Skip Header

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

Paxillin

Gene

PXN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • beta-catenin binding Source: UniProtKB
  • vinculin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cell-matrix adhesion Source: InterPro
  • cellular response to reactive oxygen species Source: BHF-UCL
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • growth hormone receptor signaling pathway Source: BHF-UCL
  • muscle contraction Source: Reactome
  • signal complex assembly Source: ProtInc
  • signal transduction Source: ProtInc
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089159-MONOMER.
ReactomeiR-HSA-180292. GAB1 signalosome.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-HSA-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP49023.
SIGNORiP49023.

Names & Taxonomyi

Protein namesi
Recommended name:
Paxillin
Gene namesi
Name:PXN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9718. PXN.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: BHF-UCL
  • microtubule associated complex Source: ProtInc
  • nucleoplasm Source: HPA
  • plasma membrane Source: UniProtKB
  • stress fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7 – 8LL → RR: Loss of interaction with PDCD10. 1 Publication2

Organism-specific databases

DisGeNETi5829.
MalaCardsiPXN.
OpenTargetsiENSG00000089159.
PharmGKBiPA34062.

Chemistry databases

ChEMBLiCHEMBL5715.

Polymorphism and mutation databases

BioMutaiPXN.
DMDMi317373486.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000758531 – 591PaxillinAdd BLAST591
Isoform 4 (identifier: P49023-4)
Initiator methionineiRemovedCombined sources

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei31Phosphotyrosine; by PTK62 Publications1
Modified residuei83PhosphoserineBy similarity1
Modified residuei85PhosphoserineCombined sources1
Modified residuei88PhosphotyrosineBy similarity1
Modified residuei106PhosphoserineCombined sources1
Modified residuei118Phosphotyrosine; by PTK62 Publications1
Modified residuei119PhosphoserineCombined sources1
Modified residuei126PhosphoserineCombined sources1
Modified residuei130PhosphoserineCombined sources1
Modified residuei132PhosphothreonineBy similarity1
Modified residuei137PhosphoserineCombined sources1
Modified residuei140PhosphoserineBy similarity1
Modified residuei143PhosphoserineCombined sources1
Modified residuei181Phosphotyrosine1 Publication1
Modified residuei230PhosphoserineBy similarity1
Modified residuei244Phosphoserine; by CDK51 Publication1
Modified residuei250Phosphoserine; by SLK1 Publication1
Modified residuei258PhosphoserineBy similarity1
Modified residuei261PhosphoserineBy similarity1
Modified residuei272PhosphoserineCombined sources1
Modified residuei303PhosphoserineCombined sources1
Modified residuei322PhosphoserineCombined sources1
Modified residuei332PhosphoserineBy similarity1
Modified residuei340PhosphoserineBy similarity1
Modified residuei533PhosphoserineCombined sources1
Isoform 4 (identifier: P49023-4)
Modified residuei2N-acetylserineCombined sources1

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. Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (PubMed:23128389).By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP49023.
MaxQBiP49023.
PaxDbiP49023.
PeptideAtlasiP49023.
PRIDEiP49023.
TopDownProteomicsiP49023-2. [P49023-2]
P49023-3. [P49023-3]

PTM databases

iPTMnetiP49023.
PhosphoSitePlusiP49023.

Miscellaneous databases

PMAP-CutDBP49023.

Expressioni

Gene expression databases

BgeeiENSG00000089159.
CleanExiHS_PXN.
ExpressionAtlasiP49023. baseline and differential.
GenevisibleiP49023. HS.

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. 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. Interacts (via cytoplasmic domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (PubMed:11035932).15 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.

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111787. 86 interactors.
DIPiDIP-33851N.
IntActiP49023. 69 interactors.
MINTiMINT-92615.
STRINGi9606.ENSP00000228307.

Structurei

Secondary structure

1591
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi144 – 154Combined sources11
Helixi261 – 271Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XGZX-ray2.50a/c/e/g/h/j/m/o/q/s/u/w141-159[»]
4XH2X-ray2.00a/c/e/g/h/j261-275[»]
ProteinModelPortaliP49023.
SMRiP49023.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49023.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini356 – 415LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST60
Domaini416 – 473LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST58
Domaini474 – 533LIM zinc-binding 3PROSITE-ProRule annotationAdd BLAST60
Domaini534 – 591LIM zinc-binding 4PROSITE-ProRule annotationAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 15LD motif 1Add BLAST13
Motifi144 – 156LD motif 2Add BLAST13
Motifi216 – 228LD motif 3Add BLAST13
Motifi265 – 276LD motif 4Add BLAST12
Motifi333 – 345LD motif 5Add BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi46 – 53Pro-rich8

Sequence similaritiesi

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

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOVERGENiHBG001512.
InParanoidiP49023.
KOiK05760.
OMAiELCWAAG.
OrthoDBiEOG091G05AW.
PhylomeDBiP49023.
TreeFamiTF314113.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24216:SF11. PTHR24216:SF11. 1 hit.
PfamiPF00412. LIM. 4 hits.
[Graphical view]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti280G → D in BAA18997 (PubMed:9054445).Curated1
Sequence conflicti327P → L in CAI46024 (PubMed:17974005).Curated1
Sequence conflicti413F → S in CAI46024 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06509973S → G.5 PublicationsCorresponds to variant rs4767884dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0404831 – 133Missing in isoform 4. 1 PublicationAdd BLAST133
Alternative sequenceiVSP_003114278 – 311Missing in isoform Alpha and isoform 4. 4 PublicationsAdd BLAST34
Alternative sequenceiVSP_003115278 – 311IQGLE…QDEGG → GSWPLEEVVLLVSISSSVQE GEKYPHPCAARHRTPSLRSP DQPPPCPQ in isoform Gamma. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_016875232.1. XM_017019743.1. [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.4. human. [P49023-1]

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:
EMBLi
GenBanki
DDBJi
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]
XP_016875232.1. XM_017019743.1. [P49023-4]
UniGeneiHs.446336.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XGZX-ray2.50a/c/e/g/h/j/m/o/q/s/u/w141-159[»]
4XH2X-ray2.00a/c/e/g/h/j261-275[»]
ProteinModelPortaliP49023.
SMRiP49023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111787. 86 interactors.
DIPiDIP-33851N.
IntActiP49023. 69 interactors.
MINTiMINT-92615.
STRINGi9606.ENSP00000228307.

Chemistry databases

ChEMBLiCHEMBL5715.

PTM databases

iPTMnetiP49023.
PhosphoSitePlusiP49023.

Polymorphism and mutation databases

BioMutaiPXN.
DMDMi317373486.

Proteomic databases

EPDiP49023.
MaxQBiP49023.
PaxDbiP49023.
PeptideAtlasiP49023.
PRIDEiP49023.
TopDownProteomicsiP49023-2. [P49023-2]
P49023-3. [P49023-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.4. human. [P49023-1]

Organism-specific databases

CTDi5829.
DisGeNETi5829.
GeneCardsiPXN.
HGNCiHGNC:9718. PXN.
HPAiCAB003841.
HPA051309.
MalaCardsiPXN.
MIMi602505. gene.
neXtProtiNX_P49023.
OpenTargetsiENSG00000089159.
PharmGKBiPA34062.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOVERGENiHBG001512.
InParanoidiP49023.
KOiK05760.
OMAiELCWAAG.
OrthoDBiEOG091G05AW.
PhylomeDBiP49023.
TreeFamiTF314113.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089159-MONOMER.
ReactomeiR-HSA-180292. GAB1 signalosome.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-446343. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
R-HSA-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLinkiP49023.
SIGNORiP49023.

Miscellaneous databases

ChiTaRSiPXN. human.
EvolutionaryTraceiP49023.
GeneWikiiPaxillin.
GenomeRNAii5829.
PMAP-CutDBP49023.
PROiP49023.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000089159.
CleanExiHS_PXN.
ExpressionAtlasiP49023. baseline and differential.
GenevisibleiP49023. HS.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24216:SF11. PTHR24216:SF11. 1 hit.
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 185 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.