Reviewed, UniProtKB/Swiss-Prot P49023 (PAXI_HUMAN)

Names and origin

Protein names

Recommended name:
    Paxillin

Gene names

Name:

PXN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 c-SRC and, when tyrosine phosphorylated, to the SH2 domain of V-CRK. Isoform beta binds to focal adhesion kinase but weakly to vinculin. Isoform gamma binds to vinculin but only weakly to focal adhesion kinase. Interacts with GIT1, NUDT16L1/SDOS, PARVA and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1 By similarity. Binds ASAP2. Interacts with unphosphorylated ITGA4. Interacts with RNF5.
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › focal adhesion.
Post-translational modification	Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
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
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell-matrix adhesion Inferred from electronic annotation. Source: InterPro cellular response to reactive oxygen species Inferred from expression pattern. Source: UniProtKB signal complex assembly Ref.3 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: UniProtKB lamellipodium Inferred from direct assay. Source: UniProtKB microtubule associated complex Traceable author statement. Source: ProtInc
Molecular function	vinculin binding Ref.3 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTK2	Q05397	2	EBI-702209,EBI-702142
PTPN12	Q05209	1	EBI-702209,EBI-2266035
PTPRB	P23467	1	EBI-702209,EBI-1265766
PTPRC	P08575	1	EBI-702209,EBI-1341
PTPRG	P23470	1	EBI-702209,EBI-2258115
PTPRJ	Q12913	1	EBI-702209,EBI-2264500
PTPRK	Q15262	1	EBI-702209,EBI-474052
PTPRO	Q16827	1	EBI-702209,EBI-723739
PTPRZ1	P23471	1	EBI-702209,EBI-2263175
rnf-5	Q09463	2	EBI-702209,EBI-963421	From a different organism.
RNF5	Q99942	3	EBI-702209,EBI-348482

Alternative products

This entry describes 3 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: IQDLEQRADGERCWAAGWPRDGGRSSPGGQDEGG → GSWPLEEVVL...SPDQPPPCPQ

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 Ref.8

Modified residue

83

1

Phosphoserine By similarity

Modified residue

85

1

Phosphoserine Ref.18 Ref.19

Modified residue

88

1

Phosphotyrosine Ref.10 Ref.16

Modified residue

106

1

Phosphoserine Ref.15 Ref.17 Ref.19

Modified residue

109

1

Phosphoserine By similarity

Modified residue

118

1

Phosphotyrosine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16

Modified residue

126

1

Phosphoserine Ref.19

Modified residue

130

1

Phosphoserine Ref.19

Modified residue

137

1

Phosphoserine Ref.19

Modified residue

181

1

Phosphotyrosine Ref.8

Modified residue

303

1

Phosphoserine Ref.14

Natural variations

Alternative sequence

278 – 311

34

Missing in isoform Alpha.

VSP_003114

Alternative sequence

278 – 311

34

IQDLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma.

VSP_003115

Experimental info

Sequence conflict

73

1

G → S in AAC05175. Ref.4

Secondary structure

1

.

.

.

591

Helix Strand Turn

Details...

Helix

143 – 155

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta [UniParc]. Last modified January 10, 2003. Version 2. Checksum: 0FFDC07047E96636	FASTA	591	64,533
	10 20 30 40 50 60 MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 70 80 90 100 110 120 TILDPLDQWQ PSGSRFIHQQ 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 ASLSDFKIQD 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. Checksum: B379BED63E8E63A5	FASTA	557	60,937
	10 20 30 40 50 60 MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 70 80 90 100 110 120 TILDPLDQWQ PSGSRFIHQQ 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. Checksum: B521D1C688D379EA	FASTA	605	66,182
	10 20 30 40 50 60 MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 70 80 90 100 110 120 TILDPLDQWQ PSGSRFIHQQ 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

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: 7534286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[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].
[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). Tissue: Placenta.
[4]	"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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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: Epithelium.
[11]	"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: Epithelium.
[12]	"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.
[13]	"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: T-cell.
[14]	"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: Epithelium.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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. , 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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AC004263 Genomic DNA. Translation: AAC05175.1.

IPI

IPI00220030.
IPI00220031.
IPI00335634.

PIR

A55933.

RefSeq

NP_001074324.1.
NP_002850.2.

UniGene

Hs.446336

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KKY	model	-	A	142-157	[»]
1KL0	model	-	B	142-157	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P49023. 13 interactions.

Proteomic databases

PRIDE

P49023.

Genome annotation databases

Ensembl

ENSG00000089159. Homo sapiens. [Contig view]

GeneID

5829.

KEGG

hsa:5829.

Organism-specific databases

GeneCards

GC12M119110.

H-InvDB

HIX0011059.
HIX0037171.

HGNC

HGNC:9718. PXN.

HPA

CAB003841.

MIM

602505. gene.

PharmGKB

PA30441.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P49023.

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_9417. Signaling by EGFR.

Gene expression databases

ArrayExpress

P49023.

Bgee

P49023.

CleanEx

HS_PXN.

GermOnline

ENSG00000089159. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.10.110.10. Znf_LIM. 3 hits.

Pfam

PF00412. LIM. 4 hits.
PF03535. Paxillin. 1 hit.
[Graphical view]

PRINTS

PR00832. PAXILLIN.

ProDom

PD000094. LIM. 4 hits.
[Graphical view] [Entries sharing at least one domain]

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 Resources

NextBio

22710.

PMAP-CutDB

P49023.

SOURCE

Search...

Entry information

Entry name

PAXI_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 10, 2003
Last modified:	June 16, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)