PIM3_HUMAN - dbPTM
PIM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIM3_HUMAN
UniProt AC Q86V86
Protein Name Serine/threonine-protein kinase pim-3
Gene Name PIM3
Organism Homo sapiens (Human).
Sequence Length 326
Subcellular Localization Cytoplasm .
Protein Description Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth..
Protein Sequence MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKAYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGATVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHSCGVVHRDIKDENLLVDLRSGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLLFRRRVSPECQQLIRWCLSLRPSERPSLDQIAAHPWMLGADGGVPESCDLRLCTLDPDDVASTTSSSESL
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
5Ubiquitination---MLLSKFGSLAHL
---CCCCCCCHHHHH
54.43-
8PhosphorylationMLLSKFGSLAHLCGP
CCCCCCCHHHHHCCC
26.0525850435
24UbiquitinationGVDHLPVKILQPAKA
CCCCCCHHHCCCCCC
35.4432015554
30UbiquitinationVKILQPAKADKESFE
HHHCCCCCCCHHHHH
64.8921906983
33UbiquitinationLQPAKADKESFEKAY
CCCCCCCHHHHHHHH
61.1822817900
38UbiquitinationADKESFEKAYQVGAV
CCHHHHHHHHHHHCE
50.8421906983
69UbiquitinationDGLPVAVKHVVKERV
CCCCEEEHHHHHHHH
22.4221906983
73UbiquitinationVAVKHVVKERVTEWG
EEEHHHHHHHHCCCC
38.4222817900
77PhosphorylationHVVKERVTEWGSLGG
HHHHHHHCCCCCCCC
32.04-
81PhosphorylationERVTEWGSLGGATVP
HHHCCCCCCCCCEEE
25.55-
86PhosphorylationWGSLGGATVPLEVVL
CCCCCCCEEEEEEEE
26.40-
96UbiquitinationLEVVLLRKVGAAGGA
EEEEEHHHHCCCCCH
45.0222053931
172UbiquitinationGVVHRDIKDENLLVD
CCCCCCCCCCCEEEE
64.3821906983
186UbiquitinationDLRSGELKLIDFGSG
ECCCCCEEEEECCCC
38.8121906983
192PhosphorylationLKLIDFGSGALLKDT
EEEEECCCCCEECCE
22.38-
197UbiquitinationFGSGALLKDTVYTDF
CCCCCEECCEEEECC
52.8021963094
211PhosphorylationFDGTRVYSPPEWIRY
CCCCEEECCHHHHCC
30.9922817900

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 PIM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIM3_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 PIM3_HUMAN !!

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

Oops, there are no PPI records of PIM3_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 PIM3_HUMAN

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Related Literatures of Post-Translational Modification

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