Reviewed, UniProtKB/Swiss-Prot P07737 (PROF1_HUMAN)

Names and origin

Protein names

Recommended name:
    Profilin-1
Alternative name(s):
    Profilin I

Gene names

Name:

PFN1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Found in a complex with XPO6, Ran, ACTB and PFN1.
Subcellular location	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the profilin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 140

139

Profilin-1

PRO_0000199571

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Modified residue

105

1

N6-acetyllysine Ref.7

Modified residue

129

1

Phosphotyrosine Ref.6 Ref.8

Cross-link

54

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Secondary structure

1

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140

Helix Strand Turn

Details...

Helix

5 – 12

8

Beta strand

17 – 24

8

Beta strand

26 – 28

3

Beta strand

30 – 34

5

Helix

40 – 42

3

Helix

45 – 51

7

Helix

58 – 60

3

Beta strand

64 – 66

3

Beta strand

69 – 76

8

Beta strand

80 – 82

3

Beta strand

85 – 90

6

Beta strand

93 – 96

4

Beta strand

100 – 105

6

Beta strand

107 – 115

9

Helix

121 – 137

17

Sequences

	Sequence		Length	Mass (Da)
	P07737-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F725119E55A289EB	FASTA	140	15,054
	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

References

	« Hide 'large scale' referencesShow '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: Epithelium.
[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. , 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.
[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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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.
[12]	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).
[13]	"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.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00216691.

PIR

A28622.

RefSeq

NP_005013.1.

UniGene

Hs.494691

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AWI	X-ray	2.20	A/B	3-140	[»]
1CF0	X-ray	2.20	A/B	3-140	[»]
1CJF	X-ray	2.30	A/B	2-140	[»]
1FIK	X-ray	2.30	A	2-139	[»]
1FIL	X-ray	2.00	A	2-139	[»]
1PFL	NMR	-	A	2-139	[»]
2PAV	X-ray	1.80	P	2-140	[»]
2PBD	X-ray	1.50	P	2-140	[»]
3CHW	X-ray	2.30	P	2-140	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:30N.

IntAct

P07737. 7 interactions.

PTM databases

PhosphoSite

P07737.

2-D gel databases

DOSAC-COBS-2DPAGE

P07737.

OGP

P07737.

REPRODUCTION-2DPAGE

IPI00216691.

Proteomic databases

PeptideAtlas

P07737.

PRIDE

P07737.

Genome annotation databases

Ensembl

ENSG00000108518. Homo sapiens. [Contig view]

GeneID

5216.

KEGG

hsa:5216.

Organism-specific databases

GeneCards

GC17M004789.

H-InvDB

HIX0013456.

HGNC

HGNC:8881. PFN1.

MIM

176610. gene.

PharmGKB

PA33219.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P07737.

HOVERGEN

P07737.

OMA

P07737. HLRRAQY.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

Bgee

P07737.

CleanEx

HS_PFN1.

GermOnline

ENSG00000108518. Homo sapiens.

Family and domain databases

InterPro

IPR002097. Profilin.
IPR005454. Profilin_mammal.
[Graphical view]

Pfam

PF00235. Profilin. 1 hit.
[Graphical view]

PRINTS

PR01639. PROFILINMAML.

SMART

SM00392. PROF. 1 hit.
[Graphical view]

PROSITE

PS00414. PROFILIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

20172.

PMAP-CutDB

P07737.

SOURCE

Search...

Entry information

Entry name

PROF1_HUMAN

Accession

Primary (citable) accession number: P07737

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)