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Q8TCT9

- HM13_HUMAN

UniProt

Q8TCT9 - HM13_HUMAN

Protein

Minor histocompatibility antigen H13

Gene

HM13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    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.By similarity4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei219 – 2191By similarity
    Active sitei265 – 2651By similarity

    GO - Molecular functioni

    1. aspartic endopeptidase activity, intramembrane cleaving Source: UniProtKB
    2. peptidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. membrane protein proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease

    Protein family/group databases

    MEROPSiA22.003.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:HM13
    Synonyms:H13, IMP1, PSL3, SPP
    ORF Names:MSTP086
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16435. HM13.

    Subcellular locationi

    Isoform 4 : Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
    4. integral component of lumenal side of endoplasmic reticulum membrane Source: UniProtKB
    5. membrane Source: UniProtKB
    6. plasma membrane Source: UniProtKB-SubCell
    7. rough endoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101N → Q: Abolishes N-glycosylation; when associated with Q-20. 1 Publication
    Mutagenesisi20 – 201N → Q: Abolishes N-glycosylation; when associated with Q-10. 1 Publication
    Mutagenesisi219 – 2191D → A: Abolishes proteolysis of PSEN1. 1 Publication
    Mutagenesisi264 – 2641G → A: No effect on proteolysis of PSEN1. 1 Publication
    Mutagenesisi265 – 2651D → A: No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. 2 Publications
    Mutagenesisi317 – 3171P → L: Abolishes proteolysis of PSEN1. 1 Publication

    Organism-specific databases

    PharmGKBiPA29314.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Minor histocompatibility antigen H13PRO_0000073907Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi10 – 101N-linked (GlcNAc...)2 Publications
    Glycosylationi20 – 201N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8TCT9.
    PaxDbiQ8TCT9.
    PRIDEiQ8TCT9.

    PTM databases

    PhosphoSiteiQ8TCT9.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    BgeeiQ8TCT9.
    GenevestigatoriQ8TCT9.

    Organism-specific databases

    HPAiHPA045089.

    Interactioni

    Subunit structurei

    Interacts with RNF139.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P4HBP072373EBI-347472,EBI-395883

    Protein-protein interaction databases

    BioGridi123505. 10 interactions.
    IntActiQ8TCT9. 8 interactions.
    MINTiMINT-3034232.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TCT9.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3131LumenalSequence AnalysisAdd
    BLAST
    Topological domaini53 – 7725CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini99 – 1002LumenalSequence Analysis
    Topological domaini122 – 15736CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini179 – 1813LumenalSequence Analysis
    Topological domaini203 – 2097CytoplasmicSequence Analysis
    Topological domaini231 – 25626LumenalSequence AnalysisAdd
    BLAST
    Topological domaini278 – 29013CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini312 – 3143LumenalSequence Analysis
    Topological domaini336 – 37742CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei32 – 5221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei78 – 9821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei101 – 12121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei158 – 17821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei182 – 20221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei210 – 23021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei257 – 27721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei291 – 31121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei315 – 33521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi317 – 3193PAL

    Domaini

    The first transmembrane domain may act as a type I signal anchor. The PAL motif is required for normal active site conformation.By similarity

    Sequence similaritiesi

    Belongs to the peptidase A22B family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG313636.
    HOVERGENiHBG024161.
    KOiK09595.
    OMAiSSEMPET.
    OrthoDBiEOG7Z3F4N.
    PhylomeDBiQ8TCT9.
    TreeFamiTF105854.

    Family and domain databases

    InterProiIPR007369. Peptidase_A22B_SPP.
    IPR006639. Preselin/SPP.
    [Graphical view]
    PANTHERiPTHR12174. PTHR12174. 1 hit.
    PfamiPF04258. Peptidase_A22B. 1 hit.
    [Graphical view]
    SMARTiSM00730. PSN. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TCT9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDSALSDPHN GSAEAGGPTN STTRPPSTPE GIALAYGSLL LMALLPIFFG    50
    ALRSVRCARG KNASDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY 100
    INLLLSMYFF VLGILALSHT ISPFMNKFFP ASFPNRQYQL LFTQGSGENK 150
    EEIINYEFDT KDLVCLGLSS IVGVWYLLRK HWIANNLFGL AFSLNGVELL 200
    HLNNVSTGCI LLGGLFIYDV FWVFGTNVMV TVAKSFEAPI KLVFPQDLLE 250
    KGLEANNFAM LGLGDVVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF 300
    GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV TEMFSYEESN 350
    PKDPAAVTES KEGTEASASK GLEKKEK 377
    Length:377
    Mass (Da):41,488
    Last modified:June 1, 2002 - v1
    Checksum:i322D231B52B33118
    GO
    Isoform 2 (identifier: Q8TCT9-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:426
    Mass (Da):46,825
    Checksum:i269AD5CC99982845
    GO
    Isoform 4 (identifier: Q8TCT9-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:394
    Mass (Da):43,423
    Checksum:i9BEC3A1C9B605D48
    GO
    Isoform 5 (identifier: Q8TCT9-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:335
    Mass (Da):36,814
    Checksum:iD22777AF67B3720B
    GO

    Sequence cautioni

    The sequence BAC11138.1 differs from that shown. Reason: Intron retention.
    The sequence AAQ13609.1 differs from that shown. Reason: Frameshift at positions 320, 329, 330 and 358.
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321S → N AA sequence (PubMed:12077416)Curated
    Sequence conflicti150 – 1501K → R in BAC11519. (PubMed:14702039)Curated
    Sequence conflicti159 – 1591D → A AA sequence (PubMed:12077416)Curated
    Sequence conflicti235 – 2351S → F in AAH08938. (PubMed:15489334)Curated
    Sequence conflicti235 – 2351S → F in AAH08959. (PubMed:15489334)Curated
    Sequence conflicti295 – 2951F → Y in AAQ13609. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti259 – 2591A → P.
    Corresponds to variant rs1044419 [ dbSNP | Ensembl ].
    VAR_014274

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei181 – 22242Missing in isoform 5. CuratedVSP_015082Add
    BLAST
    Alternative sequencei347 – 3471E → ESSAEILPHTPRLTHFPTVS GSPASLADSMQQKLAGPRRR RPQNPSAIYE in isoform 2. 1 PublicationVSP_005196
    Alternative sequencei348 – 37730ESNPK…EKKEK → SSAEILPHTPRLTHFPTVSG SPASLADSMQQKLAGPRRRR PQNPSAM in isoform 4. 2 PublicationsVSP_015083Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13182.1. [Q8TCT9-1]
    CCDS13183.1. [Q8TCT9-4]
    CCDS42861.1. [Q8TCT9-2]
    RefSeqiNP_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.
    UniGeneiHs.373741.

    Genome annotation databases

    EnsembliENST00000335574; ENSP00000335294; ENSG00000101294. [Q8TCT9-4]
    ENST00000340852; ENSP00000343032; ENSG00000101294. [Q8TCT9-1]
    ENST00000398174; ENSP00000381237; ENSG00000101294. [Q8TCT9-2]
    GeneIDi81502.
    KEGGihsa:81502.
    UCSCiuc002wwc.3. human. [Q8TCT9-2]
    uc002wwd.3. human. [Q8TCT9-4]
    uc002wwe.3. human. [Q8TCT9-1]

    Polymorphism databases

    DMDMi25008563.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13182.1. [Q8TCT9-1 ]
    CCDS13183.1. [Q8TCT9-4 ]
    CCDS42861.1. [Q8TCT9-2 ]
    RefSeqi NP_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.
    UniGenei Hs.373741.

    3D structure databases

    ProteinModelPortali Q8TCT9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123505. 10 interactions.
    IntActi Q8TCT9. 8 interactions.
    MINTi MINT-3034232.

    Protein family/group databases

    MEROPSi A22.003.

    PTM databases

    PhosphoSitei Q8TCT9.

    Polymorphism databases

    DMDMi 25008563.

    Proteomic databases

    MaxQBi Q8TCT9.
    PaxDbi Q8TCT9.
    PRIDEi Q8TCT9.

    Protocols and materials databases

    DNASUi 81502.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335574 ; ENSP00000335294 ; ENSG00000101294 . [Q8TCT9-4 ]
    ENST00000340852 ; ENSP00000343032 ; ENSG00000101294 . [Q8TCT9-1 ]
    ENST00000398174 ; ENSP00000381237 ; ENSG00000101294 . [Q8TCT9-2 ]
    GeneIDi 81502.
    KEGGi hsa:81502.
    UCSCi uc002wwc.3. human. [Q8TCT9-2 ]
    uc002wwd.3. human. [Q8TCT9-4 ]
    uc002wwe.3. human. [Q8TCT9-1 ]

    Organism-specific databases

    CTDi 81502.
    GeneCardsi GC20P030106.
    HGNCi HGNC:16435. HM13.
    HPAi HPA045089.
    MIMi 607106. gene.
    neXtProti NX_Q8TCT9.
    PharmGKBi PA29314.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313636.
    HOVERGENi HBG024161.
    KOi K09595.
    OMAi SSEMPET.
    OrthoDBi EOG7Z3F4N.
    PhylomeDBi Q8TCT9.
    TreeFami TF105854.

    Miscellaneous databases

    ChiTaRSi HM13. human.
    GeneWikii HM13.
    GenomeRNAii 81502.
    NextBioi 71746.
    PROi Q8TCT9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8TCT9.
    Genevestigatori Q8TCT9.

    Family and domain databases

    InterProi IPR007369. Peptidase_A22B_SPP.
    IPR006639. Preselin/SPP.
    [Graphical view ]
    PANTHERi PTHR12174. PTHR12174. 1 hit.
    Pfami PF04258. Peptidase_A22B. 1 hit.
    [Graphical view ]
    SMARTi SM00730. PSN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHM13_HUMAN
    AccessioniPrimary (citable) accession number: Q8TCT9
    Secondary accession number(s): B2RAY5
    , E1P5L3, Q15K36, Q540H8, Q5JWP2, Q5JWP3, Q5JWP4, Q5JWP5, Q7Z4F2, Q86Y35, Q95H87, Q9H110, Q9H111
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3