LPXN_HUMAN - dbPTM
LPXN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LPXN_HUMAN
UniProt AC O60711
Protein Name Leupaxin
Gene Name LPXN
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region. Cell projection, podosome. Cell membrane. Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linki
Protein Description Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling..
Protein Sequence MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEELDALL
-------CHHHHHHH		9.0125944712
2 (in isoform 2)Phosphorylation-68.2327050516
9 (in isoform 2)Phosphorylation-62.4827050516
14PhosphorylationLLEELERSTLQDSDE
HHHHHHHHHCCCCCC		24.8823401153
15PhosphorylationLEELERSTLQDSDEY
HHHHHHHHCCCCCCC		34.3628787133
19PhosphorylationERSTLQDSDEYSNPA
HHHHCCCCCCCCCCC		21.2723401153
20PhosphorylationRSTLQDSDEYSNPAP
HHHCCCCCCCCCCCC		68.1227642862
22PhosphorylationTLQDSDEYSNPAPLP
HCCCCCCCCCCCCCC		20.8119605366
23PhosphorylationLQDSDEYSNPAPLPL
CCCCCCCCCCCCCCC		34.0021082442
24PhosphorylationQDSDEYSNPAPLPLD
CCCCCCCCCCCCCCC		35.5324719451
27PhosphorylationDEYSNPAPLPLDQHS
CCCCCCCCCCCCHHC		35.4527642862
34PhosphorylationPLPLDQHSRKETNLD
CCCCCHHCCCCCCCH		39.1423403867
39PhosphorylationQHSRKETNLDETSEI
HHCCCCCCCHHHHHH		46.7327642862
48PhosphorylationDETSEILSIQDNTSP
HHHHHHEECCCCCCC		24.7026074081
53PhosphorylationILSIQDNTSPLPAQL
HEECCCCCCCCCCEE		39.7626074081
54PhosphorylationLSIQDNTSPLPAQLV
EECCCCCCCCCCEEE		30.6026074081
62PhosphorylationPLPAQLVYTTNIQEL
CCCCEEEEEECHHEE		19.2120543562
63PhosphorylationLPAQLVYTTNIQELN
CCCEEEEEECHHEEE		13.0928787133
64PhosphorylationPAQLVYTTNIQELNV
CCEEEEEECHHEEEE		16.7928787133
72PhosphorylationNIQELNVYSEAQEPK
CHHEEEEECCCCCCC		10.3426074081
73PhosphorylationIQELNVYSEAQEPKE
HHEEEEECCCCCCCC		23.3626074081
81PhosphorylationEAQEPKESPPPSKTS
CCCCCCCCCCCCHHH		49.1626657352
85PhosphorylationPKESPPPSKTSAAAQ
CCCCCCCCHHHHHHH		55.1026074081
86UbiquitinationKESPPPSKTSAAAQL
CCCCCCCHHHHHHHH		52.88-
87PhosphorylationESPPPSKTSAAAQLD
CCCCCCHHHHHHHHH		28.1226074081
88PhosphorylationSPPPSKTSAAAQLDE
CCCCCHHHHHHHHHH		21.4626074081
101PhosphorylationDELMAHLTEMQAKVA
HHHHHHHHHHHHHHH		21.3926074081
106UbiquitinationHLTEMQAKVAVRADA
HHHHHHHHHHHHCCC		17.52-
121UbiquitinationGKKHLPDKQDHKASL
CCCCCCCHHHHHHHH		56.54-
125UbiquitinationLPDKQDHKASLDSML
CCCHHHHHHHHHHHH		48.21-
127PhosphorylationDKQDHKASLDSMLGG
CHHHHHHHHHHHHCH		37.2025850435
130PhosphorylationDHKASLDSMLGGLEQ
HHHHHHHHHHCHHHH		22.6225850435
132PhosphorylationKASLDSMLGGLEQEL
HHHHHHHHCHHHHHH		5.9527251275
149UbiquitinationLGIATVPKGHCASCQ
HCCEEECCCCCCCCC		57.88-
157UbiquitinationGHCASCQKPIAGKVI
CCCCCCCCCCCHHHH		42.6021890473
157AcetylationGHCASCQKPIAGKVI
CCCCCCCCCCCHHHH		42.6025953088
170PhosphorylationVIHALGQSWHPEHFV
HHHHHCCCCCHHHEE		26.0827080861
175PhosphorylationGQSWHPEHFVCTHCK
CCCCCHHHEEECCCC		25.5327251275
187PhosphorylationHCKEEIGSSPFFERS
CCCHHHCCCCCHHCC		40.2629255136
188PhosphorylationCKEEIGSSPFFERSG
CCHHHCCCCCHHCCC		22.1029255136
192PhosphorylationIGSSPFFERSGLAYC
HCCCCCHHCCCEECC		46.4427251275
194PhosphorylationSSPFFERSGLAYCPN
CCCCHHCCCEECCCC		30.8427080861
198PhosphorylationFERSGLAYCPNDYHQ
HHCCCEECCCCCHHH		17.3027080861
203PhosphorylationLAYCPNDYHQLFSPR
EECCCCCHHHCCCCH		9.7128450419
208PhosphorylationNDYHQLFSPRCAYCA
CCHHHCCCCHHHHHH		21.7428188228
213PhosphorylationLFSPRCAYCAAPILD
CCCCHHHHHHHHHHH		6.05-
260UbiquitinationDKKPYCRKDFLAMFS
CCCCCCCHHHHHHHC		49.632189047
265UbiquitinationCRKDFLAMFSPKCGG
CCHHHHHHHCCCCCC		3.5821890473
265UbiquitinationCRKDFLAMFSPKCGG
CCHHHHHHHCCCCCC		3.5821890473
265 (in isoform 2)Ubiquitination-3.58-
265UbiquitinationCRKDFLAMFSPKCGG
CCHHHHHHHCCCCCC		3.5821890473
267PhosphorylationKDFLAMFSPKCGGCN
HHHHHHHCCCCCCCC		15.4622617229
272PhosphorylationMFSPKCGGCNRPVLE
HHCCCCCCCCHHHHH		18.2624719451
327PhosphorylationHYHHRRGTLCHGCGQ
EEECCCCCCCCCCCC		25.1326699800
332PhosphorylationRGTLCHGCGQPITGR
CCCCCCCCCCCCCCC		1.7227251275
342PhosphorylationPITGRCISAMGYKFH
CCCCCHHHHCCCCCC		18.8128450419
347AcetylationCISAMGYKFHPEHFV
HHHHCCCCCCHHHHH		31.3125953088
364UbiquitinationFCLTQLSKGIFREQN
HHHHHHHHCCHHHCC		65.70-
373UbiquitinationIFREQNDKTYCQPCF
CHHHCCCCCCCCCCC		49.28-
375PhosphorylationREQNDKTYCQPCFNK
HHCCCCCCCCCCCHH		8.5318083107
380PhosphorylationKTYCQPCFNKLFPL-
CCCCCCCCHHHCCC-		13.2227642862
382UbiquitinationYCQPCFNKLFPL---
CCCCCCHHHCCC---		31.11-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
72YPhosphorylationKinaseLYNP07948
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LPXN_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LPXN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN426_HUMANZNF426physical
16189514
PF21A_HUMANPHF21Aphysical
16189514
IMP3_HUMANIMP3physical
16189514
P121A_HUMANPOM121physical
16189514
FAK2_HUMANPTK2Bphysical
9565592
MP2K7_HUMANMAP2K7physical
21988832
ZN175_HUMANZNF175physical
21988832
SFI1_HUMANSFI1physical
25416956
PKHN1_HUMANPLEKHN1physical
25416956
PKHH2_HUMANPLEKHH2physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
PKHH2_HUMANPLEKHH2physical
28514442
PTN12_HUMANPTPN12physical
28514442
FAK1_HUMANPTK2physical
28514442
ARHG6_HUMANARHGEF6physical
28514442
GIT2_HUMANGIT2physical
28514442
PPIP2_HUMANPSTPIP2physical
28514442
PKHH1_HUMANPLEKHH1physical
28514442
ARHG7_HUMANARHGEF7physical
28514442
PCNT_HUMANPCNTphysical
28514442
GIT1_HUMANGIT1physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
ATX2_HUMANATXN2physical
28514442
CK5P2_HUMANCDK5RAP2physical
28514442
RBMS1_HUMANRBMS1physical
28514442
CEP68_HUMANCEP68physical
28514442
PDLI7_HUMANPDLIM7physical
28514442
LIMD1_HUMANLIMD1physical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
PCM1_HUMANPCM1physical
28514442
EDC3_HUMANEDC3physical
28514442
PAK1_HUMANPAK1physical
28514442
ZN281_HUMANZNF281physical
28514442
LPP_HUMANLPPphysical
28514442
PAK2_HUMANPAK2physical
28514442
PARVA_HUMANPARVAphysical
28514442
CCDC6_HUMANCCDC6physical
28514442
MIO_HUMANMIOSphysical
28514442
TRIP6_HUMANTRIP6physical
28514442
QRIC1_HUMANQRICH1physical
28514442
MIB1_HUMANMIB1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LPXN_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND TYR-22, AND MASSSPECTROMETRY.
"Leupaxin is similar to paxillin in focal adhesion targeting andtyrosine phosphorylation but has distinct roles in cell adhesion andspreading.";
Chen P.W., Kroog G.S.;
Cell Adh. Migr. 4:527-540(2010).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-22; TYR-62AND TYR-72.
"Leupaxin negatively regulates B cell receptor signaling.";
Chew V., Lam K.P.;
J. Biol. Chem. 282:27181-27191(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-72 BY LYN, ANDINTERACTION WITH LYN.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory