ERLN2_HUMAN - dbPTM
ERLN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERLN2_HUMAN
UniProt AC O94905
Protein Name Erlin-2
Gene Name ERLIN2
Organism Homo sapiens (Human).
Sequence Length 339
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) such as ITPR1. [PubMed: 19240031]
Protein Sequence MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLADKLSFGLEDEPLETATKEN
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
18PhosphorylationASSFFCASLFSAVHK
HHHHHHHHHHHHHHH		31.00-
21PhosphorylationFFCASLFSAVHKIEE
HHHHHHHHHHHHHHC		34.37-
34PhosphorylationEEGHIGVYYRGGALL
HCCCCEEEEECCEEE		5.1330576142
61PhosphorylationPFITSYKSVQTTLQT
HHHHCCCCCCCEECC		15.9526437602
106N-linked_GlycosylationAVYDIVKNYTADYDK
HHHHHHHHCCCCHHH		28.6117502376
113UbiquitinationNYTADYDKALIFNKI
HCCCCHHHHHHHHHH		38.57-
172UbiquitinationIQAVRVTKPNIPEAI
EEEEEECCCCHHHHH		32.96-
190 (in isoform 1)Ubiquitination-61.3121906983
190UbiquitinationYELMESEKTKLLIAA
HHHHHCHHHHHHHHH		61.312190698
191PhosphorylationELMESEKTKLLIAAQ
HHHHCHHHHHHHHHH		23.9125599653
192UbiquitinationLMESEKTKLLIAAQK
HHHCHHHHHHHHHHH		52.98-
199UbiquitinationKLLIAAQKQKVVEKE
HHHHHHHHHHHHHHH		47.57-
228PhosphorylationVAQVAEITYGQKVME
HHHHHHHHHCCHHHH		17.0728152594
229PhosphorylationAQVAEITYGQKVMEK
HHHHHHHHCCHHHHH		24.1828152594
238PhosphorylationQKVMEKETEKKISEI
CHHHHHHHHHHHHHH		65.2625599653
241UbiquitinationMEKETEKKISEIEDA
HHHHHHHHHHHHHHH		45.28-
263PhosphorylationAKADAECYTAMKIAE
HHCCHHHHHHHHHHH		6.7722817900
267AcetylationAECYTAMKIAEANKL
HHHHHHHHHHHHHCC		35.98-
275AcetylationIAEANKLKLTPEYLQ
HHHHHCCCCCHHHHH		52.5025953088
277PhosphorylationEANKLKLTPEYLQLM
HHHCCCCCHHHHHHH		16.70-
280PhosphorylationKLKLTPEYLQLMKYK
CCCCCHHHHHHHHHH		10.8420049867
285AcetylationPEYLQLMKYKAIASN
HHHHHHHHHHHHHCC		52.7925038526
296PhosphorylationIASNSKIYFGKDIPN
HHCCCEEEECCCCCC		15.2622817900
308PhosphorylationIPNMFMDSAGSVSKQ
CCCCHHCCCCHHHHH		23.8120860994
311PhosphorylationMFMDSAGSVSKQFEG
CHHCCCCHHHHHHHH		23.9620860994
313PhosphorylationMDSAGSVSKQFEGLA
HCCCCHHHHHHHHHH		23.5725693802
322UbiquitinationQFEGLADKLSFGLED
HHHHHHHHHCCCCCC		40.18-
334O-linked_GlycosylationLEDEPLETATKEN--
CCCCCCCHHCCCC--		47.5155829213
336O-linked_GlycosylationDEPLETATKEN----
CCCCCHHCCCC----		46.4355829217
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 ERLN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERLN2_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 ERLN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERLN1_HUMANERLIN1physical
19240031
AMFR_HUMANAMFRphysical
21343306
RN139_HUMANRNF139physical
21343306
SYVN1_HUMANSYVN1physical
21343306
TMUB1_HUMANTMUB1physical
21343306
PSMD2_HUMANPSMD2physical
17502376
SYVN1_HUMANSYVN1physical
17502376
AMFR_HUMANAMFRphysical
17502376
UFD1_HUMANUFD1Lphysical
17502376
DERL1_HUMANDERL1physical
17502376
HMDH_HUMANHMGCRphysical
17502376
CD3D_HUMANCD3Dphysical
17502376
FLOT1_HUMANFLOT1physical
22939629
K2C7_HUMANKRT7physical
22939629
RAB2A_HUMANRAB2Aphysical
22939629
FLOT2_HUMANFLOT2physical
22939629
HNRL2_HUMANHNRNPUL2physical
22939629
PDCD6_HUMANPDCD6physical
22939629
ERLN1_HUMANERLIN1physical
22690709
SCAP_HUMANSCAPphysical
22690709
INSI1_HUMANINSIG1physical
22690709
AMFR_HUMANAMFRphysical
24217618
SCAP_HUMANSCAPphysical
24217618
INSI1_HUMANINSIG1physical
24217618
SRBP1_HUMANSREBF1physical
24217618
SRBP2_HUMANSREBF2physical
24217618
ERLN1_HUMANERLIN1physical
24217618
SRPRB_HUMANSRPRBphysical
21343306
CASP8_HUMANCASP8physical
21343306
CALX_HUMANCANXphysical
21343306
TCPA_HUMANTCP1physical
21343306
CCD47_HUMANCCDC47physical
21343306
AT2A2_HUMANATP2A2physical
21343306
SC61B_HUMANSEC61Bphysical
21343306
ENPL_HUMANHSP90B1physical
21343306
GRP78_HUMANHSPA5physical
21343306
ERLN1_HUMANERLIN1physical
21343306
UBC_HUMANUBCphysical
21343306
HSP74_HUMANHSPA4physical
21343306
XPO2_HUMANCSE1Lphysical
21343306
TIF1B_HUMANTRIM28physical
21343306
HAX1_HUMANHAX1physical
21343306
MIRO1_HUMANRHOT1physical
21343306
TIM50_HUMANTIMM50physical
21343306
HNRPM_HUMANHNRNPMphysical
22119785
MBRL_HUMANTMEM259physical
22119785
DUS3_HUMANDUSP3physical
22119785
TBB5_HUMANTUBBphysical
22119785
ERLN1_HUMANERLIN1physical
22119785
GRP78_HUMANHSPA5physical
26186194
ARSK_HUMANARSKphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
FKB14_HUMANFKBP14physical
26186194
GSTM5_HUMANGSTM5physical
26186194
AMGO1_HUMANAMIGO1physical
26186194
CD109_HUMANCD109physical
26186194
CA2D1_HUMANCACNA2D1physical
26186194
SEPR_HUMANFAPphysical
26209915
RN170_HUMANRNF170physical
25882839
GSTM5_HUMANGSTM5physical
28514442
FKB14_HUMANFKBP14physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
GALNS_HUMANGALNSphysical
28514442
GRP78_HUMANHSPA5physical
28514442
CA2D1_HUMANCACNA2D1physical
28514442
CD109_HUMANCD109physical
28514442
STOM_HUMANSTOMphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611225Spastic paraplegia 18, autosomal recessive (SPG18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERLN2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"SPFH2 mediates the endoplasmic reticulum-associated degradation ofinositol 1,4,5-trisphosphate receptors and other substrates inmammalian cells.";
Pearce M.M., Wang Y., Kelley G.G., Wojcikiewicz R.J.H.;
J. Biol. Chem. 282:20104-20115(2007).
Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-106, ANDMUTAGENESIS OF ASN-106.

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