd
BLAST
Coiled coili1677 – 169923Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 22728Gln-richAdd
BLAST
Compositional biasi758 – 1268511Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264408.
GeneTreeiENSGT00760000119258.
HOGENOMiHOG000112618.
HOVERGENiHBG107923.
InParanoidiQ9NZ56.
KOiK02184.
OMAiEHRPKDA.
OrthoDBiEOG78M01H.
PhylomeDBiQ9NZ56.
TreeFamiTF326072.

Family and domain databases

InterProiIPR000591. DEP_dom.
IPR015425. FH2_Formin.
IPR001265. Formin_Cappuccino_subfam.
IPR009408. Formin_homology_1.
[Graphical view]
PfamiPF06346. Drf_FH1. 4 hits.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSiPR00828. FORMIN.
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
PROSITEiPS51444. FH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NZ56-1) [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
MGNQDGKLKR SAGDALHEGG GGAEDALGPR DVEATKKGSG GKKALGKHGK
60 70 80 90 100
GGGGGGGGGE SGKKKSKSDS RASVFSNLRI RKNLSKGKGA GGSREDVLDS
110 120 130 140 150
QALQTGELDS AHSLLTKTPD LSLSADEAGL SDTECADPFE VTGPGGPGPA
160 170 180 190 200
EARVGGRPIA EDVETAAGAQ DGQRTSSGSD TDIYSFHSAT EQEDLLSDIQ
210 220 230 240 250
QAIRLQQQQQ QQLQLQLQQQ QQQQQLQGAE EPAAPPTAVS PQPGAFLGLD
260 270 280 290 300
RFLLGPSGGA GEAPGSPDTE QALSALSDLP ESLAAEPREP QQPPSPGGLP
310 320 330 340 350
VSEAPSLPAA QPAAKDSPSS TAFPFPEAGP GEEAAGAPVR GAGDTDEEGE
360 370 380 390 400
EDAFEDAPRG SPGEEWAPEV GEDAPQRLGE EPEEEAQGPD APAAASLPGS
410 420 430 440 450
PAPSQRCFKP YPLITPCYIK TTTRQLSSPN HSPSQSPNQS PRIKRRPEPS
460 470 480 490 500
LSRGSRTALA SVAAPAKKHR ADGGLAAGLS RSADWTEELG ARTPRVGGSA
510 520 530 540 550
HLLERGVASD SGGGVSPALA AKASGAPAAA DGFQNVFTGR TLLEKLFSQQ
560 570 580 590 600
ENGPPEEAEK FCSRIIAMGL LLPFSDCFRE PCNQNAQTNA ASFDQDQLYT
610 620 630 640 650
WAAVSQPTHS LDYSEGQFPR RVPSMGPPSK PPDEEHRLED AETESQSAVS
660 670 680 690 700
ETPQKRSDAV QKEVVDMKSE GQATVIQQLE QTIEDLRTKI AELERQYPAL
710 720 730 740 750
DTEVASGHQG LENGVTASGD VCLEALRLEE KEVRHHRILE AKSIQTSPTE
760 770 780 790 800
EGGVLTLPPV DGLPGRPPCP PGAESGPQTK FCSEISLIVS PRRISVQLDS
810 820 830 840 850
HQPTQSISQP PPPPSLLWSA GQGQPGSQPP HSISTEFQTS HEHSVSSAFK
860 870 880 890 900
NSCNIPSPPP LPCTESSSSM PGLGMVPPPP PPLPGMTVPT LPSTAIPQPP
910 920 930 940 950
PLQGTEMLPP PPPPLPGAGI PPPPPLPGAG ILPLPPLPGA GIPPPPPLPG
960 970 980 990 1000
AAIPPPPPLP GAGIPLPPPL PGAGIPPPPP LPGAGIPPPP PLPGAGIPPP
1010 1020 1030 1040 1050
PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPGAG IPPPPPLPGA
1060 1070 1080 1090 1100
GIPPPPPLPG AGIPPPPPLP GAGIPPPPPL PGAGIPPPPP LPGAGIPPPP
1110 1120 1130 1140 1150
PLPGVGIPPP PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPRVG
1160 1170 1180 1190 1200
IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GVGIPPPPPL PGVGIPPPPP
1210 1220 1230 1240 1250
LPGAGIPPPP PLPGMGIPPA PAPPLPPPGT GIPPPPLLPV SGPPLLPQVG
1260 1270 1280 1290 1300
SSTLPTPQVC GFLPPPLPSG LFGLGMNQDK GSRKQPIEPC RPMKPLYWTR
1310 1320 1330 1340 1350
IQLHSKRDSS TSLIWEKIEE PSIDCHEFEE LFSKTAVKER KKPISDTISK
1360 1370 1380 1390 1400
TKAKQVVKLL SNKRSQAVGI LMSSLHLDMK DIQHAVVNLD NSVVDLETLQ
1410 1420 1430 1440 1450
ALYENRAQSD ELEKIEKHGR SSKDKENAKS LDKPEQFLYE LSLIPNFSER
1460 1470 1480 1490 1500
VFCILFQSTF SESICSIRRK LELLQKLCET LKNGPGVMQV LGLVLAFGNY
1510 1520 1530 1540 1550
MNGGNKTRGQ ADGFGLDILP KLKDVKSSDN SRSLLSYIVS YYLRNFDEDA
1560 1570 1580 1590 1600
GKEQCLFPLP EPQDLFQASQ MKFEDFQKDL RKLKKDLKAC EVEAGKVYQV
1610 1620 1630 1640 1650
SSKEHMQPFK ENMEQFIIQA KIDQEAEENS LTETHKCFLE TTAYFFMKPK
1660 1670 1680 1690 1700
LGEKEVSPNA FFSIWHEFSS DFKDFWKKEN KLLLQERVKE AEEVCRQKKG
1710 1720
KSLYKIKPRH DSGIKAKISM KT
Length:1,722
Mass (Da):180,106
Last modified:January 15, 2008 - v4
Checksum:i26525AC7868A949C
GO
Isoform 2 (identifier: Q9NZ56-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-1405: Missing.

Note: No experimental confirmation available.

Show »
Length:318
Mass (Da):36,871
Checksum:i3FA270C7B4D1E07A
GO

Sequence cautioni

The sequence AAF72884.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti644 – 6441E → EDDGE in BAD92390. 1 PublicationCurated
Sequence conflicti768 – 7681P → T in BAD92390. 1 PublicationCurated
Sequence conflicti1426 – 14272EN → TR in AAF72885. (PubMed:10781961)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1148 – 11481R → G.1 Publication
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_059290
Natural varianti1291 – 12911R → G.
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_049094
Natural varianti1468 – 14681R → H.1 Publication
Corresponds to variant rs3795677 [ dbSNP | Ensembl ].
VAR_033932

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 14051404Missing in isoform 2. 1 PublicationVSP_056095Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298141 mRNA. Translation: BAG60417.1.
AL359918
, AL513342, AL590490, AL646016 Genomic DNA. Translation: CAQ10135.1.
AL513342
, AL359918, AL590490, AL646016 Genomic DNA. Translation: CAQ10526.1.
AL590490
, AL359918, AL513342, AL646016 Genomic DNA. Translation: CAQ10976.1.
AL646016
, AL359918, AL513342, AL590490 Genomic DNA. Translation: CAQ08405.1.
AB209153 mRNA. Translation: BAD92390.1.
AF218941 mRNA. Translation: AAF72884.1. Sequence problems.
AF218942 mRNA. Translation: AAF72885.1.
CCDSiCCDS31069.2. [Q9NZ56-1]
RefSeqiNP_064450.3. NM_020066.4. [Q9NZ56-1]
UniGeneiHs.24889.

Genome annotation databases

EnsembliENST00000319653; ENSP00000318884; ENSG00000155816. [Q9NZ56-1]
GeneIDi56776.
KEGGihsa:56776.
UCSCiuc010pyd.2. human. [Q9NZ56-1]

Polymorphism databases

DMDMi166215083.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298141 mRNA. Translation: BAG60417.1 .
AL359918
, AL513342 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10135.1 .
AL513342
, AL359918 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10526.1 .
AL590490
, AL359918 , AL513342 , AL646016 Genomic DNA. Translation: CAQ10976.1 .
AL646016
, AL359918 , AL513342 , AL590490 Genomic DNA. Translation: CAQ08405.1 .
AB209153 mRNA. Translation: BAD92390.1 .
AF218941 mRNA. Translation: AAF72884.1 . Sequence problems.
AF218942 mRNA. Translation: AAF72885.1 .
CCDSi CCDS31069.2. [Q9NZ56-1 ]
RefSeqi NP_064450.3. NM_020066.4. [Q9NZ56-1 ]
UniGenei Hs.24889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YLE X-ray 1.80 B 1694-1722 [» ]
3R7G X-ray 2.20 B 1701-1722 [» ]
ProteinModelPortali Q9NZ56.
SMRi Q9NZ56. Positions 1308-1699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121199. 6 interactions.
STRINGi 9606.ENSP00000318884.

PTM databases

PhosphoSitei Q9NZ56.

Polymorphism databases

DMDMi 166215083.

Proteomic databases

MaxQBi Q9NZ56.
PaxDbi Q9NZ56.
PRIDEi Q9NZ56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319653 ; ENSP00000318884 ; ENSG00000155816 . [Q9NZ56-1 ]
GeneIDi 56776.
KEGGi hsa:56776.
UCSCi uc010pyd.2. human. [Q9NZ56-1 ]

Organism-specific databases

CTDi 56776.
GeneCardsi GC01P240177.
H-InvDB HIX0021237.
HGNCi HGNC:14074. FMN2.
HPAi HPA004937.
MIMi 606373. gene.
neXtProti NX_Q9NZ56.
PharmGKBi PA28185.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264408.
GeneTreei ENSGT00760000119258.
HOGENOMi HOG000112618.
HOVERGENi HBG107923.
InParanoidi Q9NZ56.
KOi K02184.
OMAi EHRPKDA.
OrthoDBi EOG78M01H.
PhylomeDBi Q9NZ56.
TreeFami TF326072.

Enzyme and pathway databases

SignaLinki Q9NZ56.

Miscellaneous databases

GenomeRNAii 56776.
NextBioi 35473751.
PROi Q9NZ56.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZ56.
CleanExi HS_FMN2.
ExpressionAtlasi Q9NZ56. baseline and differential.
Genevestigatori Q9NZ56.

Family and domain databases

InterProi IPR000591. DEP_dom.
IPR015425. FH2_Formin.
IPR001265. Formin_Cappuccino_subfam.
IPR009408. Formin_homology_1.
[Graphical view ]
Pfami PF06346. Drf_FH1. 4 hits.
PF02181. FH2. 1 hit.
[Graphical view ]
PRINTSi PR00828. FORMIN.
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
PROSITEi PS51444. FH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 2).
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1722 (ISOFORM 1), VARIANTS GLY-1148 AND HIS-1468.
    Tissue: Brain.
  4. "Formin-2, a novel formin homology protein of the cappuccino subfamily, is highly expressed in the developing and adult central nervous system."
    Leader B., Leder P.
    Mech. Dev. 93:221-231(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 396-727 AND 1426-1722 (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  5. "Effects of genistein on beta-catenin signaling and subcellular distribution of actin-binding proteins in human umbilical CD105-positive stromal cells."
    Shieh D.B., Li R.Y., Liao J.M., Chen G.D., Liou Y.M.
    J. Cell. Physiol. 223:423-434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.
  6. "Differential role of actin-binding proteins in controlling the adipogenic differentiation of human CD105-positive Wharton's Jelly cells."
    Peng K.W., Liou Y.M.
    Biochim. Biophys. Acta 1820:469-481(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21."
    Yamada K., Ono M., Perkins N.D., Rocha S., Lamond A.I.
    Mol. Cell 49:922-933(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDKN1A, SUBCELLULAR LOCATION, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex."
    Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.
    J. Biol. Chem. 286:30732-30739(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1694-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1.
  9. "Structure and function of the interacting domains of Spire and Fmn-family formins."
    Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
    Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1701-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1, MUTAGENESIS OF LYS-1715; LYS-1717 AND LYS-1721.

Entry informationi

Entry nameiFMN2_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ56
Secondary accession number(s): B0QZA7
, B4DP05, Q59GF6, Q5VU37, Q9NZ55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 15, 2008
Last modified: November 26, 2014
This is version 117 of the entry and version 4 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 1
    Human chromosome 1: 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

External Data

Dasty 3