LRRT1_HUMAN - dbPTM
LRRT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRT1_HUMAN
UniProt AC Q86UE6
Protein Name Leucine-rich repeat transmembrane neuronal protein 1
Gene Name LRRTM1
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Cell junction, synapse, postsynaptic cell membrane
Single-pass type I membrane protein.
Protein Description Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level..
Protein Sequence MDFLLLGLCLYWLLRRPSGVVLCLLGACFQMLPAAPSGCPQLCRCEGRLLYCEALNLTEAPHNLSGLLGLSLRYNSLSELRAGQFTGLMQLTWLYLDHNHICSVQGDAFQKLRRVKELTLSSNQITQLPNTTFRPMPNLRSVDLSYNKLQALAPDLFHGLRKLTTLHMRANAIQFVPVRIFQDCRSLKFLDIGYNQLKSLARNSFAGLFKLTELHLEHNDLVKVNFAHFPRLISLHSLCLRRNKVAIVVSSLDWVWNLEKMDLSGNEIEYMEPHVFETVPHLQSLQLDSNRLTYIEPRILNSWKSLTSITLAGNLWDCGRNVCALASWLNNFQGRYDGNLQCASPEYAQGEDVLDAVYAFHLCEDGAEPTSGHLLSAVTNRSDLGPPASSATTLADGGEGQHDGTFEPATVALPGGEHAENAVQIHKVVTGTMALIFSFLIVVLVLYVSWKCFPASLRQLRQCFVTQRRKQKQKQTMHQMAAMSAQEYYVDYKPNHIEGALVIINEYGSCTCHQQPARECEV
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
56N-linked_GlycosylationLLYCEALNLTEAPHN
EEEEEECCCCCCCCC
52.55UniProtKB CARBOHYD
63N-linked_GlycosylationNLTEAPHNLSGLLGL
CCCCCCCCHHHHHHH
34.54UniProtKB CARBOHYD
65PhosphorylationTEAPHNLSGLLGLSL
CCCCCCHHHHHHHHH
32.48-
71PhosphorylationLSGLLGLSLRYNSLS
HHHHHHHHHCCCCHH
14.70-
76PhosphorylationGLSLRYNSLSELRAG
HHHHCCCCHHHHHCC
25.0826270265
78PhosphorylationSLRYNSLSELRAGQF
HHCCCCHHHHHCCCC
34.1126270265
130N-linked_GlycosylationNQITQLPNTTFRPMP
CCCCCCCCCCCCCCC
61.41UniProtKB CARBOHYD
141PhosphorylationRPMPNLRSVDLSYNK
CCCCCCCCCCCCHHH
24.1327499020
164PhosphorylationFHGLRKLTTLHMRAN
HHHHHHHHHHHHHHC
30.2823663014
165PhosphorylationHGLRKLTTLHMRANA
HHHHHHHHHHHHHCC
25.7123663014
204PhosphorylationLKSLARNSFAGLFKL
HHHHHHHCCHHHHHH
15.7725003641
302PhosphorylationIEPRILNSWKSLTSI
ECHHHHHCCCCCCEE
32.22-
380N-linked_GlycosylationHLLSAVTNRSDLGPP
CHHHHHCCHHHCCCC
34.56UniProtKB CARBOHYD
476PhosphorylationRKQKQKQTMHQMAAM
HHHHHHHHHHHHHHH
24.5330576142
484PhosphorylationMHQMAAMSAQEYYVD
HHHHHHHHHHHHHCC
23.2925002506
488PhosphorylationAAMSAQEYYVDYKPN
HHHHHHHHHCCCCCC
9.1925002506
489PhosphorylationAMSAQEYYVDYKPNH
HHHHHHHHCCCCCCC
6.0125002506
492PhosphorylationAQEYYVDYKPNHIEG
HHHHHCCCCCCCEEE
20.5030576142

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 LRRT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRT1_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 LRRT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AREL1_HUMANAREL1physical
28514442
AT2A3_HUMANATP2A3physical
28514442
NSMA_HUMANSMPD2physical
28514442
CNPY3_HUMANCNPY3physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
MARC1_HUMANMARC1physical
28514442
RAB12_HUMANRAB12physical
28514442
CA043_HUMANC1orf43physical
28514442
TYW1_HUMANTYW1physical
28514442
NSUN3_HUMANNSUN3physical
28514442
PDZD8_HUMANPDZD8physical
28514442
PDE3B_HUMANPDE3Bphysical
28514442
STIM1_HUMANSTIM1physical
28514442
PIGA_HUMANPIGAphysical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
TSN6_HUMANTSPAN6physical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
SUN1_HUMANSUN1physical
28514442
CISD2_HUMANCISD2physical
28514442
LRP11_HUMANLRP11physical
28514442
TM131_HUMANTMEM131physical
28514442
NDC1_HUMANNDC1physical
28514442
LRFN3_HUMANLRFN3physical
28514442
TM223_HUMANTMEM223physical
28514442
K319L_HUMANKIAA0319Lphysical
28514442
FRAS1_HUMANFRAS1physical
28514442
AT131_HUMANATP13A1physical
28514442
TTC17_HUMANTTC17physical
28514442
TM39A_HUMANTMEM39Aphysical
28514442
RETST_HUMANRETSATphysical
28514442
SPTC2_HUMANSPTLC2physical
28514442
NGBR_HUMANNUS1physical
28514442
UBE4A_HUMANUBE4Aphysical
28514442
PCX3_HUMANPCNXL3physical
28514442
OSBP1_HUMANOSBPphysical
28514442
CSTN1_HUMANCLSTN1physical
28514442
PLPL6_HUMANPNPLA6physical
28514442
TBB8_HUMANTUBB8physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRRT1_HUMAN

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Related Literatures of Post-Translational Modification

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