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Q8VI36 (PAXI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paxillin
Gene names
Name:Pxn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.3 Ref.5 Ref.6

Subcellular location

Cytoplasm › cytoskeleton By similarity. Cell junction › focal adhesion By similarity. Cytoplasm › cell cortex. Note: Colocalizes with integrins at the cell periphery. Ref.3

Post-translational modification

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. Ref.4 Ref.10

Sequence similarities

Belongs to the paxillin family.

Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from direct assay PubMed 14636584. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from direct assay PubMed 14636584. Source: MGI

cellular component movement

Inferred from mutant phenotype PubMed 11784865. Source: MGI

cytoskeleton organization

Inferred from mutant phenotype PubMed 11784865. Source: MGI

focal adhesion assembly

Inferred from direct assay PubMed 14636584. Source: MGI

integrin-mediated signaling pathway

Inferred from mutant phenotype PubMed 11784865. Source: MGI

lamellipodium assembly

Inferred from direct assay PubMed 14636584. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 15467718. Source: MGI

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from direct assay PubMed 10809671PubMed 11807098PubMed 14636584PubMed 15728191PubMed 16399995PubMed 18794329. Source: MGI

lamellipodium

Inferred from direct assay PubMed 14636584. Source: MGI

   Molecular_functionreceptor signaling complex scaffold activity

Traceable author statement PubMed 11784865. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta (identifier: Q8VI36-1)

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.
Isoform Alpha (identifier: Q8VI36-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Paxillin
PRO_0000075854

Regions

Domain356 – 41560LIM zinc-binding 1
Domain416 – 47358LIM zinc-binding 2
Domain474 – 53360LIM zinc-binding 3
Domain534 – 59158LIM zinc-binding 4
Motif3 – 1513LD motif 1
Motif144 – 15613LD motif 2
Motif216 – 22813LD motif 3
Motif265 – 27612LD motif 4
Motif333 – 34513LD motif 5
Compositional bias46 – 538Pro-rich

Amino acid modifications

Modified residue311Phosphotyrosine; by PTK6 By similarity
Modified residue831Phosphoserine Ref.8 Ref.9
Modified residue881Phosphotyrosine Ref.9
Modified residue1061Phosphoserine By similarity
Modified residue1091Phosphoserine By similarity
Modified residue1181Phosphotyrosine; by PTK6 Ref.7 Ref.9 Ref.10
Modified residue1191Phosphoserine By similarity
Modified residue1261Phosphoserine By similarity
Modified residue1301Phosphoserine By similarity
Modified residue1371Phosphoserine By similarity
Modified residue1811Phosphotyrosine By similarity
Modified residue2441Phosphoserine; by CDK5 By similarity
Modified residue3221Phosphoserine By similarity

Natural variations

Alternative sequence278 – 31134Missing in isoform Alpha.
VSP_016357

Experimental info

Sequence conflict711P → R in BAE42452. Ref.2
Sequence conflict2121D → N in BAE34151. Ref.2
Sequence conflict2941G → S in BAE34151. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B41A1892E6F60544

FASTA59164,476
        10         20         30         40         50         60 
MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 

        70         80         90        100        110        120 
TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT QDGVGSLCSR AGEEEHVYSF 

       130        140        150        160        170        180 
PNKQKSAEPS PTVMSSSLGS NLSELDRLLL ELNAVQHSPP GFPADEAESS PPLPGALSPL 

       190        200        210        220        230        240 
YGIPENNTPL GGKAGPLVKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 

       250        260        270        280        290        300 
EMSSPQRVTS SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR 

       310        320        330        340        350        360 
QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA 

       370        380        390        400        410        420 
CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH SLFSPRCYYC 

       430        440        450        460        470        480 
NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA 

       490        500        510        520        530        540 
RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK 

       550        560        570        580        590 
PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C

« Hide

Isoform Alpha [UniParc].

Checksum: 483D880CF16289B5
Show »

FASTA55760,811

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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, MASS SPECTROMETRY.
Tissue: Brain.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.
Tissue: Melanoma.
[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, MASS SPECTROMETRY.
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00128703.
IPI00165881.
RefSeqNP_035353.1. NM_011223.2.
NP_598676.2. NM_133915.2.
UniGeneMm.18714.

3D structure databases

ProteinModelPortalQ8VI36.
SMRQ8VI36. Positions 357-590.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8VI36. 5 interactions.
MINTMINT-141924.

PTM databases

PhosphoSiteQ8VI36.

Proteomic databases

PaxDbQ8VI36.
PRIDEQ8VI36.

Protocols and materials databases

DNASU19303.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528.
GeneID19303.
KEGGmmu:19303.
UCSCuc008zeb.1. mouse.

Organism-specific databases

CTD5829.
MGIMGI:108295. Pxn.

Phylogenomic databases

eggNOGNOG267887.
GeneTreeENSGT00700000104021.
HOGENOMHOG000018764.
HOVERGENHBG001512.
InParanoidQ8VI36.
KOK05760.
OrthoDBEOG4TMR25.

Gene expression databases

ArrayExpressQ8VI36.
BgeeQ8VI36.
CleanExMM_PXN.
GenevestigatorQ8VI36.
GermOnlineENSMUSG00000029528. Mus musculus.

Family and domain databases

Gene3D2.10.110.10. 4 hits.
InterProIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 4 hits.
[Graphical view]
PRINTSPR00832. PAXILLIN.
SMARTSM00132. LIM. 4 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPXN. mouse.
NextBio296261.
PMAP-CutDBQ8VI36.
SOURCESearch...

Entry information

Entry namePAXI_MOUSE
AccessionPrimary (citable) accession number: Q8VI36
Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2002
Last modified: May 29, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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