Q8TCT9 (HM13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Minor histocompatibility antigen H13
EC=3.4.23.-

Alternative name(s):
Intramembrane protease 1
Short name=IMP-1
Short name=IMPAS-1
Short name=hIMP1
Presenilin-like protein 3
Signal peptide peptidase

Gene names

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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
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. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Ref.1 Ref.12 Ref.13 Ref.14
Subunit structure	Interacts with RNF139. Ref.16
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Isoform 4: Cell membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Widely expressed with highest levels in kidney, liver, placenta, lung, leukocytes and small intestine and reduced expression in heart and skeletal muscle. Expressed abundantly in the CNS with highest levels in thalamus and medulla. Ref.2 Ref.3
Domain	The first transmembrane domain may act as a type I signal anchor By similarity. The PAL motif is required for normal active site conformation By similarity.
Post-translational modification	N-glycosylated. Ref.1
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: 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	Cell membrane Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	membrane protein proteolysis Inferred from direct assay Ref.14. Source: UniProtKB
Cellular_component	cell surface Inferred from sequence or structural similarity. Source: UniProtKB integral to cytosolic side of endoplasmic reticulum membrane Inferred from direct assay Ref.15. Source: UniProtKB integral to lumenal side of endoplasmic reticulum membrane Inferred from direct assay Ref.15. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell rough endoplasmic reticulum Inferred from direct assay PubMed 15998642PubMed 16829952. Source: UniProtKB
Molecular_function	aspartic endopeptidase activity, intramembrane cleaving Inferred from mutant phenotype PubMed 16873890. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.15PubMed 15998642PubMed 16873890. Source: UniProtKB
Complete GO annotation...

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	Helical; Potential
	Topological domain	53 – 77	25	Cytoplasmic Potential
	Transmembrane	78 – 98	21	Helical; Potential
	Topological domain	99 – 100	2	Lumenal Potential
	Transmembrane	101 – 121	21	Helical; Potential
	Topological domain	122 – 157	36	Cytoplasmic Potential
	Transmembrane	158 – 178	21	Helical; Potential
	Topological domain	179 – 181	3	Lumenal Potential
	Transmembrane	182 – 202	21	Helical; Potential
	Topological domain	203 – 209	7	Cytoplasmic Potential
	Transmembrane	210 – 230	21	Helical; Potential
	Topological domain	231 – 256	26	Lumenal Potential
	Transmembrane	257 – 277	21	Helical; Potential
	Topological domain	278 – 290	13	Cytoplasmic Potential
	Transmembrane	291 – 311	21	Helical; Potential
	Topological domain	312 – 314	3	Lumenal Potential
	Transmembrane	315 – 335	21	Helical; Potential
	Topological domain	336 – 377	42	Cytoplasmic Potential
	Motif	317 – 319	3	PAL
Sites
	Active site	219	1	By similarity
	Active site	265	1	By similarity
Amino acid modifications
	Glycosylation	10	1	N-linked (GlcNAc...) Ref.17
	Glycosylation	20	1	N-linked (GlcNAc...) Ref.17
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. Corresponds to variant rs1044419 [ dbSNP | Ensembl ].		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	219	1	D → A: Abolishes proteolysis of PSEN1. Ref.14
	Mutagenesis	264	1	G → A: No effect on proteolysis of PSEN1. Ref.14
	Mutagenesis	265	1	D → A: No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. Ref.1 Ref.14
	Mutagenesis	317	1	P → L: Abolishes proteolysis of PSEN1. Ref.14
	Sequence conflict	132	1	S → N AA sequence Ref.1
	Sequence conflict	150	1	K → R in BAC11519. Ref.8
	Sequence conflict	159	1	D → A AA sequence Ref.1
	Sequence conflict	235	1	S → F in AAH08938. Ref.11
	Sequence conflict	235	1	S → F in AAH08959. Ref.11
	Sequence conflict	295	1	F → Y in AAQ13609. Ref.7

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 [UniParc]. 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 [UniParc]. 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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Placenta.
[3]	"Novel class of polytopic proteins with domains associated with putative protease activity." Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I. Biokhimiia 67:826-834(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY. Tissue: Blood and Hippocampus.
[4]	"Cell-surface expression of a new splice variant of the mouse signal peptide peptidase." Urny J., Hermans-Borgmeyer I., Schaller H.C. Biochim. Biophys. Acta 1759:159-165(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[5]	"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).
[6]	"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).
[7]	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.
[8]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary gland, Retinoblastoma and Testis.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	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].
[11]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Muscle.
[12]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Impas 1 possesses endoproteolytic activity against multipass membrane protein substrate cleaving the presenilin 1 holoprotein." Moliaka Y.K., Grigorenko A., Madera D., Rogaev E.I. FEBS Lett. 557:185-192(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-219; GLY-264; ASP-265 AND PRO-317.
[15]	"Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins." Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U., Rovelli G., Martoglio B. J. Biol. Chem. 279:50790-50798(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[16]	"The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER." Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A., Gemmill R.M., Lehner P.J. J. Cell Biol. 186:685-692(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF139.
[17]	"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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-10 AND ASN-20, MASS SPECTROMETRY. Tissue: Liver.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ420895 mRNA. Translation: CAD13132.1. AF515663 mRNA. Translation: AAN77099.1. AY169310 mRNA. Translation: AAO12535.1. AY169311 mRNA. Translation: AAO12536.1. AY169312 mRNA. Translation: AAO12537.1. DQ168450 mRNA. Translation: ABA56163.1. AJ345029 mRNA. Translation: CAC87790.1. AF483215 mRNA. Translation: AAM22076.1. 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. CH471077 Genomic DNA. Translation: EAW76437.1. CH471077 Genomic DNA. Translation: EAW76435.1. CH471077 Genomic DNA. Translation: EAW76438.1. BC008938 mRNA. Translation: AAH08938.1. BC008959 mRNA. Translation: AAH08959.1. BC062595 mRNA. Translation: AAH62595.1.
IPI	IPI00152441. IPI00220687. IPI00329296. IPI00552772.
RefSeq	NP_110416.1. NM_030789.2. NP_848695.1. NM_178580.1. NP_848696.1. NM_178581.1. NP_848697.1. NM_178582.1.
UniGene	Hs.373741.
3D structure databases
ProteinModelPortal	Q8TCT9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TCT9. 6 interactions.
Protein family/group databases
MEROPS	A22.003.
PTM databases
PhosphoSite	Q8TCT9.
Polymorphism databases
DMDM	25008563.
Proteomic databases
PaxDb	Q8TCT9.
PRIDE	Q8TCT9.
Protocols and materials databases
DNASU	81502.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335574; ENSP00000335294; ENSG00000101294. ENST00000340852; ENSP00000343032; ENSG00000101294. ENST00000344042; ENSP00000341347; ENSG00000101294. ENST00000376127; ENSP00000365296; ENSG00000101294. ENST00000398174; ENSP00000381237; ENSG00000101294.
GeneID	81502.
KEGG	hsa:81502.
UCSC	uc002wwc.3. human. uc002wwd.3. human. uc002wwe.3. human.
Organism-specific databases
CTD	81502.
GeneCards	GC20P030106.
HGNC	HGNC:16435. HM13.
HPA	HPA045089.
MIM	607106. gene.
neXtProt	NX_Q8TCT9.
PharmGKB	PA29314.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG313636.
HOVERGEN	HBG024161.
KO	K09595.
OMA	TGCILLC.
OrthoDB	EOG4TF0K9.
Gene expression databases
Bgee	Q8TCT9.
Genevestigator	Q8TCT9.
GermOnline	ENSG00000101294. Homo sapiens.
Family and domain databases
InterPro	IPR006639. Peptidase_A22. IPR007369. Peptidase_A22B_SPP. [Graphical view]
PANTHER	PTHR12174. PTHR12174. 1 hit.
Pfam	PF04258. Peptidase_A22B. 1 hit. [Graphical view]
SMART	SM00730. PSN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HM13. human.
GenomeRNAi	81502.
NextBio	71746.
SOURCE	Search...

Entry information

Entry name

HM13_HUMAN

Accession

Primary (citable) accession number: Q8TCT9
Secondary accession number(s): B2RAY5 , E1P5L3, Q15K36, 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:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.