UniProt Accession

 HM13_HUMAN; Q8TCT9; B2RAY5; E1P5L3; Q15K36; Q540H8; Q5JWP2; Q5JWP3; Q5JWP4; Q5JWP5; Q7Z4F2; Q86Y35; Q95H87; Q9H110; Q9H111 

Genbank Protein ID

 AJ420895; AF515663; AY169310; AY169311; AY169312; DQ168450; AJ345029; AF483215; AF172086; AK074686; AK075283; AK314410; AL110115; AL121751; AL110115; AL121751; AL110115; AL121751; AL121751; AL110115; AL121751; AL110115; AL121751; AL110115; CH471077; CH471077; CH471077; CH471077; BC008938; BC008959; BC062595 

Genbank Nucleotide ID

 CAD13132.1; AAN77099.1; AAO12535.1; AAO12536.1; AAO12537.1; ABA56163.1; CAC87790.1; AAM22076.1; AAQ13609.1; BAC11138.1; BAC11519.1; BAG37032.1; CAI20173.1; CAI20173.1; CAI20174.1; CAI20174.1; CAI20175.2; CAI20175.2; CAI19152.1; CAI19152.1; CAI19153.1; CAI19153.1; CAI19154.2; CAI19154.2; EAW76436.1; EAW76437.1; EAW76435.1; EAW76438.1; AAH08938.1; AAH08959.1; AAH62595.1 

Protein Name

 Minor histocompatibility antigen H13 

Protein Synonyms/Alias

 Intramembrane protease 1; IMP-1; IMPAS-1; hIMP1; Presenilin-like protein 3; Signal peptide peptidase 

Gene Name

 HM13 

Gene Synonyms/Alias

 H13; IMP1; PSL3; SPP; MSTP086 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
61	SVRCARGKNASDMPE	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
150	TQGSGENKEEIINYE	ubiquitination	[1]
241	KSFEAPIKLVFPQDL	ubiquitination	[1, 2, 3, 5, 6, 7, 8, 9]
284	LRFDISLKKNTHTYF	ubiquitination	[1]
352	SYEESNPKDPAAVTE	ubiquitination	[1]
361	PAAVTESKEGTEASA	ubiquitination	[1]
370	GTEASASKGLEKKEK	ubiquitination	[1]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 

Functional Description

 Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. May play a role in graft rejection (By similarity). 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. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. 

Sequence Annotation

 MOTIF 317 319 PAL.
 ACT_SITE 219 219 By similarity.
 ACT_SITE 265 265 By similarity.
 CARBOHYD 10 10 N-linked (GlcNAc...).
 CARBOHYD 20 20 N-linked (GlcNAc...).  

Keyword

 Alternative splicing; Cell membrane; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Polymorphism; Protease; Reference proteome; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 377 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; ISS:UniProtKB.
 GO:0071458; C:integral to cytosolic side of endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
 GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IMP:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB. 

Interpro

 IPR006639; Peptidase_A22.
 IPR007369; Peptidase_A22B_SPP. 

Pfam

 PF04258; Peptidase_A22B 

SMART

 SM00730; PSN 

PROSITE

  

PRINTS