PEG10_HUMAN - dbPTM
PEG10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEG10_HUMAN
UniProt AC Q86TG7
Protein Name Retrotransposon-derived protein PEG10
Gene Name PEG10
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Nucleus. Cytoplasm. Detected predominantly in the cytoplasm of breast and prostate carcinomas, in hepatocellular carcinoma (HCC) and B-cell chronic lymphocytic leukemia (B-CLL) cells and in the Hep-G2 cell line. Colocalized with ALK1.
Protein Description Prevents apoptosis in hepatocellular carcinoma (HCC) cells through interaction with SIAH1, a mediator of apoptosis. May also have a role in cell growth promotion and hepatoma formation. Inhibits the TGF-beta signaling by interacting with the TGF-beta receptor ALK1. When overexpressed, induces the formation of cellular extension, such as filipodia in association with ALK1. Involved at the immediate early stage of adipocyte differentiation (By similarity). May bind to the 5'-GCCTGTCTTT-3' DNA sequence of the MB1 domain in the myelin basic protein (MBP) promoter (By similarity)..
Protein Sequence MTERRRDELSEEINNLREKVMKQSEENNNLQSQVQKLTEENTTLREQVEPTPEDEDDDIELRGAAAAAAPPPPIEEECPEDLPEKFDGNPDMLAPFMAQCQIFMEKSTRDFSVDRVRVCFVTSMMTGRAARWASAKLERSHYLMHNYPAFMMEMKHVFEDPQRREVAKRKIRRLRQGMGSVIDYSNAFQMIAQDLDWNEPALIDQYHEGLSDHIQEELSHLEVAKSLSALIGQCIHIERRLARAAAARKPRSPPRALVLPHIASHHQVDPTEPVGGARMRLTQEEKERRRKLNLCLYCGTGGHYADNCPAKASKSSPAGKLPGPAVEGPSATGPEIIRSPQDDASSPHLQVMLQIHLPGRHTLFVRAMIDSGASGNFIDHEYVAQNGIPLRIKDWPILVEAIDGRPIASGPVVHETHDLIVDLGDHREVLSFDVTQSPFFPVVLGVRWLSTHDPNITWSTRSIVFDSEYCRYHCRMYSPIPPSLPPPAPQPPLYYPVDGYRVYQPVRYYYVQNVYTPVDEHVYPDHRLVDPHIEMIPGAHSIPSGHVYSLSEPEMAALRDFVARNVKDGLITPTIAPNGAQVLQVKRGWKLQVSYDCRAPNNFTIQNQYPRLSIPNLEDQAHLATYTEFVPQIPGYQTYPTYAAYPTYPVGFAWYPVGRDGQGRSLYVPVMITWNPHWYRQPPVPQYPPPQPPPPPPPPPPPPSYSTL
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
10PhosphorylationERRRDELSEEINNLR
HHHHHHHHHHHHHHH		31.0026091039
19AcetylationEINNLREKVMKQSEE
HHHHHHHHHHHHHHH		40.9922369027
22SumoylationNLREKVMKQSEENNN
HHHHHHHHHHHHHCC		54.37-
22 (in isoform 1)Ubiquitination-54.3721890473
22UbiquitinationNLREKVMKQSEENNN
HHHHHHHHHHHHHCC		54.37-
24PhosphorylationREKVMKQSEENNNLQ
HHHHHHHHHHHCCHH		41.1623401153
32PhosphorylationEENNNLQSQVQKLTE
HHHCCHHHHHHHHHH		35.1723401153
36UbiquitinationNLQSQVQKLTEENTT
CHHHHHHHHHHHCCH		59.53-
36 (in isoform 1)Ubiquitination-59.5321890473
38PhosphorylationQSQVQKLTEENTTLR
HHHHHHHHHHCCHHH		48.5720068231
42PhosphorylationQKLTEENTTLREQVE
HHHHHHCCHHHHHCC		30.4121406692
43PhosphorylationKLTEENTTLREQVEP
HHHHHCCHHHHHCCC		35.0923025827
51PhosphorylationLREQVEPTPEDEDDD
HHHHCCCCCCCCCCC		26.2930175587
56UbiquitinationEPTPEDEDDDIELRG
CCCCCCCCCCCCHHH		71.81-
56SumoylationEPTPEDEDDDIELRG
CCCCCCCCCCCCHHH		71.81-
70UbiquitinationGAAAAAAPPPPIEEE
HHHHHCCCCCCCCCC		36.88-
72PhosphorylationAAAAAPPPPIEEECP
HHHCCCCCCCCCCCC		41.25-
85PhosphorylationCPEDLPEKFDGNPDM
CCCCCCHHCCCCHHH		46.98-
98 (in isoform 2)Ubiquitination-13.8421906983
112 (in isoform 2)Ubiquitination-27.6521906983
112PhosphorylationEKSTRDFSVDRVRVC
CCCCCCCCCCEEEEE		27.6523898821
136 (in isoform 1)Ubiquitination-48.6721890473
136UbiquitinationAARWASAKLERSHYL
HHHHHHHHHHHHHHH		48.67-
155AcetylationPAFMMEMKHVFEDPQ
HHHHHHHHHHHCCHH		24.2621466224
170UbiquitinationRREVAKRKIRRLRQG
HHHHHHHHHHHHHHC		39.60-
212 (in isoform 2)Ubiquitination-48.2021906983
228PhosphorylationLEVAKSLSALIGQCI
HHHHHHHHHHHHHHH		28.2828348404
252PhosphorylationAAARKPRSPPRALVL
HHHCCCCCCCCEEHH		48.0227174698
264PhosphorylationLVLPHIASHHQVDPT
EHHHCHHHCCCCCCC		22.3927174698
271PhosphorylationSHHQVDPTEPVGGAR
HCCCCCCCCCCCCHH		48.7521406692
282PhosphorylationGGARMRLTQEEKERR
CCHHCCCCHHHHHHH		24.4620068231
286UbiquitinationMRLTQEEKERRRKLN
CCCCHHHHHHHHHCC		56.63-
286PhosphorylationMRLTQEEKERRRKLN
CCCCHHHHHHHHHCC		56.63-
291UbiquitinationEEKERRRKLNLCLYC
HHHHHHHHCCEEEEC		39.66-
298PhosphorylationKLNLCLYCGTGGHYA
HCCEEEECCCCCCCC		2.25-
313 (in isoform 2)Phosphorylation-32.1525072903
315PhosphorylationCPAKASKSSPAGKLP
CCCCCCCCCCCCCCC		38.7720068231
315 (in isoform 2)Phosphorylation-38.7722617229
316PhosphorylationPAKASKSSPAGKLPG
CCCCCCCCCCCCCCC		23.6220068231
316 (in isoform 2)Phosphorylation-23.6226055452
321 (in isoform 2)Phosphorylation-6.0826055452
459PhosphorylationHDPNITWSTRSIVFD
CCCCCEEEEEEEEEC		12.8020068231
460PhosphorylationDPNITWSTRSIVFDS
CCCCEEEEEEEEECH		21.7220068231
469PhosphorylationSIVFDSEYCRYHCRM
EEEECHHHHHHHEEE		6.0327642862
494PhosphorylationPAPQPPLYYPVDGYR
CCCCCCCEECCCCEE		16.11-
495PhosphorylationAPQPPLYYPVDGYRV
CCCCCCEECCCCEEE		12.40-
500PhosphorylationLYYPVDGYRVYQPVR
CEECCCCEEEECEEE		7.76-
507MethylationYRVYQPVRYYYVQNV
EEEECEEEEEEEEEE		22.03-
516PhosphorylationYYVQNVYTPVDEHVY
EEEEEEECCCCCCCC		16.74-
523PhosphorylationTPVDEHVYPDHRLVD
CCCCCCCCCCCCCCC		12.5927642862
567UbiquitinationDFVARNVKDGLITPT
HHHHHHCCCCCCCCE		50.0221890473
567 (in isoform 1)Ubiquitination-50.0221890473
572PhosphorylationNVKDGLITPTIAPNG
HCCCCCCCCEECCCC		21.3028348404
574PhosphorylationKDGLITPTIAPNGAQ
CCCCCCCEECCCCCE		22.5628348404
586UbiquitinationGAQVLQVKRGWKLQV
CCEEEEEECCEEEEE		32.0321890473
586 (in isoform 1)Ubiquitination-32.0321890473
590UbiquitinationLQVKRGWKLQVSYDC
EEEECCEEEEEEEEC		31.68-
590 (in isoform 1)Ubiquitination-31.6821890473
594PhosphorylationRGWKLQVSYDCRAPN
CCEEEEEEEECCCCC		11.4228348404
595PhosphorylationGWKLQVSYDCRAPNN
CEEEEEEEECCCCCC		21.8728555341
598MethylationLQVSYDCRAPNNFTI
EEEEEECCCCCCEEE		50.62-
611MethylationTIQNQYPRLSIPNLE
EECCCCCCCCCCCHH		35.81-
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 PEG10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEG10_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 PEG10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIAH1_HUMANSIAH1physical
12810624
SIAH2_HUMANSIAH2physical
12810624
ACVL1_HUMANACVRL1physical
15611116
ACVR1_HUMANACVR1physical
15611116
BMR1A_HUMANBMPR1Aphysical
15611116
ACV1B_HUMANACVR1Bphysical
15611116
TGFR1_HUMANTGFBR1physical
15611116
BMR1B_HUMANBMPR1Bphysical
15611116
TGFR2_HUMANTGFBR2physical
15611116
AVR2A_HUMANACVR2Aphysical
15611116
AVR2B_HUMANACVR2Bphysical
15611116
RN181_HUMANRNF181physical
21988832
HNRH1_HUMANHNRNPH1physical
22863883
HNRL1_HUMANHNRNPUL1physical
22863883
TAU_HUMANMAPTphysical
23666762
LDOC1_HUMANLDOC1physical
25416956
RTL8B_HUMANFAM127Cphysical
25416956
LDOC1_HUMANLDOC1physical
26186194
USP9X_HUMANUSP9Xphysical
26186194
RTL8C_HUMANFAM127Aphysical
26186194
RTL8B_HUMANFAM127Cphysical
26186194
RTL8A_HUMANFAM127Bphysical
26186194
IQCB1_HUMANIQCB1physical
26186194
CE290_HUMANCEP290physical
26186194
RTL8A_HUMANFAM127Bphysical
28514442
RTL8B_HUMANFAM127Cphysical
28514442
LDOC1_HUMANLDOC1physical
28514442
RTL8C_HUMANFAM127Aphysical
28514442
USP9X_HUMANUSP9Xphysical
28514442
IQCB1_HUMANIQCB1physical
28514442
CE290_HUMANCEP290physical
28514442
TCAF1_HUMANFAM115Aphysical
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 PEG10_HUMAN

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Related Literatures of Post-Translational Modification

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