PIM1_HUMAN - dbPTM
PIM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIM1_HUMAN
UniProt AC P11309
Protein Name Serine/threonine-protein kinase pim-1
Gene Name PIM1
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Isoform 2: Cytoplasm. Nucleus.
Isoform 1: Cell membrane.
Protein Description Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis..
Protein Sequence MPHEPHEPLTPPFSALPDPAGAPSRRQSRQRPQLSSDSPSAFRASRSHSRNATRSHSHSHSPRHSLRHSPGSGSCGSSSGHRPCADILEVGMLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK
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---MPHEPHEPLTPP
---CCCCCCCCCCCC		33.82-
8PhosphorylationMPHEPHEPLTPPFSA
CCCCCCCCCCCCCCC		38.2023186163
14PhosphorylationEPLTPPFSALPDPAG
CCCCCCCCCCCCCCC		34.3727251275
23PhosphorylationLPDPAGAPSRRQSRQ
CCCCCCCCCHHHHCC		27.7015657054
24PhosphorylationPDPAGAPSRRQSRQR
CCCCCCCCHHHHCCC		39.2927251275
24UbiquitinationPDPAGAPSRRQSRQR
CCCCCCCCHHHHCCC		39.29-
28PhosphorylationGAPSRRQSRQRPQLS
CCCCHHHHCCCCCCC		28.6827251275
31UbiquitinationSRRQSRQRPQLSSDS
CHHHHCCCCCCCCCC		21.59-
31 (in isoform 2)Ubiquitination-21.59-
67UbiquitinationHSPRHSLRHSPGSGS
CCCCCCCCCCCCCCC		31.11-
67 (in isoform 2)Ubiquitination-31.1121906983
94UbiquitinationILEVGMLLSKINSLA
HHHHHHHHHHHHHHH		3.48-
96 (in isoform 1)Ubiquitination-45.9721890473
96UbiquitinationEVGMLLSKINSLAHL
HHHHHHHHHHHHHHH		45.9721890473
98PhosphorylationGMLLSKINSLAHLRA
HHHHHHHHHHHHHHC		34.4115657054
99PhosphorylationMLLSKINSLAHLRAA
HHHHHHHHHHHHHCC		30.3323917254
114PhosphorylationPCNDLHATKLAPGKE
CCCCCCCCCCCCCCC		18.8227174698
122UbiquitinationKLAPGKEKEPLESQY
CCCCCCCCCCCHHHC		69.03-
137PhosphorylationQVGPLLGSGGFGSVY
CCCCCCCCCCCCCEE		35.39-
158UbiquitinationDNLPVAIKHVEKDRI
CCCCEEEEEEECCCC		31.6821906983
158 (in isoform 1)Ubiquitination-31.6821890473
169UbiquitinationKDRISDWGELPNGTR
CCCCCCCCCCCCCCC		31.39-
183UbiquitinationRVPMEVVLLKKVSSG
CCCEEEEEEEEHHCC		7.58-
183 (in isoform 2)Ubiquitination-7.5821906983
189PhosphorylationVLLKKVSSGFSGVIR
EEEEEHHCCCCHHHH		47.0115657054
194UbiquitinationVSSGFSGVIRLLDWF
HHCCCCHHHHHHHHH		1.92-
194 (in isoform 2)Ubiquitination-1.9221906983
260UbiquitinationGVLHRDIKDENILID
CCCCCCCCCCCEEEE		64.38-
261PhosphorylationVLHRDIKDENILIDL
CCCCCCCCCCEEEEC		55.2815657054
274UbiquitinationDLNRGELKLIDFGSG
ECCCCEEEEEECCCC		38.8121906983
274 (in isoform 1)Ubiquitination-38.8121890473
280PhosphorylationLKLIDFGSGALLKDT
EEEEECCCCCEECCE		22.38-
285UbiquitinationFGSGALLKDTVYTDF
CCCCCEECCEEEECC		52.802190698
285 (in isoform 1)Ubiquitination-52.8021890473
299PhosphorylationFDGTRVYSPPEWIRY
CCCCEEECCHHHHCC		30.9922817900
308PhosphorylationPEWIRYHRYHGRSAA
HHHHCCCCCCCHHHH		19.06-
352PhosphorylationFFRQRVSSECQHLIR
HHHHHHCHHHHHHHH		39.2615657054
399PhosphorylationEIHLHSLSPGPSK--
EEEEEECCCCCCC--		30.72-
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
65SPhosphorylationKinasePKCAP17252
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIM1_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 PIM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
11237709
SNX6_HUMANSNX6physical
11591366
SND1_HUMANSND1physical
9809063
MPIP1_HUMANCDC25Aphysical
10373478
NFAC1_HUMANNFATC1physical
11823475
CBX3_HUMANCBX3physical
10664448
CDN1A_HUMANCDKN1Aphysical
12431783
NUMA1_HUMANNUMA1physical
12111331
CBX1_HUMANCBX1physical
12111331
H32_HUMANHIST2H3Cphysical
17643117
MAX_HUMANMAXphysical
17643117
MYC_HUMANMYCphysical
17643117
SKP2_HUMANSKP2physical
20663873
CDC20_HUMANCDC20physical
20663873
MDR1_HUMANABCB1physical
20460432
PIN1_HUMANPIN1physical
17297438
FZR1_HUMANFZR1physical
20663873
MDM2_HUMANMDM2physical
19166854
MDM2_HUMANMDM2physical
18467333
MARK3_HUMANMARK3physical
15319445
PIM1_HUMANPIM1physical
15319445
HS90A_HUMANHSP90AA1physical
15798097
HSP74_HUMANHSPA4physical
15798097
A4_HUMANAPPphysical
21832049
FXR2_HUMANFXR2physical
25416956
ZBTB1_HUMANZBTB1physical
25416956
TFPT_HUMANTFPTphysical
25416956
BANP_HUMANBANPphysical
25416956
HEXI2_HUMANHEXIM2physical
25416956
BEND7_HUMANBEND7physical
25416956
EDC3_HUMANEDC3physical
26186194
DCP1B_HUMANDCP1Bphysical
26186194
DCP1A_HUMANDCP1Aphysical
26186194
DDX6_HUMANDDX6physical
26186194
MARK3_HUMANMARK3physical
26186194
DCAF4_HUMANDCAF4physical
26186194
2A5B_HUMANPPP2R5Bphysical
17297438
MARK3_HUMANMARK3physical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
EDC3_HUMANEDC3physical
28514442
DCAF4_HUMANDCAF4physical
28514442
DCP1A_HUMANDCP1Aphysical
28514442
DDX6_HUMANDDX6physical
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
DB00131Adenosine monophosphate
Regulatory Network of PIM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Pim-1 ligand-bound structures reveal the mechanism ofserine/threonine kinase inhibition by LY294002.";
Jacobs M.D., Black J., Futer O., Swenson L., Hare B., Fleming M.,Saxena K.;
J. Biol. Chem. 280:13728-13734(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 124-396 IN COMPLEXES WITHADENOSINE AND INHIBITORS STAUROSPORINE AND LY294002, CATALYTICACTIVITY, COFACTOR, ENZYME REGULATION, MASS SPECTROMETRY, ANDPHOSPHORYLATION AT SER-99; THR-114; SER-189 AND SER-352.

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