PDIA2_HUMAN - dbPTM
PDIA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDIA2_HUMAN
UniProt AC Q13087
Protein Name Protein disulfide-isomerase A2
Gene Name PDIA2
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins..
Protein Sequence MSRQLLPVLLLLLLRASCPWGQEQGARSPSEEPPEEEIPKEDGILVLSRHTLGLALREHPALLVEFYAPWCGHCQALAPEYSKAAAVLAAESMVVTLAKVDGPAQRELAEEFGVTEYPTLKFFRNGNRTHPEEYTGPRDAEGIAEWLRRRVGPSAMRLEDEAAAQALIGGRDLVVIGFFQDLQDEDVATFLALAQDALDMTFGLTDRPRLFQQFGLTKDTVVLFKKFDEGRADFPVDEELGLDLGDLSRFLVTHSMRLVTEFNSQTSAKIFAARILNHLLLFVNQTLAAHRELLAGFGEAAPRFRGQVLFVVVDVAADNEHVLQYFGLKAEAAPTLRLVNLETTKKYAPVDGGPVTAASITAFCHAVLNGQVKPYLLSQEIPPDWDQRPVKTLVGKNFEQVAFDETKNVFVKFYAPWCTHCKEMAPAWEALAEKYQDHEDIIIAELDATANELDAFAVHGFPTLKYFPAGPGRKVIEYKSTRDLETFSKFLDNGGVLPTEEPPEEPAAPFPEPPANSTMGSKEEL
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
48PhosphorylationEDGILVLSRHTLGLA
CCCEEEECCHHHHHH
17.9724719451
127N-linked_GlycosylationLKFFRNGNRTHPEEY
EECCCCCCCCCHHHH
49.5823167757
260PhosphorylationTHSMRLVTEFNSQTS
HCHHHHHHHCCHHHH
39.1829083192
264PhosphorylationRLVTEFNSQTSAKIF
HHHHHCCHHHHHHHH
39.9129083192
266PhosphorylationVTEFNSQTSAKIFAA
HHHCCHHHHHHHHHH
30.3929083192
267PhosphorylationTEFNSQTSAKIFAAR
HHCCHHHHHHHHHHH
21.6729083192
284N-linked_GlycosylationNHLLLFVNQTLAAHR
HHHHHHHHHHHHHHH
23.0623167757
286PhosphorylationLLLFVNQTLAAHREL
HHHHHHHHHHHHHHH
17.11-
478PhosphorylationPGRKVIEYKSTRDLE
CCCEEEEECCCCCHH
10.1030576142
479AcetylationGRKVIEYKSTRDLET
CCEEEEECCCCCHHH
32.3420167786
481PhosphorylationKVIEYKSTRDLETFS
EEEEECCCCCHHHHH
24.8530576142
516N-linked_GlycosylationPFPEPPANSTMGSKE
CCCCCCCCCCCCCCC
43.7323167757

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 PDIA2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDIA2_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 PDIA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P4HA3_HUMANP4HA3physical
14500733
HM13_HUMANHM13physical
19942855
ERO1A_HUMANERO1Lphysical
10970843
P4HTM_HUMANP4HTMphysical
12485997
CO2A1_HUMANCOL2A1physical
12485997
SMS_HUMANSSTphysical
15590633
ENV_HV1H2envphysical
20458450
ERO1A_HUMANERO1Lphysical
25258311
MTP_HUMANMTTPphysical
25108285

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 PDIA2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP