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P62962 (PROF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Profilin-1
Alternative name(s):
Profilin I
Gene names
Name:Pfn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR By similarity.

Subunit structure

Interacts with VASP. Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio. Found in a complex with XPO6, Ran, ACTB and PFN1 By similarity. Interacts with HTT By similarity.

Subcellular location

Cytoplasmcytoskeleton.

Post-translational modification

Phosphorylation at Ser-138 reduces its affinity for G-actin and blocks its interaction with HTT, reducing its ability to inhibit androgen receptor (AR) and HTT aggregation By similarity.

Sequence similarities

Belongs to the profilin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandActin-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from genetic interaction PubMed 10069337. Source: MGI

positive regulation of DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of viral transcription

Inferred from electronic annotation. Source: Ensembl

regulation of actin polymerization or depolymerization

Traceable author statement PubMed 11274401. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 15615774. Source: MGI

sequestering of actin monomers

Traceable author statement PubMed 11274401. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11274401. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 15615774. Source: MGI

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRho GTPase binding

Inferred from physical interaction PubMed 10445846. Source: BHF-UCL

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033723EBI-647096,EBI-78473From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 140139Profilin-1
PRO_0000199572

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1291Phosphotyrosine By similarity
Modified residue1381Phosphoserine; by ROCK1 By similarity
Cross-link54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P62962 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1DC8B60D545FF70E

FASTA14014,957
        10         20         30         40         50         60 
MAGWNAYIDS LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VSITPAEVGV LVGKDRSSFF 

        70         80         90        100        110        120 
VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN VTVTMTAKTL VLLMGKEGVH 

       130        140 
GGLINKKCYE MASHLRRSQY 

« Hide

References

« Hide 'large scale' references
[1]"Total coding sequence of profilin cDNA from Mus musculus macrophage."
Sri Widada J., Ferraz C., Liautard J.P.
Nucleic Acids Res. 17:2855-2855(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic liver.
[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].
Tissue: Mammary tumor.
[4]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 39-54; 57-70 AND 76-89, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14425 mRNA. Translation: CAA32586.1.
AK011066 mRNA. Translation: BAB27373.1.
BC002080 mRNA. Translation: AAH02080.1.
PIRS04067.
RefSeqNP_035202.1. NM_011072.4.
UniGeneMm.2647.

3D structure databases

ProteinModelPortalP62962.
SMRP62962. Positions 2-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202126. 10 interactions.
DIPDIP-38075N.
IntActP62962. 6 interactions.
MINTMINT-1868701.

PTM databases

PhosphoSiteP62962.

2D gel databases

REPRODUCTION-2DPAGEIPI00224740.
P62962.

Proteomic databases

PaxDbP62962.
PRIDEP62962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018437; ENSMUSP00000018437; ENSMUSG00000018293.
GeneID18643.
KEGGmmu:18643.
UCSCuc007jvv.2. mouse.

Organism-specific databases

CTD5216.
MGIMGI:97549. Pfn1.

Phylogenomic databases

eggNOGNOG269129.
HOGENOMHOG000171592.
HOVERGENHBG053683.
InParanoidP62962.
KOK05759.
OMAHLRRAQY.
OrthoDBEOG7JMGGT.
PhylomeDBP62962.
TreeFamTF331744.

Gene expression databases

ArrayExpressP62962.
BgeeP62962.
CleanExMM_PFN1.
GenevestigatorP62962.

Family and domain databases

InterProIPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]
PfamPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSPR01639. PROFILINMAML.
SMARTSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMSSF55770. SSF55770. 1 hit.
PROSITEPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294634.
PROP62962.
SOURCESearch...

Entry information

Entry namePROF1_MOUSE
AccessionPrimary (citable) accession number: P62962
Secondary accession number(s): P10924
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot