LIMS1_HUMAN - dbPTM
LIMS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIMS1_HUMAN
UniProt AC P48059
Protein Name LIM and senescent cell antigen-like-containing domain protein 1
Gene Name LIMS1
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Cell junction, focal adhesion. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation..
Protein Sequence MANALASATCERCKGGFAPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVNCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLAETLGRK
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
2Acetylation------MANALASAT
------CCHHHHHHH		15.2512665801
2 (in isoform 4)Phosphorylation-15.25-
9 (in isoform 2)Phosphorylation-16.6528348404
9PhosphorylationANALASATCERCKGG
CHHHHHHHHHHCCCC		16.65-
11 (in isoform 2)Phosphorylation-57.6827251275
15 (in isoform 5)Phosphorylation-39.82-
24 (in isoform 5)Phosphorylation-10.7322617229
36 (in isoform 5)Phosphorylation-5.1628122231
89PhosphorylationVIKAMNNSWHPECFR
HHHHHHCCCCHHHHC		23.0428857561
107UbiquitinationCQEVLADIGFVKNAG
HHHHHHHHCCHHCCC		3.7223000965
111UbiquitinationLADIGFVKNAGRHLC
HHHHCCHHCCCCCCC		38.53-
113UbiquitinationDIGFVKNAGRHLCRP
HHCCHHCCCCCCCCC		15.6423000965
118UbiquitinationKNAGRHLCRPCHNRE
HCCCCCCCCCCCCHH		3.5923000965
126UbiquitinationRPCHNREKARGLGKY
CCCCCHHHHHHHHHH		39.9023000965
130UbiquitinationNREKARGLGKYICQK
CHHHHHHHHHHHHHH		4.4523000965
132AcetylationEKARGLGKYICQKCH
HHHHHHHHHHHHHHC		36.1625953088
132UbiquitinationEKARGLGKYICQKCH
HHHHHHHHHHHHHHC		36.1623000965
136UbiquitinationGLGKYICQKCHAIID
HHHHHHHHHHCCEEC		41.6823000965
137UbiquitinationLGKYICQKCHAIIDE
HHHHHHHHHCCEECC		24.4723000965
137AcetylationLGKYICQKCHAIIDE
HHHHHHHHHCCEECC		24.4725953088
138UbiquitinationGKYICQKCHAIIDEQ
HHHHHHHHCCEECCC		0.7823000965
141UbiquitinationICQKCHAIIDEQPLI
HHHHHCCEECCCCCC		1.4923000965
144UbiquitinationKCHAIIDEQPLIFKN
HHCCEECCCCCCCCC		43.6323000965
149UbiquitinationIDEQPLIFKNDPYHP
ECCCCCCCCCCCCCC		8.7823000965
163UbiquitinationPDHFNCANCGKELTA
CCCCCCCCCCCCCCC		36.9623000965
169UbiquitinationANCGKELTADARELK
CCCCCCCCCCHHHHC		24.4723000965
174UbiquitinationELTADARELKGELYC
CCCCCHHHHCCEEEE		57.4623000965
176UbiquitinationTADARELKGELYCLP
CCCHHHHCCEEEEEE		45.6533845483
180PhosphorylationRELKGELYCLPCHDK
HHHCCEEEEEECCCC		6.4029496907
180UbiquitinationRELKGELYCLPCHDK
HHHCCEEEEEECCCC		6.4033845483
188UbiquitinationCLPCHDKMGVPICGA
EEECCCCCCCCCCCC		9.0123000965
194UbiquitinationKMGVPICGACRRPIE
CCCCCCCCCCCCCCC		28.5623000965
199UbiquitinationICGACRRPIEGRVVN
CCCCCCCCCCCCEEE		15.0523000965
199 (in isoform 3)Ubiquitination-15.05-
213UbiquitinationNAMGKQWHVEHFVCA
ECCCCCEEEEEEEEE		16.7633845483
224SumoylationFVCAKCEKPFLGHRH
EEEECCCCCCCCCCH		51.01-
224SumoylationFVCAKCEKPFLGHRH
EEEECCCCCCCCCCH		51.01-
238UbiquitinationHYERKGLAYCETHYN
HHHHCCCHHHHHHHH		18.6533845483
265PhosphorylationVIEGDVVSALNKAWC
CCCCCHHHHCHHCEE		27.2128857561
279PhosphorylationCVNCFACSTCNTKLT
ECCCEECCCCCCEEE		32.3428857561
286PhosphorylationSTCNTKLTLKNKFVE
CCCCCEEEECCCCEE		36.9224719451
290MalonylationTKLTLKNKFVEFDMK
CEEEECCCCEECCCH		49.5626320211
290UbiquitinationTKLTLKNKFVEFDMK
CEEEECCCCEECCCH		49.5629967540
290AcetylationTKLTLKNKFVEFDMK
CEEEECCCCEECCCH		49.5625953088
294UbiquitinationLKNKFVEFDMKPVCK
ECCCCEECCCHHHHH		10.5229967540
297AcetylationKFVEFDMKPVCKKCY
CCEECCCHHHHHHHH		35.8226822725
301MalonylationFDMKPVCKKCYEKFP
CCCHHHHHHHHHHCC		46.2226320211
301AcetylationFDMKPVCKKCYEKFP
CCCHHHHHHHHHHCC		46.2225953088
302UbiquitinationDMKPVCKKCYEKFPL
CCHHHHHHHHHHCCH		36.6029967540
317SumoylationELKKRLKKLAETLGR
HHHHHHHHHHHHHCC		58.48-
317SumoylationELKKRLKKLAETLGR
HHHHHHHHHHHHHCC		58.48-
317MalonylationELKKRLKKLAETLGR
HHHHHHHHHHHHHCC		58.4826320211
317UbiquitinationELKKRLKKLAETLGR
HHHHHHHHHHHHHCC		58.4824816145
321PhosphorylationRLKKLAETLGRK---
HHHHHHHHHCCC---		28.9823403867
321UbiquitinationRLKKLAETLGRK---
HHHHHHHHHCCC---		28.9824816145
327UbiquitinationETLGRK---------
HHHCCC---------		29967540
329UbiquitinationLGRK-----------
HCCC-----------		24816145
352Ubiquitination----------------------------------
----------------------------------		29967540
354Ubiquitination------------------------------------
------------------------------------		24816145
379Ubiquitination-------------------------------------------------------------
-------------------------------------------------------------		24816145
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
-KUbiquitinationE3 ubiquitin ligaseRNF6Q9Y252
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIMS1_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 LIMS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTIP_HUMANRBBP8physical
16189514
LPXN_HUMANLPXNphysical
16189514
EHMT2_HUMANEHMT2physical
16189514
ILK_HUMANILKphysical
10022929
NCK2_HUMANNCK2physical
9843575
MBIP1_HUMANMBIPphysical
19060904
TAU_HUMANMAPTphysical
23554879
CHIP_HUMANSTUB1physical
23554879
RSU1_HUMANRSU1physical
25416956
TYSY_HUMANTYMSphysical
26186194
MY18A_HUMANMYO18Aphysical
26186194
ILK_HUMANILKphysical
26186194
PARVA_HUMANPARVAphysical
26186194
PARVB_HUMANPARVBphysical
26186194
NEUA_HUMANCMASphysical
26186194
SRRT_HUMANSRRTphysical
26186194
RBGP1_HUMANRABGAP1physical
26186194
REPS1_HUMANREPS1physical
26186194
MYH7_HUMANMYH7physical
26186194
PAXI_HUMANPXNphysical
26186194
TRIP6_HUMANTRIP6physical
26186194
BMP2K_HUMANBMP2Kphysical
26186194
ILK_HUMANILKphysical
26344197
PARVA_HUMANPARVAphysical
28514442
PARVB_HUMANPARVBphysical
28514442
ILK_HUMANILKphysical
28514442
NEUA_HUMANCMASphysical
28514442
MY18A_HUMANMYO18Aphysical
28514442
MYH4_HUMANMYH4physical
28514442
RBGP1_HUMANRABGAP1physical
28514442
TRIP6_HUMANTRIP6physical
28514442
TYSY_HUMANTYMSphysical
28514442
BMP2K_HUMANBMP2Kphysical
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 LIMS1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.

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