LMLN_HUMAN - dbPTM
LMLN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMLN_HUMAN
UniProt AC Q96KR4
Protein Name Leishmanolysin-like peptidase
Gene Name LMLN
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Cytoplasm. Lipid droplet. Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells.
Protein Description Metalloprotease essential for the coordination of mitotic progression, and also plays a role in cell migration..
Protein Sequence MVTTLGPKMAAEWGGGVGYSGSGPGRSRWRWSGSVWVRSVLLLLGGLRASATSTPVSLGSSPPCRHHVPSDTEVINKVHLKANHVVKRDVDEHLRIKTVYDKSVEELLPEKKNLVKNKLFPQAISYLEKTFQVRRPAGTILLSRQCATNQYLRKENDPHRYCTGECAAHTKCGPVIVPEEHLQQCRVYRGGKWPHGAVGVPDQEGISDADFVLYVGALATERCSHENIISYAAYCQQEANMDRPIAGYANLCPNMISTQPQEFVGMLSTVKHEVIHALGFSAGLFAFYHDKDGNPLTSRFADGLPPFNYSLGLYQWSDKVVRKVERLWDVRDNKIVRHTVYLLVTPRVVEEARKHFDCPVLEGMELENQGGVGTELNHWEKRLLENEAMTGSHTQNRVLSRITLALMEDTGRQMLSPYCDTLRSNPLQLTCRQDQRAVAVCNLQKFPKPLPQEYQYFDELSGIPAEDLPYYGGSVEIADYCPFSQEFSWHLSGEYQRSSDCRILENQPEIFKNYGAEKYGPHSVCLIQKSAFVMEKCERKLSYPDWGSGCYQVSCSPQGLKVWVQDTSYLCSRAGQVLPVSIQMNGWIHDGNLLCPSCWDFCELCPPETDPPATNLTRALPLDLCSCSSSLVVTLWLLLGNLFPLLAGFLLCIWH
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
20PhosphorylationWGGGVGYSGSGPGRS
CCCCCCCCCCCCCCC
22.1329759185
22PhosphorylationGGVGYSGSGPGRSRW
CCCCCCCCCCCCCCC
35.5529759185
27PhosphorylationSGSGPGRSRWRWSGS
CCCCCCCCCCCCCCC
41.9529759185
98PhosphorylationDEHLRIKTVYDKSVE
HHHCCEEEEECCCHH
23.1721712546
139PhosphorylationQVRRPAGTILLSRQC
CCCCCCCEEEEEEEH
15.57-
143PhosphorylationPAGTILLSRQCATNQ
CCCEEEEEEEHHHHH
19.50-
151PhosphorylationRQCATNQYLRKENDP
EEHHHHHHHHHCCCC
15.56-
161PhosphorylationKENDPHRYCTGECAA
HCCCCCCCCCCCCCC
7.42-
163PhosphorylationNDPHRYCTGECAAHT
CCCCCCCCCCCCCCC
27.38-
170PhosphorylationTGECAAHTKCGPVIV
CCCCCCCCCCCCEEC
24.25-
298PhosphorylationKDGNPLTSRFADGLP
CCCCCCCHHCCCCCC
32.84-
314PhosphorylationFNYSLGLYQWSDKVV
CCCEEEHHHCCHHHH
13.21-
317PhosphorylationSLGLYQWSDKVVRKV
EEEHHHCCHHHHHHH
16.42-
339PhosphorylationDNKIVRHTVYLLVTP
CCEEEEEEEEEEECH
10.5729083192
341PhosphorylationKIVRHTVYLLVTPRV
EEEEEEEEEEECHHH
8.7529083192
345PhosphorylationHTVYLLVTPRVVEEA
EEEEEEECHHHHHHH
12.8324719451
348 (in isoform 2)Phosphorylation-7.1822210691
351 (in isoform 2)Phosphorylation-42.0122210691
365 (in isoform 2)Phosphorylation-64.8822210691
400 (in isoform 3)Phosphorylation-20.8422210691
401 (in isoform 2)Phosphorylation-23.0422210691
403 (in isoform 3)Phosphorylation-12.6022210691
417 (in isoform 3)Phosphorylation-29.7922210691
453 (in isoform 3)Phosphorylation-32.4422210691
514PhosphorylationQPEIFKNYGAEKYGP
CCHHHHHCCCHHHCC
20.5018083107
519PhosphorylationKNYGAEKYGPHSVCL
HHCCCHHHCCCEEEE
27.6518083107

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 LMLN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMLN_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 LMLN_HUMAN !!

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

Oops, there are no PPI records of LMLN_HUMAN !!

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 LMLN_HUMAN

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Related Literatures of Post-Translational Modification

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