Reviewed, UniProtKB/Swiss-Prot Q8TCT9 (HM13_HUMAN)

Names and origin

Protein names

Recommended name:
    Minor histocompatibility antigen H13
    EC=3.4.23.-
Alternative name(s):
    Signal peptide peptidase
    Presenilin-like protein 3
    Intramembrane protease 1
      Short name=IMP-1
      Short name=hIMP1

Gene names

Name:	HM13
Synonyms:	H13, IMP1, PSL3, SPP
ORF Names:	MSTP086

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Widely expressed with highest levels in kidney, liver, placenta, heart, lung, leukocytes and small intestine. Expressed abundantly in the CNS with highest levels in thalamus and medulla. Ref.2
Post-translational modification	N-glycosylated. Ref.1 Ref.14
Sequence similarities	Belongs to the peptidase A22B family.
Sequence caution	The sequence AAQ13609.1 differs from that shown. Reason: Frameshift at positions 320, 329, 330 and 358. The sequence BAC11138.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention. The sequence CAI19152.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI20173.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane
Molecular function	Hydrolase Protease
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT5	O95870	1	EBI-347472,EBI-348517

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TCT9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8TCT9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     347-347: E → ESSAEILPHTPRLTHFPTVSGSPASLADSMQQKLAGPRRRRPQNPSAIYE

Isoform 4 (identifier: Q8TCT9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     348-377: ESNPKDPAAVTESKEGTEASASKGLEKKEK → SSAEILPHTP...RRRPQNPSAM

Isoform 5 (identifier: Q8TCT9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     181-222: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Minor histocompatibility antigen H13		PRO_0000073907
Regions
	Topological domain	1 – 31	31	Lumenal Potential
	Transmembrane	32 – 52	21	Potential
	Topological domain	53 – 77	25	Cytoplasmic Potential
	Transmembrane	78 – 98	21	Potential
	Topological domain	99 – 100	2	Lumenal Potential
	Transmembrane	101 – 121	21	Potential
	Topological domain	122 – 209	88	Cytoplasmic Potential
	Transmembrane	210 – 230	21	Potential
	Topological domain	231 – 256	26	Lumenal Potential
	Transmembrane	257 – 277	21	Potential
	Topological domain	278 – 291	14	Cytoplasmic Potential
	Transmembrane	292 – 312	21	Potential
	Topological domain	313 – 315	3	Lumenal Potential
	Transmembrane	316 – 336	21	Potential
	Topological domain	337 – 377	41	Cytoplasmic Potential
Sites
	Active site	219	1	By similarity
	Active site	265	1	By similarity
Amino acid modifications
	Glycosylation	10	1	N-linked (GlcNAc...) Ref.14
	Glycosylation	20	1	N-linked (GlcNAc...) Ref.14
Natural variations
	Alternative sequence	181 – 222	42	Missing in isoform 5.		VSP_015082
	Alternative sequence	347	1	E → ESSAEILPHTPRLTHFPTVS GSPASLADSMQQKLAGPRRR RPQNPSAIYE in isoform 2.		VSP_005196
	Alternative sequence	348 – 377	30	ESNPK…EKKEK → SSAEILPHTPRLTHFPTVSG SPASLADSMQQKLAGPRRRR PQNPSAM in isoform 4.		VSP_015083
	Natural variant	259	1	A → P: dbSNP rs1044419.		VAR_014274
Experimental info
	Mutagenesis	10	1	N → Q: Abolishes N-glycosylation; when associated with Q-20. Ref.1
	Mutagenesis	20	1	N → Q: Abolishes N-glycosylation; when associated with Q-10. Ref.1
	Mutagenesis	265	1	D → A: No effect on inhibitor binding; abolishes catalytic activity. Ref.1
	Sequence conflict	132	1	S → N AA sequence Ref.1
	Sequence conflict	150	1	K → R in BAC11519. Ref.7
	Sequence conflict	159	1	D → A AA sequence Ref.1
	Sequence conflict	235	1	S → F in AAH08938. Ref.10
	Sequence conflict	235	1	S → F in AAH08959. Ref.10
	Sequence conflict	295	1	F → Y in AAQ13609. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 322D231B52B33118	FASTA	377	41,488
	10 20 30 40 50 60 MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG 70 80 90 100 110 120 KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT 130 140 150 160 170 180 ISPFMNKFFP ASFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS IVGVWYLLRK 190 200 210 220 230 240 HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI 250 260 270 280 290 300 KLVFPQDLLE KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF 310 320 330 340 350 360 GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYEESN PKDPAAVTES 370 KEGTEASASK GLEKKEK
	Isoform 2. Checksum: 269AD5CC99982845	FASTA	426	46,825
	10 20 30 40 50 60 MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG 70 80 90 100 110 120 KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT 130 140 150 160 170 180 ISPFMNKFFP ASFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS IVGVWYLLRK 190 200 210 220 230 240 HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI 250 260 270 280 290 300 KLVFPQDLLE KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF 310 320 330 340 350 360 GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYESSA EILPHTPRLT 370 380 390 400 410 420 HFPTVSGSPA SLADSMQQKL AGPRRRRPQN PSAIYEESNP KDPAAVTESK EGTEASASKG LEKKEK
	Isoform 4. Checksum: 9BEC3A1C9B605D48	FASTA	394	43,423
	10 20 30 40 50 60 MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG 70 80 90 100 110 120 KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT 130 140 150 160 170 180 ISPFMNKFFP ASFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS IVGVWYLLRK 190 200 210 220 230 240 HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI 250 260 270 280 290 300 KLVFPQDLLE KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF 310 320 330 340 350 360 GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYESSA EILPHTPRLT 370 380 390 HFPTVSGSPA SLADSMQQKL AGPRRRRPQN PSAM
	Isoform 5. Checksum: D22777AF67B3720B	FASTA	335	36,814
	10 20 30 40 50 60 MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG 70 80 90 100 110 120 KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT 130 140 150 160 170 180 ISPFMNKFFP ASFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS IVGVWYLLRK 190 200 210 220 230 240 VFGTNVMVTV AKSFEAPIKL VFPQDLLEKG LEANNFAMLG LGDVVIPGIF IALLLRFDIS 250 260 270 280 290 300 LKKNTHTYFY TSFAAYIFGL GLTIFIMHIF KHAQPALLYL VPACIGFPVL VALAKGEVTE 310 320 330 MFSYEESNPK DPAAVTESKE GTEASASKGL EKKEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of signal peptide peptidase, a presenilin-type aspartic protease." Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B. Science 296:2215-2218(2002) [PubMed: 12077416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-73; 128-136; 137-161; 242-251 AND 338-352, FUNCTION, GLYCOSYLATION, MUTAGENESIS OF ASN-10; ASN-20 AND ASP-265. Tissue: Cervix carcinoma.
[2]	"Expression of the presenilin-like signal peptide peptidase (SPP) in mouse adult brain and during development." Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H. Gene Expr. Patterns 3:685-691(2003) [PubMed: 12972007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Placenta.
[3]	"Characterization of a new protein family with homology to presenilins." Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Genomic analysis of the H13 minor histocompatibility antigen gene." Brown A.C., Roopenian D.C. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Characterization of a novel class of conserved intra-membrane proteolysis associated proteins (IMPAS)." Grigorenko A.P., Moliaka Y.K., Rogaev E.I. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4). Tissue: Blood and Hippocampus.
[6]	Liu Y.Q., Gong J., Yu L.T., Sheng H., Qin B.M., Zhao B., Liu B., Wang X.Y., Zhang Q., Song L., Gao Y., Zhang C.L., Ye J., Ji X.J., Liu B.H., Lu H., Xu H.S., Chen J.Z. , Cai M.Q., Zheng W.Y., Teng C.Y., Liu Q., Lin J., Zhang A.M., Gao R.L., Hui R.T. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Aorta.
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary gland, Retinoblastoma and Testis.
[8]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Muscle.
[11]	"Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes." Lemberg M.K., Bland F.A., Weihofen A., Braud V.M., Martoglio B. J. Immunol. 167:6441-6446(2001) [PubMed: 11714810] [Abstract] Cited for: FUNCTION.
[12]	"Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets." McLauchlan J., Lemberg M.K., Hope G., Martoglio B. EMBO J. 21:3980-3988(2002) [PubMed: 12145199] [Abstract] Cited for: FUNCTION.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-10 AND ASN-20, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ420895 mRNA. Translation: CAD13132.1. AF515663 mRNA. Translation: AAN77099.1. AJ345029 mRNA. Translation: CAC87790.1. AF483215 mRNA. Translation: AAM22076.1. AY169310 mRNA. Translation: AAO12535.1. AY169311 mRNA. Translation: AAO12536.1. AY169312 mRNA. Translation: AAO12537.1. AF172086 mRNA. Translation: AAQ13609.1. Frameshift. AK074686 mRNA. Translation: BAC11138.1. Sequence problems. AK075283 mRNA. Translation: BAC11519.1. AK314410 mRNA. Translation: BAG37032.1. AL110115, AL121751 Genomic DNA. Translation: CAI20173.1. Sequence problems. AL110115, AL121751 Genomic DNA. Translation: CAI20174.1. AL110115, AL121751 Genomic DNA. Translation: CAI20175.2. AL121751, AL110115 Genomic DNA. Translation: CAI19152.1. Sequence problems. AL121751, AL110115 Genomic DNA. Translation: CAI19153.1. AL121751, AL110115 Genomic DNA. Translation: CAI19154.2. CH471077 Genomic DNA. Translation: EAW76436.1. BC008938 mRNA. Translation: AAH08938.1. BC008959 mRNA. Translation: AAH08959.1. BC062595 mRNA. Translation: AAH62595.1.
IPI	IPI00152441. IPI00220687. IPI00329296. IPI00552772.
RefSeq	NP_110416.1. NP_848695.1. NP_848696.1. NP_848697.1.
UniGene	Hs.373741
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TCT9. 1 interaction.
STRING	Q8TCT9.
Protein family/group databases
MEROPS	A22.003.
Proteomic databases
PRIDE	Q8TCT9.
Genome annotation databases
Ensembl	ENST00000340852; ENSP00000343032; ENSG00000101294; Homo sapiens. [Genome view]
GeneID	81502.
KEGG	hsa:81502.
UCSC	uc002wwb.1. human. uc002wwc.1. human. uc002wwd.1. human. uc002wwe.1. human.
Organism-specific databases
CTD	81502.
GeneCards	GC20P029565.
H-InvDB	HIX0015711.
HGNC	HGNC:16435. HM13.
MIM	607106. gene.
PharmGKB	PA29314.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q8TCT9.
OMA	LEANNFA
Gene expression databases
ArrayExpress	Q8TCT9.
Bgee	Q8TCT9.
Genevestigator	Q8TCT9.
GermOnline	ENSG00000101294. Homo sapiens.
Family and domain databases
InterPro	IPR006639. Peptidase_A22. IPR007369. Peptidase_A22B_SPP. [Graphical view]
PANTHER	PTHR12174. Peptidase_A22B. 1 hit.
Pfam	PF04258. Peptidase_A22B. 1 hit. [Graphical view]
SMART	SM00730. PSN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	71746.
SOURCE	Search...

Entry information

Entry name

HM13_HUMAN

Accession

Primary (citable) accession number: Q8TCT9
Secondary accession number(s): B2RAY5 , Q540H8, Q5JWP2, Q5JWP3, Q5JWP4, Q5JWP5, Q7Z4F2, Q86Y35, Q95H87, Q9H110, Q9H111

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	June 1, 2002
Last modified:	November 24, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.