ERIC1_HUMAN - dbPTM
ERIC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERIC1_HUMAN
UniProt AC Q86X53
Protein Name Glutamate-rich protein 1
Gene Name ERICH1
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization
Protein Description
Protein Sequence MAAHRKHVFVEKVLQRLFPPVPSGQGKREPQTLAVQNPPKKVTSEKVSQKHAEPLTDTGSETPTARRLYTASGPPEGYVPCWPEPSSCGSPENASSGDDTEDQDPHDQPKRRRIRKHKSKKKFKNPNNVLIEQAELEKQQSLLQEKSQRQHTDGTTISKNKKRKLKKKQQIKRKKAAGLAAKAAGVSFMYQPEDSSNEGEGVGEACEEDGVDTSEEDPTLAGEEDVKDTREEDGADASEEDLTRARQEEGADASEEDPTPAGEEDVKDAREEDGVDTIEEDLTRAGEEDGKDTREEDGADASEEDPTWAGEEEGADSGEEDGADASEEDDTITNEKAHSILNFLKSTQEMYFYDGVSRDAASAALADAAEELLDRLASHSMLPSDVSILYHMKTLLLLQDTERLKHALEMFPEHCTMPPDHARVISAFFSYWITHILPEKSSD
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
12AcetylationRKHVFVEKVLQRLFP
HCHHHHHHHHHHHCC
42.8319608861
23PhosphorylationRLFPPVPSGQGKREP
HHCCCCCCCCCCCCC
43.94-
50AcetylationTSEKVSQKHAEPLTD
CCHHHHHHHCCCCCC
36.9625953088
56PhosphorylationQKHAEPLTDTGSETP
HHHCCCCCCCCCCCC
42.0821712546
58PhosphorylationHAEPLTDTGSETPTA
HCCCCCCCCCCCCCC
37.0529396449
60PhosphorylationEPLTDTGSETPTARR
CCCCCCCCCCCCCCC
40.1530576142
62PhosphorylationLTDTGSETPTARRLY
CCCCCCCCCCCCCCC
27.8629255136
64PhosphorylationDTGSETPTARRLYTA
CCCCCCCCCCCCCCC
39.9729255136
118AcetylationRRRIRKHKSKKKFKN
HHHHHHHHCCCCCCC
67.9920167786
121AcetylationIRKHKSKKKFKNPNN
HHHHHCCCCCCCCCC
71.2220167786
124UbiquitinationHKSKKKFKNPNNVLI
HHCCCCCCCCCCHHH
79.12-
155PhosphorylationQRQHTDGTTISKNKK
HHHCCCCCCCCHHHH
24.62-
158PhosphorylationHTDGTTISKNKKRKL
CCCCCCCCHHHHHHH
28.25-
229PhosphorylationGEEDVKDTREEDGAD
CCCCCCCCCHHCCCC
33.9724247654
238PhosphorylationEEDGADASEEDLTRA
HHCCCCCCHHHHHHH
41.9129255136
243PhosphorylationDASEEDLTRARQEEG
CCCHHHHHHHHHHHC
34.3123927012
254PhosphorylationQEEGADASEEDPTPA
HHHCCCCCCCCCCCC
41.9129255136
259PhosphorylationDASEEDPTPAGEEDV
CCCCCCCCCCCHHHH
37.7829255136
277PhosphorylationREEDGVDTIEEDLTR
HHHHCCCCHHHHHHH
28.0721815630
283PhosphorylationDTIEEDLTRAGEEDG
CCHHHHHHHHCCCCC
30.6927732954
302PhosphorylationEEDGADASEEDPTWA
HHCCCCCCCCCCCCC
41.9125137130
317PhosphorylationGEEEGADSGEEDGAD
CCCCCCCCCCCCCCC
47.7925137130
326PhosphorylationEEDGADASEEDDTIT
CCCCCCCCCCCCCCC
41.9125137130
339PhosphorylationITNEKAHSILNFLKS
CCHHHHHHHHHHHHH
33.3625159151

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 ERIC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERIC1_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 ERIC1_HUMAN !!

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

Oops, there are no PPI records of ERIC1_HUMAN !!

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERIC1_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-12, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND THR-277, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.

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