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O43462

- MBTP2_HUMAN

UniProt

O43462 - MBTP2_HUMAN

Protein

Membrane-bound transcription factor site-2 protease

Gene

MBTPS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Intramembrane proteolysis of sterol-regulatory element-binding proteins (SREBPs) within the first transmembrane segment thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Site-2 cleavage comes after site-1 cleavage which takes place in the lumenal loop.

    Catalytic activityi

    Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi171 – 1711Zinc; catalytic
    Active sitei172 – 1721
    Metal bindingi175 – 1751Zinc; catalytic

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: ProtInc

    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: ProtInc
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.85. 2681.
    ReactomeiREACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_18348. ATF6-alpha activates chaperones.

    Protein family/group databases

    MEROPSiM50.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane-bound transcription factor site-2 protease (EC:3.4.24.85)
    Alternative name(s):
    Endopeptidase S2P
    Sterol regulatory element-binding proteins intramembrane protease
    Short name:
    SREBPs intramembrane protease
    Gene namesi
    Name:MBTPS2
    Synonyms:S2P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:15455. MBTPS2.

    Subcellular locationi

    Membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    IFAP syndrome with or without BRESHECK syndrome (IFAPS) [MIM:308205]: A syndrome characterized by a peculiar triad of follicular ichthyosis, total or subtotal atrichia, and photophobia of varying degree. Histopathologically, the epidermal granular layer is generally well-preserved or thickened at the infundibulum. Hair follicles are poorly developed and tend to be surrounded by an inflammatory infiltrate. A subgroup of patients is described with lamellar rather than follicular ichthyosis. Non-consistent features may include growth and psychomotor retardation, aganglionic megacolon, seizures and nail dystrophy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063054
    Natural varianti226 – 2261W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063055
    Natural varianti227 – 2271H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063056
    Natural varianti429 – 4291R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063057
    Natural varianti475 – 4751F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063058
    Keratosis follicularis spinulosa decalvans X-linked (KFSDX) [MIM:308800]: A rare disorder affecting the skin and the eye. Affected men show thickening of the skin of the neck, ears, and extremities, especially the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti508 – 5081N → S in KFSDX; sterol responsiveness is reduced by half. 1 Publication
    VAR_064409

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi171 – 1711H → F: Loss of activity. 1 Publication
    Mutagenesisi172 – 1721E → A or Q: Loss of activity. 1 Publication
    Mutagenesisi172 – 1721E → D: Partial loss of activity. 1 Publication
    Mutagenesisi175 – 1751H → F: Loss of activity. 1 Publication
    Mutagenesisi467 – 4671D → N: Loss of activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Ichthyosis

    Organism-specific databases

    MIMi308205. phenotype.
    308800. phenotype.
    Orphaneti85284. BRESEK syndrome.
    2273. Ichthyosis follicularis - alopecia - photophobia.
    2340. Keratosis follicularis spinulosa decalvans.
    659. Mutilating palmoplantar keratoderma with periorificial keratotic plaques.
    PharmGKBiPA30672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 519519Membrane-bound transcription factor site-2 proteasePRO_0000088482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi337 – 3371N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiO43462.
    PaxDbiO43462.
    PRIDEiO43462.

    PTM databases

    PhosphoSiteiO43462.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiO43462.
    BgeeiO43462.
    CleanExiHS_MBTPS2.
    GenevestigatoriO43462.

    Organism-specific databases

    HPAiCAB009486.
    HPA005494.

    Interactioni

    Protein-protein interaction databases

    BioGridi119495. 1 interaction.
    STRINGi9606.ENSP00000368798.

    Structurei

    3D structure databases

    ProteinModelPortaliO43462.
    SMRiO43462. Positions 252-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 33Cytoplasmic1 Publication
    Topological domaini25 – 7450Lumenal1 PublicationAdd
    BLAST
    Topological domaini108 – 14437Lumenal1 PublicationAdd
    BLAST
    Topological domaini252 – 446195Lumenal1 PublicationAdd
    BLAST
    Topological domaini477 – 49216LumenalSequence AnalysisAdd
    BLAST
    Topological domaini514 – 5196CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4 – 2421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei75 – 9521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei96 – 10712HelicalSequence AnalysisAdd
    BLAST
    Transmembranei145 – 16925HelicalSequence AnalysisAdd
    BLAST
    Transmembranei174 – 18613HelicalSequence AnalysisAdd
    BLAST
    Transmembranei187 – 20923HelicalSequence AnalysisAdd
    BLAST
    Transmembranei229 – 25123HelicalSequence AnalysisAdd
    BLAST
    Transmembranei447 – 46418HelicalSequence AnalysisAdd
    BLAST
    Transmembranei465 – 47612HelicalSequence AnalysisAdd
    BLAST
    Transmembranei493 – 51321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi109 – 13628Poly-SerAdd
    BLAST
    Compositional biasi285 – 386102Cys-richAdd
    BLAST
    Compositional biasi380 – 3845Poly-Ser

    Sequence similaritiesi

    Belongs to the peptidase M50A family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0750.
    HOGENOMiHOG000231255.
    HOVERGENiHBG006397.
    InParanoidiO43462.
    KOiK07765.
    OMAiHLQYTVS.
    OrthoDBiEOG7WMCJB.
    PhylomeDBiO43462.
    TreeFamiTF314478.

    Family and domain databases

    InterProiIPR001193. MBTPS2.
    IPR001478. PDZ.
    IPR008915. Peptidase_M50.
    [Graphical view]
    PANTHERiPTHR13325. PTHR13325. 1 hit.
    PfamiPF02163. Peptidase_M50. 1 hit.
    [Graphical view]
    PRINTSiPR01000. SREBPS2PTASE.
    SUPFAMiSSF50156. SSF50156. 1 hit.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O43462-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIPVSLVVVV VGGWTVVYLT DLVLKSSVYF KHSYEDWLEN NGLSISPFHI    50
    RWQTAVFNRA FYSWGRRKAR MLYQWFNFGM VFGVIAMFSS FFLLGKTLMQ 100
    TLAQMMADSP SSYSSSSSSS SSSSSSSSSS SSSSSSLHNE QVLQVVVPGI 150
    NLPVNQLTYF FTAVLISGVV HEIGHGIAAI REQVRFNGFG IFLFIIYPGA 200
    FVDLFTTHLQ LISPVQQLRI FCAGIWHNFV LALLGILALV LLPVILLPFY 250
    YTGVGVLITE VAEDSPAIGP RGLFVGDLVT HLQDCPVTNV QDWNECLDTI 300
    AYEPQIGYCI SASTLQQLSF PVRAYKRLDG STECCNNHSL TDVCFSYRNN 350
    FNKRLHTCLP ARKAVEATQV CRTNKDCKKS SSSSFCIIPS LETHTRLIKV 400
    KHPPQIDMLY VGHPLHLHYT VSITSFIPRF NFLSIDLPVV VETFVKYLIS 450
    LSGALAIVNA VPCFALDGQW ILNSFLDATL TSVIGDNDVK DLIGFFILLG 500
    GSVLLAANVT LGLWMVTAR 519
    Length:519
    Mass (Da):57,444
    Last modified:June 1, 1998 - v1
    Checksum:i247D69E0FD7747BD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871M → I in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063054
    Natural varianti226 – 2261W → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063055
    Natural varianti227 – 2271H → L in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063056
    Natural varianti429 – 4291R → H in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063057
    Natural varianti475 – 4751F → S in IFAPS; does not affect subcellular localization; impairs activity. 1 Publication
    VAR_063058
    Natural varianti508 – 5081N → S in KFSDX; sterol responsiveness is reduced by half. 1 Publication
    VAR_064409

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019612 mRNA. Translation: AAC51937.1.
    U73479 Genomic DNA. Translation: AAD08632.1.
    U72788 Genomic DNA. Translation: AAD08631.1.
    CCDSiCCDS14201.1.
    RefSeqiNP_056968.1. NM_015884.3.
    UniGeneiHs.443490.

    Genome annotation databases

    EnsembliENST00000379484; ENSP00000368798; ENSG00000012174.
    GeneIDi51360.
    KEGGihsa:51360.
    UCSCiuc004dae.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019612 mRNA. Translation: AAC51937.1 .
    U73479 Genomic DNA. Translation: AAD08632.1 .
    U72788 Genomic DNA. Translation: AAD08631.1 .
    CCDSi CCDS14201.1.
    RefSeqi NP_056968.1. NM_015884.3.
    UniGenei Hs.443490.

    3D structure databases

    ProteinModelPortali O43462.
    SMRi O43462. Positions 252-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119495. 1 interaction.
    STRINGi 9606.ENSP00000368798.

    Protein family/group databases

    MEROPSi M50.001.

    PTM databases

    PhosphoSitei O43462.

    Proteomic databases

    MaxQBi O43462.
    PaxDbi O43462.
    PRIDEi O43462.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379484 ; ENSP00000368798 ; ENSG00000012174 .
    GeneIDi 51360.
    KEGGi hsa:51360.
    UCSCi uc004dae.3. human.

    Organism-specific databases

    CTDi 51360.
    GeneCardsi GC0XP021857.
    HGNCi HGNC:15455. MBTPS2.
    HPAi CAB009486.
    HPA005494.
    MIMi 300294. gene.
    308205. phenotype.
    308800. phenotype.
    neXtProti NX_O43462.
    Orphaneti 85284. BRESEK syndrome.
    2273. Ichthyosis follicularis - alopecia - photophobia.
    2340. Keratosis follicularis spinulosa decalvans.
    659. Mutilating palmoplantar keratoderma with periorificial keratotic plaques.
    PharmGKBi PA30672.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0750.
    HOGENOMi HOG000231255.
    HOVERGENi HBG006397.
    InParanoidi O43462.
    KOi K07765.
    OMAi HLQYTVS.
    OrthoDBi EOG7WMCJB.
    PhylomeDBi O43462.
    TreeFami TF314478.

    Enzyme and pathway databases

    BRENDAi 3.4.24.85. 2681.
    Reactomei REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
    REACT_18348. ATF6-alpha activates chaperones.

    Miscellaneous databases

    ChiTaRSi MBTPS2. human.
    GenomeRNAii 51360.
    NextBioi 54814.
    PROi O43462.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43462.
    Bgeei O43462.
    CleanExi HS_MBTPS2.
    Genevestigatori O43462.

    Family and domain databases

    InterProi IPR001193. MBTPS2.
    IPR001478. PDZ.
    IPR008915. Peptidase_M50.
    [Graphical view ]
    PANTHERi PTHR13325. PTHR13325. 1 hit.
    Pfami PF02163. Peptidase_M50. 1 hit.
    [Graphical view ]
    PRINTSi PR01000. SREBPS2PTASE.
    SUPFAMi SSF50156. SSF50156. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs."
      Rawson R.B., Zelenski N.G., Nijhawan D., Ye J., Sakai J., Hasan M.T., Chang T.Y., Brown M.S., Goldstein J.L.
      Mol. Cell 1:47-57(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF HIS-171; GLU-172; HIS-175 AND ASP-467.
      Tissue: Fibroblast.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Membrane topology of S2P, a protein required for intramembranous cleavage of sterol regulatory element-binding proteins."
      Zelenski N.G., Rawson R.B., Brown M.S., Goldstein J.L.
      J. Biol. Chem. 274:21973-21980(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, GLYCOSYLATION AT ASN-337.
    4. "Asparagine-proline sequence within membrane-spanning segment of SREBP triggers intramembrane cleavage by site-2 protease."
      Ye J., Dave U.P., Grishin N.V., Goldstein J.L., Brown M.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:5123-5128(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. "IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response."
      Oeffner F., Fischer G., Happle R., Konig A., Betz R.C., Bornholdt D., Neidel U., Boente Mdel C., Redler S., Romero-Gomez J., Salhi A., Vera-Casano A., Weirich C., Grzeschik K.H.
      Am. J. Hum. Genet. 84:459-467(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, VARIANTS IFAPS ILE-87; LEU-226; LEU-227; HIS-429 AND SER-475, CHARACTERIZATION OF VARIANTS IFAPS ILE-87; LEU-226; LEU-227; HIS-429 AND SER-475.
    6. Cited for: VARIANT KFSDX SER-508, CHARACTERIZATION OF VARIANT KFSDX SER-508.

    Entry informationi

    Entry nameiMBTP2_HUMAN
    AccessioniPrimary (citable) accession number: O43462
    Secondary accession number(s): Q9UM70, Q9UMD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 129 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, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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