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P07737 (PROF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 134. 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·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
OrganismHomo sapiens (Human)
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. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. Ref.10

Subunit structure

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. Interacts with VASP. Interacts with HTT. Ref.10 Ref.20

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.

Sequence similarities

Belongs to the profilin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 140139Profilin-1
PRO_0000199571

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.11
Modified residue851Phosphoserine Ref.13
Modified residue1051N6-acetyllysine Ref.7 Ref.14
Modified residue1081N6-acetyllysine Ref.14
Modified residue1291Phosphotyrosine Ref.6 Ref.8 Ref.12
Modified residue1381Phosphoserine; by ROCK1 Ref.10
Cross-link54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P07737 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F725119E55A289EB

FASTA14015,054
        10         20         30         40         50         60 
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY 

        70         80         90        100        110        120 
VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH 

       130        140 
GGLINKKCYE MASHLRRSQY 

« Hide

References

« Hide 'large scale' references
[1]"Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis."
Kwiatkowski D.J., Bruns G.A.P.
J. Biol. Chem. 263:5910-5915(1988) [PubMed: 3356709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Colon, Lung, Pancreas and Placenta.
[3]"The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence."
Ampe C., Markey F., Lindberg U., Vandekerckhove J.
FEBS Lett. 228:17-21(1988) [PubMed: 3342873] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-140, ACETYLATION AT ALA-2.
[4]"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: 7758455] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes."
Stueven T., Hartmann E., Goerlich D.
EMBO J. 22:5928-5940(2003) [PubMed: 14592989] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; ACTB AND XPO6.
[6]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, MASS SPECTROMETRY.
[7]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"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-129, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[9]"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry."
Meierhofer D., Wang X., Huang L., Kaiser P.
J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-54, MASS SPECTROMETRY.
[10]"Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation."
Shao J., Welch W.J., Diprospero N.A., Diamond M.I.
Mol. Cell. Biol. 28:5196-5208(2008) [PubMed: 18573880] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HTT, PHOSPHORYLATION AT SER-138.
[11]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[12]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[13]"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-85, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-108, MASS SPECTROMETRY.
[15]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern."
Metzler W.J., Constantine K.L., Friedrichs M.S., Bell A.J., Ernst E.G., Lavoie T.B., Mueller L.
Biochemistry 32:13818-13829(1993) [PubMed: 8268157] [Abstract]
Cited for: STRUCTURE BY NMR.
[17]Fedorov A.A., Pollard T.D., Almo S.C.
Submitted (APR-1996) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[18]"Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation."
Mahoney N.M., Janmey P.A., Almo S.C.
Nat. Struct. Biol. 4:953-960(1997) [PubMed: 9360613] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
[19]"Profilin binds proline-rich ligands in two distinct amide backbone orientations."
Mahoney N.M., Rozwarski D.A., Fedorov E., Fedorov A.A., Almo S.C.
Nat. Struct. Biol. 6:666-671(1999) [PubMed: 10404225] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
[20]"Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP."
Ferron F., Rebowski G., Lee S.H., Dominguez R.
EMBO J. 26:4597-4606(2007) [PubMed: 17914456] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-140 IN COMPLEXES WITH VASP AND MONOMERIC ACTIN, INTERACTION WITH VASP.
[21]"Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding."
Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R.
Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008) [PubMed: 18689676] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-140 IN COMPLEX WITH VASP AND ACTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03191 mRNA. Translation: AAA36486.1.
BC002475 mRNA. Translation: AAH02475.1.
BC006768 mRNA. Translation: AAH06768.1.
BC013439 mRNA. Translation: AAH13439.1.
BC015164 mRNA. Translation: AAH15164.1.
BC057828 mRNA. Translation: AAH57828.1.
IPIIPI00216691.
PIRA28622.
RefSeqNP_005013.1. NM_005022.2.
UniGeneHs.494691.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWIX-ray2.20A/B3-140[»]
1CF0X-ray2.20A/B3-140[»]
1CJFX-ray2.30A/B2-140[»]
1FIKX-ray2.30A2-139[»]
1FILX-ray2.00A2-139[»]
1PFLNMR-A2-139[»]
2PAVX-ray1.80P2-140[»]
2PBDX-ray1.50P2-140[»]
3CHWX-ray2.30P2-140[»]
ProteinModelPortalP07737.
SMRP07737. Positions 2-140.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-30N.
IntActP07737. 20 interactions.
MINTMINT-1372667.
STRINGP07737.

Protein family/group databases

Allergome907. Hom s Profilin.

PTM databases

PhosphoSiteP07737.

Polymorphism databases

DMDM130979.

2D gel databases

DOSAC-COBS-2DPAGEP07737.
OGPP07737.
REPRODUCTION-2DPAGEIPI00216691.
UCD-2DPAGEP07737.

Proteomic databases

PeptideAtlasP07737.
PRIDEP07737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225655; ENSP00000225655; ENSG00000108518.
GeneID5216.
KEGGhsa:5216.
UCSCuc002gaa.1. human.

Organism-specific databases

CTD5216.
GeneCardsGC17M004848.
H-InvDBHIX0013456.
HGNCHGNC:8881. PFN1.
HPACAB037140.
MIM176610. gene.
neXtProtNX_P07737.
PharmGKBPA33219.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG16742.
HOGENOMHBG506540.
HOVERGENHBG053683.
InParanoidP07737.
OMAHLRRAQY.
OrthoDBEOG4SN1Q1.
PhylomeDBP07737.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP07737.
BgeeP07737.
CleanExHS_PFN1.
GenevestigatorP07737.
GermOnlineENSG00000108518. Homo sapiens.

Family and domain databases

InterProIPR002097. Profilin.
IPR005454. Profilin_mammal.
[Graphical view]
KOK05759.
PfamPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSPR01639. PROFILINMAML.
SMARTSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMSSF55770. Profilin. 1 hit.
PROSITEPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20172.
PMAP-CutDBP07737.
SOURCESearch...

Entry information

Entry namePROF1_HUMAN
AccessionPrimary (citable) accession number: P07737
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 134 of the entry and version 2 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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families