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P49023 (PAXI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 134. 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·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paxillin
Gene names
Name:PXN
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 beta binds to PTK2/FAK1 but weakly to vinculin. Isoform gamma binds to vinculin but only weakly to PTK2/FAK1. Interacts with GIT1, NUDT16L1/SDOS, PARVA 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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.22 Ref.31 Ref.33 Ref.34

Subcellular location

Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cytoplasm › cell cortex By similarity. Note: Colocalizes with integrins at the cell periphery By similarity. Ref.31

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.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30

Sequence similarities

Belongs to the paxillin family.

Contains 4 LIM zinc-binding domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTK2Q053977EBI-702209,EBI-702142
rnf-5Q094632EBI-702209,EBI-963421From a different organism.
RNF5Q999426EBI-702209,EBI-348482

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.27
Modified residue311Phosphotyrosine; by PTK6 Ref.11 Ref.13 Ref.28
Modified residue831Phosphoserine Ref.29
Modified residue841Phosphoserine Ref.23
Modified residue851Phosphoserine Ref.25 Ref.26 Ref.29 Ref.30
Modified residue881Phosphotyrosine Ref.14 Ref.20 Ref.23 Ref.28
Modified residue1061Phosphoserine Ref.19 Ref.24 Ref.26 Ref.27
Modified residue1091Phosphoserine By similarity
Modified residue1181Phosphotyrosine; by PTK6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.28
Modified residue1261Phosphoserine Ref.26 Ref.30
Modified residue1301Phosphoserine Ref.26
Modified residue1371Phosphoserine Ref.26
Modified residue1811Phosphotyrosine Ref.11
Modified residue2441Phosphoserine; by CDK5 Ref.21
Modified residue3031Phosphoserine Ref.18
Modified residue3181Phosphothreonine Ref.29

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.31
Sequence conflict2801G → D in BAA18997. Ref.3
Sequence conflict3271P → L in CAI46024. Ref.5
Sequence conflict4131F → S in CAI46024. Ref.5

Secondary structure

1 ... 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: 7534286] [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: 9054445] [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: 14702039] [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: 17974005] [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: 16541075] [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: 15489334] [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: 10604475] [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: 10938112] [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: 10749932] [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: 11774284] [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: 12861019] [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: 15572663] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-31 AND TYR-118, INTERACTION WITH PTK6.
[14]"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)."
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.
J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[16]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, MASS SPECTROMETRY.
[17]"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.
Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[20]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[21]"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: 18042622] [Abstract]
Cited for: PHOSPHORYLATION AT SER-244.
[22]"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: 17297458] [Abstract]
Cited for: INTERACTION WITH NEK3.
[23]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; TYR-88 AND TYR-118, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[24]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[25]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[26]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126; SER-130 AND SER-137, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[27]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[28]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31; TYR-88 AND TYR-118, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[29]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND THR-318, MASS SPECTROMETRY.
[30]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[31]"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: 20489202] [Abstract]
Cited for: INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, MUTAGENESIS OF 7-LEU-LEU-8.
[32]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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: 14527389] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2/FAK1, INTERACTION WITH PTK2/FAK1.
[34]"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: 19358827] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2B/PYK2, INTERACTION WITH PTK2B/PYK2.
+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.
IPIIPI00220030.
IPI00220031.
IPI00335634.
IPI00890738.
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[»]
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[»]
ProteinModelPortalP49023.
SMRP49023. Positions 357-590.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-33851N.
IntActP49023. 20 interactions.
MINTMINT-92615.
STRINGP49023.

Polymorphism databases

DMDM27735219.

Proteomic databases

PRIDEP49023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228307; ENSP00000228307; ENSG00000089159.
ENST00000424649; ENSP00000391283; ENSG00000089159.
ENST00000458477; ENSP00000395536; ENSG00000089159.
GeneID5829.
KEGGhsa:5829.
UCSCuc001txt.3. human.
uc001txv.3. human.
uc001txx.3. human.
uc001txy.3. human.

Organism-specific databases

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

Phylogenomic databases

eggNOGNOG267887.
GeneTreeENSGT00640000091240.
HOVERGENHBG001512.
KOK05760.

Enzyme and pathway databases

Pathway_Interaction_DBangiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf6cyclingpathway. Arf6 signaling events.
ephbfwdpathway. EPHB forward signaling.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
igf1_pathway. IGF1 pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP49023.
BgeeP49023.
CleanExHS_PXN.
GenevestigatorP49023.
GermOnlineENSG00000089159. Homo sapiens.

Family and domain databases

Gene3DG3DSA:2.10.110.10. Znf_LIM. 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

EvolutionaryTraceP49023.
NextBio22710.
PMAP-CutDBP49023.
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 18, 2012
This is version 134 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

Human chromosome 12

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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