ERF3B_HUMAN - dbPTM
ERF3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERF3B_HUMAN
UniProt AC Q8IYD1
Protein Name Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
Gene Name GSPT2
Organism Homo sapiens (Human).
Sequence Length 628
Subcellular Localization Cytoplasm .
Protein Description Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons..
Protein Sequence MDSGSSSSDSAPDCWDQVDMESPGSAPSGDGVSSAVAEAQREPLSSAFSRKLNVNAKPFVPNVHAAEFVPSFLRGPTQPPTLPAGSGSNDETCTGAGYPQGKRMGRGAPVEPSREEPLVSLEGSNSAVTMELSEPVVENGEVEMALEESWEHSKEVSEAEPGGGSSGDSGPPEESGQEMMEEKEEIRKSKSVIVPSGAPKKEHVNVVFIGHVDAGKSTIGGQIMFLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETERKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSIERYEECKEKLVPFLKKVGFSPKKDIHFMPCSGLTGANIKEQSDFCPWYTGLPFIPYLDNLPNFNRSIDGPIRLPIVDKYKDMGTVVLGKLESGSIFKGQQLVMMPNKHNVEVLGILSDDTETDFVAPGENLKIRLKGIEEEEILPGFILCDPSNLCHSGRTFDVQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALISLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD
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
71PhosphorylationHAAEFVPSFLRGPTQ
HHHHCCHHHHCCCCC		31.4528348404
102AcetylationGAGYPQGKRMGRGAP
CCCCCCCCCCCCCCC		33.6825953088
113PhosphorylationRGAPVEPSREEPLVS
CCCCCCCCCCCCCEE		38.5324719451
149PhosphorylationVEMALEESWEHSKEV
EEEEEEHHHHHHCCC		28.5226074081
191PhosphorylationEEIRKSKSVIVPSGA
HHHHHCCCEEECCCC		24.9421406692
196PhosphorylationSKSVIVPSGAPKKEH
CCCEEECCCCCCCCC		36.3720860994
237AcetylationVDKRTLEKYEREAKE
CCHHHHHHHHHHHHH		56.3722641683
237UbiquitinationVDKRTLEKYEREAKE
CCHHHHHHHHHHHHH		56.3724816145
238PhosphorylationDKRTLEKYEREAKEK
CHHHHHHHHHHHHHH		15.7328152594
245UbiquitinationYEREAKEKNRETWYL
HHHHHHHHCHHHHHE		61.67-
249PhosphorylationAKEKNRETWYLSWAL
HHHHCHHHHHEEEEE		19.03-
253PhosphorylationNRETWYLSWALDTNQ
CHHHHHEEEEECCCH		8.4624719451
258PhosphorylationYLSWALDTNQEERDK
HEEEEECCCHHHHHC		39.3824719451
267UbiquitinationQEERDKGKTVEVGRA
HHHHHCCCEEEEHHE		55.9524816145
281UbiquitinationAYFETERKHFTILDA
EEEECCCCEEEEEEC		36.5229967540
284PhosphorylationETERKHFTILDAPGH
ECCCCEEEEEECCCC		21.9828857561
316UbiquitinationVLVISARKGEFETGF
EEEEEECCCCCCCCC		63.6133845483
321PhosphorylationARKGEFETGFEKGGQ
ECCCCCCCCCCCCCC		53.11-
325MethylationEFETGFEKGGQTREH
CCCCCCCCCCCCHHH		67.11-
325AcetylationEFETGFEKGGQTREH
CCCCCCCCCCCCHHH		67.1124638353
325UbiquitinationEFETGFEKGGQTREH
CCCCCCCCCCCCHHH		67.1133845483
337UbiquitinationREHAMLAKTAGVKHL
HHHHHHHHHHCCCEE		34.6429967540
337AcetylationREHAMLAKTAGVKHL
HHHHHHHHHHCCCEE		34.64-
369UbiquitinationRYEECKEKLVPFLKK
HHHHHHHHHHHHHHH		40.04-
375UbiquitinationEKLVPFLKKVGFSPK
HHHHHHHHHCCCCCC		45.8832015554
375AcetylationEKLVPFLKKVGFSPK
HHHHHHHHHCCCCCC		45.887672429
376AcetylationKLVPFLKKVGFSPKK
HHHHHHHHCCCCCCC		50.147672439
376UbiquitinationKLVPFLKKVGFSPKK
HHHHHHHHCCCCCCC		50.14-
380PhosphorylationFLKKVGFSPKKDIHF
HHHHCCCCCCCCEEE		29.8529496963
382AcetylationKKVGFSPKKDIHFMP
HHCCCCCCCCEEEEE		62.987672449
383AcetylationKVGFSPKKDIHFMPC
HCCCCCCCCEEEEEC		66.3626051181
439PhosphorylationRLPIVDKYKDMGTVV
CCEEEECCCCCCEEE		14.0423607784
444PhosphorylationDKYKDMGTVVLGKLE
ECCCCCCEEEEEECC		10.7823607784
454PhosphorylationLGKLESGSIFKGQQL
EEECCCCCCCCCEEE		33.8524719451
577UbiquitinationKTRPRFVKQDQVCIA
CCCCCCCCHHHHHHH		45.5021906983
598AcetylationTICLETFKDFPQMGR
EEEEEECCCCCCCCC		66.92129841
598UbiquitinationTICLETFKDFPQMGR
EEEEEECCCCCCCCC		66.92-
607PhosphorylationFPQMGRFTLRDEGKT
CCCCCCEEECCCCCE		21.3724719451
613UbiquitinationFTLRDEGKTIAIGKV
EEECCCCCEEEEEEE		34.4133845483
619UbiquitinationGKTIAIGKVLKLVPE
CCEEEEEEEEEECCC		37.9833845483
619AcetylationGKTIAIGKVLKLVPE
CCEEEEEEEEEECCC		37.98-
622UbiquitinationIAIGKVLKLVPEKD-
EEEEEEEEECCCCC-		50.8833845483
622AcetylationIAIGKVLKLVPEKD-
EEEEEEEEECCCCC-		50.8822641671
627UbiquitinationVLKLVPEKD------
EEEECCCCC------		63.7724816145
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 ERF3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERF3B_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 ERF3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TCPB_HUMANCCT2physical
22939629
PABP1_HUMANPABPC1physical
18447585
RENT1_HUMANUPF1physical
18447585
SNX2_HUMANSNX2physical
22863883
PAPS2_HUMANPAPSS2physical
26344197
ERF3A_HUMANGSPT1physical
28514442
SRS12_HUMANSRSF12physical
28514442
ERF1_HUMANETF1physical
28514442
NCBP3_HUMANC17orf85physical
28514442
CLK3_HUMANCLK3physical
28514442
LAR1B_HUMANLARP1Bphysical
28514442
CASC3_HUMANCASC3physical
28514442
PABP4_HUMANPABPC4physical
28514442
PABP1_HUMANPABPC1physical
28514442
LARP1_HUMANLARP1physical
28514442
IF2B3_HUMANIGF2BP3physical
28514442
MOV10_HUMANMOV10physical
28514442
RENT1_HUMANUPF1physical
28514442
ELAV2_HUMANELAVL2physical
28514442
ZC11A_HUMANZC3H11Aphysical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
CLK2_HUMANCLK2physical
28514442
NCBP1_HUMANNCBP1physical
28514442
HNRPC_HUMANHNRNPCphysical
28514442
F120A_HUMANFAM120Aphysical
28514442
ZCHC3_HUMANZCCHC3physical
28514442
YTDC1_HUMANYTHDC1physical
28514442
SRSF1_HUMANSRSF1physical
28514442
ZCH18_HUMANZC3H18physical
28514442
PAIP1_HUMANPAIP1physical
28514442
RBBP6_HUMANRBBP6physical
28514442
IF2B1_HUMANIGF2BP1physical
28514442
DHX30_HUMANDHX30physical
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 ERF3B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237; LYS-325; LYS-619 ANDLYS-622, AND MASS SPECTROMETRY.

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