P49023 (PAXI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Paxillin

Gene names

Name:

PXN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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.23 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cytoplasm › cell cortex By similarity. Note: Colocalizes with integrins at the cell periphery By similarity. Ref.23
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 process	Cell adhesion
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from electronic annotation. Source: Compara branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara 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: Compara cellular response to reactive oxygen species Inferred from expression pattern PubMed 12686598. Source: BHF-UCL cytoskeleton organization Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome focal adhesion assembly Inferred from electronic annotation. Source: Compara growth hormone receptor signaling pathway Inferred from direct assay PubMed 10925297. Source: BHF-UCL integrin-mediated signaling pathway Inferred from electronic annotation. Source: Compara lamellipodium assembly Inferred from electronic annotation. Source: Compara muscle contraction Traceable author statement. Source: Reactome peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara signal complex assembly Traceable author statement Ref.3. Source: ProtInc
Cellular_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell 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 plasma membrane Inferred from direct assay PubMed 17449030. Source: UniProtKB
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ITGA4	P13612	3	EBI-702209,EBI-703044
ITGB1	P05556-1	2	EBI-702209,EBI-6082935
PTK2	Q05397	13	EBI-702209,EBI-702142
rnf-5	Q09463	2	EBI-702209,EBI-963421	From a different organism.
RNF5	Q99942	6	EBI-702209,EBI-348482
Src	P05480	2	EBI-702209,EBI-298680	From a different organism.

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 591

591

Paxillin

PRO_0000075853

Regions

Domain

356 – 415

60

LIM zinc-binding 1

Domain

416 – 473

58

LIM zinc-binding 2

Domain

474 – 533

60

LIM zinc-binding 3

Domain

534 – 591

58

LIM zinc-binding 4

Motif

3 – 15

13

LD motif 1

Motif

144 – 156

13

LD motif 2

Motif

216 – 228

13

LD motif 3

Motif

265 – 276

12

LD motif 4

Motif

333 – 345

13

LD motif 5

Compositional bias

46 – 53

8

Pro-rich

Amino acid modifications

Modified residue

31

1

Phosphotyrosine; by PTK6 Ref.11 Ref.13

Modified residue

83

1

Phosphoserine By similarity

Modified residue

85

1

Phosphoserine Ref.20 Ref.22 Ref.24

Modified residue

88

1

Phosphotyrosine By similarity

Modified residue

106

1

Phosphoserine Ref.15 Ref.18 Ref.20

Modified residue

109

1

Phosphoserine By similarity

Modified residue

118

1

Phosphotyrosine; by PTK6 Ref.11 Ref.13

Modified residue

119

1

Phosphoserine Ref.24

Modified residue

126

1

Phosphoserine Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

130

1

Phosphoserine Ref.20

Modified residue

137

1

Phosphoserine Ref.20

Modified residue

181

1

Phosphotyrosine Ref.11

Modified residue

244

1

Phosphoserine; by CDK5 Ref.16

Modified residue

322

1

Phosphoserine Ref.20

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 4.

VSP_040483

Alternative sequence

278 – 311

34

Missing in isoform Alpha and isoform 4.

VSP_003114

Alternative sequence

278 – 311

34

IQGLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma.

VSP_003115

Natural variant

73

1

S → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs4767884 [ dbSNP | Ensembl ].

VAR_065099

Experimental info

Mutagenesis

7 – 8

2

LL → RR: Loss of interaction with PDCD10. Ref.23

Sequence conflict

280

1

G → D in BAA18997. Ref.3

Sequence conflict

327

1

P → L in CAI46024. Ref.5

Sequence conflict

413

1

F → S in CAI46024. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

591

Helix Strand Turn

Details...

Helix

3 – 11

9

Helix

144 – 154

11

Helix

263 – 273

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta [UniParc]. Last modified January 11, 2011. Version 3. Checksum: ABF6C0BE5939623F	FASTA	591	64,505
	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
	Isoform Alpha [UniParc]. Checksum: 94A6C321E4735076	FASTA	557	60,967
	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 ASLSDFKFMA QGKTGSSSPP GGPPKPGSQL 310 320 330 340 350 360 DSMLGSLQSD LNKLGVATVA KGVCGACKKP IAGQVVTAMG KTWHPEHFVC THCQEEIGSR 370 380 390 400 410 420 NFFERDGQPY CEKDYHNLFS PRCYYCNGPI LDKVVTALDR TWHPEHFFCA QCGAFFGPEG 430 440 450 460 470 480 FHEKDGKAYC RKDYFDMFAP KCGGCARAIL ENYISALNTL WHPECFVCRE CFTPFVNGSF 490 500 510 520 530 540 FEHDGQPYCE VHYHERRGSL CSGCQKPITG RCITAMAKKF HPEHFVCAFC LKQLNKGTFK 550 EQNDKPYCQN CFLKLFC
	Isoform Gamma [UniParc]. Checksum: 0121D1C68C6F7398	FASTA	605	66,212
	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 ASLSDFKGSW PLEEVVLLVS ISSSVQEGEK 310 320 330 340 350 360 YPHPCAARHR TPSLRSPDQP PPCPQFMAQG KTGSSSPPGG PPKPGSQLDS MLGSLQSDLN 370 380 390 400 410 420 KLGVATVAKG VCGACKKPIA GQVVTAMGKT WHPEHFVCTH CQEEIGSRNF FERDGQPYCE 430 440 450 460 470 480 KDYHNLFSPR CYYCNGPILD KVVTALDRTW HPEHFFCAQC GAFFGPEGFH EKDGKAYCRK 490 500 510 520 530 540 DYFDMFAPKC GGCARAILEN YISALNTLWH PECFVCRECF TPFVNGSFFE HDGQPYCEVH 550 560 570 580 590 600 YHERRGSLCS GCQKPITGRC ITAMAKKFHP EHFVCAFCLK QLNKGTFKEQ NDKPYCQNCF LKLFC
	Isoform 4 [UniParc]. Checksum: 74D536A48B653D6D	FASTA	424	46,604
	10 20 30 40 50 60 MSTSLGSNLS ELDRLLLELN AVQHNPPGFP ADEANSSPPL PGALSPLYGV PETNSPLGGK 70 80 90 100 110 120 AGPLTKEKPK RNGGRGLEDV RPSVESLLDE LESSVPSPVP AITVNQGEMS SPQRVTSTQQ 130 140 150 160 170 180 QTRISASSAT RELDELMASL SDFKFMAQGK TGSSSPPGGP PKPGSQLDSM LGSLQSDLNK 190 200 210 220 230 240 LGVATVAKGV CGACKKPIAG QVVTAMGKTW HPEHFVCTHC QEEIGSRNFF ERDGQPYCEK 250 260 270 280 290 300 DYHNLFSPRC YYCNGPILDK VVTALDRTWH PEHFFCAQCG AFFGPEGFHE KDGKAYCRKD 310 320 330 340 350 360 YFDMFAPKCG GCARAILENY ISALNTLWHP ECFVCRECFT PFVNGSFFEH DGQPYCEVHY 370 380 390 400 410 420 HERRGSLCSG CQKPITGRCI TAMAKKFHPE HFVCAFCLKQ LNKGTFKEQN DKPYCQNCFL KLFC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"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.
[24]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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].
[26]	"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, MASS SPECTROMETRY.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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 , 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.

IPI

IPI00220030.
IPI00220031.
IPI00335634.
IPI00890738.

PIR

A55933.

RefSeq

NP_001074324.1. NM_001080855.2.
NP_001230685.1. NM_001243756.1.
NP_002850.2. NM_002859.3.
NP_079433.3. NM_025157.4.

UniGene

Hs.446336.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3U3C	X-ray	3.70	B/C	139-160	[»]
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	[»]

ProteinModelPortal

P49023.

SMR

P49023. Positions 357-590.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33851N.

IntAct

P49023. 28 interactions.

MINT

MINT-92615.

STRING

9606.ENSP00000228307.

PTM databases

PhosphoSite

P49023.

Polymorphism databases

DMDM

27735219.

Proteomic databases

PaxDb

P49023.

PRIDE

P49023.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228307; ENSP00000228307; ENSG00000089159.
ENST00000267257; ENSP00000267257; ENSG00000089159.
ENST00000424649; ENSP00000391283; ENSG00000089159.
ENST00000458477; ENSP00000395536; ENSG00000089159.

GeneID

5829.

KEGG

hsa:5829.

UCSC

uc001txt.3. human.
uc001txv.3. human.
uc001txx.3. human.
uc001txy.3. human.

Organism-specific databases

CTD

5829.

GeneCards

GC12M120648.

HGNC

HGNC:9718. PXN.

HPA

CAB003841.

MIM

602505. gene.

neXtProt

NX_P49023.

PharmGKB

PA34062.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG267887.

HOVERGEN

HBG001512.

KO

K05760.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_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.

Reactome

REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_17044. Muscle contraction.

Gene expression databases

ArrayExpress

P49023.

Bgee

P49023.

CleanEx

HS_PXN.

Genevestigator

P49023.

GermOnline

ENSG00000089159. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 4 hits.

InterPro

IPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 4 hits.
[Graphical view]

PRINTS

PR00832. PAXILLIN.

SMART

SM00132. LIM. 4 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5715.

ChiTaRS

PXN. human.

EvolutionaryTrace

P49023.

GenomeRNAi

5829.

NextBio

22710.

PMAP-CutDB

P49023.

SOURCE

Search...

Entry information

Entry name

PAXI_HUMAN

Accession

Primary (citable) accession number: P49023
Secondary accession number(s): B2RAI3 , B7ZMB4, O14970, O14971, O60360, Q5HYA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.