LACRT_HUMAN - dbPTM
LACRT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LACRT_HUMAN
UniProt AC Q9GZZ8
Protein Name Extracellular glycoprotein lacritin
Gene Name LACRT
Organism Homo sapiens (Human).
Sequence Length 138
Subcellular Localization Secreted.
Protein Description Modulates secretion by lacrimal acinar cells..
Protein Sequence MKFTTLLFLAAVAGALVYAEDASSDSTGADPAQEAGTSKPNEEISGPAEPASPPETTTTAQETSAAAVQGTAKVTSSRQELNPLKSIVEKSILLTEQALAKAGKGMHGGVPGGKQFIENGSEFAQKLLKKFSLLKPWA
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
75O-linked_GlycosylationVQGTAKVTSSRQELN
HHCCEEECCCCHHHC
21.9355829599
76O-linked_GlycosylationQGTAKVTSSRQELNP
HCCEEECCCCHHHCC
26.8955829603
77O-linked_GlycosylationGTAKVTSSRQELNPL
CCEEECCCCHHHCCH
28.7255829607
119N-linked_GlycosylationGGKQFIENGSEFAQK
CHHHHHHCHHHHHHH
55.2516740002
121PhosphorylationKQFIENGSEFAQKLL
HHHHHCHHHHHHHHH
40.91-
132PhosphorylationQKLLKKFSLLKPWA-
HHHHHHHCCCCCCC-
41.4924719451

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 LACRT_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LACRT_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 LACRT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDC1_HUMANSDC1physical
16982797
VTNC_HUMANVTNphysical
11419941
FINC_HUMANFN1physical
11419941
NID1_HUMANNID1physical
11419941
A4_HUMANAPPphysical
21832049
SDC1_HUMANSDC1physical
23504321
TGM2_HUMANTGM2physical
23425695
PLXA2_HUMANPLXNA2physical
28514442
PCYXL_HUMANPCYOX1Lphysical
28514442
ARSK_HUMANARSKphysical
28514442
K319L_HUMANKIAA0319Lphysical
28514442
NDST2_HUMANNDST2physical
28514442
EMC4_HUMANEMC4physical
28514442
SELN_HUMANSEPN1physical
28514442
ACOX1_HUMANACOX1physical
28514442
RN114_HUMANRNF114physical
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 LACRT_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119, AND MASSSPECTROMETRY.

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