ALR_HUMAN - dbPTM
ALR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALR_HUMAN
UniProt AC P55789
Protein Name FAD-linked sulfhydryl oxidase ALR
Gene Name GFER
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Isoform 1: Mitochondrion intermembrane space. Mitochondrion .
Isoform 2: Cytoplasm. Secreted.
Protein Description Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.; Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration..
Protein Sequence MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD
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
7Methylation-MAAPGERGRFHGGN
-CCCCCCCCCCCCCC
47.72-
26SulfoxidationPGGARSEMMDDLATD
CCCCCHHHHHHHHHH
3.6321406390
50PhosphorylationDAAASASTPAQAPTS
HHHHCCCCCCCCCCC
23.5128555341
56PhosphorylationSTPAQAPTSDSPVAE
CCCCCCCCCCCCCHH
48.4518691976
57PhosphorylationTPAQAPTSDSPVAED
CCCCCCCCCCCCHHH
34.7218669648
59PhosphorylationAQAPTSDSPVAEDAS
CCCCCCCCCCHHHHH
22.5019409522
66PhosphorylationSPVAEDASRRRPCRA
CCCHHHHHHCCCCCC
38.3529978859
78UbiquitinationCRACVDFKTWMRTQQ
CCCHHCHHHHHHHHH
36.4922817900
79PhosphorylationRACVDFKTWMRTQQK
CCHHCHHHHHHHHHH
25.20-
83PhosphorylationDFKTWMRTQQKRDTK
CHHHHHHHHHHHCCC
21.17-
137PhosphorylationAQFIHLFSKFYPCEE
HHHHHHHHHHCCHHH
28.3724719451
183UbiquitinationEVNRKLGKPDFDCSK
HHHHHHCCCCCCCHH
52.4229967540
190UbiquitinationKPDFDCSKVDERWRD
CCCCCCHHCCHHHHC
61.1029967540

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 ALR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ALR_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 ALR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALR_HUMANGFERphysical
11709497
CSN5_HUMANCOPS5physical
11709497
ALR_HUMANGFERphysical
14500725
CSN5_HUMANCOPS5physical
14500725
CSN1_HUMANGPS1physical
15304329
CSN2_HUMANCOPS2physical
15304329
CSN5_HUMANCOPS5physical
15304329
CSN8_HUMANCOPS8physical
15304329
SMAD2_HUMANSMAD2physical
21988832
PKHF2_HUMANPLEKHF2physical
25416956
GRHPR_HUMANGRHPRphysical
26344197
PCBP1_HUMANPCBP1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613076Myopathy, mitochondrial progressive, with congenital cataract, hearing loss and developmental delay (MPMCHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASSSPECTROMETRY.

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