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P07737 (PROF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
Epididymis tissue protein Li 184a
Profilin I
Gene names
Name:PFN1
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. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. Ref.12

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.12 Ref.22

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Expressed in epididymis (at protein level). Ref.2

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.

Involvement in disease

Amyotrophic lateral sclerosis 18 (ALS18) [MIM:614808]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

Sequence similarities

Belongs to the profilin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   DiseaseAmyotrophic lateral sclerosis
Disease mutation
Neurodegeneration
   LigandActin-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

blood coagulation

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of actin filament bundle assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

negative regulation of actin filament polymerization

Inferred from direct assay Ref.9. Source: UniProt

negative regulation of stress fiber assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

neural tube closure

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of ATPase activity

Inferred from direct assay Ref.9. Source: UniProt

positive regulation of DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from genetic interaction PubMed 23153535. Source: UniProt

positive regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

positive regulation of ruffle assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

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

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin binding

Inferred from physical interaction Ref.22Ref.9. Source: UniProtKB

adenyl-nucleotide exchange factor activity

Inferred from direct assay Ref.9. Source: UniProt

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.9. Source: UniProt

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

proline-rich region binding

Inferred from physical interaction Ref.22. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WASF1Q925582EBI-713780,EBI-1548747
WaslO088164EBI-713780,EBI-6142604From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 140139Profilin-1
PRO_0000199571

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.13 Ref.17
Modified residue851Phosphoserine Ref.14
Modified residue1051N6-acetyllysine Ref.15
Modified residue1081N6-acetyllysine Ref.15
Modified residue1291Phosphotyrosine Ref.11
Modified residue1381Phosphoserine; by ROCK1 Ref.12
Cross-link54Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Natural variant711C → G in ALS18; the mutant protein is detected in the insoluble fraction of cells. Ref.24
VAR_068925
Natural variant1141M → T in ALS18; the mutant protein is detected in the insoluble fraction of cells. Ref.24
VAR_068926
Natural variant1171E → G in ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells. Ref.24
Corresponds to variant rs140547520 [ dbSNP | Ensembl ].
VAR_068927
Natural variant1181G → V in ALS18; the mutant protein is detected in the insoluble fraction of cells. Ref.24
VAR_068928

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Epididymis.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Tissue: Brain.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]Mural R.J., Istrail S., Sutton 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].
[7]"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: Colon, Lung, Pancreas and Placenta.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-140, ACETYLATION AT ALA-2.
[9]"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.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; ACTB AND XPO6.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HTT, PHOSPHORYLATION AT SER-138.
[13]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"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].
[18]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]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).
[20]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
[21]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
[22]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-140 IN COMPLEXES WITH VASP AND MONOMERIC ACTIN, INTERACTION WITH VASP.
[23]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-140 IN COMPLEX WITH VASP AND ACTIN.
[24]"Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis."
Wu C.H., Fallini C., Ticozzi N., Keagle P.J., Sapp P.C., Piotrowska K., Lowe P., Koppers M., McKenna-Yasek D., Baron D.M., Kost J.E., Gonzalez-Perez P., Fox A.D., Adams J., Taroni F., Tiloca C., Leclerc A.L., Chafe S.C. expand/collapse author list , Mangroo D., Moore M.J., Zitzewitz J.A., Xu Z.S., van den Berg L.H., Glass J.D., Siciliano G., Cirulli E.T., Goldstein D.B., Salachas F., Meininger V., Rossoll W., Ratti A., Gellera C., Bosco D.A., Bassell G.J., Silani V., Drory V.E., Brown R.H. Jr., Landers J.E.
Nature 488:499-503(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118, CHARACTERIZATION OF VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03191 mRNA. Translation: AAA36486.1.
GU727630 mRNA. Translation: ADU87632.1.
BT007001 mRNA. Translation: AAP35647.1.
AK312168 mRNA. Translation: BAG35102.1.
CR407670 mRNA. Translation: CAG28598.1.
CH471108 Genomic DNA. Translation: EAW90381.1.
CH471108 Genomic DNA. Translation: EAW90383.1.
CH471108 Genomic DNA. Translation: EAW90384.1.
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.
PIRA28622.
RefSeqNP_005013.1. NM_005022.3.
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-ray2.30A2-140[»]
1FILX-ray2.00A2-140[»]
1PFLNMR-A2-140[»]
2PAVX-ray1.80P2-140[»]
2PBDX-ray1.50P2-140[»]
3CHWX-ray2.30P2-140[»]
ProteinModelPortalP07737.
SMRP07737. Positions 2-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111237. 45 interactions.
DIPDIP-30N.
IntActP07737. 37 interactions.
MINTMINT-1372667.
STRING9606.ENSP00000225655.

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

PaxDbP07737.
PeptideAtlasP07737.
PRIDEP07737.

Protocols and materials databases

DNASU5216.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225655; ENSP00000225655; ENSG00000108518.
GeneID5216.
KEGGhsa:5216.
UCSCuc002gaa.4. human.

Organism-specific databases

CTD5216.
GeneCardsGC17M004848.
HGNCHGNC:8881. PFN1.
HPACAB037134.
CAB037140.
MIM176610. gene.
614808. phenotype.
neXtProtNX_P07737.
Orphanet803. Amyotrophic lateral sclerosis.
PharmGKBPA33219.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269129.
HOGENOMHOG000171592.
HOVERGENHBG053683.
InParanoidP07737.
KOK05759.
OMAHLRRAQY.
OrthoDBEOG7JMGGT.
PhylomeDBP07737.
TreeFamTF331744.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP07737.
BgeeP07737.
CleanExHS_PFN1.
GenevestigatorP07737.

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

ChiTaRSPFN1. human.
EvolutionaryTraceP07737.
GeneWikiProfilin_1.
GenomeRNAi5216.
NextBio20172.
PMAP-CutDBP07737.
PROP07737.
SOURCESearch...

Entry information

Entry namePROF1_HUMAN
AccessionPrimary (citable) accession number: P07737
Secondary accession number(s): Q53Y44
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 159 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

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

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