HM13
entrez
81502
canonical
uniprot
Q8TCT9
canonical
ensembl
ENSG00000101294
resolver
ensp
ENSP00000343032
resolver
ensp
ENSP00000381237
resolver
ensp
ENSP00000479020
resolver
ensp
ENSP00000497632
resolver
ensp
ENSP00000501423
resolver
enst
ENST00000498035
resolver
enst
ENST00000650367
resolver
genesymbol
HM13
resolver
genesymbol_syn
H13
resolver
genesymbol_syn
IMP1
resolver
genesymbol_syn
PSL3
resolver
genesymbol_syn
SPP
resolver
hgnc
HGNC:16435
resolver
uniprot
A0A0C4DGU3
resolver
uniprot
A0A0S2Z5V7
resolver
uniprot
B2RAY5
resolver
uniprot
E1P5L3
resolver
uniprot
Q15K36
resolver
uniprot
Q540H8
resolver
uniprot
Q5JWP2
resolver
uniprot
Q5JWP3
resolver
uniprot
Q5JWP4
resolver
uniprot
Q5JWP5
resolver
uniprot
Q7Z4F2
resolver
uniprot
Q86Y35
resolver
uniprot
Q95H87
resolver
uniprot
Q9H110
resolver
uniprot
Q9H111
resolver
uniprot_entry
A0A0C4DGU3_HUMAN
resolver
uniprot_entry
A0A0S2Z5V7_HUMAN
resolver
uniprot_entry
SPP_HUMAN
resolver
uniprot_sec
B2RAY5
resolver
uniprot_sec
E1P5L3
resolver
uniprot_sec
Q15K36
resolver
uniprot_sec
Q540H8
resolver
uniprot_sec
Q5JWP2
resolver
uniprot_sec
Q5JWP3
resolver
uniprot_sec
Q5JWP4
resolver
uniprot_sec
Q5JWP5
resolver
uniprot_sec
Q7Z4F2
resolver
uniprot_sec
Q86Y35
resolver
uniprot_sec
Q95H87
resolver
uniprot_sec
Q9H110
resolver
uniprot_sec
Q9H111
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the protease inhibitor 1,3-di-(N-Carboxybenzoyl-L-leucyl-L-leucyl)amino acetone (also known as (Z-LL)2 ketone). {ECO:0000269|PubMed:15716490, ECO:0000269|PubMed:17517891}.
uniprot
proteins
amino_acid_sequence
MDSALSDPHNGSAEAGGPTNSTTRPPSTPEGIALAYGSLLLMALLPIFFGALRSVRCARGKNASDMPETITSRDAARFPIIASCTLLGLYLFFKIFSQEYINLLLSMYFFVLGILALSHTISPFMNKFFPASFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSIVGVWYLLRKHWIANNLFGLAFSLNGVELLHLNNVSTGCILLGGLFIYDVFWVFGTNVMVTVAKSFEAPIKLVFPQDLLEKGLEANNFAMLGLGDVVIPGIFIALLLRFDISLKKNTHTYFYTSFAAYIFGLGLTIFIMHIFKHAQPALLYLVPACIGFPVLVALAKGEVTEMFSYEESNPKDPAAVTESKEGTEASASKGLEKKEK
uniprot
proteins
ec_number
3.4.23.-
uniprot
proteins
function
FUNCTION: Catalyzes intramembrane proteolysis of signal peptides that have been removed from precursors of secretory and membrane proteins, resulting in the release of the fragment from the ER membrane into the cytoplasm (PubMed:12077416, PubMed:15716490, PubMed:17517891). Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides (PubMed:11714810). May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein (PubMed:12145199). Involved in the intramembrane cleavage of the integral membrane protein PSEN1 (PubMed:11714810, PubMed:12077416, PubMed:14741365). Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (PubMed:25239945). May play a role in graft rejection (By similarity). {ECO:0000250|UniProtKB:Q9D8V0, ECO:0000269|PubMed:11714810, ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:12145199, ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:15716490, ECO:0000269|PubMed:17517891, ECO:0000269|PubMed:25239945}.
uniprot
proteins
mass_dalton
41488
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="N->Q: Abolishes N-glycosylation; when associated with Q-20."; /evidence="ECO:0000269|PubMed:12077416"; MUTAGEN 20; /note="N->Q: Abolishes N-glycosylation; when associated with Q-10."; /evidence="ECO:0000269|PubMed:12077416"; MUTAGEN 219; /note="D->A: Abolishes proteolysis of PSEN1."; /evidence="ECO:0000269|PubMed:14741365"; MUTAGEN 264; /note="G->A: No effect on proteolysis of PSEN1."; /evidence="ECO:0000269|PubMed:14741365"; MUTAGEN 265; /note="D->A: No effect on inhibitor binding; abolishes signal peptide peptidase activity. Abolishes proteolysis of PSEN1. Abolishes proteolysis of XBP1 isoform 1 and increases interaction with XBP1 isoform 1."; /evidence="ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:14741365, ECO:0000269|PubMed:25239945"; MUTAGEN 317; /note="P->L: Abolishes proteolysis of PSEN1."; /evidence="ECO:0000269|PubMed:14741365
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547, ECO:0000269|PubMed:19159218}.
uniprot
proteins
protein_family
Peptidase A22B family
uniprot
proteins
pubmed
11714810
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12077416
uniprot
proteins
pubmed
12139484
uniprot
proteins
pubmed
12145199
uniprot
proteins
pubmed
12972007
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14741365
uniprot
proteins
pubmed
15385547
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15716490
uniprot
proteins
pubmed
15998642
uniprot
proteins
pubmed
16730383
uniprot
proteins
pubmed
17517891
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19720873
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25239945
uniprot
proteins
pubmed
25944712
uniprot
proteins
sequence_length
377
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:12077416, ECO:0000269|PubMed:15385547}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250|UniProtKB:Q9D8V0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9D8V0}.
uniprot
proteins
transmembrane_region
TRANSMEM 32..52; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 78..98; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 101..121; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 158..178; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 182..202; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 210..230; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 257..277; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 291..311; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 315..335; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins