RHBDL2
entrez
54933
canonical
uniprot
Q9NX52
canonical
ensembl
ENSG00000158315
resolver
ensp
ENSP00000362081
resolver
genesymbol
RHBDL2
resolver
hgnc
HGNC:16083
resolver
uniprot
B2RNT3
resolver
uniprot
B7Z1Y9
resolver
uniprot
B9EH75
resolver
uniprot
Q6P175
resolver
uniprot
Q8NER8
resolver
uniprot
Q96E02
resolver
uniprot_entry
B7Z1Y9_HUMAN
resolver
uniprot_entry
RHBL2_HUMAN
resolver
uniprot_sec
B2RNT3
resolver
uniprot_sec
B9EH75
resolver
uniprot_sec
Q6P175
resolver
uniprot_sec
Q8NER8
resolver
uniprot_sec
Q96E02
resolver
amino_acid_sequence
MAAVHDLEMESMNLNMGREMKEELEEEEKMREDGGGKDRAKSKKVHRIVSKWMLPEKSRGTYLERANCFPPPVFIISISLAELAVFIYYAVWKPQKQWITLDTGILESPFIYSPEKREEAWRFISYMLVHAGVQHILGNLCMQLVLGIPLEMVHKGLRVGLVYLAGVIAGSLASSIFDPLRYLVGASGGVYALMGGYFMNVLVNFQEMIPAFGIFRLLIIILIIVLDMGFALYRRFFVPEDGSPVSFAAHIAGGFAGMSIGYTVFSCFDKALLKDPRFWIAIAAYLACVLFAVFFNIFLSPAN
uniprot
proteins
ec_number
3.4.21.105
uniprot
proteins
function
FUNCTION: Regulator of proteosome activity independent of enzymatic activity (PubMed:26109405). Involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors (PubMed:11672525, PubMed:15047175). Known substrate: EFNB3 (PubMed:15047175). {ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:15047175, ECO:0000269|PubMed:26109405}.
uniprot
proteins
mass_dalton
34021
uniprot
proteins
mutagenesis
MUTAGEN 121; /note="W->A: Reduces protease activity."; /evidence="ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:19850051"; MUTAGEN 122; /note="R->A: Abolishes protease activity, prevents processing and alters localization to the plasma membrane of N-terminal fragment."; /evidence="ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:19850051"; MUTAGEN 139; /note="N->A: Reduces protease activity."; /evidence="ECO:0000269|PubMed:11672525"; MUTAGEN 185; /note="G->A: Abolishes protease activity."; /evidence="ECO:0000269|PubMed:11672525"; MUTAGEN 187; /note="S->A,G: Abolishes protease activity. No change in regulation of proteosome activity."; /evidence="ECO:0000269|PubMed:11672525, ECO:0000269|PubMed:15047175, ECO:0000269|PubMed:26109405"; MUTAGEN 250; /note="H->A: Abolishes protease activity."; /evidence="ECO:0000269|PubMed:11672525
uniprot
proteins
post_translational_modification
PTM: Proteolytic processing of the proenzyme produces a N-terminal fragment (NTF) and a C-terminal fragment (CTF). The processing is required for activation of the protease. {ECO:0000269|PubMed:19850051}.
uniprot
proteins
protein_family
Peptidase S54 family
uniprot
proteins
pubmed
11672525
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15047175
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
19850051
uniprot
proteins
pubmed
26109405
uniprot
proteins
sequence_length
303
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Rhomboid-related protein 2, C-terminal fragment]: Cell membrane {ECO:0000269|PubMed:19850051}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 72..92; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 128..148; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 159..179; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 183..203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 212..232; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 245..265; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 278..298; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins