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P35080 (PROF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Profilin-2
Alternative name(s):
Profilin II
Gene names
Name:PFN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Subunit structure

Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Highly expressed in brain, skeletal muscle and kidney and less strongly in heart, placenta, lung and liver.

Sequence similarities

Belongs to the profilin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

negative regulation of actin filament polymerization

Inferred from direct assay Ref.7. Source: UniProt

negative regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

negative regulation of ruffle assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

positive regulation of ATPase activity

Inferred from direct assay Ref.7. Source: UniProt

positive regulation of actin filament bundle assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

positive regulation of actin filament polymerization

Inferred from genetic interaction PubMed 23153535. Source: UniProt

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

positive regulation of stress fiber assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

regulation of synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin monomer binding

Inferred from physical interaction Ref.7. Source: UniProt

adenyl-nucleotide exchange factor activity

Inferred from direct assay Ref.7. Source: UniProt

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.7. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GOLGB1Q147892EBI-473138,EBI-709973
HTTP428584EBI-473138,EBI-466029
WaslO088163EBI-473138,EBI-6142604From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform IIa (identifier: P35080-1)

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.
Isoform IIb (identifier: P35080-2)

The sequence of this isoform differs from the canonical sequence as follows:
     109-140: VLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF → ALVIVMGKEGVHGGTLNKKAYELALYLRRSDV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 140139Profilin-2
PRO_0000199575

Amino acid modifications

Modified residue21N-acetylalanine Ref.9

Natural variations

Alternative sequence109 – 14032VLVFV…RDSGF → ALVIVMGKEGVHGGTLNKKA YELALYLRRSDV in isoform IIb.
VSP_005217

Experimental info

Sequence conflict651T → A in AAH18049. Ref.5

Secondary structure

............................. 140
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: F43884E1427C9A99

FASTA14015,046
        10         20         30         40         50         60 
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF 

        70         80         90        100        110        120 
TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH 

       130        140 
GGGLNKKAYS MAKYLRDSGF 

« Hide

Isoform IIb [UniParc].

Checksum: B4CAC8A1ED8C658B
Show »

FASTA14015,088

References

« Hide 'large scale' references
[1]"Cloning and expression of a novel human profilin variant, profilin II."
Honore B., Madsen P.S., Andersen A.H., Leffers H.
FEBS Lett. 330:151-155(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB).
Tissue: Epithelium.
[2]"Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties."
Lambrechts A., Braun A., Jonckheere V., Aszodi A., Lanier L.M., Robbens J., Van Colen I., Vandekerckhove J., Faessler R., Ampe C.
Mol. Cell. Biol. 20:8209-8219(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIA).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IIA AND IIB).
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS IIA AND IIB).
Tissue: Brain, Lung and Spinal cord.
[6]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 30-69; 76-89; 92-105 AND 109-116, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[7]"Distinct biochemical characteristics of the two human profilin isoforms."
Gieselmann R., Kwiatkowski D.J., Janmey P.A., Witke W.
Eur. J. Biochem. 229:621-628(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"X-ray structure determination of human profilin II: a comparative structural analysis of human profilins."
Nodelman I.M., Bowman G.D., Lindberg U., Schutt C.E.
J. Mol. Biol. 294:1271-1285(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10678 mRNA. Translation: AAA03022.1.
AF228738 mRNA. Translation: AAG24949.1.
AK311780 mRNA. Translation: BAG34723.1.
AK311782 mRNA. Translation: BAG34725.1.
CH471052 Genomic DNA. Translation: EAW78850.1.
BC002964 mRNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78852.1.
BC018049 mRNA. Translation: AAH18049.1.
BC043646 mRNA. Translation: AAH43646.1.
BC095444 mRNA. Translation: AAH95444.1.
PIRS36804.
RefSeqNP_002619.1. NM_002628.4.
NP_444252.1. NM_053024.3.
UniGeneHs.91747.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D1JX-ray2.20A/B/C/D2-136[»]
ProteinModelPortalP35080.
SMRP35080. Positions 2-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111238. 31 interactions.
IntActP35080. 26 interactions.
MINTMINT-1370857.
STRING9606.ENSP00000239940.

PTM databases

PhosphoSiteP35080.

Polymorphism databases

DMDM20178322.

2D gel databases

REPRODUCTION-2DPAGEP35080.

Proteomic databases

PaxDbP35080.
PRIDEP35080.

Protocols and materials databases

DNASU5217.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000239940; ENSP00000239940; ENSG00000070087. [P35080-1]
ENST00000452853; ENSP00000410464; ENSG00000070087. [P35080-2]
GeneID5217.
KEGGhsa:5217.
UCSCuc003ext.1. human. [P35080-1]
uc003exu.1. human. [P35080-2]

Organism-specific databases

CTD5217.
GeneCardsGC03M149682.
HGNCHGNC:8882. PFN2.
HPACAB037073.
HPA035611.
MIM176590. gene.
neXtProtNX_P35080.
PharmGKBPA33220.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295243.
HOGENOMHOG000171592.
HOVERGENHBG053683.
InParanoidP35080.
KOK05759.
OMALGGKKCS.
OrthoDBEOG7JMGGT.
PhylomeDBP35080.
TreeFamTF331744.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP35080.
BgeeP35080.
CleanExHS_PFN2.
GenevestigatorP35080.

Family and domain databases

InterProIPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]
PfamPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSPR00392. PROFILIN.
PR01639. PROFILINMAML.
SMARTSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMSSF55770. SSF55770. 1 hit.
PROSITEPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPFN2. human.
EvolutionaryTraceP35080.
GeneWikiPFN2.
GenomeRNAi5217.
NextBio20176.
PROP35080.
SOURCESearch...

Entry information

Entry namePROF2_HUMAN
AccessionPrimary (citable) accession number: P35080
Secondary accession number(s): B2R4C8 expand/collapse secondary AC list , D3DNI4, Q4VBQ4, Q8WVF9, Q9HBK2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM