PEF1_HUMAN - dbPTM
PEF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEF1_HUMAN
UniProt AC Q9UBV8
Protein Name Peflin {ECO:0000303|PubMed:10486255}
Gene Name PEF1 {ECO:0000312|HGNC:HGNC:30009}
Organism Homo sapiens (Human).
Sequence Length 284
Subcellular Localization Cytoplasm . Endoplasmic reticulum . Membrane
Peripheral membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane
Peripheral membrane protein . Membrane-associated in the presence of Ca(2+) (PubMed:11278427). Localizes to endoplasmic
Protein Description Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats. [PubMed: 27716508 In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification]
Protein Sequence MASYPYRQGCPGAAGQAPGAPPGSYYPGPPNSGGQYGSGLPPGGGYGGPAPGGPYGPPAGGGPYGHPNPGMFPSGTPGGPYGGAAPGGPYGQPPPSSYGAQQPGLYGQGGAPPNVDPEAYSWFQSVDSDHSGYISMKELKQALVNCNWSSFNDETCLMMINMFDKTKSGRIDVYGFSALWKFIQQWKNLFQQYDRDRSGSISYTELQQALSQMGYNLSPQFTQLLVSRYCPRSANPAMQLDRFIQVCTQLQVLTEAFREKDTAVQGNIRLSFEDFVTMTASRML
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
3Phosphorylation-----MASYPYRQGC
-----CCCCCCCCCC
25.9123186163
7Dimethylation-MASYPYRQGCPGAA
-CCCCCCCCCCCCCC
23.16-
7Methylation-MASYPYRQGCPGAA
-CCCCCCCCCCCCCC
23.1652719565
133PhosphorylationVDSDHSGYISMKELK
CCCCCCCEECHHHHH
7.8822817900
137UbiquitinationHSGYISMKELKQALV
CCCEECHHHHHHHHH
53.77PubMed
165UbiquitinationMMINMFDKTKSGRID
EEEECCCCCCCCCCC
46.73PubMed
166PhosphorylationMINMFDKTKSGRIDV
EEECCCCCCCCCCCE
32.0829759185
167UbiquitinationINMFDKTKSGRIDVY
EECCCCCCCCCCCEE
57.56PubMed
168PhosphorylationNMFDKTKSGRIDVYG
ECCCCCCCCCCCEEH
38.2429759185
174PhosphorylationKSGRIDVYGFSALWK
CCCCCCEEHHHHHHH
14.5429759185
177PhosphorylationRIDVYGFSALWKFIQ
CCCEEHHHHHHHHHH
20.3529759185
200PhosphorylationYDRDRSGSISYTELQ
HCCCCCCCCCHHHHH
15.03-
202PhosphorylationRDRSGSISYTELQQA
CCCCCCCCHHHHHHH
27.92-
211PhosphorylationTELQQALSQMGYNLS
HHHHHHHHHCCCCCC
22.5722210691
218PhosphorylationSQMGYNLSPQFTQLL
HHCCCCCCHHHHHHH
17.0222210691
222PhosphorylationYNLSPQFTQLLVSRY
CCCCHHHHHHHHHHH
17.0422210691
227PhosphorylationQFTQLLVSRYCPRSA
HHHHHHHHHHCCCCC
19.9422210691
2602-HydroxyisobutyrylationLTEAFREKDTAVQGN
HHHHHHCCCCCCCCC
57.00-
260UbiquitinationLTEAFREKDTAVQGN
HHHHHHCCCCCCCCC
57.00-

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 ligaseKLHL12Q53G59
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEF1_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 PEF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDCD6_HUMANPDCD6physical
11278427
DAZP2_HUMANDAZAP2physical
19060904
K0930_HUMANKIAA0930physical
26186194
H2A2B_HUMANHIST2H2ABphysical
26186194
FAS_HUMANFASNphysical
26344197
PDCD6_HUMANPDCD6physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
SUCB2_HUMANSUCLG2physical
26344197
DMRTB_HUMANDMRTB1physical
21516116
K0930_HUMANKIAA0930physical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442

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 PEF1_HUMAN

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Related Literatures of Post-Translational Modification

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