S14L2_HUMAN - dbPTM
S14L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S14L2_HUMAN
UniProt AC O76054
Protein Name SEC14-like protein 2
Gene Name SEC14L2
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Cytoplasm. Nucleus. Cytoplasmic in absence of alpha-tocopherol, and nuclear in presence of alpha-tocopherol.
Protein Description Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell..
Protein Sequence MSGRVGDLSPRQKEALAKFRENVQDVLPALPNPDDYFLLRWLRARSFDLQKSEAMLRKHVEFRKQKDIDNIISWQPPEVIQQYLSGGMCGYDLDGCPVWYDIIGPLDAKGLLFSASKQDLLRTKMRECELLLQECAHQTTKLGRKVETITIIYDCEGLGLKHLWKPAVEAYGEFLCMFEENYPETLKRLFVVKAPKLFPVAYNLIKPFLSEDTRKKIMVLGANWKEVLLKHISPDQVPVEYGGTMTDPDGNPKCKSKINYGGDIPRKYYVRDQVKQQYEHSVQISRGSSHQVEYEILFPGCVLRWQFMSDGADVGFGIFLKTKMGERQRAGEMTEVLPNQRYNSHLVPEDGTLTCSDPGIYVLRFDNTYSFIHAKKVNFTVEVLLPDKASEEKMKQLGAGTPK
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
9PhosphorylationSGRVGDLSPRQKEAL
CCCCCCCCHHHHHHH		23.8329255136
36PhosphorylationALPNPDDYFLLRWLR
CCCCHHHHHHHHHHH		11.9624275569
46PhosphorylationLRWLRARSFDLQKSE
HHHHHHHCCCCHHHH		23.3328258704
51SuccinylationARSFDLQKSEAMLRK
HHCCCCHHHHHHHHH		58.52-
51SuccinylationARSFDLQKSEAMLRK
HHCCCCHHHHHHHHH		58.52-
113UbiquitinationLDAKGLLFSASKQDL
CCHHCCCCCCCHHHH		7.4321890473
114PhosphorylationDAKGLLFSASKQDLL
CHHCCCCCCCHHHHH		31.4424719451
116PhosphorylationKGLLFSASKQDLLRT
HCCCCCCCHHHHHHH		29.6528348404
117UbiquitinationGLLFSASKQDLLRTK
CCCCCCCHHHHHHHH		47.77-
171PhosphorylationWKPAVEAYGEFLCMF
CHHHHHHHHHHHHHH		12.0425072903
182PhosphorylationLCMFEENYPETLKRL
HHHHCCCCHHHHHHH		13.0125072903
185PhosphorylationFEENYPETLKRLFVV
HCCCCHHHHHHHEEE		32.8325072903
196UbiquitinationLFVVKAPKLFPVAYN
HEEEECCCHHHHHHH		68.5621890473
196UbiquitinationLFVVKAPKLFPVAYN
HEEEECCCHHHHHHH		68.5621890473
225UbiquitinationMVLGANWKEVLLKHI
EEECCCHHHHHHHHC		37.44-
230UbiquitinationNWKEVLLKHISPDQV
CHHHHHHHHCCCCCC		34.43-
241PhosphorylationPDQVPVEYGGTMTDP
CCCCCCEECCEEECC		22.53-
253SuccinylationTDPDGNPKCKSKINY
ECCCCCCCCCCCCCC		59.29-
253SuccinylationTDPDGNPKCKSKINY
ECCCCCCCCCCCCCC		59.29-
255UbiquitinationPDGNPKCKSKINYGG
CCCCCCCCCCCCCCC		61.99-
257SuccinylationGNPKCKSKINYGGDI
CCCCCCCCCCCCCCC		22.07-
257SuccinylationGNPKCKSKINYGGDI
CCCCCCCCCCCCCCC		22.07-
260PhosphorylationKCKSKINYGGDIPRK
CCCCCCCCCCCCCCE		26.42-
268PhosphorylationGGDIPRKYYVRDQVK
CCCCCCEEEEHHHHH		14.42-
278PhosphorylationRDQVKQQYEHSVQIS
HHHHHHHEEEEEEEE		17.0824043423
281PhosphorylationVKQQYEHSVQISRGS
HHHHEEEEEEEECCC		12.0828857561
285PhosphorylationYEHSVQISRGSSHQV
EEEEEEEECCCCCEE		17.3124043423
288PhosphorylationSVQISRGSSHQVEYE
EEEEECCCCCEEEEE		24.4427251275
289PhosphorylationVQISRGSSHQVEYEI
EEEECCCCCEEEEEE		22.2922817900
294PhosphorylationGSSHQVEYEILFPGC
CCCCEEEEEEECCCC		14.93-
333SulfoxidationERQRAGEMTEVLPNQ
CCHHHCCCEECCCCC		3.6621406390
361PhosphorylationTCSDPGIYVLRFDNT
EECCCCEEEEEECCE		10.19-
369PhosphorylationVLRFDNTYSFIHAKK
EEEECCEEEEEEEEE		14.08-
393SuccinylationPDKASEEKMKQLGAG
CCCCCHHHHHHCCCC		47.55-
393SuccinylationPDKASEEKMKQLGAG
CCCCCHHHHHHCCCC		47.55-
395UbiquitinationKASEEKMKQLGAGTP
CCCHHHHHHCCCCCC		54.13-
401PhosphorylationMKQLGAGTPK-----
HHHCCCCCCC-----		27.6328857561
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
289SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S14L2_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 S14L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S14L2_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
DB00163Vitamin E
Regulatory Network of S14L2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory