ERLEC_HUMAN - dbPTM
ERLEC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERLEC_HUMAN
UniProt AC Q96DZ1
Protein Name Endoplasmic reticulum lectin 1
Gene Name ERLEC1
Organism Homo sapiens (Human).
Sequence Length 483
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins..
Protein Sequence MEEGGGGVRSLVPGGPVLLVLCGLLEASGGGRALPQLSDDIPFRVNWPGTEFSLPTTGVLYKEDNYVIMTTAHKEKYKCILPLVTSGDEEEEKDYKGPNPRELLEPLFKQSSCSYRIESYWTYEVCHGKHIRQYHEEKETGQKINIHEYYLGNMLAKNLLFEKEREAEEKEKSNEIPTKNIEGQMTPYYPVGMGNGTPCSLKQNRPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCSHPKYRFRASPVNDIFCQSLPGSPFKPLTLRQLEQQEEILRVPFRRNKEEDLQSTKEERFPAIHKSIAIGSQPVLTVGTTHISKLTDDQLIKEFLSGSYCFRGGVGWWKYEFCYGKHVHQYHEDKDSGKTSVVVGTWNQEEHIEWAKKNTARAYHLQDDGTQTVRMVSHFYGNGDICDITDKPRQVTVKLKCKESDSPHAVTVYMLEPHSCQYILGVESPVICKILDTADENGLLSLPN
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
66PhosphorylationVLYKEDNYVIMTTAH
EEEECCCEEEEEECC		12.04-
70O-linked_GlycosylationEDNYVIMTTAHKEKY
CCCEEEEEECCHHHE		15.09OGP
71O-linked_GlycosylationDNYVIMTTAHKEKYK
CCEEEEEECCHHHEE		14.91OGP
78UbiquitinationTAHKEKYKCILPLVT
ECCHHHEEEEEEECC		26.35-
93UbiquitinationSGDEEEEKDYKGPNP
CCCHHHHCCCCCCCH		70.41-
95PhosphorylationDEEEEKDYKGPNPRE
CHHHHCCCCCCCHHH		28.98-
96UbiquitinationEEEEKDYKGPNPREL
HHHHCCCCCCCHHHH		77.39-
109UbiquitinationELLEPLFKQSSCSYR
HHHHHHHCCCCCEEE		57.88-
115PhosphorylationFKQSSCSYRIESYWT
HCCCCCEEEEEEEEE		21.6721394647
119PhosphorylationSCSYRIESYWTYEVC
CCEEEEEEEEEEEEC		24.4929449344
120PhosphorylationCSYRIESYWTYEVCH
CEEEEEEEEEEEECC		6.7529449344
122PhosphorylationYRIESYWTYEVCHGK
EEEEEEEEEEECCCC		11.1129449344
123PhosphorylationRIESYWTYEVCHGKH
EEEEEEEEEECCCCH		7.6929449344
143UbiquitinationEEKETGQKINIHEYY
HHHCCCCCCCCCHHH		38.78-
157UbiquitinationYLGNMLAKNLLFEKE
HHHHHHHHHHHHHHH		44.13-
163UbiquitinationAKNLLFEKEREAEEK
HHHHHHHHHHHHHHH		55.53-
179UbiquitinationKSNEIPTKNIEGQMT
HHCCCCCCCCCCCCC		51.04-
195N-linked_GlycosylationYYPVGMGNGTPCSLK
CCCCCCCCCCCCCCC		42.12UniProtKB CARBOHYD
202UbiquitinationNGTPCSLKQNRPRSS
CCCCCCCCCCCCCCC		29.27-
254PhosphorylationPKYRFRASPVNDIFC
CCCCCCCCCCCCCCC		25.7320068231
263PhosphorylationVNDIFCQSLPGSPFK
CCCCCCCCCCCCCCC		37.4020068231
267PhosphorylationFCQSLPGSPFKPLTL
CCCCCCCCCCCCCCH		25.8120068231
270UbiquitinationSLPGSPFKPLTLRQL
CCCCCCCCCCCHHHH		42.37-
273PhosphorylationGSPFKPLTLRQLEQQ
CCCCCCCCHHHHHHH		28.5520068231
300 (in isoform 1)Ubiquitination-63.9321906983
300UbiquitinationEEDLQSTKEERFPAI
HHHHHCCHHHHCHHH		63.932190698
328UbiquitinationVGTTHISKLTDDQLI
ECCCCHHHCCCHHHH		55.60-
398PhosphorylationKKNTARAYHLQDDGT
HHHCCCEEEECCCCC		9.4922817900
439PhosphorylationVKLKCKESDSPHAVT
EEEEECCCCCCCEEE		28.9630576142
446PhosphorylationSDSPHAVTVYMLEPH
CCCCCEEEEEEECCC		13.5030576142
463PhosphorylationQYILGVESPVICKIL
CEEECCCCCEEEEEC		23.2830576142
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 ERLEC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERLEC_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 ERLEC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ENPL_HUMANHSP90B1physical
18264092
GRP78_HUMANHSPA5physical
18264092
SE1L1_HUMANSEL1Lphysical
18264092
SYVN1_HUMANSYVN1physical
18264092
OS9_HUMANOS9physical
21118962
GRP78_HUMANHSPA5physical
21118962
A1AT_HUMANSERPINA1physical
19917667
VPP3_HUMANTCIRG1physical
22939629
RM24_HUMANMRPL24physical
22939629
RM52_HUMANMRPL52physical
22939629
A1AT_HUMANSERPINA1physical
23356641
FBXL4_HUMANFBXL4physical
24035498
S27A3_HUMANSLC27A3physical
22119785
SYVN1_HUMANSYVN1physical
22119785
OS9_HUMANOS9physical
22119785
UB2G2_HUMANUBE2G2physical
22119785
DERL2_HUMANDERL2physical
22119785
UB2J1_HUMANUBE2J1physical
22119785
SE1L1_HUMANSEL1Lphysical
22119785
CPVL_HUMANCPVLphysical
22119785
FA8A1_HUMANFAM8A1physical
22119785
ATF6A_HUMANATF6physical
26186194
CNTP3_HUMANCNTNAP3physical
26186194
ATF6B_HUMANATF6Bphysical
26186194
CLN5_HUMANCLN5physical
26186194
EMIL3_HUMANEMILIN3physical
26186194
GDF11_HUMANGDF11physical
26186194
GLU2B_HUMANPRKCSHphysical
26344197
CNTP3_HUMANCNTNAP3physical
28514442
ATF6A_HUMANATF6physical
28514442
ATF6B_HUMANATF6Bphysical
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 ERLEC_HUMAN

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Related Literatures of Post-Translational Modification

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