LANC2_MOUSE - dbPTM
LANC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LANC2_MOUSE
UniProt AC Q9JJK2
Protein Name LanC-like protein 2
Gene Name Lancl2
Organism Mus musculus (Mouse).
Sequence Length 450
Subcellular Localization Nucleus . Cytoplasm . Cell membrane . Localizes to the juxta-nuclear vesicles. Associates with the cortical actin cytoskeleton. Cholesterol depletion by methyl-beta-cyclodextrin causes partial dissociation from the cell membrane in vitro and an enhan
Protein Description Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes..
Protein Sequence MGETMSKRLKFHLGEAEMEERSFPNPFPDYEAAASAAGLAAGSAEETGRVCPLPTTEDPGLPFHPNGKIVPNFIKRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTGDQTYLLRSLDYVKRTLRNLSGRRVTFLCGDAGPLAVGAVIYHKLKSECESQECITKLLQMHRTIVCQESELPDELLYGRAGYLYALLYLNTEIGPGTVGETAIKEVVSAIIESGKSLSREERKSERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPEAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHVLLQAYQVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTSGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAVHFLSDILVPETARFPAFELGFLQKD
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
2Myristoylation------MGETMSKRL
------CCCCHHHHH
38.80-
75UbiquitinationKIVPNFIKRIQTKIK
CCCHHHHHHHHHHHH
39.0322790023
82UbiquitinationKRIQTKIKDLLQQME
HHHHHHHHHHHHHHH
43.8322790023
149S-palmitoylationGRRVTFLCGDAGPLA
CCEEEEECCCCCHHH
3.9628680068
166UbiquitinationAVIYHKLKSECESQE
HHHHHHHHHHHHCHH
49.3522790023
177UbiquitinationESQECITKLLQMHRT
HCHHHHHHHHHHHCC
27.5622790023
187S-nitrosylationQMHRTIVCQESELPD
HHHCCEECCCCCCCC
3.0824895380
198PhosphorylationELPDELLYGRAGYLY
CCCCHHHHCHHHHHH
19.7222817900
229PhosphorylationTAIKEVVSAIIESGK
HHHHHHHHHHHHHCC
20.9427180971
234PhosphorylationVVSAIIESGKSLSRE
HHHHHHHHCCCCCHH
40.9027180971
259PhosphorylationYQWHRKQYVGAAHGM
HHHHHHHHHHHHHHH
12.1322817900
290UbiquitinationETLTEMVKPSIDYVR
HHHHHHHCCCCCHHH
31.5622790023
292PhosphorylationLTEMVKPSIDYVRHK
HHHHHCCCCCHHHCC
23.5220415495
295PhosphorylationMVKPSIDYVRHKKFR
HHCCCCCHHHCCCCC
9.5629899451
314PhosphorylationPSSLSNETDRLVHWC
CCCCCCHHHHHHHHH
30.5729899451

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

Oops, there are no upstream regulatory protein records of LANC2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LANC2_MOUSE !!

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 LANC2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LANC2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LANC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198; TYR-259 ANDTYR-295, AND MASS SPECTROMETRY.

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