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Q8TCT9 (HM13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P4HBP072373EBI-347472,EBI-395883

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Minor histocompatibility antigen H13
PRO_0000073907

Regions

Topological domain1 – 3131Lumenal Potential
Transmembrane32 – 5221Helical; Potential
Topological domain53 – 7725Cytoplasmic Potential
Transmembrane78 – 9821Helical; Potential
Topological domain99 – 1002Lumenal Potential
Transmembrane101 – 12121Helical; Potential
Topological domain122 – 15736Cytoplasmic Potential
Transmembrane158 – 17821Helical; Potential
Topological domain179 – 1813Lumenal Potential
Transmembrane182 – 20221Helical; Potential
Topological domain203 – 2097Cytoplasmic Potential
Transmembrane210 – 23021Helical; Potential
Topological domain231 – 25626Lumenal Potential
Transmembrane257 – 27721Helical; Potential
Topological domain278 – 29013Cytoplasmic Potential
Transmembrane291 – 31121Helical; Potential
Topological domain312 – 3143Lumenal Potential
Transmembrane315 – 33521Helical; Potential
Topological domain336 – 37742Cytoplasmic Potential
Motif317 – 3193PAL

Sites

Active site2191 By similarity
Active site2651 By similarity

Amino acid modifications

Glycosylation101N-linked (GlcNAc...) Ref.17
Glycosylation201N-linked (GlcNAc...) Ref.17

Natural variations

Alternative sequence181 – 22242Missing in isoform 5.
VSP_015082
Alternative sequence3471E → ESSAEILPHTPRLTHFPTVS GSPASLADSMQQKLAGPRRR RPQNPSAIYE in isoform 2.
VSP_005196
Alternative sequence348 – 37730ESNPK…EKKEK → SSAEILPHTPRLTHFPTVSG SPASLADSMQQKLAGPRRRR PQNPSAM in isoform 4.
VSP_015083
Natural variant2591A → P.
Corresponds to variant rs1044419 [ dbSNP | Ensembl ].
VAR_014274

Experimental info

Mutagenesis101N → Q: Abolishes N-glycosylation; when associated with Q-20. Ref.1
Mutagenesis201N → Q: Abolishes N-glycosylation; when associated with Q-10. Ref.1
Mutagenesis2191D → A: Abolishes proteolysis of PSEN1. Ref.14
Mutagenesis2641G → A: No effect on proteolysis of PSEN1. Ref.14
Mutagenesis2651D → A: No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. Ref.1 Ref.14
Mutagenesis3171P → L: Abolishes proteolysis of PSEN1. Ref.14
Sequence conflict1321S → N AA sequence Ref.1
Sequence conflict1501K → R in BAC11519. Ref.8
Sequence conflict1591D → A AA sequence Ref.1
Sequence conflict2351S → F in AAH08938. Ref.11
Sequence conflict2351S → F in AAH08959. Ref.11
Sequence conflict2951F → Y in AAQ13609. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 322D231B52B33118

FASTA37741,488
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 269AD5CC99982845
Show »

FASTA42646,825
Isoform 4 [UniParc].

Checksum: 9BEC3A1C9B605D48
Show »

FASTA39443,423
Isoform 5 [UniParc].

Checksum: D22777AF67B3720B
Show »

FASTA33536,814

References

« Hide '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.
Biochemistry (Mosc.) 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
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.
CCDSCCDS13182.1. [Q8TCT9-1]
CCDS13183.1. [Q8TCT9-4]
CCDS42861.1. [Q8TCT9-2]
RefSeqNP_110416.1. NM_030789.3. [Q8TCT9-1]
NP_848695.1. NM_178580.2. [Q8TCT9-4]
NP_848696.1. NM_178581.2. [Q8TCT9-2]
NP_848697.1. NM_178582.2.
UniGeneHs.373741.

3D structure databases

ProteinModelPortalQ8TCT9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123505. 9 interactions.
IntActQ8TCT9. 8 interactions.
MINTMINT-3034232.

Protein family/group databases

MEROPSA22.003.

PTM databases

PhosphoSiteQ8TCT9.

Polymorphism databases

DMDM25008563.

Proteomic databases

MaxQBQ8TCT9.
PaxDbQ8TCT9.
PRIDEQ8TCT9.

Protocols and materials databases

DNASU81502.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335574; ENSP00000335294; ENSG00000101294. [Q8TCT9-4]
ENST00000340852; ENSP00000343032; ENSG00000101294. [Q8TCT9-1]
ENST00000376127; ENSP00000365296; ENSG00000101294. [Q8TCT9-5]
ENST00000398174; ENSP00000381237; ENSG00000101294. [Q8TCT9-2]
GeneID81502.
KEGGhsa:81502.
UCSCuc002wwc.3. human. [Q8TCT9-2]
uc002wwd.3. human. [Q8TCT9-4]
uc002wwe.3. human. [Q8TCT9-1]

Organism-specific databases

CTD81502.
GeneCardsGC20P030106.
HGNCHGNC:16435. HM13.
HPAHPA045089.
MIM607106. gene.
neXtProtNX_Q8TCT9.
PharmGKBPA29314.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313636.
HOVERGENHBG024161.
KOK09595.
OMASSEMPET.
OrthoDBEOG7Z3F4N.
PhylomeDBQ8TCT9.
TreeFamTF105854.

Gene expression databases

BgeeQ8TCT9.
GenevestigatorQ8TCT9.

Family and domain databases

InterProIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERPTHR12174. PTHR12174. 1 hit.
PfamPF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHM13. human.
GeneWikiHM13.
GenomeRNAi81502.
NextBio71746.
PROQ8TCT9.
SOURCESearch...

Entry information

Entry nameHM13_HUMAN
AccessionPrimary (citable) accession number: Q8TCT9
Secondary accession number(s): B2RAY5 expand/collapse secondary AC list , 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: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM