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Q9NZ56 (FMN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-2
Gene names
Name:FMN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1722 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Subunit structure

Interacts with SPIRE1. Binds actin. Interacts with CDKN1A. Ref.4 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cytoplasmcytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; 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. Ref.4 Ref.6

Tissue specificity

Expressed almost exclusively in the developing and mature central nervous system. Ref.3

Induction

Up-regulated in response to cellular stress, hypoxia and DNA damage via NF-kappa-B. Ref.6

Sequence similarities

Belongs to the formin homology family. Cappuccino subfamily.

Contains 1 FH1 (formin homology 1) domain.

Contains 1 FH2 (formin homology 2) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
Protein transport
Stress response
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   LigandActin-binding
   Molecular functionDevelopmental protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.6. Source: UniProtKB

cellular response to hypoxia

Inferred from mutant phenotype Ref.6. Source: UniProtKB

establishment of meiotic spindle localization

Inferred from sequence or structural similarity. Source: BHF-UCL

formin-nucleated actin cable assembly

Inferred from sequence or structural similarity. Source: UniProtKB

homologous chromosome movement towards spindle pole involved in homologous chromosome segregation

Inferred from sequence or structural similarity. Source: BHF-UCL

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

intracellular transport

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from mutant phenotype Ref.6. Source: UniProtKB

oogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

polar body extrusion after meiotic divisions

Inferred from sequence or structural similarity. Source: BHF-UCL

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.4. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.6. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionactin binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17221722Formin-2
PRO_0000194888

Regions

Domain758 – 1268511FH1
Domain1283 – 1698416FH2
Region1715 – 17228Important for interaction with SPIRE1
Coiled coil193 – 23139 Potential
Coiled coil670 – 70637 Potential
Coiled coil1567 – 159731 Potential
Coiled coil1677 – 169923 Potential
Compositional bias200 – 22728Gln-rich
Compositional bias758 – 1268511Pro-rich

Natural variations

Natural variant11481R → G. Ref.2
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_059290
Natural variant12911R → G.
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_049094
Natural variant14681R → H. Ref.2
Corresponds to variant rs3795677 [ dbSNP | Ensembl ].
VAR_033932

Experimental info

Mutagenesis17151K → A or E: Abolishes interaction with SPIRE1. Ref.8
Mutagenesis17171K → A: Strongly reduces interaction with SPIRE1. Ref.8
Mutagenesis17211K → A or E: Strongly reduces interaction with SPIRE1. Ref.8
Sequence conflict6441E → EDDGE in BAD92390. Ref.2
Sequence conflict7681P → T in BAD92390. Ref.2
Sequence conflict1426 – 14272EN → TR in AAF72885. Ref.3

Secondary structure

..... 1722
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NZ56 [UniParc].

Last modified January 15, 2008. Version 4.
Checksum: 26525AC7868A949C

FASTA1,722180,106
        10         20         30         40         50         60 
MGNQDGKLKR SAGDALHEGG GGAEDALGPR DVEATKKGSG GKKALGKHGK GGGGGGGGGE 

        70         80         90        100        110        120 
SGKKKSKSDS RASVFSNLRI RKNLSKGKGA GGSREDVLDS QALQTGELDS AHSLLTKTPD 

       130        140        150        160        170        180 
LSLSADEAGL SDTECADPFE VTGPGGPGPA EARVGGRPIA EDVETAAGAQ DGQRTSSGSD 

       190        200        210        220        230        240 
TDIYSFHSAT EQEDLLSDIQ QAIRLQQQQQ QQLQLQLQQQ QQQQQLQGAE EPAAPPTAVS 

       250        260        270        280        290        300 
PQPGAFLGLD RFLLGPSGGA GEAPGSPDTE QALSALSDLP ESLAAEPREP QQPPSPGGLP 

       310        320        330        340        350        360 
VSEAPSLPAA QPAAKDSPSS TAFPFPEAGP GEEAAGAPVR GAGDTDEEGE EDAFEDAPRG 

       370        380        390        400        410        420 
SPGEEWAPEV GEDAPQRLGE EPEEEAQGPD APAAASLPGS PAPSQRCFKP YPLITPCYIK 

       430        440        450        460        470        480 
TTTRQLSSPN HSPSQSPNQS PRIKRRPEPS LSRGSRTALA SVAAPAKKHR ADGGLAAGLS 

       490        500        510        520        530        540 
RSADWTEELG ARTPRVGGSA HLLERGVASD SGGGVSPALA AKASGAPAAA DGFQNVFTGR 

       550        560        570        580        590        600 
TLLEKLFSQQ ENGPPEEAEK FCSRIIAMGL LLPFSDCFRE PCNQNAQTNA ASFDQDQLYT 

       610        620        630        640        650        660 
WAAVSQPTHS LDYSEGQFPR RVPSMGPPSK PPDEEHRLED AETESQSAVS ETPQKRSDAV 

       670        680        690        700        710        720 
QKEVVDMKSE GQATVIQQLE QTIEDLRTKI AELERQYPAL DTEVASGHQG LENGVTASGD 

       730        740        750        760        770        780 
VCLEALRLEE KEVRHHRILE AKSIQTSPTE EGGVLTLPPV DGLPGRPPCP PGAESGPQTK 

       790        800        810        820        830        840 
FCSEISLIVS PRRISVQLDS HQPTQSISQP PPPPSLLWSA GQGQPGSQPP HSISTEFQTS 

       850        860        870        880        890        900 
HEHSVSSAFK NSCNIPSPPP LPCTESSSSM PGLGMVPPPP PPLPGMTVPT LPSTAIPQPP 

       910        920        930        940        950        960 
PLQGTEMLPP PPPPLPGAGI PPPPPLPGAG ILPLPPLPGA GIPPPPPLPG AAIPPPPPLP 

       970        980        990       1000       1010       1020 
GAGIPLPPPL PGAGIPPPPP LPGAGIPPPP PLPGAGIPPP PPLPGAGIPP PPPLPGAGIP 

      1030       1040       1050       1060       1070       1080 
PPPPLPGAGI PPPPPLPGAG IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GAGIPPPPPL 

      1090       1100       1110       1120       1130       1140 
PGAGIPPPPP LPGAGIPPPP PLPGVGIPPP PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI 

      1150       1160       1170       1180       1190       1200 
PPPPPLPRVG IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GVGIPPPPPL PGVGIPPPPP 

      1210       1220       1230       1240       1250       1260 
LPGAGIPPPP PLPGMGIPPA PAPPLPPPGT GIPPPPLLPV SGPPLLPQVG SSTLPTPQVC 

      1270       1280       1290       1300       1310       1320 
GFLPPPLPSG LFGLGMNQDK GSRKQPIEPC RPMKPLYWTR IQLHSKRDSS TSLIWEKIEE 

      1330       1340       1350       1360       1370       1380 
PSIDCHEFEE LFSKTAVKER KKPISDTISK TKAKQVVKLL SNKRSQAVGI LMSSLHLDMK 

      1390       1400       1410       1420       1430       1440 
DIQHAVVNLD NSVVDLETLQ ALYENRAQSD ELEKIEKHGR SSKDKENAKS LDKPEQFLYE 

      1450       1460       1470       1480       1490       1500 
LSLIPNFSER VFCILFQSTF SESICSIRRK LELLQKLCET LKNGPGVMQV LGLVLAFGNY 

      1510       1520       1530       1540       1550       1560 
MNGGNKTRGQ ADGFGLDILP KLKDVKSSDN SRSLLSYIVS YYLRNFDEDA GKEQCLFPLP 

      1570       1580       1590       1600       1610       1620 
EPQDLFQASQ MKFEDFQKDL RKLKKDLKAC EVEAGKVYQV SSKEHMQPFK ENMEQFIIQA 

      1630       1640       1650       1660       1670       1680 
KIDQEAEENS LTETHKCFLE TTAYFFMKPK LGEKEVSPNA FFSIWHEFSS DFKDFWKKEN 

      1690       1700       1710       1720 
KLLLQERVKE AEEVCRQKKG KSLYKIKPRH DSGIKAKISM KT 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[2]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, VARIANTS GLY-1148 AND HIS-1468.
Tissue: Brain.
[3]"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, TISSUE SPECIFICITY.
Tissue: Brain.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL359918 expand/collapse EMBL AC list , AL513342, AL590490, AL646016 Genomic DNA. Translation: CAQ10135.1.
AL513342 expand/collapse EMBL AC list , AL359918, AL590490, AL646016 Genomic DNA. Translation: CAQ10526.1.
AL590490 expand/collapse EMBL AC list , AL359918, AL513342, AL646016 Genomic DNA. Translation: CAQ10976.1.
AL646016 expand/collapse EMBL AC list , 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.
CCDSCCDS31069.2.
RefSeqNP_064450.3. NM_020066.4.
UniGeneHs.24889.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YLEX-ray1.80B1694-1722[»]
3R7GX-ray2.20B1701-1722[»]
ProteinModelPortalQ9NZ56.
SMRQ9NZ56. Positions 1308-1699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000318884.

PTM databases

PhosphoSiteQ9NZ56.

Polymorphism databases

DMDM166215083.

Proteomic databases

MaxQBQ9NZ56.
PaxDbQ9NZ56.
PRIDEQ9NZ56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319653; ENSP00000318884; ENSG00000155816.
GeneID56776.
KEGGhsa:56776.
UCSCuc010pyd.2. human.

Organism-specific databases

CTD56776.
GeneCardsGC01P240177.
H-InvDBHIX0021237.
HGNCHGNC:14074. FMN2.
HPAHPA004937.
MIM606373. gene.
neXtProtNX_Q9NZ56.
PharmGKBPA28185.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264408.
HOGENOMHOG000112618.
HOVERGENHBG107923.
InParanoidQ9NZ56.
KOK02184.
OMAEHRPKDA.
OrthoDBEOG78M01H.
PhylomeDBQ9NZ56.
TreeFamTF326072.

Enzyme and pathway databases

SignaLinkQ9NZ56.

Gene expression databases

ArrayExpressQ9NZ56.
BgeeQ9NZ56.
CleanExHS_FMN2.
GenevestigatorQ9NZ56.

Family and domain databases

InterProIPR000591. DEP_dom.
IPR015425. FH2_Formin.
IPR009408. Formin_homology_1.
[Graphical view]
PfamPF06346. Drf_FH1. 4 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTSM00498. FH2. 1 hit.
[Graphical view]
PROSITEPS51444. FH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi56776.
NextBio62219.
PROQ9NZ56.
SOURCESearch...

Entry information

Entry nameFMN2_HUMAN
AccessionPrimary (citable) accession number: Q9NZ56
Secondary accession number(s): B0QZA7 expand/collapse secondary AC list , Q59GF6, Q5VU37, Q9NZ55
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 114 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM