ERLN1_HUMAN - dbPTM
ERLN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERLN1_HUMAN
UniProt AC O75477
Protein Name Erlin-1
Gene Name ERLIN1
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein . Associated with lipid raft-like domains of the endoplasmic reticulum membrane.
Protein Description Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex. [PubMed: 24217618]
Protein Sequence MTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIRTGRESSLPSKEALEPSGENVIQNKESTG
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
2Phosphorylation------MTQARVLVA
------CCHHHHHHH		30.82-
20PhosphorylationGLVAVLLYASIHKIE
HHHHHHHHHHHHHHH		8.3030576142
22PhosphorylationVAVLLYASIHKIEEG
HHHHHHHHHHHHHHC		16.2130576142
42PhosphorylationYRGGALLTSPSGPGY
EECCEEEECCCCCCE		39.1724719451
43PhosphorylationRGGALLTSPSGPGYH
ECCEEEECCCCCCEE		19.6224719451
49PhosphorylationTSPSGPGYHIMLPFI
ECCCCCCEEEEEEEH		7.4224719451
58PhosphorylationIMLPFITTFRSVQTT
EEEEEHHCCCCCCCC		16.5428857561
61PhosphorylationPFITTFRSVQTTLQT
EEHHCCCCCCCCCCC		17.8728857561
63PhosphorylationITTFRSVQTTLQTDE
HHCCCCCCCCCCCCC		29.98-
64PhosphorylationTTFRSVQTTLQTDEV
HCCCCCCCCCCCCCC		27.5828857561
65PhosphorylationTFRSVQTTLQTDEVK
CCCCCCCCCCCCCCC		10.3628857561
68PhosphorylationSVQTTLQTDEVKNVP
CCCCCCCCCCCCCCC		36.9228857561
106N-linked_GlycosylationAVFDIVRNYTADYDK
HHHHHHHHCCCCCCC		27.8419159218
107PhosphorylationVFDIVRNYTADYDKT
HHHHHHHCCCCCCCE		7.8529083192
108PhosphorylationFDIVRNYTADYDKTL
HHHHHHCCCCCCCEE		19.3229083192
108N-linked_GlycosylationFDIVRNYTADYDKTL
HHHHHHCCCCCCCEE		19.3220068230
108N-linked_GlycosylationFDIVRNYTADYDKTL
HHHHHHCCCCCCCEE		19.3220068230
111PhosphorylationVRNYTADYDKTLIFN
HHHCCCCCCCEEHHH		19.5129083192
113UbiquitinationNYTADYDKTLIFNKI
HCCCCCCCEEHHHHH		38.71-
115UbiquitinationTADYDKTLIFNKIHH
CCCCCCEEHHHHHHH		5.3222817900
151UbiquitinationIDENLKQALQKDLNL
HCHHHHHHHHHHHCC		15.4622817900
154UbiquitinationNLKQALQKDLNLMAP
HHHHHHHHHHCCCCC		66.1021890473
156UbiquitinationKQALQKDLNLMAPGL
HHHHHHHHCCCCCCE		7.3621906983
156UbiquitinationKQALQKDLNLMAPGL
HHHHHHHHCCCCCCE		7.3621890473
176UbiquitinationRVTKPKIPEAIRRNF
EECCCCCHHHHHHCH		30.9624816145
190UbiquitinationFELMEAEKTKLLIAA
HHHHHHHHHHHHHHH		58.99-
191PhosphorylationELMEAEKTKLLIAAQ
HHHHHHHHHHHHHHH		20.5925599653
1922-HydroxyisobutyrylationLMEAEKTKLLIAAQK
HHHHHHHHHHHHHHH		52.98-
192UbiquitinationLMEAEKTKLLIAAQK
HHHHHHHHHHHHHHH		52.9822817900
194UbiquitinationEAEKTKLLIAAQKQK
HHHHHHHHHHHHHHH		2.3922817900
199UbiquitinationKLLIAAQKQKVVEKE
HHHHHHHHHHHHHHH		47.57-
2012-HydroxyisobutyrylationLIAAQKQKVVEKEAE
HHHHHHHHHHHHHHH		56.11-
201UbiquitinationLIAAQKQKVVEKEAE
HHHHHHHHHHHHHHH		56.1127667366
2222-HydroxyisobutyrylationVIEAEKIAQVAKIRF
HHHHHHHHHHHHHHH		14.63-
226AcetylationEKIAQVAKIRFQQKV
HHHHHHHHHHHHHHH		35.2426051181
226UbiquitinationEKIAQVAKIRFQQKV
HHHHHHHHHHHHHHH		35.24-
228UbiquitinationIAQVAKIRFQQKVME
HHHHHHHHHHHHHHH		23.71-
238UbiquitinationQKVMEKETEKRISEI
HHHHHHHHHHHHHHH		58.8524816145
238PhosphorylationQKVMEKETEKRISEI
HHHHHHHHHHHHHHH		58.8525599653
257UbiquitinationFLAREKAKADAEYYA
HHHHHHHHHHHHHHH		58.84-
259UbiquitinationAREKAKADAEYYAAH
HHHHHHHHHHHHHHH		38.95-
2592-HydroxyisobutyrylationAREKAKADAEYYAAH
HHHHHHHHHHHHHHH		38.95-
262PhosphorylationKAKADAEYYAAHKYA
HHHHHHHHHHHHHHH		10.5028152594
263PhosphorylationAKADAEYYAAHKYAT
HHHHHHHHHHHHHHH		6.7128152594
264PhosphorylationKADAEYYAAHKYATS
HHHHHHHHHHHHHHC		11.37-
265PhosphorylationADAEYYAAHKYATSN
HHHHHHHHHHHHHCC		5.42-
267UbiquitinationAEYYAAHKYATSNKH
HHHHHHHHHHHCCCC		31.67-
267AcetylationAEYYAAHKYATSNKH
HHHHHHHHHHHCCCC		31.6719608861
269AcetylationYYAAHKYATSNKHKL
HHHHHHHHHCCCCCC		14.8919608861
269UbiquitinationYYAAHKYATSNKHKL
HHHHHHHHHCCCCCC		14.8919608861
275AcetylationYATSNKHKLTPEYLE
HHHCCCCCCCHHHHH		56.5226051181
275UbiquitinationYATSNKHKLTPEYLE
HHHCCCCCCCHHHHH		56.52-
277PhosphorylationTSNKHKLTPEYLELK
HCCCCCCCHHHHHHH		20.91-
280PhosphorylationKHKLTPEYLELKKYQ
CCCCCHHHHHHHHHH		13.4828152594
282PhosphorylationKLTPEYLELKKYQAI
CCCHHHHHHHHHHHH		58.61-
286UbiquitinationEYLELKKYQAIASNS
HHHHHHHHHHHHCCC		11.1129967540
287UbiquitinationYLELKKYQAIASNSK
HHHHHHHHHHHCCCE		34.86-
319PhosphorylationLKYSDIRTGRESSLP
CCHHHHCCCCCCCCC		40.7125693802
323PhosphorylationDIRTGRESSLPSKEA
HHCCCCCCCCCCHHH		35.5020068231
324PhosphorylationIRTGRESSLPSKEAL
HCCCCCCCCCCHHHC		39.2823401153
326PhosphorylationTGRESSLPSKEALEP
CCCCCCCCCHHHCCC		45.3520068231
327PhosphorylationGRESSLPSKEALEPS
CCCCCCCCHHHCCCC		48.7120068231
328UbiquitinationRESSLPSKEALEPSG
CCCCCCCHHHCCCCC		45.10-
329PhosphorylationESSLPSKEALEPSGE
CCCCCCHHHCCCCCC		63.9320068231
330UbiquitinationSSLPSKEALEPSGEN
CCCCCHHHCCCCCCC		22.4422817900
334PhosphorylationSKEALEPSGENVIQN
CHHHCCCCCCCCCCC		49.7325159151
336PhosphorylationEALEPSGENVIQNKE
HHCCCCCCCCCCCCC		53.30-
342UbiquitinationGENVIQNKESTG---
CCCCCCCCCCCC---		36.34-
344PhosphorylationNVIQNKESTG-----
CCCCCCCCCC-----		39.7925627689
344UbiquitinationNVIQNKESTG-----
CCCCCCCCCC-----		39.79-
345PhosphorylationVIQNKESTG------
CCCCCCCCC------		48.2625627689
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 ERLN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERLN1_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 ERLN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERLN2_HUMANERLIN2physical
19240031
AMFR_HUMANAMFRphysical
21343306
RN139_HUMANRNF139physical
21343306
SYVN1_HUMANSYVN1physical
21343306
ERLN2_HUMANERLIN2physical
22939629
NDUAC_HUMANNDUFA12physical
22939629
SSRG_HUMANSSR3physical
22939629
RALY_HUMANRALYphysical
22939629
ERLN2_HUMANERLIN2physical
24217618
INSI1_HUMANINSIG1physical
24217618
SCAP_CRIGRScapphysical
24217618
SC22A_HUMANSEC22Aphysical
25416956
FA2H_HUMANFA2Hphysical
25416956
TM199_HUMANTMEM199physical
25416956
AGR3_HUMANAGR3physical
25416956
DUS3_HUMANDUSP3physical
28514442
CF120_HUMANC6orf120physical
28514442
STOM_HUMANSTOMphysical
27173435
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 ERLN1_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-267, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106, AND MASSSPECTROMETRY.

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