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P35080

- PROF2_HUMAN

UniProt

P35080 - PROF2_HUMAN

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Protein
Profilin-2
Gene
PFN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. actin monomer binding Source: UniProt
  2. adenyl-nucleotide exchange factor activity Source: UniProt
  3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProt
  4. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. actin cytoskeleton organization Source: InterPro
  2. negative regulation of actin filament polymerization Source: UniProt
  3. negative regulation of epithelial cell migration Source: UniProt
  4. negative regulation of ruffle assembly Source: UniProt
  5. positive regulation of ATPase activity Source: UniProt
  6. positive regulation of actin filament bundle assembly Source: UniProt
  7. positive regulation of actin filament polymerization Source: UniProt
  8. positive regulation of peptidyl-serine phosphorylation Source: UniProt
  9. positive regulation of stress fiber assembly Source: UniProt
  10. regulation of synaptic vesicle exocytosis Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_19351. Signaling by Robo receptor.

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-2
Alternative name(s):
Profilin II
Gene namesi
Name:PFN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:8882. PFN2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProt
  4. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33220.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 140139Profilin-2
PRO_0000199575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP35080.
PaxDbiP35080.
PRIDEiP35080.

2D gel databases

REPRODUCTION-2DPAGEP35080.

PTM databases

PhosphoSiteiP35080.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP35080.
BgeeiP35080.
CleanExiHS_PFN2.
GenevestigatoriP35080.

Organism-specific databases

HPAiCAB037073.
HPA035611.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGB1Q147892EBI-473138,EBI-709973
HTTP428584EBI-473138,EBI-466029
WaslO088163EBI-473138,EBI-6142604From a different organism.

Protein-protein interaction databases

BioGridi111238. 32 interactions.
IntActiP35080. 26 interactions.
MINTiMINT-1370857.
STRINGi9606.ENSP00000239940.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 117
Beta strandi17 – 248
Beta strandi26 – 283
Beta strandi30 – 345
Helixi40 – 423
Helixi45 – 528
Helixi58 – 625
Beta strandi64 – 663
Beta strandi69 – 8012
Beta strandi85 – 906
Beta strandi93 – 953
Beta strandi100 – 1056
Beta strandi107 – 1159
Helixi121 – 13717

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D1JX-ray2.20A/B/C/D2-138[»]
ProteinModelPortaliP35080.
SMRiP35080. Positions 2-140.

Miscellaneous databases

EvolutionaryTraceiP35080.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.

Phylogenomic databases

eggNOGiNOG295243.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiP35080.
KOiK05759.
OMAiLAYHVAC.
OrthoDBiEOG7JMGGT.
PhylomeDBiP35080.
TreeFamiTF331744.

Family and domain databases

InterProiIPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view]
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01639. PROFILINMAML.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform IIa (identifier: P35080-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM    50
IVGKDREGFF TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN 100
VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF 140
Length:140
Mass (Da):15,046
Last modified:January 23, 2007 - v3
Checksum:iF43884E1427C9A99
GO
Isoform IIb (identifier: P35080-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:140
Mass (Da):15,088
Checksum:iB4CAC8A1ED8C658B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei109 – 14032VLVFV…RDSGF → ALVIVMGKEGVHGGTLNKKA YELALYLRRSDV in isoform IIb.
VSP_005217Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651T → A in AAH18049. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3148.1. [P35080-1]
CCDS46934.1. [P35080-2]
PIRiS36804.
RefSeqiNP_002619.1. NM_002628.4. [P35080-2]
NP_444252.1. NM_053024.3. [P35080-1]
UniGeneiHs.91747.

Genome annotation databases

EnsembliENST00000239940; ENSP00000239940; ENSG00000070087. [P35080-1]
ENST00000452853; ENSP00000410464; ENSG00000070087. [P35080-2]
GeneIDi5217.
KEGGihsa:5217.
UCSCiuc003ext.1. human. [P35080-1]
uc003exu.1. human. [P35080-2]

Polymorphism databases

DMDMi20178322.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3148.1. [P35080-1 ]
CCDS46934.1. [P35080-2 ]
PIRi S36804.
RefSeqi NP_002619.1. NM_002628.4. [P35080-2 ]
NP_444252.1. NM_053024.3. [P35080-1 ]
UniGenei Hs.91747.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D1J X-ray 2.20 A/B/C/D 2-138 [» ]
ProteinModelPortali P35080.
SMRi P35080. Positions 2-140.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111238. 32 interactions.
IntActi P35080. 26 interactions.
MINTi MINT-1370857.
STRINGi 9606.ENSP00000239940.

PTM databases

PhosphoSitei P35080.

Polymorphism databases

DMDMi 20178322.

2D gel databases

REPRODUCTION-2DPAGE P35080.

Proteomic databases

MaxQBi P35080.
PaxDbi P35080.
PRIDEi P35080.

Protocols and materials databases

DNASUi 5217.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000239940 ; ENSP00000239940 ; ENSG00000070087 . [P35080-1 ]
ENST00000452853 ; ENSP00000410464 ; ENSG00000070087 . [P35080-2 ]
GeneIDi 5217.
KEGGi hsa:5217.
UCSCi uc003ext.1. human. [P35080-1 ]
uc003exu.1. human. [P35080-2 ]

Organism-specific databases

CTDi 5217.
GeneCardsi GC03M149682.
HGNCi HGNC:8882. PFN2.
HPAi CAB037073.
HPA035611.
MIMi 176590. gene.
neXtProti NX_P35080.
PharmGKBi PA33220.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295243.
HOGENOMi HOG000171592.
HOVERGENi HBG053683.
InParanoidi P35080.
KOi K05759.
OMAi LAYHVAC.
OrthoDBi EOG7JMGGT.
PhylomeDBi P35080.
TreeFami TF331744.

Enzyme and pathway databases

Reactomei REACT_19351. Signaling by Robo receptor.

Miscellaneous databases

ChiTaRSi PFN2. human.
EvolutionaryTracei P35080.
GeneWikii PFN2.
GenomeRNAii 5217.
NextBioi 20176.
PROi P35080.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35080.
Bgeei P35080.
CleanExi HS_PFN2.
Genevestigatori P35080.

Family and domain databases

InterProi IPR005454. Profilin_chordates.
IPR027310. Profilin_CS.
IPR005455. Profilin_eukaryotes/bac.
[Graphical view ]
Pfami PF00235. Profilin. 1 hit.
[Graphical view ]
PRINTSi PR00392. PROFILIN.
PR01639. PROFILINMAML.
SMARTi SM00392. PROF. 1 hit.
[Graphical view ]
SUPFAMi SSF55770. SSF55770. 1 hit.
PROSITEi PS00414. PROFILIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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).

Entry informationi

Entry nameiPROF2_HUMAN
AccessioniPrimary (citable) accession number: P35080
Secondary accession number(s): B2R4C8
, D3DNI4, Q4VBQ4, Q8WVF9, Q9HBK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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