ERP44_HUMAN - dbPTM
ERP44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERP44_HUMAN
UniProt AC Q9BS26
Protein Name Endoplasmic reticulum resident protein 44
Gene Name ERP44
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Endoplasmic reticulum lumen .
Protein Description Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum..
Protein Sequence MHPAVFLSLPDLRCSLLLLVTWVFTPVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLAPSEYRYTLLRDRDEL
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
96PhosphorylationRVDCDQHSDIAQRYR
EEECCCCCHHHHHHH
25.6928634120
106AcetylationAQRYRISKYPTLKLF
HHHHHHHCCCHHHHH
53.5326210075
130UbiquitinationYRGQRSVKALADYIR
HCCHHHHHHHHHHHH
38.64-
135PhosphorylationSVKALADYIRQQKSD
HHHHHHHHHHHCCCC
7.7528152594
137MethylationKALADYIRQQKSDPI
HHHHHHHHHCCCCHH
27.01-
1402-HydroxyisobutyrylationADYIRQQKSDPIQEI
HHHHHHCCCCHHHHH
48.79-
140UbiquitinationADYIRQQKSDPIQEI
HHHHHHCCCCHHHHH
48.79-
166PhosphorylationSKRNIIGYFEQKDSD
HHCCEEEEEEECCCC
8.11-
1702-HydroxyisobutyrylationIIGYFEQKDSDNYRV
EEEEEEECCCCCHHH
52.59-
189GlutathionylationANILHDDCAFLSAFG
HHHHCCCHHHHHHHC
3.4322555962
200UbiquitinationSAFGDVSKPERYSGD
HHHCCCCCCCCCCCC
51.23-
204PhosphorylationDVSKPERYSGDNIIY
CCCCCCCCCCCCCEE
18.4928331001
205PhosphorylationVSKPERYSGDNIIYK
CCCCCCCCCCCCEEC
45.9828331001
269SulfoxidationPFLILFHMKEDTESL
CEEEEEECCCCCCHH
3.8928465586
289PhosphorylationEVARQLISEKGTINF
HHHHHHHCCCCCEEE
41.6824719451
2912-HydroxyisobutyrylationARQLISEKGTINFLH
HHHHHCCCCCEEEEE
55.34-
291UbiquitinationARQLISEKGTINFLH
HHHHHCCCCCEEEEE
55.34-
301GlutathionylationINFLHADCDKFRHPL
EEEEECCHHHCCCCC
6.7722555962
3032-HydroxyisobutyrylationFLHADCDKFRHPLLH
EEECCHHHCCCCCHH
51.10-
303AcetylationFLHADCDKFRHPLLH
EEECCHHHCCCCCHH
51.1026822725
318GlutathionylationIQKTPADCPVIAIDS
CCCCCCCCCEEEEEC
2.9322555962
343AcetylationKDVLIPGKLKQFVFD
HHCCCCCCEEEEEEE
47.3526822725
3452-HydroxyisobutyrylationVLIPGKLKQFVFDLH
CCCCCCEEEEEEECC
45.21-
367O-linked_GlycosylationFHHGPDPTDTAPGEQ
CCCCCCCCCCCCCHH
54.0555834395
369O-linked_GlycosylationHGPDPTDTAPGEQAQ
CCCCCCCCCCCHHHH
36.9122661428
380PhosphorylationEQAQDVASSPPESSF
HHHHHHHHCCCCHHH
43.1328985074
380O-linked_GlycosylationEQAQDVASSPPESSF
HHHHHHHHCCCCHHH
43.1322661428
381O-linked_GlycosylationQAQDVASSPPESSFQ
HHHHHHHCCCCHHHH
34.4355834413
385O-linked_GlycosylationVASSPPESSFQKLAP
HHHCCCCHHHHHHCC
42.0755834419
386O-linked_GlycosylationASSPPESSFQKLAPS
HHCCCCHHHHHHCCH
29.9955834425
393O-linked_GlycosylationSFQKLAPSEYRYTLL
HHHHHCCHHHHHEEC
41.4755832941
393PhosphorylationSFQKLAPSEYRYTLL
HHHHHCCHHHHHEEC
41.47-
395PhosphorylationQKLAPSEYRYTLLRD
HHHCCHHHHHEECCC
17.17-

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 ERP44_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERP44_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 ERP44_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERO1A_HUMANERO1Lphysical
11847130
KCRB_HUMANCKBphysical
22863883
CNN2_HUMANCNN2physical
22863883
FHL2_HUMANFHL2physical
22863883
ISOC1_HUMANISOC1physical
22863883
SYLC_HUMANLARSphysical
22863883
NUDC1_HUMANNUDCD1physical
22863883
OSGEP_HUMANOSGEPphysical
22863883
PAK2_HUMANPAK2physical
22863883
PDC10_HUMANPDCD10physical
22863883
PUR4_HUMANPFASphysical
22863883
PLD3_HUMANPLD3physical
22863883
TBCB_HUMANTBCBphysical
22863883
UBFD1_HUMANUBFD1physical
22863883
VINC_HUMANVCLphysical
22863883
1433Z_HUMANYWHAZphysical
22863883
PNPO_HUMANPNPOphysical
26344197
SNX2_HUMANSNX2physical
26344197
AL7A1_HUMANALDH7A1physical
26496610
NRDC_HUMANNRD1physical
26496610
PIAS1_HUMANPIAS1physical
26496610
FA13A_HUMANFAM13Aphysical
26496610
PACN2_HUMANPACSIN2physical
26496610
E41LB_HUMANEPB41L4Bphysical
26496610
KMT2C_HUMANKMT2Cphysical
26496610
CSN7B_HUMANCOPS7Bphysical
26496610
TM189_HUMANTMEM189physical
26496610
FOG1_HUMANZFPM1physical
28514442
MEX3A_HUMANMEX3Aphysical
28514442
STXB4_HUMANSTXBP4physical
28514442
PXDN_HUMANPXDNphysical
28514442
MIGA1_HUMANFAM73Aphysical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
ZN212_HUMANZNF212physical
28514442
DAPK1_HUMANDAPK1physical
28514442
BCOR_HUMANBCORphysical
28514442
ZN777_HUMANZNF777physical
28514442
ZMYM1_HUMANZMYM1physical
28514442
TNIP1_HUMANTNIP1physical
28514442
IP3KC_HUMANITPKCphysical
28514442
GNL3L_HUMANGNL3Lphysical
28514442
RPIA_HUMANRPIAphysical
28514442
CTIP_HUMANRBBP8physical
28514442
ERO1B_HUMANERO1LBphysical
28514442
UB2Q1_HUMANUBE2Q1physical
28514442
HXA5_HUMANHOXA5physical
28514442
DPOD2_HUMANPOLD2physical
28514442
SUMF1_HUMANSUMF1physical
28514442
FIGN_HUMANFIGNphysical
28514442
FINC_HUMANFN1physical
28514442
BTD_HUMANBTDphysical
28514442
PRI2_HUMANPRIM2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERP44_HUMAN

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Related Literatures of Post-Translational Modification

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