HERP1_HUMAN - dbPTM
HERP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HERP1_HUMAN
UniProt AC Q15011
Protein Name Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
Gene Name HERPUD1
Organism Homo sapiens (Human).
Sequence Length 391
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interaction is required for efficient degradation of CD3D via the ERAD pathway. [PubMed: 18307982]
Protein Sequence MESETEPEPVTLLVKSPNQRHRDLELSGDRGWSVGHLKAHLSRVYPERPRPEDQRLIYSGKLLLDHQCLRDLLPKQEKRHVLHLVCNVKSPSKMPEINAKVAESTEEPAGSNRGQYPEDSSSDGLRQREVLRNLSSPGWENISRPEAAQQAFQGLGPGFSGYTPYGWLQLSWFQQIYARQYYMQYLAATAASGAFVPPPSAQEIPVVSAPAPAPIHNQFPAENQPANQNAAPQVVVNPGANQNLRMNAQGGPIVEEDDEINRDWLDWTYSAATFSVFLSILYFYSSLSRFLMVMGATVVMYLHHVGWFPFRPRPVQNFPNDGPPPDVVNQDPNNNLQEGTDPETEDPNHLPPDRDVLDGEQTSPSFMSTAWLVFKTFFASLLPEGPPAIAN
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
1Acetylation-------MESETEPE
-------CCCCCCCC
13.2722814378
3Phosphorylation-----MESETEPEPV
-----CCCCCCCCCE
48.8223186163
11PhosphorylationETEPEPVTLLVKSPN
CCCCCCEEEEECCCC
25.7023186163
33PhosphorylationLSGDRGWSVGHLKAH
ECCCCCCCHHHHHHH
22.5028857561
38UbiquitinationGWSVGHLKAHLSRVY
CCCHHHHHHHHHHHC
28.25-
59PhosphorylationEDQRLIYSGKLLLDH
HHCCEEECCEEECCH
23.58-
61UbiquitinationQRLIYSGKLLLDHQC
CCEEECCEEECCHHH
29.9821906983
61 (in isoform 3)Ubiquitination-29.9821906983
61 (in isoform 2)Ubiquitination-29.9821906983
61 (in isoform 1)Ubiquitination-29.9821906983
75UbiquitinationCLRDLLPKQEKRHVL
HHHHHCCHHHHHHHE
71.68-
89UbiquitinationLHLVCNVKSPSKMPE
EEEEEECCCCCCCCC
42.53-
89AcetylationLHLVCNVKSPSKMPE
EEEEEECCCCCCCCC
42.5320167786
90PhosphorylationHLVCNVKSPSKMPEI
EEEEECCCCCCCCCH
30.0720068231
92PhosphorylationVCNVKSPSKMPEINA
EEECCCCCCCCCHHH
48.9929214152
93UbiquitinationCNVKSPSKMPEINAK
EECCCCCCCCCHHHE
62.96-
99 (in isoform 2)Ubiquitination-17.2321906983
99 (in isoform 3)Ubiquitination-17.2321906983
100UbiquitinationKMPEINAKVAESTEE
CCCCHHHECCCCCCC
37.172190698
100 (in isoform 1)Ubiquitination-37.1721906983
135PhosphorylationREVLRNLSSPGWENI
HHHHHHHCCCCCHHC
37.7315489334
136PhosphorylationEVLRNLSSPGWENIS
HHHHHHCCCCCHHCC
30.5121815630
189PhosphorylationYMQYLAATAASGAFV
HHHHHHHHHHCCCCC
19.7028787133
200PhosphorylationGAFVPPPSAQEIPVV
CCCCCCCCHHCCCEE
48.6428787133
375UbiquitinationSTAWLVFKTFFASLL
HHHHHHHHHHHHHHC
36.62-

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
-KUbiquitinationE3 ubiquitin ligaseAMFRQ9UKV5
PMID:17310145
-KUbiquitinationE3 ubiquitin ligaseSH3RF1Q7Z6J0
PMID:17420289

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HERP1_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
59Phosphorylation50 (9)RHrs2217332
  • Metabolic syndrome
20694148

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LFA3_HUMANCD58physical
16169070
RFA2_HUMANRPA2physical
16169070
STAR9_HUMANSTARD9physical
16169070
UBQL1_HUMANUBQLN1physical
18307982
UBQL2_HUMANUBQLN2physical
18307982
UBQL4_HUMANUBQLN4physical
18307982
SYVN1_HUMANSYVN1physical
16289116
DERL1_HUMANDERL1physical
16289116
TERA_HUMANVCPphysical
16289116
SELS_HUMANVIMPphysical
16289116
SYUA_HUMANSNCAphysical
20604806
SNCAP_HUMANSNCAIPphysical
20604806
SIAH1_HUMANSIAH1physical
20604806
SYVN1_HUMANSYVN1physical
21149444
XRCC6_HUMANXRCC6physical
21900206
GDIR1_HUMANARHGDIAphysical
21900206
PSN1_HUMANPSEN1physical
14550564
UBC_HUMANUBCphysical
14550564
A4_HUMANAPPphysical
21832049
CAN15_HUMANCAPN15physical
26186194
SH3R1_HUMANSH3RF1physical
17420289
CAN15_HUMANCAPN15physical
28514442
TBK1_HUMANTBK1physical
28954889

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 HERP1_HUMAN

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Related Literatures of Post-Translational Modification

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