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Q96PY5 (FMNL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formin-like protein 2
Alternative name(s):
Formin homology 2 domain-containing protein 2
Gene names
Name:FMNL2
Synonyms:FHOD2, KIAA1902
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1086 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics. Ref.8

Subcellular location

Cytoplasm By similarity.

Domain

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments By similarity.

Sequence similarities

Belongs to the formin homology family.

Contains 1 DAD (diaphanous autoregulatory) domain.

Contains 1 FH2 (formin homology 2) domain.

Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.

Sequence caution

The sequence AAI13879.1 differs from that shown. Reason: Aberrant splicing.

The sequence AAI14439.1 differs from that shown. Reason: Aberrant splicing.

The sequence AAX88959.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAB67795.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMLipoprotein
Myristate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcortical actin cytoskeleton organization

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cytoskeleton organization

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of cell morphogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PY5-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q96PY5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1057-1086: VLKTVPFTARTAKRGSRFFCEPVLTEEYHY → DLRNQPYRRADAVRRSVRRRFDDQNLRSVNGAEITM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 10861085Formin-like protein 2
PRO_0000289093

Regions

Domain23 – 469447GBD/FH3
Domain616 – 1007392FH2
Domain1040 – 107940DAD
Compositional bias525 – 60379Pro-rich

Amino acid modifications

Lipidation21N-myristoyl glycine Ref.7

Natural variations

Alternative sequence1057 – 108630VLKTV…EEYHY → DLRNQPYRRADAVRRSVRRR FDDQNLRSVNGAEITM in isoform 2.
VSP_025887
Natural variant3521Y → C.
Corresponds to variant rs34119671 [ dbSNP | Ensembl ].
VAR_032570
Natural variant5041M → T.
Corresponds to variant rs11897929 [ dbSNP | Ensembl ].
VAR_032571

Experimental info

Sequence conflict5701P → PP in BAB67795. Ref.1
Sequence conflict5701P → PP in AAI67159. Ref.3
Sequence conflict5701P → PP in CAD39058. Ref.4
Sequence conflict5791A → S in BAB67795. Ref.1
Sequence conflict5791A → S in AAI67159. Ref.3
Sequence conflict9641T → R in CAD39058. Ref.4

Sequences

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

Last modified May 26, 2009. Version 3.
Checksum: 951ED0A26232F640

FASTA1,086123,321
        10         20         30         40         50         60 
MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK 

        70         80         90        100        110        120 
WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG 

       130        140        150        160        170        180 
WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTVES SVDKSKPWSR SIEDLHRGSN 

       190        200        210        220        230        240 
LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM 

       250        260        270        280        290        300 
VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF 

       310        320        330        340        350        360 
EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE 

       370        380        390        400        410        420 
SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI 

       430        440        450        460        470        480 
VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT 

       490        500        510        520        530        540 
IKIQKKGDGD IAILPVVASG TLSMGSEVVA GNSVGPTMGA ASSGPLPPPP PPLPPSSDTP 

       550        560        570        580        590        600 
ETVQNGPVTP PMPPPPPPPP PPPPPPPPPP PPPLPGPAAE TVPAPPLAPP LPSAPPLPGT 

       610        620        630        640        650        660 
SSPTVVFNSG LAAVKIKKPI KTKFRMPVFN WVALKPNQIN GTVFNEIDDE RILEDLNVDE 

       670        680        690        700        710        720 
FEEIFKTKAQ GPAIDLSSSK QKIPQKGSNK VTLLEANRAK NLAITLRKAG KTADEICKAI 

       730        740        750        760        770        780 
HVFDLKTLPV DFVECLMRFL PTENEVKVLR LYERERKPLE NLSDEDRFMM QFSKIERLMQ 

       790        800        810        820        830        840 
KMTIMAFIGN FAESIQMLTP QLHAIIAASV SIKSSQKLKK ILEIILALGN YMNSSKRGAV 

       850        860        870        880        890        900 
YGFKLQSLDL LLDTKSTDRK QTLLHYISNV VKEKYHQVSL FYNELHYVEK AAAVSLENVL 

       910        920        930        940        950        960 
LDVKELQRGM DLTKREYTMH DHNTLLKEFI LNNEGKLKKL QDDAKIAQDA FDDVVKYFGE 

       970        980        990       1000       1010       1020 
NPKTTPPSVF FPVFVRFVKA YKQAEEENEL RKKQEQALME KLLEQEALME QQDPKSPSHK 

      1030       1040       1050       1060       1070       1080 
SKRQQQELIA ELRRRQVKDN RHVYEGKDGA IEDIITVLKT VPFTARTAKR GSRFFCEPVL 


TEEYHY 

« Hide

Isoform 2 [UniParc].

Checksum: A20AA3D76733A717
Show »

FASTA1,092124,107

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"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. expand/collapse author list , 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].
[3]"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 2).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-1086 (ISOFORM 2).
Tissue: Amygdala.
[5]"Identification and characterization of human FMNL1, FMNL2 and FMNL3 genes in silico."
Katoh M., Katoh M.
Int. J. Oncol. 22:1161-1168(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORMS 1 AND 2).
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[8]"Identification and characterization of a set of conserved and new regulators of cytoskeletal organisation, cell morphology and migration."
Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.
BMC Biol. 9:54-54(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB067489 mRNA. Translation: BAB67795.1. Different initiation.
AC012066 Genomic DNA. No translation available.
AC012443 Genomic DNA. Translation: AAX88959.1. Sequence problems.
AC093794 Genomic DNA. No translation available.
BC113878 mRNA. Translation: AAI13879.1. Sequence problems.
BC114438 mRNA. Translation: AAI14439.1. Sequence problems.
BC167159 mRNA. Translation: AAI67159.1.
AL834396 mRNA. Translation: CAD39058.1.
CCDSCCDS46429.1. [Q96PY5-3]
RefSeqNP_443137.2. NM_052905.3. [Q96PY5-3]
XP_006712291.1. XM_006712228.1. [Q96PY5-1]
UniGeneHs.654630.

3D structure databases

ProteinModelPortalQ96PY5.
SMRQ96PY5. Positions 222-368, 617-1021.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125355. 6 interactions.
IntActQ96PY5. 2 interactions.
MINTMINT-1199986.
STRING9606.ENSP00000288670.

PTM databases

PhosphoSiteQ96PY5.

Polymorphism databases

DMDM238054383.

Proteomic databases

MaxQBQ96PY5.
PaxDbQ96PY5.
PRIDEQ96PY5.

Protocols and materials databases

DNASU114793.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288670; ENSP00000288670; ENSG00000157827. [Q96PY5-3]
GeneID114793.
KEGGhsa:114793.
UCSCuc002tye.3. human. [Q96PY5-3]

Organism-specific databases

CTD114793.
GeneCardsGC02P153191.
HGNCHGNC:18267. FMNL2.
HPAHPA005464.
neXtProtNX_Q96PY5.
PharmGKBPA28144.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270361.
HOGENOMHOG000231209.
HOVERGENHBG053118.
InParanoidQ96PY5.
OMATENEAMA.
OrthoDBEOG7F7W8J.
PhylomeDBQ96PY5.
TreeFamTF325155.

Gene expression databases

ArrayExpressQ96PY5.
BgeeQ96PY5.
CleanExHS_FMNL2.
GenevestigatorQ96PY5.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027656. FMNL2.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
IPR017987. Wilms_tumour.
[Graphical view]
PANTHERPTHR23213:SF180. PTHR23213:SF180. 1 hit.
PfamPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
PRINTSPR00049. WILMSTUMOUR.
SMARTSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFMNL2. human.
GeneWikiFMNL2.
GenomeRNAi114793.
NextBio79219.
PROQ96PY5.

Entry information

Entry nameFMNL2_HUMAN
AccessionPrimary (citable) accession number: Q96PY5
Secondary accession number(s): B2RZH5 expand/collapse secondary AC list , Q14CC9, Q4ZG52, Q8N3E0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 96 of the entry and version 3 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

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 2

Human chromosome 2: entries, gene names and cross-references to MIM