LANC1_HUMAN - dbPTM
LANC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LANC1_HUMAN
UniProt AC O43813
Protein Name LanC-like protein 1
Gene Name LANCL1
Organism Homo sapiens (Human).
Sequence Length 399
Subcellular Localization Cytoplasm . Cell membrane
Peripheral membrane protein .
Protein Description May play a role in EPS8 signaling. Binds glutathione..
Protein Sequence MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL
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------MAQRAFPNP
------CCCCCCCCC
13.9419413330
10PhosphorylationQRAFPNPYADYNKSL
CCCCCCCCCCCCHHH
20.81-
15AcetylationNPYADYNKSLAEGYF
CCCCCCCHHHHCCCC
40.3923954790
15UbiquitinationNPYADYNKSLAEGYF
CCCCCCCHHHHCCCC
40.3921906983
21PhosphorylationNKSLAEGYFDAAGRL
CHHHHCCCCCCCCCC
6.9827642862
29PhosphorylationFDAAGRLTPEFSQRL
CCCCCCCCHHHHHHH
21.29-
29O-linked_GlycosylationFDAAGRLTPEFSQRL
CCCCCCCCHHHHHHH
21.2923301498
33PhosphorylationGRLTPEFSQRLTNKI
CCCCHHHHHHHHHHH
16.8423532336
52UbiquitinationQQMERGLKSADPRDG
HHHHHHHHCCCCCCC
46.55-
95PhosphorylationAHGYVKQSLNCLTKR
HHHHHHHHHHHCCCC
18.8121406692
100PhosphorylationKQSLNCLTKRSITFL
HHHHHHCCCCEEEEE
26.9821406692
101UbiquitinationQSLNCLTKRSITFLC
HHHHHCCCCEEEEEC
31.06-
101AcetylationQSLNCLTKRSITFLC
HHHHHCCCCEEEEEC
31.0625953088
123AcetylationVAAVLYHKMNNEKQA
HHHHHHHHHCCHHHH
29.7530589831
128UbiquitinationYHKMNNEKQAEDCIT
HHHHCCHHHHHHHHH
57.8621906983
128AcetylationYHKMNNEKQAEDCIT
HHHHCCHHHHHHHHH
57.8625953088
135PhosphorylationKQAEDCITRLIHLNK
HHHHHHHHHHHHHHC
26.25-
142AcetylationTRLIHLNKIDPHAPN
HHHHHHHCCCCCCCC
55.6419608861
142UbiquitinationTRLIHLNKIDPHAPN
HHHHHHHCCCCCCCC
55.6419608861
153PhosphorylationHAPNEMLYGRIGYIY
CCCCHHHHHHHHHHH
11.7523917254
173UbiquitinationNKNFGVEKIPQSHIQ
CCCCCCCCCCHHHHH
58.23-
185PhosphorylationHIQQICETILTSGEN
HHHHHHHHHHHCCHH
19.5124076635
188PhosphorylationQICETILTSGENLAR
HHHHHHHHCCHHHHH
30.7324076635
189PhosphorylationICETILTSGENLARK
HHHHHHHCCHHHHHH
40.4426437602
203PhosphorylationKRNFTAKSPLMYEWY
HCCCCCCCCCHHHHH
22.3222210691
207PhosphorylationTAKSPLMYEWYQEYY
CCCCCCHHHHHHHHH
15.8222210691
245UbiquitinationGKLHSLVKPSVDYVC
CCCHHCCCCCCCEEE
36.55-
245AcetylationGKLHSLVKPSVDYVC
CCCHHCCCCCCCEEE
36.5525953088
250PhosphorylationLVKPSVDYVCQLKFP
CCCCCCCEEEEEECC
10.85-
319PhosphorylationYGLLKKGYGLCHGSA
HCHHHCCCCCCCCCC
18.79-
330PhosphorylationHGSAGNAYAFLTLYN
CCCCCCHHHHHHHHH
11.24-
336PhosphorylationAYAFLTLYNLTQDMK
HHHHHHHHHHHHHHH
11.68-

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 LANC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LANC1_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 LANC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SERPH_HUMANSERPINH1physical
22939629
A16A1_HUMANALDH16A1physical
26186194
DEOC_HUMANDERAphysical
26186194
TBCD9_HUMANTBC1D9physical
26186194
TBC9B_HUMANTBC1D9Bphysical
26186194
FIGN_HUMANFIGNphysical
26186194
MYO7A_HUMANMYO7Aphysical
26186194
IPP_HUMANIPPphysical
26186194
OCAD1_HUMANOCIAD1physical
26186194
UBN2_HUMANUBN2physical
26186194
FIGN_HUMANFIGNphysical
28514442
DEOC_HUMANDERAphysical
28514442
IPP_HUMANIPPphysical
28514442
A16A1_HUMANALDH16A1physical
28514442
UBN2_HUMANUBN2physical
28514442
TBCD9_HUMANTBC1D9physical
28514442
TBC9B_HUMANTBC1D9Bphysical
28514442
MYO7A_HUMANMYO7Aphysical
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 LANC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.

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