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Profilin-1 (Epididymis tissue protein Li 184a) (Profilin I)

 PROF1_HUMAN             Reviewed;         140 AA.
P07737; Q53Y44;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-JUN-2018, entry version 204.
RecName: Full=Profilin-1;
AltName: Full=Epididymis tissue protein Li 184a;
AltName: Full=Profilin I;
Name=PFN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3356709;
Kwiatkowski D.J., Bruns G.A.P.;
"Human profilin. Molecular cloning, sequence comparison, and
chromosomal analysis.";
J. Biol. Chem. 263:5910-5915(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Epididymis;
PubMed=20736409; DOI=10.1074/mcp.M110.001719;
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.;
"Systematic mapping and functional analysis of a family of human
epididymal secretory sperm-located proteins.";
Mol. Cell. Proteomics 9:2517-2528(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Lung, Pancreas, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-140, AND ACETYLATION AT ALA-2.
PubMed=3342873; DOI=10.1016/0014-5793(88)80575-1;
Ampe C., Markey F., Lindberg U., Vandekerckhove J.;
"The primary structure of human platelet profilin: reinvestigation of
the calf spleen profilin sequence.";
FEBS Lett. 228:17-21(1988).
[9]
CHARACTERIZATION.
PubMed=7758455; DOI=10.1111/j.1432-1033.1995.tb20506.x;
Gieselmann R., Kwiatkowski D.J., Janmey P.A., Witke W.;
"Distinct biochemical characteristics of the two human profilin
isoforms.";
Eur. J. Biochem. 229:621-628(1995).
[10]
IDENTIFICATION IN A COMPLEX WITH RAN; ACTB AND XPO6.
PubMed=14592989; DOI=10.1093/emboj/cdg565;
Stueven T., Hartmann E., Goerlich D.;
"Exportin 6: a novel nuclear export receptor that is specific for
profilin.actin complexes.";
EMBO J. 22:5928-5940(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
FUNCTION, INTERACTION WITH HTT, AND PHOSPHORYLATION AT SER-138.
PubMed=18573880; DOI=10.1128/MCB.00079-08;
Shao J., Welch W.J., Diprospero N.A., Diamond M.I.;
"Phosphorylation of profilin by ROCK1 regulates polyglutamine
aggregation.";
Mol. Cell. Biol. 28:5196-5208(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-108, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
STRUCTURE BY NMR.
PubMed=8268157; DOI=10.1021/bi00213a010;
Metzler W.J., Constantine K.L., Friedrichs M.S., Bell A.J.,
Ernst E.G., Lavoie T.B., Mueller L.;
"Characterization of the three-dimensional solution structure of human
profilin: 1H, 13C, and 15N NMR assignments and global folding
pattern.";
Biochemistry 32:13818-13829(1993).
[24]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Fedorov A.A., Pollard T.D., Almo S.C.;
Submitted (APR-1996) to the PDB data bank.
[25]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
PubMed=9360613; DOI=10.1038/nsb1197-953;
Mahoney N.M., Janmey P.A., Almo S.C.;
"Structure of the profilin-poly-L-proline complex involved in
morphogenesis and cytoskeletal regulation.";
Nat. Struct. Biol. 4:953-960(1997).
[26]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH POLY-PRO.
PubMed=10404225; DOI=10.1038/10722;
Mahoney N.M., Rozwarski D.A., Fedorov E., Fedorov A.A., Almo S.C.;
"Profilin binds proline-rich ligands in two distinct amide backbone
orientations.";
Nat. Struct. Biol. 6:666-671(1999).
[27]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-140 IN COMPLEXES WITH VASP
AND MONOMERIC ACTIN, AND INTERACTION WITH VASP.
PubMed=17914456; DOI=10.1038/sj.emboj.7601874;
Ferron F., Rebowski G., Lee S.H., Dominguez R.;
"Structural basis for the recruitment of profilin-actin complexes
during filament elongation by Ena/VASP.";
EMBO J. 26:4597-4606(2007).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-140 IN COMPLEX WITH VASP
AND ACTIN.
PubMed=18689676; DOI=10.1073/pnas.0805852105;
Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R.;
"Modulation of actin structure and function by phosphorylation of Tyr-
53 and profilin binding.";
Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008).
[29]
VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND VAL-118, AND
CHARACTERIZATION OF VARIANTS ALS18 GLY-71; THR-114; GLY-117 AND
VAL-118.
PubMed=22801503; DOI=10.1038/nature11280;
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., 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.;
"Mutations in the profilin 1 gene cause familial amyotrophic lateral
sclerosis.";
Nature 488:499-503(2012).
-!- 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.
{ECO:0000269|PubMed:18573880}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:14592989, ECO:0000269|PubMed:17914456,
ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18689676}.
-!- INTERACTION:
P07830:act21 (xeno); NbExp=3; IntAct=EBI-713780, EBI-7195234;
P68135:ACTA1 (xeno); NbExp=2; IntAct=EBI-713780, EBI-367540;
P60709:ACTB; NbExp=2; IntAct=EBI-713780, EBI-353944;
Q92558:WASF1; NbExp=2; IntAct=EBI-713780, EBI-1548747;
O08816:Wasl (xeno); NbExp=4; IntAct=EBI-713780, EBI-6142604;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
{ECO:0000269|PubMed:20736409}.
-!- PTM: 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.
{ECO:0000269|PubMed:18573880}.
-!- 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. {ECO:0000269|PubMed:22801503}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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EMBL; J03191; AAA36486.1; -; mRNA.
EMBL; GU727630; ADU87632.1; -; mRNA.
EMBL; BT007001; AAP35647.1; -; mRNA.
EMBL; AK312168; BAG35102.1; -; mRNA.
EMBL; CR407670; CAG28598.1; -; mRNA.
EMBL; CH471108; EAW90381.1; -; Genomic_DNA.
EMBL; CH471108; EAW90383.1; -; Genomic_DNA.
EMBL; CH471108; EAW90384.1; -; Genomic_DNA.
EMBL; BC002475; AAH02475.1; -; mRNA.
EMBL; BC006768; AAH06768.1; -; mRNA.
EMBL; BC013439; AAH13439.1; -; mRNA.
EMBL; BC015164; AAH15164.1; -; mRNA.
EMBL; BC057828; AAH57828.1; -; mRNA.
CCDS; CCDS11061.1; -.
PIR; A28622; A28622.
RefSeq; NP_005013.1; NM_005022.3.
UniGene; Hs.494691; -.
PDB; 1AWI; X-ray; 2.20 A; A/B=3-140.
PDB; 1CF0; X-ray; 2.20 A; A/B=3-140.
PDB; 1CJF; X-ray; 2.30 A; A/B=2-140.
PDB; 1FIK; X-ray; 2.30 A; A=2-140.
PDB; 1FIL; X-ray; 2.00 A; A=2-140.
PDB; 1PFL; NMR; -; A=2-140.
PDB; 2PAV; X-ray; 1.80 A; P=2-140.
PDB; 2PBD; X-ray; 1.50 A; P=2-140.
PDB; 3CHW; X-ray; 2.30 A; P=2-140.
PDB; 4X1L; X-ray; 2.16 A; A=1-140.
PDB; 4X1M; X-ray; 2.17 A; A=1-140.
PDB; 4X25; X-ray; 2.23 A; A/B=1-140.
PDBsum; 1AWI; -.
PDBsum; 1CF0; -.
PDBsum; 1CJF; -.
PDBsum; 1FIK; -.
PDBsum; 1FIL; -.
PDBsum; 1PFL; -.
PDBsum; 2PAV; -.
PDBsum; 2PBD; -.
PDBsum; 3CHW; -.
PDBsum; 4X1L; -.
PDBsum; 4X1M; -.
PDBsum; 4X25; -.
ProteinModelPortal; P07737; -.
SMR; P07737; -.
BioGrid; 111237; 76.
CORUM; P07737; -.
DIP; DIP-30N; -.
IntAct; P07737; 50.
MINT; P07737; -.
STRING; 9606.ENSP00000225655; -.
DrugBank; DB07908; 7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN.
Allergome; 907; Hom s Profilin.
iPTMnet; P07737; -.
PhosphoSitePlus; P07737; -.
SwissPalm; P07737; -.
BioMuta; PFN1; -.
DMDM; 130979; -.
DOSAC-COBS-2DPAGE; P07737; -.
OGP; P07737; -.
REPRODUCTION-2DPAGE; IPI00216691; -.
UCD-2DPAGE; P07737; -.
EPD; P07737; -.
PaxDb; P07737; -.
PeptideAtlas; P07737; -.
PRIDE; P07737; -.
ProteomicsDB; 52024; -.
TopDownProteomics; P07737; -.
DNASU; 5216; -.
Ensembl; ENST00000225655; ENSP00000225655; ENSG00000108518.
GeneID; 5216; -.
KEGG; hsa:5216; -.
UCSC; uc002gaa.5; human.
CTD; 5216; -.
DisGeNET; 5216; -.
EuPathDB; HostDB:ENSG00000108518.7; -.
GeneCards; PFN1; -.
GeneReviews; PFN1; -.
HGNC; HGNC:8881; PFN1.
HPA; CAB037134; -.
HPA; CAB037140; -.
MalaCards; PFN1; -.
MIM; 176610; gene.
MIM; 614808; phenotype.
neXtProt; NX_P07737; -.
OpenTargets; ENSG00000108518; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
PharmGKB; PA33219; -.
eggNOG; KOG1755; Eukaryota.
eggNOG; ENOG41126PD; LUCA.
GeneTree; ENSGT00390000010143; -.
HOGENOM; HOG000171592; -.
HOVERGEN; HBG053683; -.
InParanoid; P07737; -.
KO; K05759; -.
OMA; HLRRAQY; -.
PhylomeDB; P07737; -.
TreeFam; TF331744; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-4086400; PCP/CE pathway.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
SIGNOR; P07737; -.
ChiTaRS; PFN1; human.
EvolutionaryTrace; P07737; -.
GeneWiki; Profilin_1; -.
GenomeRNAi; 5216; -.
PMAP-CutDB; P07737; -.
PRO; PR:P07737; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108518; -.
CleanEx; HS_PFN1; -.
ExpressionAtlas; P07737; baseline and differential.
Genevisible; P07737; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IPI:UniProtKB.
GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IMP:UniProtKB.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IBA:GO_Central.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:UniProtKB.
GO; GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:1900029; P:positive regulation of ruffle assembly; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
CDD; cd00148; PROF; 1.
InterPro; IPR005455; PFN.
InterPro; IPR036140; PFN_sf.
InterPro; IPR005454; Profilin1/2/3_vertebrate.
InterPro; IPR027310; Profilin_CS.
Pfam; PF00235; Profilin; 1.
PRINTS; PR01639; PROFILINMAML.
SMART; SM00392; PROF; 1.
SUPFAM; SSF55770; SSF55770; 1.
PROSITE; PS00414; PROFILIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding;
Amyotrophic lateral sclerosis; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disease mutation;
Isopeptide bond; Neurodegeneration; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:3342873}.
CHAIN 2 140 Profilin-1.
/FTId=PRO_0000199571.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:3342873}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:P62963}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 129 129 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 138 138 Phosphoserine; by ROCK1.
{ECO:0000269|PubMed:18573880}.
CROSSLNK 54 54 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 54 54 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
VARIANT 71 71 C -> G (in ALS18; the mutant protein is
detected in the insoluble fraction of
cells; dbSNP:rs387907264).
{ECO:0000269|PubMed:22801503}.
/FTId=VAR_068925.
VARIANT 114 114 M -> T (in ALS18; the mutant protein is
detected in the insoluble fraction of
cells; dbSNP:rs387907265).
{ECO:0000269|PubMed:22801503}.
/FTId=VAR_068926.
VARIANT 117 117 E -> G (in ALS18; unknown pathological
significance; like the wild-type the
mutant protein is detected in the soluble
fraction of cells; dbSNP:rs140547520).
{ECO:0000269|PubMed:22801503}.
/FTId=VAR_068927.
VARIANT 118 118 G -> V (in ALS18; the mutant protein is
detected in the insoluble fraction of
cells; dbSNP:rs387907266).
{ECO:0000269|PubMed:22801503}.
/FTId=VAR_068928.
HELIX 5 12 {ECO:0000244|PDB:2PBD}.
STRAND 13 15 {ECO:0000244|PDB:4X1L}.
STRAND 17 28 {ECO:0000244|PDB:2PBD}.
STRAND 30 34 {ECO:0000244|PDB:2PBD}.
HELIX 40 42 {ECO:0000244|PDB:2PBD}.
HELIX 45 52 {ECO:0000244|PDB:2PBD}.
HELIX 58 60 {ECO:0000244|PDB:2PBD}.
STRAND 64 66 {ECO:0000244|PDB:2PBD}.
STRAND 69 77 {ECO:0000244|PDB:2PBD}.
STRAND 78 80 {ECO:0000244|PDB:1FIL}.
TURN 81 83 {ECO:0000244|PDB:2PBD}.
STRAND 85 90 {ECO:0000244|PDB:2PBD}.
STRAND 93 96 {ECO:0000244|PDB:1AWI}.
STRAND 100 105 {ECO:0000244|PDB:2PBD}.
STRAND 107 115 {ECO:0000244|PDB:2PBD}.
HELIX 121 137 {ECO:0000244|PDB:2PBD}.
SEQUENCE 140 AA; 15054 MW; F725119E55A289EB CRC64;
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY
VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH
GGLINKKCYE MASHLRRSQY


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