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P62962

- PROF1_MOUSE

UniProt

P62962 - PROF1_MOUSE

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Protein
Profilin-1
Gene
Pfn1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. Rho GTPase binding Source: BHF-UCL
  2. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  3. protein binding Source: IntAct

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. cellular response to growth factor stimulus Source: Ensembl
  3. neural tube closure Source: MGI
  4. positive regulation of DNA metabolic process Source: Ensembl
  5. positive regulation of stress fiber assembly Source: Ensembl
  6. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  7. positive regulation of viral transcription Source: Ensembl
  8. regulation of actin polymerization or depolymerization Source: MGI
  9. regulation of transcription from RNA polymerase II promoter Source: MGI
  10. sequestering of actin monomers Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_214043. PCP/CE pathway.
REACT_221567. Signaling by Robo receptor.

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-1
Alternative name(s):
Profilin I
Gene namesi
Name:Pfn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97549. Pfn1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoskeleton Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. extracellular region Source: Reactome
  5. neuron projection Source: Ensembl
  6. nucleus Source: MGI
  7. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 140139Profilin-1
PRO_0000199572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Cross-linki54 – 54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei108 – 1081N6-acetyllysine By similarity
Modified residuei129 – 1291Phosphotyrosine By similarity
Modified residuei138 – 1381Phosphoserine; by ROCK1 By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62962.
PaxDbiP62962.
PRIDEiP62962.

2D gel databases

REPRODUCTION-2DPAGEIPI00224740.
P62962.

PTM databases

PhosphoSiteiP62962.

Expressioni

Gene expression databases

ArrayExpressiP62962.
BgeeiP62962.
CleanExiMM_PFN1.
GenevestigatoriP62962.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
ESR1P033723EBI-647096,EBI-78473From a different organism.

Protein-protein interaction databases

BioGridi202126. 11 interactions.
DIPiDIP-38075N.
IntActiP62962. 6 interactions.
MINTiMINT-1868701.

Structurei

3D structure databases

ProteinModelPortaliP62962.
SMRiP62962. Positions 2-140.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.

Phylogenomic databases

eggNOGiNOG269129.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiP62962.
KOiK05759.
OrthoDBiEOG7JMGGT.
PhylomeDBiP62962.
TreeFamiTF331744.

Family and domain databases

InterProiIPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR01639. PROFILINMAML.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62962-1 [UniParc]FASTAAdd to Basket

« Hide

MAGWNAYIDS LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VSITPAEVGV    50
LVGKDRSSFF VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN 100
VTVTMTAKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY 140
Length:140
Mass (Da):14,957
Last modified:January 23, 2007 - v2
Checksum:i1DC8B60D545FF70E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14425 mRNA. Translation: CAA32586.1.
AK011066 mRNA. Translation: BAB27373.1.
BC002080 mRNA. Translation: AAH02080.1.
CCDSiCCDS24960.1.
PIRiS04067.
RefSeqiNP_035202.1. NM_011072.4.
UniGeneiMm.2647.

Genome annotation databases

EnsembliENSMUST00000018437; ENSMUSP00000018437; ENSMUSG00000018293.
GeneIDi18643.
KEGGimmu:18643.
UCSCiuc007jvv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14425 mRNA. Translation: CAA32586.1 .
AK011066 mRNA. Translation: BAB27373.1 .
BC002080 mRNA. Translation: AAH02080.1 .
CCDSi CCDS24960.1.
PIRi S04067.
RefSeqi NP_035202.1. NM_011072.4.
UniGenei Mm.2647.

3D structure databases

ProteinModelPortali P62962.
SMRi P62962. Positions 2-140.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202126. 11 interactions.
DIPi DIP-38075N.
IntActi P62962. 6 interactions.
MINTi MINT-1868701.

PTM databases

PhosphoSitei P62962.

2D gel databases

REPRODUCTION-2DPAGE IPI00224740.
P62962.

Proteomic databases

MaxQBi P62962.
PaxDbi P62962.
PRIDEi P62962.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018437 ; ENSMUSP00000018437 ; ENSMUSG00000018293 .
GeneIDi 18643.
KEGGi mmu:18643.
UCSCi uc007jvv.2. mouse.

Organism-specific databases

CTDi 5216.
MGIi MGI:97549. Pfn1.

Phylogenomic databases

eggNOGi NOG269129.
HOGENOMi HOG000171592.
HOVERGENi HBG053683.
InParanoidi P62962.
KOi K05759.
OrthoDBi EOG7JMGGT.
PhylomeDBi P62962.
TreeFami TF331744.

Enzyme and pathway databases

Reactomei REACT_214043. PCP/CE pathway.
REACT_221567. Signaling by Robo receptor.

Miscellaneous databases

NextBioi 294634.
PROi P62962.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62962.
Bgeei P62962.
CleanExi MM_PFN1.
Genevestigatori P62962.

Family and domain databases

InterProi IPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view ]
Pfami PF00235. Profilin. 1 hit.
[Graphical view ]
PRINTSi PR01639. PROFILINMAML.
SMARTi SM00392. PROF. 1 hit.
[Graphical view ]
SUPFAMi SSF55770. SSF55770. 1 hit.
PROSITEi PS00414. PROFILIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPROF1_MOUSE
AccessioniPrimary (citable) accession number: P62962
Secondary accession number(s): P10924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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