Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49023

- PAXI_HUMAN

UniProt

P49023 - PAXI_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Paxillin

Gene

PXN

Organism
Homo sapiens (Human)
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).

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. vinculin binding Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. branching morphogenesis of an epithelial tube Source: Ensembl
  3. cell adhesion Source: ProtInc
  4. cell junction assembly Source: Reactome
  5. cellular component movement Source: Ensembl
  6. cellular response to reactive oxygen species Source: BHF-UCL
  7. cytoskeleton organization Source: Ensembl
  8. epidermal growth factor receptor signaling pathway Source: Reactome
  9. focal adhesion assembly Source: Ensembl
  10. growth hormone receptor signaling pathway Source: BHF-UCL
  11. integrin-mediated signaling pathway Source: Ensembl
  12. lamellipodium assembly Source: Ensembl
  13. muscle contraction Source: Reactome
  14. peptidyl-tyrosine phosphorylation Source: Ensembl
  15. regulation of cell shape Source: Ensembl
  16. signal complex assembly Source: ProtInc
  17. signal transduction Source: ProtInc
  18. substrate adhesion-dependent cell spreading Source: Ensembl
  19. transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_12578. GAB1 signalosome.
REACT_20558. Smooth Muscle Contraction.
REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
SignaLinkiP49023.

Names & Taxonomyi

Protein namesi
Recommended name:
Paxillin
Gene namesi
Name:PXN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9718. PXN.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. focal adhesion Source: UniProtKB
  3. lamellipodium Source: BHF-UCL
  4. microtubule associated complex Source: ProtInc
  5. nucleus Source: HPA
  6. plasma membrane Source: UniProtKB
  7. stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 82LL → RR: Loss of interaction with PDCD10. 1 Publication

Organism-specific databases

PharmGKBiPA34062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591PaxillinPRO_0000075853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei31 – 311Phosphotyrosine; by PTK62 Publications
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei85 – 851Phosphoserine3 Publications
Modified residuei88 – 881PhosphotyrosineBy similarity
Modified residuei106 – 1061Phosphoserine3 Publications
Modified residuei118 – 1181Phosphotyrosine; by PTK62 Publications
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei126 – 1261Phosphoserine4 Publications
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei181 – 1811Phosphotyrosine1 Publication
Modified residuei244 – 2441Phosphoserine; by CDK51 Publication
Modified residuei322 – 3221Phosphoserine1 Publication

Post-translational modificationi

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.By similarity9 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49023.
PaxDbiP49023.
PRIDEiP49023.

PTM databases

PhosphoSiteiP49023.

Miscellaneous databases

PMAP-CutDBP49023.

Expressioni

Gene expression databases

BgeeiP49023.
CleanExiHS_PXN.
ExpressionAtlasiP49023. baseline and differential.
GenevestigatoriP49023.

Organism-specific databases

HPAiCAB003841.
HPA051309.

Interactioni

Subunit structurei

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 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.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSKP412402EBI-702209,EBI-1380630
CTNNB1P352224EBI-702209,EBI-491549
GAB1Q134802EBI-702209,EBI-517684
GIT2Q141612EBI-702209,EBI-1046878
ITGA4P136123EBI-702209,EBI-703044
ITGB1P05556-12EBI-702209,EBI-6082935
PIK3R1P279862EBI-702209,EBI-79464
PTK2Q0539715EBI-702209,EBI-702142
PTPN11Q061243EBI-702209,EBI-297779
rnf-5Q094632EBI-702209,EBI-963421From a different organism.
RNF5Q999426EBI-702209,EBI-348482
Sorbs1Q62417-28EBI-702209,EBI-7072893From a different organism.
SrcP054802EBI-702209,EBI-298680From a different organism.

Protein-protein interaction databases

BioGridi111787. 75 interactions.
DIPiDIP-33851N.
IntActiP49023. 50 interactions.
MINTiMINT-92615.
STRINGi9606.ENSP00000228307.

Structurei

Secondary structure

1
591
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi144 – 15411Combined sources
Helixi263 – 27311Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3U3FX-ray3.10E/F/G/H/I/J261-277[»]
4EDNX-ray2.90K/L/M/N/O/P/Q1-20[»]
4R32X-ray3.70B/C139-160[»]
ProteinModelPortaliP49023.
SMRiP49023. Positions 357-590.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49023.

Family & Domainsi

Domains and Repeats

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

Motif

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

Compositional bias

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

Sequence similaritiesi

Belongs to the paxillin family.Curated
Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG267887.
GeneTreeiENSGT00760000118910.
HOVERGENiHBG001512.
InParanoidiP49023.
KOiK05760.
OMAiLSDFKFM.
OrthoDBiEOG70ZZQN.
PhylomeDBiP49023.
TreeFamiTF314113.

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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform Beta (identifier: P49023-1) [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

        10         20         30         40         50
MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP
60 70 80 90 100
PPPSSEALNG TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP
110 120 130 140 150
QDSVGSPCSR VGEEEHVYSF PNKQKSAEPS PTVMSTSLGS NLSELDRLLL
160 170 180 190 200
ELNAVQHNPP GFPADEANSS PPLPGALSPL YGVPETNSPL GGKAGPLTKE
210 220 230 240 250
KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS
260 270 280 290 300
TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG
310 320 330 340 350
RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV
360 370 380 390 400
ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD
410 420 430 440 450
GQPYCEKDYH NLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF
460 470 480 490 500
GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF
510 520 530 540 550
VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM
560 570 580 590
AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C
Length:591
Mass (Da):64,505
Last modified:January 11, 2011 - v3
Checksum:iABF6C0BE5939623F
GO
Isoform Alpha (identifier: P49023-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:557
Mass (Da):60,967
Checksum:i94A6C321E4735076
GO
Isoform Gamma (identifier: P49023-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG → GSWPLEEVVL...SPDQPPPCPQ

Show »
Length:605
Mass (Da):66,212
Checksum:i0121D1C68C6F7398
GO
Isoform 4 (identifier: P49023-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:424
Mass (Da):46,604
Checksum:i74D536A48B653D6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801G → D in BAA18997. (PubMed:9054445)Curated
Sequence conflicti327 – 3271P → L in CAI46024. (PubMed:17974005)Curated
Sequence conflicti413 – 4131F → S in CAI46024. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731S → G.5 Publications
Corresponds to variant rs4767884 [ dbSNP | Ensembl ].
VAR_065099

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 4. 1 PublicationVSP_040483Add
BLAST
Alternative sequencei278 – 31134Missing in isoform Alpha and isoform 4. 4 PublicationsVSP_003114Add
BLAST
Alternative sequencei278 – 31134IQGLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma. 1 PublicationVSP_003115Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14588 mRNA. Translation: AAC50104.1.
U87946
, 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.
CCDSiCCDS44996.1. [P49023-2]
CCDS44997.1. [P49023-1]
CCDS44998.1. [P49023-4]
CCDS58281.1. [P49023-3]
PIRiA55933.
RefSeqiNP_001074324.1. NM_001080855.2. [P49023-1]
NP_001230685.1. NM_001243756.1. [P49023-3]
NP_002850.2. NM_002859.3. [P49023-2]
NP_079433.3. NM_025157.4. [P49023-4]
UniGeneiHs.446336.

Genome annotation databases

EnsembliENST00000228307; ENSP00000228307; ENSG00000089159. [P49023-1]
ENST00000267257; ENSP00000267257; ENSG00000089159. [P49023-3]
ENST00000424649; ENSP00000391283; ENSG00000089159. [P49023-2]
ENST00000458477; ENSP00000395536; ENSG00000089159. [P49023-4]
GeneIDi5829.
KEGGihsa:5829.
UCSCiuc001txt.3. human. [P49023-1]
uc001txv.3. human. [P49023-3]
uc001txx.3. human. [P49023-4]
uc001txy.3. human. [P49023-2]

Polymorphism databases

DMDMi317373486.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14588 mRNA. Translation: AAC50104.1 .
U87946
, 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 .
CCDSi CCDS44996.1. [P49023-2 ]
CCDS44997.1. [P49023-1 ]
CCDS44998.1. [P49023-4 ]
CCDS58281.1. [P49023-3 ]
PIRi A55933.
RefSeqi NP_001074324.1. NM_001080855.2. [P49023-1 ]
NP_001230685.1. NM_001243756.1. [P49023-3 ]
NP_002850.2. NM_002859.3. [P49023-2 ]
NP_079433.3. NM_025157.4. [P49023-4 ]
UniGenei Hs.446336.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KKY model - A 142-157 [» ]
1KL0 model - B 142-157 [» ]
1OW6 X-ray 2.35 D/F 262-274 [» ]
1OW7 X-ray 2.60 D/E/F 262-274 [» ]
1OW8 X-ray 2.85 D/F 141-153 [» ]
2K2R NMR - B 3-12 [» ]
2O9V X-ray 1.63 B 45-54 [» ]
2VZD X-ray 2.10 C/D 1-20 [» ]
2VZG X-ray 1.80 A 141-160 [» ]
2VZI X-ray 2.20 A 262-315 [» ]
3GM1 X-ray 2.95 C/D/E/F 262-274 [» ]
3PY7 X-ray 2.29 A 1-10 [» ]
3RQE X-ray 2.80 E 2-15 [» ]
3RQF X-ray 2.70 E 141-153 [» ]
3RQG X-ray 2.50 E 262-274 [» ]
3U3F X-ray 3.10 E/F/G/H/I/J 261-277 [» ]
4EDN X-ray 2.90 K/L/M/N/O/P/Q 1-20 [» ]
4R32 X-ray 3.70 B/C 139-160 [» ]
ProteinModelPortali P49023.
SMRi P49023. Positions 357-590.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111787. 75 interactions.
DIPi DIP-33851N.
IntActi P49023. 50 interactions.
MINTi MINT-92615.
STRINGi 9606.ENSP00000228307.

Chemistry

ChEMBLi CHEMBL5715.

PTM databases

PhosphoSitei P49023.

Polymorphism databases

DMDMi 317373486.

Proteomic databases

MaxQBi P49023.
PaxDbi P49023.
PRIDEi P49023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228307 ; ENSP00000228307 ; ENSG00000089159 . [P49023-1 ]
ENST00000267257 ; ENSP00000267257 ; ENSG00000089159 . [P49023-3 ]
ENST00000424649 ; ENSP00000391283 ; ENSG00000089159 . [P49023-2 ]
ENST00000458477 ; ENSP00000395536 ; ENSG00000089159 . [P49023-4 ]
GeneIDi 5829.
KEGGi hsa:5829.
UCSCi uc001txt.3. human. [P49023-1 ]
uc001txv.3. human. [P49023-3 ]
uc001txx.3. human. [P49023-4 ]
uc001txy.3. human. [P49023-2 ]

Organism-specific databases

CTDi 5829.
GeneCardsi GC12M120648.
HGNCi HGNC:9718. PXN.
HPAi CAB003841.
HPA051309.
MIMi 602505. gene.
neXtProti NX_P49023.
PharmGKBi PA34062.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267887.
GeneTreei ENSGT00760000118910.
HOVERGENi HBG001512.
InParanoidi P49023.
KOi K05760.
OMAi LSDFKFM.
OrthoDBi EOG70ZZQN.
PhylomeDBi P49023.
TreeFami TF314113.

Enzyme and pathway databases

Reactomei REACT_12578. GAB1 signalosome.
REACT_20558. Smooth Muscle Contraction.
REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
SignaLinki P49023.

Miscellaneous databases

ChiTaRSi PXN. human.
EvolutionaryTracei P49023.
GeneWikii Paxillin.
GenomeRNAii 5829.
NextBioi 22710.
PMAP-CutDB P49023.
PROi P49023.
SOURCEi Search...

Gene expression databases

Bgeei P49023.
CleanExi HS_PXN.
ExpressionAtlasi P49023. baseline and differential.
Genevestigatori P49023.

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. "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.
    , 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. 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.
    , 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. 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. 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. "CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer."
    Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.
    Nat. Immunol. 11:155-161(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD36.
  26. "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.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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].
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 45-54 IN COMPLEX WITH SORBS1, INTERACTION WITH SORBS1.
  32. "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.
  33. "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.
  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH PTK2B/PYK2, INTERACTION WITH PTK2B/PYK2.
  35. "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.

Entry informationi

Entry nameiPAXI_HUMAN
AccessioniPrimary (citable) accession number: P49023
Secondary accession number(s): B2RAI3
, B7ZMB4, O14970, O14971, O60360, Q5HYA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3