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Q14703

- MBTP1_HUMAN

UniProt

Q14703 - MBTP1_HUMAN

Protein

Membrane-bound transcription factor site-1 protease

Gene

MBTPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Serine protease that catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs). Other known substrates are BDNF, GNPTAB and ATF6. Cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4. Cleaves known substrates after Arg-Ser-Val-Leu (SERBP-2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu. Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes.1 Publication

    Catalytic activityi

    Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3.

    Cofactori

    Calcium.

    Enzyme regulationi

    Inhibited by divalent copper and zinc ions, but not by nickel or cobalt. Inhibited by its prosegment, but not smaller fragments thereof.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei186 – 1872Cleavage; by autolysis
    Active sitei218 – 2181Charge relay systemBy similarity
    Active sitei249 – 2491Charge relay systemBy similarity
    Active sitei414 – 4141Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. cholesterol metabolic process Source: UniProtKB-KW
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. lipid metabolic process Source: RefGenome
    6. lysosome organization Source: UniProtKB
    7. proteolysis Source: UniProtKB
    8. regulation of transcription factor import into nucleus Source: Ensembl
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_18348. ATF6-alpha activates chaperones.
    SignaLinkiQ14703.

    Protein family/group databases

    MEROPSiS08.063.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane-bound transcription factor site-1 protease (EC:3.4.21.112)
    Alternative name(s):
    Endopeptidase S1P
    Subtilisin/kexin-isozyme 1
    Short name:
    SKI-1
    Gene namesi
    Name:MBTPS1
    Synonyms:KIAA0091, S1P, SKI1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:15456. MBTPS1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: May sort to other organelles, including lysosomal and/or endosomal compartments.

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: ProtInc
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: RefGenome
    4. Golgi membrane Source: Reactome
    5. Golgi stack Source: Ensembl
    6. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30671.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Propeptidei18 – 186169PRO_0000027051Add
    BLAST
    Chaini187 – 1052866Membrane-bound transcription factor site-1 proteasePRO_0000027052Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi939 – 9391N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The 148 kDa zymogen is processed progressively into two membrane-bound 120 and 106 kDa forms in the endoplasmic reticulum, and late into a secreted 98 kDa form. The propeptide is autocatalytically removed through an intramolecular cleavage after Leu-186. Further cleavage generates 14, 10, and 8 kDa intermediates.

    Keywords - PTMi

    Autocatalytic cleavage, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ14703.
    PaxDbiQ14703.
    PRIDEiQ14703.

    PTM databases

    PhosphoSiteiQ14703.

    Miscellaneous databases

    PMAP-CutDBQ14703.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Inductioni

    Down-regulated by sterols.

    Gene expression databases

    ArrayExpressiQ14703.
    BgeeiQ14703.
    CleanExiHS_MBTPS1.
    GenevestigatoriQ14703.

    Organism-specific databases

    HPAiHPA006239.

    Interactioni

    Protein-protein interaction databases

    BioGridi114259. 11 interactions.
    IntActiQ14703. 7 interactions.
    MINTiMINT-6774172.
    STRINGi9606.ENSP00000344223.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14703.
    SMRiQ14703. Positions 53-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini187 – 998812LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1022 – 105231CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei999 – 102123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini214 – 472259Peptidase S8Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1023 – 105028Arg/Lys/Pro-rich (basic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S8 family.Curated
    Contains 1 peptidase S8 domain.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1404.
    HOGENOMiHOG000030053.
    HOVERGENiHBG052421.
    InParanoidiQ14703.
    KOiK08653.
    OMAiLPERMEG.
    OrthoDBiEOG7TBC1F.
    PhylomeDBiQ14703.
    TreeFamiTF324501.

    Family and domain databases

    Gene3Di3.40.50.200. 2 hits.
    InterProiIPR000209. Peptidase_S8/S53_dom.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF00082. Peptidase_S8. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF52743. SSF52743. 2 hits.
    PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q14703-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLVNIWLLL LVVLLCGKKH LGDRLEKKSF EKAPCPGCSH LTLKVEFSST     50
    VVEYEYIVAF NGYFTAKARN SFISSALKSS EVDNWRIIPR NNPSSDYPSD 100
    FEVIQIKEKQ KAGLLTLEDH PNIKRVTPQR KVFRSLKYAE SDPTVPCNET 150
    RWSQKWQSSR PLRRASLSLG SGFWHATGRH SSRRLLRAIP RQVAQTLQAD 200
    VLWQMGYTGA NVRVAVFDTG LSEKHPHFKN VKERTNWTNE RTLDDGLGHG 250
    TFVAGVIASM RECQGFAPDA ELHIFRVFTN NQVSYTSWFL DAFNYAILKK 300
    IDVLNLSIGG PDFMDHPFVD KVWELTANNV IMVSAIGNDG PLYGTLNNPA 350
    DQMDVIGVGG IDFEDNIARF SSRGMTTWEL PGGYGRMKPD IVTYGAGVRG 400
    SGVKGGCRAL SGTSVASPVV AGAVTLLVST VQKRELVNPA SMKQALIASA 450
    RRLPGVNMFE QGHGKLDLLR AYQILNSYKP QASLSPSYID LTECPYMWPY 500
    CSQPIYYGGM PTVVNVTILN GMGVTGRIVD KPDWQPYLPQ NGDNIEVAFS 550
    YSSVLWPWSG YLAISISVTK KAASWEGIAQ GHVMITVASP AETESKNGAE 600
    QTSTVKLPIK VKIIPTPPRS KRVLWDQYHN LRYPPGYFPR DNLRMKNDPL 650
    DWNGDHIHTN FRDMYQHLRS MGYFVEVLGA PFTCFDASQY GTLLMVDSEE 700
    EYFPEEIAKL RRDVDNGLSL VIFSDWYNTS VMRKVKFYDE NTRQWWMPDT 750
    GGANIPALNE LLSVWNMGFS DGLYEGEFTL ANHDMYYASG CSIAKFPEDG 800
    VVITQTFKDQ GLEVLKQETA VVENVPILGL YQIPAEGGGR IVLYGDSNCL 850
    DDSHRQKDCF WLLDALLQYT SYGVTPPSLS HSGNRQRPPS GAGSVTPERM 900
    EGNHLHRYSK VLEAHLGDPK PRPLPACPRL SWAKPQPLNE TAPSNLWKHQ 950
    KLLSIDLDKV VLPNFRSNRP QVRPLSPGES GAWDIPGGIM PGRYNQEVGQ 1000
    TIPVFAFLGA MVVLAFFVVQ INKAKSRPKR RKPRVKRPQL MQQVHPPKTP 1050
    SV 1052
    Length:1,052
    Mass (Da):117,749
    Last modified:November 1, 1996 - v1
    Checksum:iCA6F013588595B45
    GO

    Sequence cautioni

    The sequence BAA07653.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti843 – 8431L → Q in BAF84462. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61I → T.
    Corresponds to variant rs34701895 [ dbSNP | Ensembl ].
    VAR_051822
    Natural varianti90 – 901R → G.
    Corresponds to variant rs34076105 [ dbSNP | Ensembl ].
    VAR_051823

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42053 mRNA. Translation: BAA07653.2. Different initiation.
    AK291773 mRNA. Translation: BAF84462.1.
    AC040169 Genomic RNA. No translation available.
    BC114555 mRNA. Translation: AAI14556.1.
    BC114961 mRNA. Translation: AAI14962.1.
    AL133583 mRNA. Translation: CAB63727.1.
    CCDSiCCDS10941.1.
    PIRiT43492.
    RefSeqiNP_003782.1. NM_003791.3.
    UniGeneiHs.75890.

    Genome annotation databases

    EnsembliENST00000343411; ENSP00000344223; ENSG00000140943.
    GeneIDi8720.
    KEGGihsa:8720.
    UCSCiuc002fhh.3. human.

    Polymorphism databases

    DMDMi17368466.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D42053 mRNA. Translation: BAA07653.2 . Different initiation.
    AK291773 mRNA. Translation: BAF84462.1 .
    AC040169 Genomic RNA. No translation available.
    BC114555 mRNA. Translation: AAI14556.1 .
    BC114961 mRNA. Translation: AAI14962.1 .
    AL133583 mRNA. Translation: CAB63727.1 .
    CCDSi CCDS10941.1.
    PIRi T43492.
    RefSeqi NP_003782.1. NM_003791.3.
    UniGenei Hs.75890.

    3D structure databases

    ProteinModelPortali Q14703.
    SMRi Q14703. Positions 53-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114259. 11 interactions.
    IntActi Q14703. 7 interactions.
    MINTi MINT-6774172.
    STRINGi 9606.ENSP00000344223.

    Chemistry

    BindingDBi Q14703.
    ChEMBLi CHEMBL5916.

    Protein family/group databases

    MEROPSi S08.063.

    PTM databases

    PhosphoSitei Q14703.

    Polymorphism databases

    DMDMi 17368466.

    Proteomic databases

    MaxQBi Q14703.
    PaxDbi Q14703.
    PRIDEi Q14703.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343411 ; ENSP00000344223 ; ENSG00000140943 .
    GeneIDi 8720.
    KEGGi hsa:8720.
    UCSCi uc002fhh.3. human.

    Organism-specific databases

    CTDi 8720.
    GeneCardsi GC16M084087.
    HGNCi HGNC:15456. MBTPS1.
    HPAi HPA006239.
    MIMi 603355. gene.
    neXtProti NX_Q14703.
    PharmGKBi PA30671.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1404.
    HOGENOMi HOG000030053.
    HOVERGENi HBG052421.
    InParanoidi Q14703.
    KOi K08653.
    OMAi LPERMEG.
    OrthoDBi EOG7TBC1F.
    PhylomeDBi Q14703.
    TreeFami TF324501.

    Enzyme and pathway databases

    Reactomei REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_18348. ATF6-alpha activates chaperones.
    SignaLinki Q14703.

    Miscellaneous databases

    ChiTaRSi MBTPS1. human.
    GenomeRNAii 8720.
    NextBioi 32705.
    PMAP-CutDB Q14703.
    PROi Q14703.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14703.
    Bgeei Q14703.
    CleanExi HS_MBTPS1.
    Genevestigatori Q14703.

    Family and domain databases

    Gene3Di 3.40.50.200. 2 hits.
    InterProi IPR000209. Peptidase_S8/S53_dom.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF00082. Peptidase_S8. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF52743. SSF52743. 2 hits.
    PROSITEi PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure and chromosomal mapping of the human site-1 protease (S1P) gene."
      Nakajima T., Iwaki K., Kodama T., Inazawa J., Emi M.
      J. Hum. Genet. 45:212-217(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Myeloid.
    2. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. "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].
      Tissue: Placenta.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1052.
      Tissue: Testis.
    7. "Biosynthesis and enzymatic characterization of human SKI-1/S1P and the processing of its inhibitory prosegment."
      Toure B.B., Munzer J.S., Basak A., Benjannet S., Rochemont J., Lazure C., Chretien M., Seidah N.G.
      J. Biol. Chem. 275:2349-2358(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Mammalian subtilisin/kexin isozyme SKI-1: a widely expressed proprotein convertase with a unique cleavage specificity and cellular localization."
      Seidah N.G., Mowla S.J., Hamelin J., Mamarbachi A.M., Benjannet S., Toure B.B., Basak A., Munzer J.S., Marcinkiewicz J., Zhong M., Barale J.-C., Lazure C., Murphy R.A., Chretien M., Marcinkiewicz M.
      Proc. Natl. Acad. Sci. U.S.A. 96:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism."
      Marschner K., Kollmann K., Schweizer M., Braulke T., Pohl S.
      Science 333:87-90(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMBTP1_HUMAN
    AccessioniPrimary (citable) accession number: Q14703
    Secondary accession number(s): A8K6V8, Q24JQ2, Q9UF67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 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 16
      Human chromosome 16: 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