RHBL4_HUMAN - dbPTM
RHBL4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHBL4_HUMAN
UniProt AC Q8TEB9
Protein Name Rhomboid-related protein 4
Gene Name RHBDD1
Organism Homo sapiens (Human).
Sequence Length 315
Subcellular Localization Membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein. Mitochondrion .
Protein Description Intramembrane-cleaving serine protease that cleaves single transmembrane or multi-pass membrane proteins in the hydrophobic plane of the membrane, luminal loops and juxtamembrane regions. Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded membrane proteins. Required for the degradation process of some specific misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Functions in BIK, MPZ, PKD1, PTCRA, RHO, STEAP3 and TRAC processing. Involved in the regulation of exosomal secretion; inhibits the TSAP6-mediated secretion pathway. Involved in the regulation of apoptosis; modulates BIK-mediated apoptotic activity. Also plays a role in the regulation of spermatogenesis; inhibits apoptotic activity in spermatogonia..
Protein Sequence MQRRSRGINTGLILLLSQIFHVGINNIPPVTLATLALNIWFFLNPQKPLYSSCLSVEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLQFAVAEFMDEPDFKRSCAVGFSGVLFALKVLNNHYCPGGFVNILGFPVPNRFACWVELVAIHLFSPGTSFAGHLAGILVGLMYTQGPLKKIMEACAGGFSSSVGYPGRQYYFNSSGSSGYQDYYPHGRPDHYEEAPRNYDTYTAGLSEEEQLERALQASLWDRGNTRNSPPPYGFHLSPEEMRRQRLHRFDSQ
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
82PhosphorylationHADDWHLYFNMASML
CCCCHHHHHHHHHHH
-
87PhosphorylationHLYFNMASMLWKGIN
HHHHHHHHHHHCCCC
-
236PhosphorylationGRQYYFNSSGSSGYQ
CCEEEECCCCCCCCC
28796482
237PhosphorylationRQYYFNSSGSSGYQD
CEEEECCCCCCCCCC
28796482
239PhosphorylationYYFNSSGSSGYQDYY
EEECCCCCCCCCCCC
28796482
240PhosphorylationYFNSSGSSGYQDYYP
EECCCCCCCCCCCCC
28796482
242PhosphorylationNSSGSSGYQDYYPHG
CCCCCCCCCCCCCCC
28796482
245PhosphorylationGSSGYQDYYPHGRPD
CCCCCCCCCCCCCCC
28796482
246PhosphorylationSSGYQDYYPHGRPDH
CCCCCCCCCCCCCCC
28796482
254PhosphorylationPHGRPDHYEEAPRNY
CCCCCCCCCCCCCCC
28796482
261PhosphorylationYEEAPRNYDTYTAGL
CCCCCCCCCCCCCCC
28796482
263PhosphorylationEAPRNYDTYTAGLSE
CCCCCCCCCCCCCCH
28796482
264PhosphorylationAPRNYDTYTAGLSEE
CCCCCCCCCCCCCHH
28796482
269PhosphorylationDTYTAGLSEEEQLER
CCCCCCCCHHHHHHH
27134283
281PhosphorylationLERALQASLWDRGNT
HHHHHHHHHHHCCCC
28857561
285MethylationLQASLWDRGNTRNSP
HHHHHHHCCCCCCCC
115491223
288PhosphorylationSLWDRGNTRNSPPPY
HHHHCCCCCCCCCCC
30108239
291PhosphorylationDRGNTRNSPPPYGFH
HCCCCCCCCCCCCCC
26055452
295PhosphorylationTRNSPPPYGFHLSPE
CCCCCCCCCCCCCHH
30108239
300PhosphorylationPPYGFHLSPEEMRRQ
CCCCCCCCHHHHHHH
28985074
314PhosphorylationQRLHRFDSQ------
HHHHHHCCC------
28355574

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 RHBL4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHBL4_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 RHBL4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
27407164

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 RHBL4_HUMAN

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Related Literatures of Post-Translational Modification

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