Skip Header

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

O95466

- FMNL_HUMAN

UniProt

O95466 - FMNL_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-like protein 1

Gene

FMNL1

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

Functioni

May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.By similarity1 Publication

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. GTPase activating protein binding Source: UniProtKB
  3. Rac GTPase binding Source: UniProtKB

GO - Biological processi

  1. actin filament severing Source: UniProtKB
  2. cortical actin cytoskeleton organization Source: UniProtKB
  3. regulation of cell shape Source: UniProtKB
  4. substrate-dependent cell migration Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-like protein 1
Alternative name(s):
CLL-associated antigen KW-13
Leukocyte formin
Gene namesi
Name:FMNL1
Synonyms:C17orf1, C17orf1B, FMNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1212. FMNL1.

Subcellular locationi

Cytoplasm By similarity. Cell membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasmic vesiclephagosome By similarity
Note: Recruited to actin-rich phagosomes during phagocytosis. Translocates to the plasma membrane upon activation by RAC1 (By similarity).By similarity
Isoform 3 : Cytoplasmcell cortex. Cell projectionbleb
Note: Colocalized with F-actin in bleb protrusions.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. phagocytic vesicle Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 11001099Formin-like protein 1PRO_0000194890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei184 – 1841Phosphoserine3 Publications
Modified residuei624 – 6241Phosphoserine4 Publications

Post-translational modificationi

Myristoylation mediates membrane localization and blebbing.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiO95466.
PaxDbiO95466.
PRIDEiO95466.

PTM databases

PhosphoSiteiO95466.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

BgeeiO95466.
CleanExiHS_FMNL1.
ExpressionAtlasiO95466. baseline and differential.
GenevestigatoriO95466.

Organism-specific databases

HPAiHPA008129.
HPA028288.

Interactioni

Subunit structurei

Interacts with RAC1, PFN1 and PFN2 (By similarity). Interacts (activated by RAC1) with SRGAP2 (via SH3 domain); regulates the actin filament severing activity of FMNL1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SRGAP2O750443EBI-720020,EBI-1051034

Protein-protein interaction databases

BioGridi107208. 63 interactions.
IntActiO95466. 5 interactions.
MINTiMINT-1188250.
STRINGi9606.ENSP00000329219.

Structurei

3D structure databases

ProteinModelPortaliO95466.
SMRiO95466. Positions 219-421, 633-1074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 468442GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini632 – 1023392FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 109032DADPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi459 – 616158Pro-richAdd
BLAST

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the N-terminus. 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).By similarity

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG149898.
GeneTreeiENSGT00760000118986.
HOVERGENiHBG053118.
InParanoidiO95466.
OMAiFSESTPM.
OrthoDBiEOG7F7W8J.
PhylomeDBiO95466.
TreeFamiTF325155.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027657. FMNL1.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERiPTHR23213:SF188. PTHR23213:SF188. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95466-1) [UniParc]FASTAAdd to Basket

Also known as: FMNL1alpha

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
MGNAAGSAEQ PAGPAAPPPK QPAPPKQPMP AAGELEERFN RALNCMNLPP
60 70 80 90 100
DKVQLLSQYD NEKKWELICD QERFQVKNPP AAYIQKLKSY VDTGGVSRKV
110 120 130 140 150
AADWMSNLGF KRRVQESTQV LRELETSLRT NHIGWVQEFL NEENRGLDVL
160 170 180 190 200
LEYLAFAQCS VTYDMESTDN GASNSEKNKP LEQSVEDLSK GPPSSVPKSR
210 220 230 240 250
HLTIKLTPAH SRKALRNSRI VSQKDDVHVC IMCLRAIMNY QSGFSLVMNH
260 270 280 290 300
PACVNEIALS LNNKNPRTKA LVLELLAAVC LVRGGHDIIL AAFDNFKEVC
310 320 330 340 350
GEQHRFEKLM EYFRNEDSNI DFMVACMQFI NIVVHSVENM NFRVFLQYEF
360 370 380 390 400
THLGLDLYLE RLRLTESDKL QVQIQAYLDN IFDVGALLED TETKNAVLEH
410 420 430 440 450
MEELQEQVAL LTERLRDAEN ESMAKIAELE KQLSQARKEL ETLRERFSES
460 470 480 490 500
TAMGPSRRPP EPEKAPPAAP TRPSALELKV EELEEKGLIR ILRGPGDAVS
510 520 530 540 550
IEILPVAVAT PSGGDAPTPG VPTGSPSPDL APAAEPAPGA APPPPPPLPG
560 570 580 590 600
LPSPQEAPPS APPQAPPLPG SPEPPPAPPL PGDLPPPPPP PPPPPGTDGP
610 620 630 640 650
VPPPPPPPPP PPGGPPDALG RRDSELGPGV KAKKPIQTKF RMPLLNWVAL
660 670 680 690 700
KPSQITGTVF TELNDEKVLQ ELDMSDFEEQ FKTKSQGPSL DLSALKSKAA
710 720 730 740 750
QKAPSKATLI EANRAKNLAI TLRKGNLGAE RICQAIEAYD LQALGLDFLE
760 770 780 790 800
LLMRFLPTEY ERSLITRFER EQRPMEELSE EDRFMLCFSR IPRLPERMTT
810 820 830 840 850
LTFLGNFPDT AQLLMPQLNA IIAASMSIKS SDKLRQILEI VLAFGNYMNS
860 870 880 890 900
SKRGAAYGFR LQSLDALLEM KSTDRKQTLL HYLVKVIAEK YPQLTGFHSD
910 920 930 940 950
LHFLDKAGSV SLDSVLADVR SLQRGLELTQ REFVRQDDCM VLKEFLRANS
960 970 980 990 1000
PTMDKLLADS KTAQEAFESV VEYFGENPKT TSPGLFFSLF SRFIKAYKKA
1010 1020 1030 1040 1050
EQEVEQWKKE AAAQEAGADT PGKGEPPAPK SPPKARRPQM DLISELKRRQ
1060 1070 1080 1090 1100
QKEPLIYESD RDGAIEDIIT VIKTVPFTAR TGKRTSRLLC EASLGEEMPL
Length:1,100
Mass (Da):121,854
Last modified:June 16, 2009 - v3
Checksum:i91F9CE2B3B526FFC
GO
Isoform 2 (identifier: O95466-2) [UniParc]FASTAAdd to Basket

Also known as: FMNL1beta

The sequence of this isoform differs from the canonical sequence as follows:
     1071-1100: VIKTVPFTARTGKRTSRLLCEASLGEEMPL → DLRNQPYIRADTGRRSARRRPPGPPLQVTSDLSL

Show »
Length:1,104
Mass (Da):122,409
Checksum:i74CFC7C3D5ABCC23
GO
Isoform 3 (identifier: O95466-3) [UniParc]FASTAAdd to Basket

Also known as: FMNL1gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1070-1070: T → TGKGLARPWSYPQSVLLCFLLTQCAILWGTGCHTASCYLFCFSFLFPFSTPLHLPHPHS

Note: Due to intron retention. Constitutively activated form, probably due to alterations in the DAD domain.

Show »
Length:1,158
Mass (Da):128,335
Checksum:i43D0BA60ABEA6AD5
GO

Sequence cautioni

The sequence AAH21906.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA07870.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti455 – 4551P → A in AAP32476. 1 PublicationCurated
Sequence conflicti455 – 4551P → A in AAL99920. 1 PublicationCurated
Sequence conflicti455 – 4551P → A in AAH73988. (PubMed:15489334)Curated
Sequence conflicti602 – 6021Missing in AAH21906. (PubMed:15489334)Curated
Sequence conflicti629 – 6291G → R in CAA07870. (PubMed:9799091)Curated
Isoform 2 (identifier: O95466-2)
Sequence conflicti1101 – 11022DL → EV in AAH21906. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1070 – 10701T → TGKGLARPWSYPQSVLLCFL LTQCAILWGTGCHTASCYLF CFSFLFPFSTPLHLPHPHS in isoform 3. 1 PublicationVSP_043845
Alternative sequencei1071 – 110030VIKTV…EEMPL → DLRNQPYIRADTGRRSARRR PPGPPLQVTSDLSL in isoform 2. 3 PublicationsVSP_013977Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY278319 mRNA. Translation: AAP32476.1.
AC008105 mRNA. No translation available.
AF432213 mRNA. Translation: AAL99920.1.
BC001710 mRNA. Translation: AAH01710.2.
BC009000 mRNA. Translation: AAH09000.2.
BC021906 mRNA. Translation: AAH21906.1. Different initiation.
BC073988 mRNA. Translation: AAH73988.1.
AJ008112 mRNA. Translation: CAA07870.1. Different initiation.
CR456759 mRNA. Translation: CAG33040.1.
FJ534522 mRNA. Translation: ACR19333.1.
CCDSiCCDS11497.1. [O95466-1]
RefSeqiNP_005883.2. NM_005892.3.
XP_006722126.1. XM_006722063.1. [O95466-3]
XP_006722131.1. XM_006722068.1. [O95466-1]
XP_006722133.1. XM_006722070.1. [O95466-2]
UniGeneiHs.100217.

Genome annotation databases

EnsembliENST00000331495; ENSP00000329219; ENSG00000184922. [O95466-1]
GeneIDi752.
KEGGihsa:752.
UCSCiuc002iin.3. human. [O95466-1]
uc002iiq.3. human. [O95466-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY278319 mRNA. Translation: AAP32476.1 .
AC008105 mRNA. No translation available.
AF432213 mRNA. Translation: AAL99920.1 .
BC001710 mRNA. Translation: AAH01710.2 .
BC009000 mRNA. Translation: AAH09000.2 .
BC021906 mRNA. Translation: AAH21906.1 . Different initiation.
BC073988 mRNA. Translation: AAH73988.1 .
AJ008112 mRNA. Translation: CAA07870.1 . Different initiation.
CR456759 mRNA. Translation: CAG33040.1 .
FJ534522 mRNA. Translation: ACR19333.1 .
CCDSi CCDS11497.1. [O95466-1 ]
RefSeqi NP_005883.2. NM_005892.3.
XP_006722126.1. XM_006722063.1. [O95466-3 ]
XP_006722131.1. XM_006722068.1. [O95466-1 ]
XP_006722133.1. XM_006722070.1. [O95466-2 ]
UniGenei Hs.100217.

3D structure databases

ProteinModelPortali O95466.
SMRi O95466. Positions 219-421, 633-1074.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107208. 63 interactions.
IntActi O95466. 5 interactions.
MINTi MINT-1188250.
STRINGi 9606.ENSP00000329219.

PTM databases

PhosphoSitei O95466.

Proteomic databases

MaxQBi O95466.
PaxDbi O95466.
PRIDEi O95466.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331495 ; ENSP00000329219 ; ENSG00000184922 . [O95466-1 ]
GeneIDi 752.
KEGGi hsa:752.
UCSCi uc002iin.3. human. [O95466-1 ]
uc002iiq.3. human. [O95466-2 ]

Organism-specific databases

CTDi 752.
GeneCardsi GC17P043299.
HGNCi HGNC:1212. FMNL1.
HPAi HPA008129.
HPA028288.
MIMi 604656. gene.
neXtProti NX_O95466.
PharmGKBi PA28186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG149898.
GeneTreei ENSGT00760000118986.
HOVERGENi HBG053118.
InParanoidi O95466.
OMAi FSESTPM.
OrthoDBi EOG7F7W8J.
PhylomeDBi O95466.
TreeFami TF325155.

Miscellaneous databases

ChiTaRSi FMNL1. human.
GeneWikii FMNL1.
GenomeRNAii 752.
NextBioi 3034.
PROi O95466.
SOURCEi Search...

Gene expression databases

Bgeei O95466.
CleanExi HS_FMNL1.
ExpressionAtlasi O95466. baseline and differential.
Genevestigatori O95466.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR014767. Diaphanous_autoregulatory.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027657. FMNL1.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view ]
PANTHERi PTHR23213:SF188. PTHR23213:SF188. 1 hit.
Pfami PF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view ]
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
PROSITEi PS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human leukocyte formin: a new protein preferentially expressed in lymphocytes."
    Favaro P.M.B., Medina S.S., Basseres D.S., Costa F.F., Saad S.T.O.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Identification of novel tumor antigens in CLL by SEREX: assessment of their potential as targets for immunotherapeutic approaches."
    Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., Barrett P., Gribben J.G.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-1100 (ISOFORM 1).
  4. "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] OF 419-1100 (ISOFORMS 1 AND 2).
    Tissue: Brain and Lymph.
  5. "The NIK protein kinase and C17orf1 genes: chromosomal mapping, gene structures and mutational screening in frontotemporal dementia and parkinsonism linked to chromosome 17."
    Aronsson F.C., Magnusson P., Andersson B., Karsten S.L., Shibasaki Y., Lendon C.L., Goate A.M., Brookes A.J.
    Hum. Genet. 103:340-345(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 629-1100 (ISOFORM 2).
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 642-1100 (ISOFORM 2).
  7. "Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and induces polarized membrane blebbing."
    Han Y., Eppinger E., Schuster I.G., Weigand L.U., Liang X., Kremmer E., Peschel C., Krackhardt A.M.
    J. Biol. Chem. 284:33409-33417(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 668-1100 (ISOFORM 3), MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-184 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: INTERACTION WITH SRGAP2.

Entry informationi

Entry nameiFMNL_HUMAN
AccessioniPrimary (citable) accession number: O95466
Secondary accession number(s): D2DGW2
, Q6DKG5, Q6IBP3, Q86UH1, Q8N671, Q8TDH1, Q96H10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 16, 2009
Last modified: November 26, 2014
This is version 129 of the entry and version 3 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3