PIMT_HUMAN - dbPTM
PIMT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIMT_HUMAN
UniProt AC P22061
Protein Name Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Gene Name PCMT1
Organism Homo sapiens (Human).
Sequence Length 227
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein..
Protein Sequence MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
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------MAWKSGGAS
------CCCCCCCCC		23.542684970
4Ubiquitination----MAWKSGGASHS
----CCCCCCCCCHH		29.6821890473
4 (in isoform 2)Ubiquitination-29.68-
42-Hydroxyisobutyrylation----MAWKSGGASHS
----CCCCCCCCCHH		29.68-
4Acetylation----MAWKSGGASHS
----CCCCCCCCCHH		29.6825953088
4Malonylation----MAWKSGGASHS
----CCCCCCCCCHH		29.6826320211
5Phosphorylation---MAWKSGGASHSE
---CCCCCCCCCHHH		31.5826437602
9PhosphorylationAWKSGGASHSELIHN
CCCCCCCCHHHHHHH		30.7128348404
11PhosphorylationKSGGASHSELIHNLR
CCCCCCHHHHHHHHH		31.4426437602
24AcetylationLRKNGIIKTDKVFEV
HHHCCCCCCCCEEEE		49.0725953088
32SulfoxidationTDKVFEVMLATDRSH
CCCEEEEEECCCCCH		1.3321406390
37MethylationEVMLATDRSHYAKCN
EEEECCCCCHHHCCC		22.45115486655
52PhosphorylationPYMDSPQSIGFQATI
CCCCCCCCCCEEEEE		28.23-
89PhosphorylationALDVGSGSGILTACF
EEECCCCHHHHHHHH		25.1021712546
95GlutathionylationGSGILTACFARMVGC
CHHHHHHHHHHHHCC		2.0022555962
95MethylationGSGILTACFARMVGC
CHHHHHHHHHHHHCC		2.00-
105UbiquitinationRMVGCTGKVIGIDHI
HHHCCCCEEECHHHH		16.7221890473
110PhosphorylationTGKVIGIDHIKELVD
CCEEECHHHHHHHHC		32.04-
113UbiquitinationVIGIDHIKELVDDSV
EECHHHHHHHHCCCH		41.3921890473
113AcetylationVIGIDHIKELVDDSV
EECHHHHHHHHCCCH		41.3926822725
119O-linked_GlycosylationIKELVDDSVNNVRKD
HHHHHCCCHHCCCCC		23.4521740066
124MethylationDDSVNNVRKDDPTLL
CCCHHCCCCCCCCEE		38.5272617153
125MalonylationDSVNNVRKDDPTLLS
CCHHCCCCCCCCEEC		63.3026320211
1252-HydroxyisobutyrylationDSVNNVRKDDPTLLS
CCHHCCCCCCCCEEC		63.30-
129PhosphorylationNVRKDDPTLLSSGRV
CCCCCCCCEECCCCE		47.5320860994
132PhosphorylationKDDPTLLSSGRVQLV
CCCCCEECCCCEEEE		33.5820860994
133PhosphorylationDDPTLLSSGRVQLVV
CCCCEECCCCEEEEE		30.5021406692
145SulfoxidationLVVGDGRMGYAEEAP
EEECCCCCCCCCCCC		6.1828465586
147PhosphorylationVGDGRMGYAEEAPYD
ECCCCCCCCCCCCCC		11.07-
163UbiquitinationIHVGAAAPVVPQALI
EECCCCCCCCCHHHH		23.94-
171UbiquitinationVVPQALIDQLKPGGR
CCCHHHHHHCCCCCE		48.92-
174UbiquitinationQALIDQLKPGGRLIL
HHHHHHCCCCCEEEE		35.66-
182MethylationPGGRLILPVGPAGGN
CCCEEEEEECCCCHH		23.25-
183UbiquitinationGGRLILPVGPAGGNQ
CCEEEEEECCCCHHH		14.91-
197 (in isoform 2)Ubiquitination-43.0121890473
197AcetylationQMLEQYDKLQDGSIK
HHHHHHHHHCCCCCC		43.0126051181
197UbiquitinationQMLEQYDKLQDGSIK
HHHHHHHHHCCCCCC		43.0121906983
202O-linked_GlycosylationYDKLQDGSIKMKPLM
HHHHCCCCCCCCCCE		27.5921740066
206 (in isoform 2)Ubiquitination-29.9621890473
206UbiquitinationQDGSIKMKPLMGVIY
CCCCCCCCCCEEEEE		29.9621890473
213PhosphorylationKPLMGVIYVPLTDKE
CCCEEEEEEECCCHH		8.1320068231
217PhosphorylationGVIYVPLTDKEKQWS
EEEEEECCCHHHHHH		38.6720068231
2192-HydroxyisobutyrylationIYVPLTDKEKQWSRW
EEEECCCHHHHHHCC		62.67-
219AcetylationIYVPLTDKEKQWSRW
EEEECCCHHHHHHCC		62.6725953088
224 (in isoform 2)Phosphorylation-26.2620068231
232UbiquitinationRWK------------
CCC------------		-
255Ubiquitination-----------------------------------
-----------------------------------		-
255 (in isoform 1)Ubiquitination-21890473
264Ubiquitination--------------------------------------------
--------------------------------------------		-
264 (in isoform 1)Ubiquitination-21890473
275Phosphorylation-------------------------------------------------------
-------------------------------------------------------		20068231
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 PIMT_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIMT_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 PIMT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
ZRAB2_HUMANZRANB2physical
22939629
PPIH_HUMANPPIHphysical
22939629
TPM4_HUMANTPM4physical
22939629
VATB2_HUMANATP6V1B2physical
22939629
PSB7_HUMANPSMB7physical
22939629
RD23A_HUMANRAD23Aphysical
22939629
RIR2_HUMANRRM2physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
SVIL_HUMANSVILphysical
22939629
UCHL3_HUMANUCHL3physical
22939629
SDHF2_HUMANSDHAF2physical
22939629
SIAS_HUMANNANSphysical
22939629
UBE2C_HUMANUBE2Cphysical
22939629
AIMP2_HUMANAIMP2physical
25416956
RPIA_HUMANRPIAphysical
25416956
A16A1_HUMANALDH16A1physical
26186194
TM102_HUMANTMEM102physical
26186194
DEOC_HUMANDERAphysical
26186194
PDPR_HUMANPDPRphysical
26186194
KTHY_HUMANDTYMKphysical
26186194
RAB3I_HUMANRAB3IPphysical
26186194
MIC1_HUMANC18orf8physical
26186194
RPIA_HUMANRPIAphysical
26186194
KC1E_HUMANCSNK1Ephysical
26186194
KLH24_HUMANKLHL24physical
26186194
KLH42_HUMANKLHL42physical
26186194
KBTB7_HUMANKBTBD7physical
26186194
KBTB6_HUMANKBTBD6physical
26186194
P5CR3_HUMANPYCRLphysical
26186194
KCTD3_HUMANKCTD3physical
26186194
SHKB1_HUMANSHKBP1physical
26186194
ABI2_HUMANABI2physical
26186194
ABI1_HUMANABI1physical
26186194
KLH26_HUMANKLHL26physical
26186194
YDJC_HUMANYDJCphysical
26186194
KLH18_HUMANKLHL18physical
26186194
MA2C1_HUMANMAN2C1physical
26186194
ALDR_HUMANAKR1B1physical
26344197
AK1C2_HUMANAKR1C2physical
26344197
COX17_HUMANCOX17physical
26344197
CYTB_HUMANCSTBphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOG_HUMANENO2physical
26344197
ETFA_HUMANETFAphysical
26344197
LDH6A_HUMANLDHAL6Aphysical
26344197
LDHB_HUMANLDHBphysical
26344197
MIF_HUMANMIFphysical
26344197
PRDX2_HUMANPRDX2physical
26344197
TRAP1_HUMANTRAP1physical
26344197
UFC1_HUMANUFC1physical
26344197
YKT6_HUMANYKT6physical
26344197
YDJC_HUMANYDJCphysical
28514442
DEOC_HUMANDERAphysical
28514442
A16A1_HUMANALDH16A1physical
28514442
TM102_HUMANTMEM102physical
28514442
MIC1_HUMANC18orf8physical
28514442
RPIA_HUMANRPIAphysical
28514442
KLH42_HUMANKLHL42physical
28514442
RAB3I_HUMANRAB3IPphysical
28514442
KTHY_HUMANDTYMKphysical
28514442
KLH18_HUMANKLHL18physical
28514442
MA2C1_HUMANMAN2C1physical
28514442
KLH24_HUMANKLHL24physical
28514442
P5CR3_HUMANPYCRLphysical
28514442
KBTB7_HUMANKBTBD7physical
28514442
KBTB6_HUMANKBTBD6physical
28514442
ABI1_HUMANABI1physical
28514442
PDPR_HUMANPDPRphysical
28514442
SHKB1_HUMANSHKBP1physical
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 PIMT_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferasefrom human erythrocytes. Common sequence motifs for protein, DNA, RNA,and small molecule S-adenosylmethionine-dependentmethyltransferases.";
Ingrosso D., Fowler A.V., Bleibaum J., Clarke S.;
J. Biol. Chem. 264:20131-20139(1989).
Cited for: PROTEIN SEQUENCE (ISOFORM 1).

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