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O75955 (FLOT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flotillin-1
Gene names
Name:FLOT1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.

Subunit structure

Heterooligomeric complex of flotillin-1 and flotillin-2 and caveolin-1 and caveolin-2 By similarity. Interacts with ECM29. Ref.12

Subcellular location

Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein. Melanosome. Endosome. Note: Membrane-associated protein of caveolae. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.6 Ref.12

Sequence similarities

Belongs to the band 7/mec-2 family. Flotillin subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcentriolar satellite

Inferred from direct assay. Source: BHF-UCL

endosome

Inferred from direct assay Ref.12. Source: UniProtKB

integral to membrane

Traceable author statement. Source: ProtInc

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane fraction

Inferred from direct assay. Source: BHF-UCL

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050675EBI-603643,EBI-77613

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Flotillin-1
PRO_0000094044

Amino acid modifications

Modified residue191Phosphoserine Ref.8 Ref.9
Modified residue2031Phosphotyrosine Ref.7
Modified residue3851Phosphoserine Ref.11
Modified residue3871Phosphothreonine Ref.10

Natural variations

Natural variant521S → N.
Corresponds to variant rs3180825 [ dbSNP | Ensembl ].
VAR_048415

Experimental info

Sequence conflict1141H → N in AAD40192. Ref.2
Sequence conflict1141H → N in AAF17215. Ref.5
Sequence conflict250 – 2534EEQR → DFSQ in AAF17215. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O75955 [UniParc].

Last modified November 28, 2002. Version 3.
Checksum: C69E5421E565F53A

FASTA42747,355
        10         20         30         40         50         60 
MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG 

        70         80         90        100        110        120 
VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI 

       130        140        150        160        170        180 
YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE 

       190        200        210        220        230        240 
AEAKRDAGIR EAKAKQEKVS AQYLSEIEMA KAQRDYELKK AAYDIEVNTR RAQADLAYQL 

       250        260        270        280        290        300 
QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYKLERLAEA 

       310        320        330        340        350        360 
EKSQLIMQAE AEAASVRMRG EAEAFAIGAR ARAEAEQMAK KAEAFQLYQE AAQLDMLLEK 

       370        380        390        400        410        420 
LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LTRLPESVER LTGVSISQVN 


HKPLRTA 

« Hide

References

« Hide 'large scale' references
[1]"Flotillin-1: gene structure: cDNA cloning from human lung and the identification of alternative polyadenylation signals."
Edgar A.J., Polak J.M.
Int. J. Biochem. Cell Biol. 33:53-64(2001) [PubMed: 11167132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[3]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-253.
Tissue: Adrenal gland.
[6]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
Tissue: Melanoma.
[7]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[8]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-387, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[12]"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
J. Biol. Chem. 285:31616-31633(2010) [PubMed: 20682791] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF089750 mRNA. Translation: AAC35387.1.
AF085357 mRNA. Translation: AAD40192.1.
BA000025 Genomic DNA. Translation: BAB63320.1.
BC001146 mRNA. Translation: AAH01146.1.
AF117234 mRNA. Translation: AAF17215.1.
IPIIPI00027438.
RefSeqNP_005794.1. NM_005803.2.
UniGeneHs.179986.

3D structure databases

ProteinModelPortalO75955.
SMRO75955. Positions 36-173.
ModBaseSearch...

Protein-protein interaction databases

IntActO75955. 13 interactions.
MINTMINT-3002104.
STRINGO75955.

PTM databases

PhosphoSiteO75955.

Proteomic databases

PRIDEO75955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376389; ENSP00000365569; ENSG00000137312.
ENST00000383382; ENSP00000372873; ENSG00000206379.
ENST00000383562; ENSP00000373056; ENSG00000206480.
ENST00000436822; ENSP00000391438; ENSG00000232280.
ENST00000444632; ENSP00000388861; ENSG00000230143.
GeneID10211.
KEGGhsa:10211.
UCSCuc003nrm.1. human.

Organism-specific databases

CTD10211.
GeneCardsGC06M030695.
HGNCHGNC:3757. FLOT1.
HPACAB007766.
HPA001393.
MIM606998. gene.
neXtProtNX_O75955.
PharmGKBPA28175.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG729052.
HOVERGENHBG051628.
InParanoidO75955.
OMAQRAIMGS.
OrthoDBEOG473PRK.
PhylomeDBO75955.

Gene expression databases

CleanExHS_FLOT1.
GenevestigatorO75955.
GermOnlineENSG00000137312. Homo sapiens.

Family and domain databases

InterProIPR001107. Band_7.
[Graphical view]
KOK07192.
PfamPF01145. Band_7. 1 hit.
[Graphical view]
SMARTSM00244. PHB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio38660.
SOURCESearch...

Entry information

Entry nameFLOT1_HUMAN
AccessionPrimary (citable) accession number: O75955
Secondary accession number(s): Q969J8, Q9UHW1, Q9UNV8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 28, 2002
Last modified: January 25, 2012
This is version 106 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.

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Human chromosome 6: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families