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Q8VI36

- PAXI_MOUSE

UniProt

Q8VI36 - PAXI_MOUSE

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Protein
Paxillin
Gene
Pxn
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) By similarity.

GO - Molecular functioni

  1. BH4 domain binding Source: MGI
  2. protein binding Source: IntAct
  3. receptor signaling complex scaffold activity Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of MAPK activity Source: MGI
  2. branching morphogenesis of an epithelial tube Source: MGI
  3. cellular component movement Source: MGI
  4. cytoskeleton organization Source: MGI
  5. focal adhesion assembly Source: MGI
  6. integrin-mediated signaling pathway Source: MGI
  7. lamellipodium assembly Source: MGI
  8. peptidyl-tyrosine phosphorylation Source: MGI
  9. positive regulation of protein kinase activity Source: MGI
  10. regulation of cell shape Source: MGI
  11. substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_206286. GAB1 signalosome.

Names & Taxonomyi

Protein namesi
Recommended name:
Paxillin
Gene namesi
Name:Pxn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:108295. Pxn.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcell cortex
Note: Colocalizes with integrins at the cell periphery.1 Publication

GO - Cellular componenti

  1. cell cortex Source: UniProtKB-SubCell
  2. cell leading edge Source: MGI
  3. cytoskeleton Source: UniProtKB-SubCell
  4. focal adhesion Source: MGI
  5. lamellipodium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Paxillin
PRO_0000075854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei31 – 311Phosphotyrosine; by PTK6 By similarity
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei88 – 881Phosphotyrosine1 Publication
Modified residuei106 – 1061Phosphoserine By similarity
Modified residuei118 – 1181Phosphotyrosine; by PTK63 Publications
Modified residuei119 – 1191Phosphoserine By similarity
Modified residuei126 – 1261Phosphoserine By similarity
Modified residuei130 – 1301Phosphoserine By similarity
Modified residuei137 – 1371Phosphoserine By similarity
Modified residuei181 – 1811Phosphotyrosine By similarity
Modified residuei244 – 2441Phosphoserine; by CDK5 By similarity
Modified residuei322 – 3221Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation By similarity. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion By similarity.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8VI36.
PaxDbiQ8VI36.
PRIDEiQ8VI36.

PTM databases

PhosphoSiteiQ8VI36.

Miscellaneous databases

PMAP-CutDBQ8VI36.

Expressioni

Gene expression databases

ArrayExpressiQ8VI36.
BgeeiQ8VI36.
CleanExiMM_PXN.
GenevestigatoriQ8VI36.

Interactioni

Subunit structurei

Interacts with VCL and SRC (via SH3 domain). Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 and PDCD10 By similarity. Interacts with SORBS1, PARVA and PARVB. Interacts with NEK3 and this interaction is prolactin-dependent By similarity. Interacts with PTK2/FAK1. Interacts with PTK6 By similarity. Interacts with PTK2B/PYK2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
L1camP116272EBI-983394,EBI-397964
Ptk2P341523EBI-983394,EBI-77070
PTPN1P180312EBI-983394,EBI-968788From a different organism.
VclQ647273EBI-983394,EBI-432047

Protein-protein interaction databases

BioGridi202525. 16 interactions.
IntActiQ8VI36. 20 interactions.
MINTiMINT-141924.

Structurei

3D structure databases

ProteinModelPortaliQ8VI36.
SMRiQ8VI36. Positions 357-590.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini356 – 41560LIM zinc-binding 1
Add
BLAST
Domaini416 – 47358LIM zinc-binding 2
Add
BLAST
Domaini474 – 53360LIM zinc-binding 3
Add
BLAST
Domaini534 – 59158LIM zinc-binding 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 1513LD motif 1
Add
BLAST
Motifi144 – 15613LD motif 2
Add
BLAST
Motifi216 – 22813LD motif 3
Add
BLAST
Motifi265 – 27612LD motif 4
Add
BLAST
Motifi333 – 34513LD motif 5
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 538Pro-rich

Sequence similaritiesi

Belongs to the paxillin family.

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG267887.
GeneTreeiENSGT00740000114891.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ8VI36.
KOiK05760.
OrthoDBiEOG70ZZQN.
PhylomeDBiQ8VI36.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 4 hits.
[Graphical view]
PRINTSiPR00832. PAXILLIN.
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Beta (identifier: Q8VI36-1) [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

MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP    50
PPPSSEALNG TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT 100
QDGVGSLCSR AGEEEHVYSF PNKQKSAEPS PTVMSSSLGS NLSELDRLLL 150
ELNAVQHSPP GFPADEAESS PPLPGALSPL YGIPENNTPL GGKAGPLVKE 200
KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS 250
SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR 300
QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV 350
ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD 400
GQPYCEKDYH SLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF 450
GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF 500
VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM 550
AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C 591
Length:591
Mass (Da):64,476
Last modified:March 1, 2002 - v1
Checksum:iB41A1892E6F60544
GO
Isoform Alpha (identifier: Q8VI36-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: Missing.

Show »
Length:557
Mass (Da):60,811
Checksum:i483D880CF16289B5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 31134Missing in isoform Alpha.
VSP_016357Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711P → R in BAE42452. 1 Publication
Sequence conflicti212 – 2121D → N in BAE34151. 1 Publication
Sequence conflicti294 – 2941G → S in BAE34151. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF293883 mRNA. Translation: AAL71910.1.
AF293882 mRNA. Translation: AAL71909.1.
AK149933 mRNA. Translation: BAE29176.1.
AK157688 mRNA. Translation: BAE34151.1.
AK167299 mRNA. Translation: BAE39404.1.
AK171436 mRNA. Translation: BAE42452.1.
CCDSiCCDS19593.1. [Q8VI36-2]
CCDS39229.1. [Q8VI36-1]
RefSeqiNP_035353.1. NM_011223.3. [Q8VI36-2]
NP_598676.2. NM_133915.3.
UniGeneiMm.18714.

Genome annotation databases

EnsembliENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528. [Q8VI36-2]
GeneIDi19303.
KEGGimmu:19303.
UCSCiuc008zeb.1. mouse. [Q8VI36-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF293883 mRNA. Translation: AAL71910.1 .
AF293882 mRNA. Translation: AAL71909.1 .
AK149933 mRNA. Translation: BAE29176.1 .
AK157688 mRNA. Translation: BAE34151.1 .
AK167299 mRNA. Translation: BAE39404.1 .
AK171436 mRNA. Translation: BAE42452.1 .
CCDSi CCDS19593.1. [Q8VI36-2 ]
CCDS39229.1. [Q8VI36-1 ]
RefSeqi NP_035353.1. NM_011223.3. [Q8VI36-2 ]
NP_598676.2. NM_133915.3.
UniGenei Mm.18714.

3D structure databases

ProteinModelPortali Q8VI36.
SMRi Q8VI36. Positions 357-590.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202525. 16 interactions.
IntActi Q8VI36. 20 interactions.
MINTi MINT-141924.

PTM databases

PhosphoSitei Q8VI36.

Proteomic databases

MaxQBi Q8VI36.
PaxDbi Q8VI36.
PRIDEi Q8VI36.

Protocols and materials databases

DNASUi 19303.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067268 ; ENSMUSP00000069624 ; ENSMUSG00000029528 . [Q8VI36-2 ]
GeneIDi 19303.
KEGGi mmu:19303.
UCSCi uc008zeb.1. mouse. [Q8VI36-2 ]

Organism-specific databases

CTDi 5829.
MGIi MGI:108295. Pxn.

Phylogenomic databases

eggNOGi NOG267887.
GeneTreei ENSGT00740000114891.
HOGENOMi HOG000018764.
HOVERGENi HBG001512.
InParanoidi Q8VI36.
KOi K05760.
OrthoDBi EOG70ZZQN.
PhylomeDBi Q8VI36.

Enzyme and pathway databases

Reactomei REACT_206286. GAB1 signalosome.

Miscellaneous databases

ChiTaRSi PXN. mouse.
NextBioi 296261.
PMAP-CutDB Q8VI36.
PROi Q8VI36.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VI36.
Bgeei Q8VI36.
CleanExi MM_PXN.
Genevestigatori Q8VI36.

Family and domain databases

Gene3Di 2.10.110.10. 4 hits.
InterProi IPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 4 hits.
[Graphical view ]
PRINTSi PR00832. PAXILLIN.
SMARTi SM00132. LIM. 4 hits.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes."
    Chay K.O., Park S.S., Mushinski J.F.
    J. Biol. Chem. 277:14521-14529(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    Strain: BALB/c.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
    Strain: C57BL/6J and NOD.
    Tissue: Placenta and Spleen.
  3. "The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells."
    Salgia R., Avraham S., Pisick E., Li J.L., Raja S., Greenfield E.A., Sattler M., Avraham H., Griffin J.D.
    J. Biol. Chem. 271:31222-31226(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B/PYK2, SUBCELLULAR LOCATION.
  4. "Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells."
    Ku H., Meier K.E.
    J. Biol. Chem. 275:11333-11340(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPK1/ERK2.
  5. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
    Nikolopoulos S.N., Turner C.E.
    J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARVA.
  6. "The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin."
    Hayashi I., Vuori K., Liddington R.C.
    Nat. Struct. Biol. 9:101-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2/FAK1.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; TYR-88 AND TYR-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway."
    Kopecki Z., O'Neill G.M., Arkell R.M., Cowin A.J.
    J. Invest. Dermatol. 131:1450-1459(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-118.

Entry informationi

Entry nameiPAXI_MOUSE
AccessioniPrimary (citable) accession number: Q8VI36
Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi