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P49023 (PAXI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paxillin
Gene names
Name:PXN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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).

Subunit structure

Binds in vitro to vinculin as well as to the SH3 domain of SRC and, when tyrosine phosphorylated, to the SH2 domain of V-CRK. Isoform betabinds to PTK2/FAK1 but weakly to vinculin. Isoform gammabinds to vinculin but only weakly to PTK2/FAK1. Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1 By similarity. Interacts with PTK2/FAK1 and PTK2B/PYK2. Binds ASAP2. Interacts with unphosphorylated ITGA4. Interacts with RNF5 and PDCD10. Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with PTK6. Interacts with SORBS1, PARVA and PARVB. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.17 Ref.24 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34

Subcellular location

Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Cytoplasmcell cortex By similarity. Note: Colocalizes with integrins at the cell periphery By similarity. Ref.24

Post-translational modification

Phosphorylated by MAPK1/ERK2 By similarity. 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. Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. Ref.11 Ref.13 Ref.16

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
Polymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Non-traceable author statement PubMed 10840040. Source: ProtInc

cell junction assembly

Traceable author statement. Source: Reactome

cellular component movement

Inferred from electronic annotation. Source: Ensembl

cellular response to reactive oxygen species

Inferred from expression pattern PubMed 12686598. Source: BHF-UCL

cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

growth hormone receptor signaling pathway

Inferred from direct assay PubMed 10925297. Source: BHF-UCL

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

signal complex assembly

Traceable author statement Ref.3. Source: ProtInc

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

focal adhesion

Inferred from direct assay PubMed 12686598PubMed 20086044. Source: BHF-UCL

lamellipodium

Inferred from direct assay PubMed 12686598. Source: BHF-UCL

microtubule associated complex

Traceable author statement PubMed 10840040. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay PubMed 17449030. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 17513457. Source: UniProtKB

vinculin binding

Inferred from physical interaction Ref.3. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta (identifier: P49023-1)

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: P49023-2)

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: Missing.
Isoform Gamma (identifier: P49023-3)

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG → GSWPLEEVVL...SPDQPPPCPQ
Isoform 4 (identifier: P49023-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     278-311: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Paxillin
PRO_0000075853

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 residue11N-acetylmethionine Ref.21
Modified residue311Phosphotyrosine; by PTK6 Ref.11 Ref.13
Modified residue831Phosphoserine By similarity
Modified residue851Phosphoserine Ref.20 Ref.23 Ref.25
Modified residue881Phosphotyrosine By similarity
Modified residue1061Phosphoserine Ref.15 Ref.18 Ref.20
Modified residue1181Phosphotyrosine; by PTK6 Ref.11 Ref.13
Modified residue1191Phosphoserine Ref.25
Modified residue1261Phosphoserine Ref.20 Ref.23 Ref.25 Ref.27
Modified residue1301Phosphoserine Ref.20
Modified residue1371Phosphoserine Ref.20
Modified residue1811Phosphotyrosine Ref.11
Modified residue2441Phosphoserine; by CDK5 Ref.16
Modified residue3221Phosphoserine Ref.20

Natural variations

Alternative sequence1 – 133133Missing in isoform 4.
VSP_040483
Alternative sequence278 – 31134Missing in isoform Alpha and isoform 4.
VSP_003114
Alternative sequence278 – 31134IQGLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma.
VSP_003115
Natural variant731S → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs4767884 [ dbSNP | Ensembl ].
VAR_065099

Experimental info

Mutagenesis7 – 82LL → RR: Loss of interaction with PDCD10. Ref.24
Sequence conflict2801G → D in BAA18997. Ref.3
Sequence conflict3271P → L in CAI46024. Ref.5
Sequence conflict4131F → S in CAI46024. Ref.5

Secondary structure

....... 591
Helix Strand Turn

Details...

Sequences

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

Last modified January 11, 2011. Version 3.
Checksum: ABF6C0BE5939623F

FASTA59164,505
        10         20         30         40         50         60 
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 

        70         80         90        100        110        120 
TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF 

       130        140        150        160        170        180 
PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL 

       190        200        210        220        230        240 
YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 

       250        260        270        280        290        300 
EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG 

       310        320        330        340        350        360 
RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA 

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

       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 YCQNCFLKLF C 

« Hide

Isoform Alpha [UniParc].

Checksum: 94A6C321E4735076
Show »

FASTA55760,967
Isoform Gamma [UniParc].

Checksum: 0121D1C68C6F7398
Show »

FASTA60566,212
Isoform 4 [UniParc].

Checksum: 74D536A48B653D6D
Show »

FASTA42446,604

References

« Hide 'large scale' references
[1]"Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL."
Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L.B., Griffin J.D.
J. Biol. Chem. 270:5039-5047(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT GLY-73.
[2]"Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-73.
[3]"Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins."
Mazaki Y., Hashimoto S., Sabe H.
J. Biol. Chem. 272:7437-7444(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), VARIANT GLY-73.
Tissue: Placenta.
[4]"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. expand/collapse author list , 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] (ISOFORM ALPHA), VARIANT GLY-73.
Tissue: Placenta.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Fetal kidney.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM ALPHA), VARIANT GLY-73.
Tissue: Brain and Testis.
[8]"Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses."
Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H.
Nature 402:676-681(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGA4.
[9]"Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly."
Zhao Z.-S., Manser E., Loo T.-H., Lim L.
Mol. Cell. Biol. 20:6354-6363(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GIT1.
[10]"A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration."
Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.
Mol. Biol. Cell 11:1315-1327(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASAP2.
[11]"Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in MM1 cancer cell migration."
Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E., Akedo H.
Int. J. Cancer 97:330-335(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
[12]"RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization."
Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., Ronai Z.
Mol. Cell. Biol. 23:5331-5345(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF5.
[13]"Brk activates rac1 and promotes cell migration and invasion by phosphorylating paxillin."
Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.
Mol. Cell. Biol. 24:10558-10572(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-31 AND TYR-118, INTERACTION WITH PTK6.
[14]"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].
[15]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Cdk5 regulates differentiation of oligodendrocyte precursor cells through the direct phosphorylation of paxillin."
Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y., Hisanaga S., Tanoue A.
J. Cell Sci. 120:4355-4366(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-244.
[17]"Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells."
Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., Clevenger C.V.
Oncogene 26:4668-4678(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEK3.
[18]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126; SER-130; SER-137 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity."
Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.
J. Biol. Chem. 285:24099-24107(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, MUTAGENESIS OF 7-LEU-LEU-8.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-119 AND SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain."
Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., Arold S.T.
Structure 11:1207-1217(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2/FAK1, INTERACTION WITH PTK2/FAK1.
[30]"Paxillin and ponsin interact in nascent costameres of muscle cells."
Gehmlich K., Pinotsis N., Hayess K., van der Ven P.F., Milting H., El Banayosy A., Korfer R., Wilmanns M., Ehler E., Furst D.O.
J. Mol. Biol. 369:665-682(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 45-54 IN COMPLEX WITH SORBS1, INTERACTION WITH SORBS1.
[31]"The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly."
Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.
J. Biol. Chem. 283:21113-21119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
[32]"Structural analysis of the interactions between paxillin LD motifs and alpha-parvin."
Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E., Hoellerer M.K.
Structure 16:1521-1531(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-315 IN COMPLEX WITH PARVA, INTERACTION WITH PARVA.
[33]"Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2."
Lulo J., Yuzawa S., Schlessinger J.
Biochem. Biophys. Res. Commun. 383:347-352(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2B/PYK2, INTERACTION WITH PTK2B/PYK2.
[34]"Structural basis for paxillin binding and focal adhesion targeting of beta-parvin."
Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A., Boggon T.J.
J. Biol. Chem. 287:32566-32577(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-20 IN COMPLEX WITH PARVB, INTERACTION WITH PARVB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14588 mRNA. Translation: AAC50104.1.
U87946 expand/collapse EMBL AC list , U87941, U87942, U87943, U87944, U87945 Genomic DNA. Translation: AAD00648.1.
D86862 mRNA. Translation: BAA18997.1.
D86863 mRNA. Translation: BAA18998.1.
AK314204 mRNA. Translation: BAG36880.1.
BX648777 mRNA. Translation: CAI46024.1.
AC004263 Genomic DNA. Translation: AAC05175.1.
BC136787 mRNA. Translation: AAI36788.1.
BC136794 mRNA. Translation: AAI36795.1.
BC144410 mRNA. Translation: AAI44411.1.
PIRA55933.
RefSeqNP_001074324.1. NM_001080855.2.
NP_001230685.1. NM_001243756.1.
NP_002850.2. NM_002859.3.
NP_079433.3. NM_025157.4.
UniGeneHs.446336.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKYmodel-A142-157[»]
1KL0model-B142-157[»]
1OW6X-ray2.35D/F262-274[»]
1OW7X-ray2.60D/E/F262-274[»]
1OW8X-ray2.85D/F141-153[»]
2K2RNMR-B3-12[»]
2O9VX-ray1.63B45-54[»]
2VZDX-ray2.10C/D1-20[»]
2VZGX-ray1.80A141-160[»]
2VZIX-ray2.20A262-315[»]
3GM1X-ray2.95C/D/E/F262-274[»]
3PY7X-ray2.29A1-10[»]
3RQEX-ray2.80E2-15[»]
3RQFX-ray2.70E141-153[»]
3RQGX-ray2.50E262-274[»]
3U3CX-ray3.70B/C139-160[»]
3U3FX-ray3.10E/F/G/H/I/J261-277[»]
4EDNX-ray2.90K/L/M/N/O/P/Q1-20[»]
ProteinModelPortalP49023.
SMRP49023. Positions 357-590.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111787. 67 interactions.
DIPDIP-33851N.
IntActP49023. 48 interactions.
MINTMINT-92615.
STRING9606.ENSP00000228307.

Chemistry

ChEMBLCHEMBL5715.

PTM databases

PhosphoSiteP49023.

Polymorphism databases

DMDM317373486.

Proteomic databases

PaxDbP49023.
PRIDEP49023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228307; ENSP00000228307; ENSG00000089159. [P49023-1]
ENST00000267257; ENSP00000267257; ENSG00000089159. [P49023-3]
ENST00000424649; ENSP00000391283; ENSG00000089159. [P49023-2]
ENST00000458477; ENSP00000395536; ENSG00000089159. [P49023-4]
GeneID5829.
KEGGhsa:5829.
UCSCuc001txt.3. human. [P49023-1]
uc001txv.3. human. [P49023-3]
uc001txx.3. human. [P49023-4]
uc001txy.3. human. [P49023-2]

Organism-specific databases

CTD5829.
GeneCardsGC12M120648.
HGNCHGNC:9718. PXN.
HPACAB003841.
HPA051309.
MIM602505. gene.
neXtProtNX_P49023.
PharmGKBPA34062.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267887.
HOVERGENHBG001512.
KOK05760.
OMALSDFKFM.
OrthoDBEOG70ZZQN.
PhylomeDBP49023.
TreeFamTF314113.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_17044. Muscle contraction.
SignaLinkP49023.

Gene expression databases

ArrayExpressP49023.
BgeeP49023.
CleanExHS_PXN.
GenevestigatorP49023.

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. human.
EvolutionaryTraceP49023.
GeneWikiPaxillin.
GenomeRNAi5829.
NextBio22710.
PMAP-CutDBP49023.
PROP49023.
SOURCESearch...

Entry information

Entry namePAXI_HUMAN
AccessionPrimary (citable) accession number: P49023
Secondary accession number(s): B2RAI3 expand/collapse secondary AC list , B7ZMB4, O14970, O14971, O60360, Q5HYA4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM