LIMS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIMS2_HUMAN
• UniProt AC: Q7Z4I7
• Protein Name: LIM and senescent cell antigen-like-containing domain protein 2
• Gene Name: LIMS2
• Organism: Homo sapiens (Human).
• Sequence Length: 341
• Subcellular Localization: Nucleus . 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. Plays a role in modulating cell spreading and migration..
• Protein Sequence: MTGSNMSDALANAVCQRCQARFSPAERIVNSNGELYHEHCFVCAQCFRPFPEGLFYEFEGRKYCEHDFQMLFAPCCGSCGEFIIGRVIKAMNNNWHPGCFRCELCDVELADLGFVKNAGRHLCRPCHNREKAKGLGKYICQRCHLVIDEQPLMFRSDAYHPDHFNCTHCGKELTAEARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNALGKQWHVEHFVCAKCEKPFLGHRHYEKKGLAYCETHYNQLFGDVCYNCSHVIEGDVVSALNKAWCVSCFSCSTCNSKLTLKNKFVEFDMKPVCKRCYEKFPLELKKRLKKLSELTSRKAQPKATDLNSA

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
2	Phosphorylation	------MTGSNMSDA ------CCCCCHHHH	49.68	28857561
4	Phosphorylation	----MTGSNMSDALA ----CCCCCHHHHHH	21.86	28857561
14 (in isoform 2)	Phosphorylation	-	2.61	-
22 (in isoform 2)	Phosphorylation	-	13.22	24501219
27 (in isoform 2)	Phosphorylation	-	40.02	22210691
31 (in isoform 2)	Phosphorylation	-	35.00	22210691
185	Phosphorylation	RELKGELYCLPCHDK HHHCCEEEEEECCCC	6.40	29496907
229	Sumoylation	FVCAKCEKPFLGHRH EEEECCCCCCCCCCH	51.01	-
229	Sumoylation	FVCAKCEKPFLGHRH EEEECCCCCCCCCCH	51.01	-
270	Phosphorylation	VIEGDVVSALNKAWC CCCCHHHHHCCCEEE	27.21	28857561
274	Ubiquitination	DVVSALNKAWCVSCF HHHHHCCCEEEEECC	44.08	-
282	Phosphorylation	AWCVSCFSCSTCNSK EEEEECCCCCCCCCE	16.10	-
289	Ubiquitination	SCSTCNSKLTLKNKF CCCCCCCEEEECCCE	31.34	-
291	Phosphorylation	STCNSKLTLKNKFVE CCCCCEEEECCCEEE	39.15	24719451
295	Ubiquitination	SKLTLKNKFVEFDMK CEEEECCCEEEECCH	49.56	-
324	O-linked_Glycosylation	KKRLKKLSELTSRKA HHHHHHHHHHHCCCC	39.17	30379171
324	Phosphorylation	KKRLKKLSELTSRKA HHHHHHHHHHHCCCC	39.17	20068231
327	Phosphorylation	LKKLSELTSRKAQPK HHHHHHHHCCCCCCC	23.57	18669648
328	Phosphorylation	KKLSELTSRKAQPKA HHHHHHHCCCCCCCC	44.39	25690035

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LIMS2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LIMS2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LIMS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ILK_HUMAN	ILK	physical	12167643
A4_HUMAN	APP	physical	21832049
K1C40_HUMAN	KRT40	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327 AND SER-328, ANDMASS SPECTROMETRY.
PubMed: 18669648